ID DLEC1_HUMAN Reviewed; 1755 AA. AC Q9Y238; Q9NSW0; Q9NTG5; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 14-DEC-2022, entry version 150. DE RecName: Full=Deleted in lung and esophageal cancer protein 1; DE AltName: Full=Deleted in lung cancer protein 1; DE Short=DLC-1; GN Name=DLEC1 {ECO:0000312|EMBL:BAA77624.1}; GN Synonyms=DLC1 {ECO:0000303|PubMed:10213508}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA77624.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, RP PUTATIVE FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP INVOLVEMENT IN LUNG CANCER; ESOPHAGEAL CANCER AND RENAL CANCER. RX PubMed=10213508; RA Daigo Y., Nishiwaki T., Kawasoe T., Tamari M., Tsuchiya E., Nakamura Y.; RT "Molecular cloning of a candidate tumor suppressor gene, DLC1, from RT chromosome 3p21.3."; RL Cancer Res. 59:1966-1972(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-1755 (ISOFORM 2), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1417-1755 (ISOFORM 3). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP VARIANT [LARGE SCALE ANALYSIS] ARG-351. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [5] RP SUBCELLULAR LOCATION, AND INTERACTION WITH ALPHA-TUBULIN; BETA-TUBULIN; RP BBS2; BBS4; BBS5; MKKS; TCP1; CCT2; CCT3; CCT4; CCT5 AND CCT7. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). CC -!- FUNCTION: Essential for spermatogenesis and male fertility (By CC similarity). May play an important role in sperm head and tail CC formation (By similarity). May act as a tumor suppressor by inhibiting CC cell proliferation. {ECO:0000250|UniProtKB:Q8BLA1, CC ECO:0000269|PubMed:10213508}. CC -!- SUBUNIT: Interacts with alpha- and beta-tubulin (PubMed:33144677). CC Interacts with BBS2, BBS4, BBS5, MKKS, TCP1, CCT2, CCT3, CCT4, CCT5 and CC CCT7 (PubMed:33144677). {ECO:0000269|PubMed:33144677}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10213508, CC ECO:0000269|PubMed:33144677}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=At least six differentially spliced products may exist. CC {ECO:0000303|PubMed:10213508}; CC Name=1 {ECO:0000303|PubMed:10213508}; CC IsoId=Q9Y238-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y238-2; Sequence=VSP_051847, VSP_051848, VSP_051849; CC Name=3; Synonyms=1S3 {ECO:0000303|PubMed:10213508}; CC IsoId=Q9Y238-3; Sequence=VSP_051850; CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Expression is CC highest in prostate and testis. {ECO:0000269|PubMed:10213508}. CC -!- DISEASE: Note=DLEC1 silencing due to promoter methylation and aberrant CC transcription are implicated in the development of different cancers, CC including esophageal (ESCR), renal and lung cancers (LNCR). CC -!- DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting CC tissues of the lung. The most common form of lung cancer is non-small CC cell lung cancer (NSCLC) that can be divided into 3 major histologic CC subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung CC cancer. NSCLC is often diagnosed at an advanced stage and has a poor CC prognosis. Note=The gene represented in this entry may be involved in CC disease pathogenesis. DLEC1 silencing due to promoter methylation and CC aberrant transcription are implicated in the development of lung CC cancer. CC -!- DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the CC esophagus. The most common types are esophageal squamous cell carcinoma CC and adenocarcinoma. Cancer of the esophagus remains a devastating CC disease because it is usually not detected until it has progressed to CC an advanced incurable stage. {ECO:0000269|PubMed:10213508}. Note=The CC gene represented in this entry may be involved in disease pathogenesis. CC DLEC1 silencing due to promoter methylation and aberrant transcription CC may be implicated in the development of esophageal cancer. CC -!- MISCELLANEOUS: [Isoform 2]: Levels of this splice isoform may be CC increased in cancer cell lines and primary cancers. CC {ECO:0000303|PubMed:10213508, ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Levels of this splice isoform are increased CC in cancer cell lines and primary cancers. CC {ECO:0000269|PubMed:10213508}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB70676.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=CAB70884.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB026898; BAA77624.1; -; Genomic_DNA. DR EMBL; AB020522; BAA77247.1; -; mRNA. DR EMBL; AC144536; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP006309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137706; CAB70884.2; ALT_INIT; Transcribed_RNA. DR EMBL; AL137282; CAB70676.1; ALT_SEQ; mRNA. DR CCDS; CCDS2672.2; -. [Q9Y238-1] DR PIR; T46351; T46351. DR PIR; T46406; T46406. DR RefSeq; NP_001308082.1; NM_001321153.1. DR RefSeq; NP_031361.2; NM_007335.3. [Q9Y238-1] DR RefSeq; NP_031363.2; NM_007337.3. [Q9Y238-3] DR AlphaFoldDB; Q9Y238; -. DR SMR; Q9Y238; -. DR BioGRID; 115266; 12. DR IntAct; Q9Y238; 2. DR STRING; 9606.ENSP00000308597; -. DR iPTMnet; Q9Y238; -. DR PhosphoSitePlus; Q9Y238; -. DR BioMuta; DLEC1; -. DR DMDM; 296434480; -. DR EPD; Q9Y238; -. DR MassIVE; Q9Y238; -. DR PaxDb; Q9Y238; -. DR PeptideAtlas; Q9Y238; -. DR ProteomicsDB; 85633; -. [Q9Y238-1] DR ProteomicsDB; 85634; -. [Q9Y238-2] DR ProteomicsDB; 85635; -. [Q9Y238-3] DR Antibodypedia; 6364; 179 antibodies from 23 providers. DR DNASU; 9940; -. DR Ensembl; ENST00000308059.11; ENSP00000308597.6; ENSG00000008226.20. [Q9Y238-1] DR Ensembl; ENST00000346219.7; ENSP00000315914.5; ENSG00000008226.20. [Q9Y238-3] DR GeneID; 9940; -. DR KEGG; hsa:9940; -. DR MANE-Select; ENST00000308059.11; ENSP00000308597.6; NM_007335.4; NP_031361.2. DR UCSC; uc003cho.2; human. [Q9Y238-1] DR CTD; 9940; -. DR DisGeNET; 9940; -. DR GeneCards; DLEC1; -. DR HGNC; HGNC:2899; DLEC1. DR HPA; ENSG00000008226; Tissue enhanced (choroid plexus, fallopian tube, testis). DR MalaCards; DLEC1; -. DR MIM; 133239; phenotype. DR MIM; 211980; phenotype. DR MIM; 604050; gene. DR neXtProt; NX_Q9Y238; -. DR OpenTargets; ENSG00000008226; -. DR Orphanet; 99977; Squamous cell carcinoma of the esophagus. DR PharmGKB; PA27353; -. DR VEuPathDB; HostDB:ENSG00000008226; -. DR eggNOG; ENOG502QQQ5; Eukaryota. DR GeneTree; ENSGT00390000006098; -. DR HOGENOM; CLU_003422_0_0_1; -. DR InParanoid; Q9Y238; -. DR OMA; YWDSLIC; -. DR OrthoDB; 373519at2759; -. DR PhylomeDB; Q9Y238; -. DR TreeFam; TF340616; -. DR PathwayCommons; Q9Y238; -. DR SignaLink; Q9Y238; -. DR BioGRID-ORCS; 9940; 9 hits in 1062 CRISPR screens. DR ChiTaRS; DLEC1; human. DR GenomeRNAi; 9940; -. DR Pharos; Q9Y238; Tbio. DR PRO; PR:Q9Y238; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9Y238; protein. DR Bgee; ENSG00000008226; Expressed in right uterine tube and 142 other tissues. DR ExpressionAtlas; Q9Y238; baseline and differential. DR Genevisible; Q9Y238; HS. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB. DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB. DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0002357; P:defense response to tumor cell; IMP:ARUK-UCL. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 7. DR InterPro; IPR033304; DLEC1. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR46348; DELETED IN LUNG AND ESOPHAGEAL CANCER PROTEIN 1; 1. DR AGR; HGNC:2899; -. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Differentiation; Reference proteome; KW Spermatogenesis; Tumor suppressor. FT CHAIN 1..1755 FT /note="Deleted in lung and esophageal cancer protein 1" FT /id="PRO_0000079929" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1339..1360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1529..1553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 704 FT /note="E -> MARLRGGRIPAMPQPSPGQPAGTQWCFQGTVFALQ (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_051847" FT VAR_SEQ 856..885 FT /note="GPALIINVSALQFGLLRLGQKATNSIQIRN -> PFSLVCSAWGRKPQTPSR FT SGTSASSQPHGA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_051848" FT VAR_SEQ 886..1755 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_051849" FT VAR_SEQ 1675..1755 FT /note="QQEPAKAAVAFRVSPNSGLLEARSANAPPTSIALQVFFTARSSELYESTMVV FT EGVLGEKSCTLRLRGQGSYDERYMLPHQP -> VVSCTSPRWWWKVCSVRSPAPCGSGA FT KAPMMRDTCCLTSPEAPPQPSAPGPSWRKNIAQGLGAALQHKDTDLGTWGPLGSSWNGR FT TPFHNGLSLGPHDMSSELT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_051850" FT VARIANT 79 FT /note="L -> R (in dbSNP:rs7625806)" FT /id="VAR_056860" FT VARIANT 192 FT /note="S -> F (in dbSNP:rs34012183)" FT /id="VAR_056861" FT VARIANT 351 FT /note="P -> R (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035908" FT VARIANT 1022 FT /note="K -> N (in dbSNP:rs36012922)" FT /id="VAR_056862" FT VARIANT 1150 FT /note="N -> D (in dbSNP:rs9840172)" FT /id="VAR_056863" FT VARIANT 1227 FT /note="L -> P (in dbSNP:rs9810085)" FT /id="VAR_056864" FT CONFLICT 704 FT /note="E -> M (in Ref. 2; CAB70884)" FT /evidence="ECO:0000305" FT CONFLICT 1442 FT /note="G -> R (in Ref. 1; BAA77624/BAA77247)" FT /evidence="ECO:0000305" SQ SEQUENCE 1755 AA; 195684 MW; CD4BDB5EEF24DF98 CRC64; METRSSKTRR SLASRTNECQ GTMWAPTSPP AGSSSPSQPT WKSSLYSSLA YSEAFHYSFA ARPRRLTQLA LAQRPEPQLL RLRPSSLRTQ DISHLLTGVF RNLYSAEVIG DEVSASLIKA RGSENERHEE FVDQLQQIRE LYKQRLDEFE MLERHITQAQ ARAIAENERV MSQAGVQDLE SLVRLPPVKS VSRWCIDSEL LRKHHLISPE DYYTDTVPFH SAPKGISLPG CSKLTFSCEK RSVQKKELNK KLEDSCRKKL AEFEDELDHT VDSLTWNLTP KAKERTREPL KKASQPRNKN WMNHLRVPQR ELDRLLLARM ESRNHFLKNP RFFPPNTRYG GKSLVFPPKK PAPIGEFQST EPEQSCADTP VFLAKPPIGF FTDYEIGPVY EMVIALQNTT TTSRYLRVLP PSTPYFALGL GMFPGKGGMV APGMTCQYIV QFFPDCLGDF DDFILVETQS AHTLLIPLQA RRPPPVLTLS PVLDCGYCLI GGVKMTRFIC KNVGFSVGRF CIMPKTSWPP LSFKAIATVG FVEQPPFGIL PSVFELAPGH AILVEVLFSP KSLGKAEQTF IIMCDNCQIK ELVTIGIGQL IALDLIYISG EKSQPDPGEL TDLTAQHFIR FEPENLRSTA RKQLIIRNAT HVELAFYWQI MKPNLQPLMP GETFSMDSIK CYPDKETAFS IMPRKGVLSP HTDHEFILSF SPHELRDFHS VLQMVLEEVP EPVSSEAESL GHSSYSVDDV IVLEIEVKGS VEPFQVLLEP YALIIPGENY IGINVKKAFK MWNNSKSPIR YLWGKISDCH IIEVEPGTGV IEPSEVGDFE LNFTGGVPGP TSQDLLCEIE DSPSPVVLHI EAVFKGPALI INVSALQFGL LRLGQKATNS IQIRNVSQLP ATWRMKESPV SLQERPEDVS PFDIEPSSGQ LHSLGECRVD ITLEALHCQH LETVLELEVE NGAWSYLPVY AEVQKPHVYL QSSQVEVRNL YLGVPTKTTI TLINGTLLPT QFHWGKLLGH QAEFCMVTVS PKHGLLGPSE ECQLKLELTA HTQEELTHLA LPCHVSGMKK PLVLGISGKP QGLQVAITIS KESSDCSTEQ WPGHPKELRL DFGSAVPLRT RVTRQLILTN RSPIRTRFSL KFEYFGSPQN SLSKKTSLPN MPPALLKTVR MQEHLAKREQ LDFMESMLSH GKGAAFFPHF SQGMLGPYQQ LCIDITGCAN MWGEYWDNLI CTVGDLLPEV IPVHMAAVGC PISSLRTTSY TIDQAQKEPA MRFGTQVSGG DTVTRTLRLN NSSPCDIRLD WETYVPEDKE DRLVELLVFY GPPFPLRDQA GNELVCPDTP EGGCLLWSPG PSSSSEFSHE TDSSVEGSSS ASNRVAQKLI SVILQAHEGV PSGHLYCISP KQVVVPAGGS STIYISFTPM VLSPEILHKV ECTGYALGFM SLDSKVEREI PGKRHRLQDF AVGPLKLDLH SYVRPAQLSV ELDYGGSMEF QCQASDLIPE QPCSGVLSEL VTTHHLKLTN TTEIPHYFRL MVSRPFSVSQ DGASQDHRAP GPGQKQECEE ETASADKQLV LQAQENMLVN VSFSLSLELL SYQKLPADQT LPGVDIQQSA SGEREMVFTQ NLLLEYTNQT TQVVPLRAVV AVPELQLSTS WVDFGTCFVS QQRVREVYLM NLSGCRSYWT MLMGQQEPAK AAVAFRVSPN SGLLEARSAN APPTSIALQV FFTARSSELY ESTMVVEGVL GEKSCTLRLR GQGSYDERYM LPHQP // ID TCPG_HUMAN Reviewed; 545 AA. AC P49368; A6NE14; Q5SZY1; Q9BR64; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 4. DT 14-DEC-2022, entry version 220. DE RecName: Full=T-complex protein 1 subunit gamma; DE Short=TCP-1-gamma; DE AltName: Full=CCT-gamma; DE AltName: Full=hTRiC5; GN Name=CCT3; Synonyms=CCTG, TRIC5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph node; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 1-15; 32-38; 49-85; 129-138; 182-191; 238-248; 295-306; RP 382-389; 428-449 AND 508-528, ACETYLATION AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Hepatoma; RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.; RL Submitted (JUL-2007) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-545. RC TISSUE=Kidney; RX PubMed=8573069; DOI=10.1042/bj3130381; RA Walkley N.A., Demaine A.G., Malik A.N.; RT "Cloning, structure and mRNA expression of human Cctg, which encodes the RT chaperonin subunit CCT gamma."; RL Biochem. J. 313:381-389(1996). RN [7] RP PROTEIN SEQUENCE OF 204-216; 331-353 AND 508-518, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 345-544. RX PubMed=8001976; DOI=10.1006/geno.1994.1438; RA Sevigny G., Joly E., Bibor-Hardy V., Lemieux N.; RT "Assignment of the human homologue of the mTRiC-P5 gene (TRIC5) to band RT 1q23 by fluorescence in situ hybridization."; RL Genomics 22:634-636(1994). RN [9] RP INTERACTION WITH PACRG. RX PubMed=14532270; DOI=10.1074/jbc.m309655200; RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; RT "A product of the human gene adjacent to parkin is a component of Lewy RT bodies and suppresses Pael receptor-induced cell death."; RL J. Biol. Chem. 278:51901-51910(2003). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059; RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J., RA Artandi S.E.; RT "Proteostatic control of telomerase function through TRiC-mediated folding RT of TCAB1."; RL Cell 159:1389-1403(2014). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-243; TYR-247; RP SER-252; THR-430 AND THR-459, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-381, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-248 AND LYS-249, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [23] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a CC molecular chaperone complex that assists the folding of proteins upon CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding CC of WRAP53/TCAB1, thereby regulating telomere maintenance CC (PubMed:25467444). As part of the TRiC complex may play a role in the CC assembly of BBSome, a complex involved in ciliogenesis regulating CC transports vesicles to the cilia (PubMed:20080638). The TRiC complex CC plays a role in the folding of actin and tubulin (Probable). CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000305}. CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked CC rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444). CC Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By CC similarity). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000250|UniProtKB:P80318, ECO:0000269|PubMed:14532270, CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC P49368; O75140-2: DEPDC5; NbExp=3; IntAct=EBI-356673, EBI-12366971; CC P49368; O75530: EED; NbExp=2; IntAct=EBI-356673, EBI-923794; CC P49368; P57678: GEMIN4; NbExp=3; IntAct=EBI-356673, EBI-356700; CC P49368; Q8TD10: MIPOL1; NbExp=6; IntAct=EBI-356673, EBI-2548751; CC P49368; Q13371: PDCL; NbExp=6; IntAct=EBI-356673, EBI-5772890; CC P49368; O15160: POLR1C; NbExp=3; IntAct=EBI-356673, EBI-1055079; CC P49368; P04049: RAF1; NbExp=5; IntAct=EBI-356673, EBI-365996; CC P49368; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-356673, EBI-720977; CC P49368; O60232: ZNRD2; NbExp=6; IntAct=EBI-356673, EBI-741415; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P49368-1; Sequence=Displayed; CC Name=2; CC IsoId=P49368-2; Sequence=VSP_042026; CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH08019.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK293477; BAG56968.1; -; mRNA. DR EMBL; AL833197; CAI46192.1; -; mRNA. DR EMBL; AL589685; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006501; AAH06501.3; -; mRNA. DR EMBL; BC008019; AAH08019.1; ALT_INIT; mRNA. DR EMBL; X74801; CAA52808.1; -; mRNA. DR EMBL; U17104; AAC50068.1; -; mRNA. DR CCDS; CCDS1140.2; -. [P49368-1] DR CCDS; CCDS30888.1; -. [P49368-2] DR PIR; S61529; A38983. DR RefSeq; NP_001008800.1; NM_001008800.2. [P49368-2] DR RefSeq; NP_005989.3; NM_005998.4. [P49368-1] DR PDB; 6NR8; EM; 7.80 A; C/K=13-525. DR PDB; 6NR9; EM; 8.50 A; C/K=13-525. DR PDB; 6NRA; EM; 7.70 A; C/K=13-525. DR PDB; 6NRB; EM; 8.70 A; C/K=13-525. DR PDB; 6NRC; EM; 8.30 A; C/K=13-525. DR PDB; 6NRD; EM; 8.20 A; C/K=13-525. DR PDB; 6QB8; EM; 3.97 A; G/g=2-545. DR PDB; 7LUM; EM; 4.50 A; H/P=1-545. DR PDB; 7LUP; EM; 6.20 A; H/P=1-545. DR PDB; 7NVL; EM; 2.50 A; G/g=1-545. DR PDB; 7NVM; EM; 3.10 A; G/g=1-545. DR PDB; 7NVN; EM; 3.00 A; G/g=1-545. DR PDB; 7NVO; EM; 3.50 A; G/g=1-545. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR PDBsum; 7LUM; -. DR PDBsum; 7LUP; -. DR PDBsum; 7NVL; -. DR PDBsum; 7NVM; -. DR PDBsum; 7NVN; -. DR PDBsum; 7NVO; -. DR AlphaFoldDB; P49368; -. DR SMR; P49368; -. DR BioGRID; 113054; 561. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P49368; -. DR DIP; DIP-32970N; -. DR IntAct; P49368; 307. DR MINT; P49368; -. DR STRING; 9606.ENSP00000295688; -. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR GlyGen; P49368; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P49368; -. DR MetOSite; P49368; -. DR PhosphoSitePlus; P49368; -. DR SwissPalm; P49368; -. DR BioMuta; CCT3; -. DR DMDM; 66774185; -. DR DOSAC-COBS-2DPAGE; P49368; -. DR OGP; P49368; -. DR SWISS-2DPAGE; P49368; -. DR CPTAC; CPTAC-474; -. DR CPTAC; CPTAC-475; -. DR EPD; P49368; -. DR jPOST; P49368; -. DR MassIVE; P49368; -. DR MaxQB; P49368; -. DR PaxDb; P49368; -. DR PeptideAtlas; P49368; -. DR PRIDE; P49368; -. DR ProteomicsDB; 55998; -. [P49368-1] DR ProteomicsDB; 55999; -. [P49368-2] DR TopDownProteomics; P49368-1; -. [P49368-1] DR Antibodypedia; 1677; 248 antibodies from 33 providers. DR DNASU; 7203; -. DR Ensembl; ENST00000295688.8; ENSP00000295688.3; ENSG00000163468.15. [P49368-1] DR Ensembl; ENST00000368259.6; ENSP00000357242.2; ENSG00000163468.15. [P49368-2] DR GeneID; 7203; -. DR KEGG; hsa:7203; -. DR MANE-Select; ENST00000295688.8; ENSP00000295688.3; NM_005998.5; NP_005989.3. DR UCSC; uc001fol.3; human. [P49368-1] DR CTD; 7203; -. DR DisGeNET; 7203; -. DR GeneCards; CCT3; -. DR HGNC; HGNC:1616; CCT3. DR HPA; ENSG00000163468; Low tissue specificity. DR MIM; 600114; gene. DR neXtProt; NX_P49368; -. DR OpenTargets; ENSG00000163468; -. DR PharmGKB; PA26180; -. DR VEuPathDB; HostDB:ENSG00000163468; -. DR eggNOG; KOG0364; Eukaryota. DR GeneTree; ENSGT00570000079224; -. DR HOGENOM; CLU_008891_7_3_1; -. DR InParanoid; P49368; -. DR OMA; RYCRIEK; -. DR PhylomeDB; P49368; -. DR TreeFam; TF105649; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P49368; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR SignaLink; P49368; -. DR BioGRID-ORCS; 7203; 794 hits in 1042 CRISPR screens. DR ChiTaRS; CCT3; human. DR GeneWiki; CCT3; -. DR GenomeRNAi; 7203; -. DR Pharos; P49368; Tbio. DR PRO; PR:P49368; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P49368; protein. DR Bgee; ENSG00000163468; Expressed in embryo and 217 other tissues. DR ExpressionAtlas; P49368; baseline and differential. DR Genevisible; P49368; HS. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal. DR GO; GO:0046931; P:pore complex assembly; IEA:Ensembl. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:1901998; P:toxin transport; IEA:Ensembl. DR CDD; cd03337; TCP1_gamma; 1. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR012719; Chap_CCT_gamma. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR TIGRFAMs; TIGR02344; chap_CCT_gamma; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. DR AGR; HGNC:1616; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; KW Cytoplasm; Direct protein sequencing; Disulfide bond; Isopeptide bond; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..545 FT /note="T-complex protein 1 subunit gamma" FT /id="PRO_0000128321" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 526..545 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P80318" FT MOD_RES 222 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 243 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 247 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 430 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 459 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT DISULFID 366..372 FT /evidence="ECO:0000250" FT CROSSLNK 15 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 248 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 249 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 381 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25114211" FT VAR_SEQ 32..69 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042026" FT VARIANT 391 FT /note="L -> F (in dbSNP:rs2230194)" FT /id="VAR_052265" FT CONFLICT 251 FT /note="E -> G (in Ref. 6; CAA52808)" FT /evidence="ECO:0000305" FT CONFLICT 345 FT /note="T -> A (in Ref. 8; AAC50068)" FT /evidence="ECO:0000305" FT HELIX 20..37 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 47..51 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 63..69 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 75..90 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:7NVO" FT HELIX 97..114 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 119..140 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 149..160 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 164..168 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 169..183 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 195..197 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 198..207 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 263..283 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 298..306 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 340..342 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 350..355 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 372..379 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 381..403 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 407..409 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 413..426 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 434..443 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 446..455 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 459..469 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 482..484 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 490..493 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 496..498 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 499..518 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 519..524 FT /evidence="ECO:0007829|PDB:7NVL" SQ SEQUENCE 545 AA; 60534 MW; 0A528762EF24F36B CRC64; MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT VVISAYRKAL DDMISTLKKI SIPVDISDSD MMLNIINSSI TTKAISRWSS LACNIALDAV KMVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIQQLCE DIIQLKPDVV ITEKGISDLA QHYLMRANIT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQENCETWGV NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQSRQGGAP DAGQE // ID TCPH_HUMAN Reviewed; 543 AA. AC Q99832; A8K7E6; A8MWI8; B7WNW9; B7Z4T9; B7Z4Z7; O14871; Q6FI26; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 14-DEC-2022, entry version 211. DE RecName: Full=T-complex protein 1 subunit eta; DE Short=TCP-1-eta; DE AltName: Full=CCT-eta; DE AltName: Full=HIV-1 Nef-interacting protein; DE Contains: DE RecName: Full=T-complex protein 1 subunit eta, N-terminally processed; GN Name=CCT7; Synonyms=CCTH, NIP7-1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9819444; DOI=10.1128/mcb.18.12.7584; RA Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.; RT "Maturation of human cyclin E requires the function of eukaryotic RT chaperonin CCT."; RL Mol. Cell. Biol. 18:7584-7589(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4). RC TISSUE=Cerebellum, and Heart; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=PNS, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 1-10; 56-67; 85-123; 127-144; 178-193; 200-217; RP 219-230; 237-247; 293-306; 314-320; 376-397; 402-418; 431-447 AND 500-535, RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma, Hepatoma, and Osteosarcoma; RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C., Boldt K., RA von Kriegsheim A.F., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-424 (ISOFORM 1). RA Fukushi M., Kimura T., Yamamoto N.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 107-123, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [10] RP INTERACTION WITH PACRG. RX PubMed=14532270; DOI=10.1074/jbc.m309655200; RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; RT "A product of the human gene adjacent to parkin is a component of Lewy RT bodies and suppresses Pael receptor-induced cell death."; RL J. Biol. Chem. 278:51901-51910(2003). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-320, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 3), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059; RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J., RA Artandi S.E.; RT "Proteostatic control of telomerase function through TRiC-mediated folding RT of TCAB1."; RL Cell 159:1389-1403(2014). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-535, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-430, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [22] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a CC molecular chaperone complex that assists the folding of proteins upon CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding CC of WRAP53/TCAB1, thereby regulating telomere maintenance CC (PubMed:25467444). The TRiC complex plays a role in the folding of CC actin and tubulin (Probable). {ECO:0000269|PubMed:25467444, CC ECO:0000305}. CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked CC rings, 12 to 16 nm in diameter (PubMed:25467444). Interacts with PACRG CC (PubMed:14532270). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:25467444, CC ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC Q99832; P78371: CCT2; NbExp=2; IntAct=EBI-357046, EBI-357407; CC Q99832; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-357046, EBI-25847826; CC Q99832; Q02575: NHLH1; NbExp=3; IntAct=EBI-357046, EBI-3930567; CC Q99832; Q6PHZ7: NR2C2; NbExp=3; IntAct=EBI-357046, EBI-2802743; CC Q99832; O15534: PER1; NbExp=3; IntAct=EBI-357046, EBI-2557276; CC Q99832; Q969T9: WBP2; NbExp=3; IntAct=EBI-357046, EBI-727055; CC Q99832; Q9BYN7-2: ZNF341; NbExp=3; IntAct=EBI-357046, EBI-16435478; CC Q99832; O60232: ZNRD2; NbExp=7; IntAct=EBI-357046, EBI-741415; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P80313}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q99832-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99832-2; Sequence=VSP_043573, VSP_043574; CC Name=3; CC IsoId=Q99832-3; Sequence=VSP_043572; CC Name=4; CC IsoId=Q99832-4; Sequence=VSP_043573; CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF026292; AAC96011.1; -; mRNA. DR EMBL; CR536511; CAG38749.1; -; mRNA. DR EMBL; AK291961; BAF84650.1; -; mRNA. DR EMBL; AK293597; BAH11543.1; -; mRNA. DR EMBL; AK297846; BAH12675.1; -; mRNA. DR EMBL; AK298153; BAH12733.1; -; mRNA. DR EMBL; AC010913; AAX88902.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99739.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99740.1; -; Genomic_DNA. DR EMBL; BC019296; AAH19296.1; -; mRNA. DR EMBL; BC088351; AAH88351.1; -; mRNA. DR EMBL; U83843; AAB41437.1; -; mRNA. DR CCDS; CCDS42696.1; -. [Q99832-2] DR CCDS; CCDS46336.1; -. [Q99832-1] DR CCDS; CCDS54366.1; -. [Q99832-4] DR CCDS; CCDS54367.1; -. [Q99832-3] DR RefSeq; NP_001009570.1; NM_001009570.2. [Q99832-2] DR RefSeq; NP_001159756.1; NM_001166284.1. [Q99832-4] DR RefSeq; NP_001159757.1; NM_001166285.1. [Q99832-3] DR RefSeq; NP_006420.1; NM_006429.3. [Q99832-1] DR RefSeq; XP_011530780.1; XM_011532478.2. [Q99832-3] DR RefSeq; XP_011530781.1; XM_011532479.1. [Q99832-3] DR PDB; 6NR8; EM; 7.80 A; G/O=12-525. DR PDB; 6NR9; EM; 8.50 A; G/O=12-525. DR PDB; 6NRA; EM; 7.70 A; G/O=12-525. DR PDB; 6NRB; EM; 8.70 A; G/O=12-525. DR PDB; 6NRC; EM; 8.30 A; G/O=12-525. DR PDB; 6NRD; EM; 8.20 A; G/O=12-525. DR PDB; 6QB8; EM; 3.97 A; H/h=1-543. DR PDB; 7LUM; EM; 4.50 A; C/K=1-543. DR PDB; 7LUP; EM; 6.20 A; C/K=1-543. DR PDB; 7NVL; EM; 2.50 A; H/h=1-543. DR PDB; 7NVM; EM; 3.10 A; H/h=1-543. DR PDB; 7NVN; EM; 3.00 A; H/h=1-543. DR PDB; 7NVO; EM; 3.50 A; H/h=1-543. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR PDBsum; 7LUM; -. DR PDBsum; 7LUP; -. DR PDBsum; 7NVL; -. DR PDBsum; 7NVM; -. DR PDBsum; 7NVN; -. DR PDBsum; 7NVO; -. DR AlphaFoldDB; Q99832; -. DR SMR; Q99832; -. DR BioGRID; 115825; 534. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; Q99832; -. DR DIP; DIP-51608N; -. DR IntAct; Q99832; 272. DR MINT; Q99832; -. DR STRING; 9606.ENSP00000258091; -. DR GlyGen; Q99832; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99832; -. DR MetOSite; Q99832; -. DR PhosphoSitePlus; Q99832; -. DR SwissPalm; Q99832; -. DR BioMuta; CCT7; -. DR DMDM; 3041738; -. DR REPRODUCTION-2DPAGE; IPI00018465; -. DR CPTAC; CPTAC-181; -. DR EPD; Q99832; -. DR jPOST; Q99832; -. DR MassIVE; Q99832; -. DR MaxQB; Q99832; -. DR PaxDb; Q99832; -. DR PeptideAtlas; Q99832; -. DR PRIDE; Q99832; -. DR ProteomicsDB; 78495; -. [Q99832-1] DR ProteomicsDB; 78496; -. [Q99832-2] DR ProteomicsDB; 78497; -. [Q99832-3] DR ProteomicsDB; 78498; -. [Q99832-4] DR Antibodypedia; 1382; 283 antibodies from 30 providers. DR DNASU; 10574; -. DR Ensembl; ENST00000258091.10; ENSP00000258091.5; ENSG00000135624.17. [Q99832-1] DR Ensembl; ENST00000398422.2; ENSP00000381456.2; ENSG00000135624.17. [Q99832-2] DR Ensembl; ENST00000539919.5; ENSP00000437824.1; ENSG00000135624.17. [Q99832-3] DR Ensembl; ENST00000540468.5; ENSP00000442058.1; ENSG00000135624.17. [Q99832-4] DR GeneID; 10574; -. DR KEGG; hsa:10574; -. DR MANE-Select; ENST00000258091.10; ENSP00000258091.5; NM_006429.4; NP_006420.1. DR UCSC; uc002siz.4; human. [Q99832-1] DR CTD; 10574; -. DR DisGeNET; 10574; -. DR GeneCards; CCT7; -. DR HGNC; HGNC:1622; CCT7. DR HPA; ENSG00000135624; Low tissue specificity. DR MalaCards; CCT7; -. DR MIM; 605140; gene. DR neXtProt; NX_Q99832; -. DR OpenTargets; ENSG00000135624; -. DR PharmGKB; PA26185; -. DR VEuPathDB; HostDB:ENSG00000135624; -. DR eggNOG; KOG0361; Eukaryota. DR GeneTree; ENSGT00550000074832; -. DR HOGENOM; CLU_008891_7_1_1; -. DR InParanoid; Q99832; -. DR OMA; HRKGNTW; -. DR OrthoDB; 335406at2759; -. DR PhylomeDB; Q99832; -. DR TreeFam; TF105641; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; Q99832; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle. DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle. DR SignaLink; Q99832; -. DR BioGRID-ORCS; 10574; 614 hits in 1074 CRISPR screens. DR ChiTaRS; CCT7; human. DR GeneWiki; CCT7; -. DR GenomeRNAi; 10574; -. DR Pharos; Q99832; Tbio. DR PRO; PR:Q99832; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q99832; protein. DR Bgee; ENSG00000135624; Expressed in ganglionic eminence and 208 other tissues. DR ExpressionAtlas; Q99832; baseline and differential. DR Genevisible; Q99832; HS. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:1901998; P:toxin transport; IEA:Ensembl. DR CDD; cd03340; TCP1_eta; 1. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR012720; Chap_CCT_eta. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF22; T-COMPLEX PROTEIN 1 SUBUNIT ETA; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR TIGRFAMs; TIGR02345; chap_CCT_eta; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. DR AGR; HGNC:1622; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Methylation; KW Nucleotide-binding; Reference proteome; Ubl conjugation. FT CHAIN 1..543 FT /note="T-complex protein 1 subunit eta" FT /id="PRO_0000128365" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..543 FT /note="T-complex protein 1 subunit eta, N-terminally FT processed" FT /id="PRO_0000434391" FT REGION 524..543 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330" FT MOD_RES 67 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 250 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P80313" FT MOD_RES 320 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 535 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 430 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..44 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043572" FT VAR_SEQ 3..89 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043573" FT VAR_SEQ 90..206 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043574" FT VARIANT 259 FT /note="T -> A (in dbSNP:rs2231427)" FT /id="VAR_052269" FT CONFLICT 282..283 FT /note="HH -> RQ (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="L -> P (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 336 FT /note="A -> P (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 364 FT /note="C -> L (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 374..376 FT /note="LRG -> SPC (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 407 FT /note="A -> P (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT CONFLICT 411 FT /note="A -> P (in Ref. 8; AAB41437)" FT /evidence="ECO:0000305" FT STRAND 14..18 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 19..37 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 62..68 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 77..89 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 94..113 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 118..139 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 148..163 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 172..184 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 195..203 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 223..227 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 236..240 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 260..283 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 287..293 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 297..305 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 316..326 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 339..341 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 346..353 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 356..362 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 370..378 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 379..401 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 411..424 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 430..442 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 444..453 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 457..469 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 473..478 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 479..482 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 483..486 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 487..491 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 493..495 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 496..515 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 516..521 FT /evidence="ECO:0007829|PDB:7NVL" FT MOD_RES Q99832-3:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 543 AA; 59367 MW; 9F1E33FA80E6238E CRC64; MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAEV GDGTTSVTLL AAEFLKQVKP YVEEGLHPQI IIRAFRTATQ LAVNKIKEIA VTVKKADKVE QRKLLEKCAM TALSSKLISQ QKAFFAKMVV DAVMMLDDLL QLKMIGIKKV QGGALEDSQL VAGVAFKKTF SYAGFEMQPK KYHNPKIALL NVELELKAEK DNAEIRVHTV EDYQAIVDAE WNILYDKLEK IHHSGAKVVL SKLPIGDVAT QYFADRDMFC AGRVPEEDLK RTMMACGGSI QTSVNALSAD VLGRCQVFEE TQIGGERYNF FTGCPKAKTC TFILRGGAEQ FMEETERSLH DAIMIVRRAI KNDSVVAGGG AIEMELSKYL RDYSRTIPGK QQLLIGAYAK ALEIIPRQLC DNAGFDATNI LNKLRARHAQ GGTWYGVDIN NEDIADNFEA FVWEPAMVRI NALTAASEAA CLIVSVDETI KNPRSTVDAP TAAGRGRGRG RPH // ID TCPD_HUMAN Reviewed; 539 AA. AC P50991; B2R6I3; B7Z8B1; F5H5W3; O14870; Q53QP9; Q96C51; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 14-DEC-2022, entry version 207. DE RecName: Full=T-complex protein 1 subunit delta; DE Short=TCP-1-delta; DE AltName: Full=CCT-delta; DE AltName: Full=Stimulator of TAR RNA-binding; GN Name=CCT4; Synonyms=CCTD, SRB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=8626763; DOI=10.1074/jbc.271.8.4201; RA Wu-Baer F., Lane W.S., Gaynor R.B.; RT "Identification of a group of cellular cofactors that stimulate the binding RT of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RT RNA."; RL J. Biol. Chem. 271:4201-4208(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9819444; DOI=10.1128/mcb.18.12.7584; RA Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.; RT "Maturation of human cyclin E requires the function of eukaryotic RT chaperonin CCT."; RL Mol. Cell. Biol. 18:7584-7589(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-8. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 420-435, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V., Barblan J., Quadroni M.; RL Submitted (MAR-2004) to UniProtKB. RN [8] RP INTERACTION WITH PACRG. RX PubMed=14532270; DOI=10.1074/jbc.m309655200; RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; RT "A product of the human gene adjacent to parkin is a component of Lewy RT bodies and suppresses Pael receptor-induced cell death."; RL J. Biol. Chem. 278:51901-51910(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-302; LYS-319 AND RP LYS-326, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE RP CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059; RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J., RA Artandi S.E.; RT "Proteostatic control of telomerase function through TRiC-mediated folding RT of TCAB1."; RL Cell 159:1389-1403(2014). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-184; SER-202 AND RP SER-444, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-19, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a CC molecular chaperone complex that assists the folding of proteins upon CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding CC of WRAP53/TCAB1, thereby regulating telomere maintenance CC (PubMed:25467444). As part of the TRiC complex may play a role in the CC assembly of BBSome, a complex involved in ciliogenesis regulating CC transports vesicles to the cilia (PubMed:20080638). The TRiC complex CC plays a role in the folding of actin and tubulin (Probable). CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000305}. CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked CC rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444). CC Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By CC similarity). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000250|UniProtKB:P80315, ECO:0000269|PubMed:14532270, CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC P50991; P51946: CCNH; NbExp=3; IntAct=EBI-356876, EBI-741406; CC P50991; P78371: CCT2; NbExp=4; IntAct=EBI-356876, EBI-357407; CC P50991; P78380: OLR1; NbExp=3; IntAct=EBI-356876, EBI-7151999; CC P50991; P17987: TCP1; NbExp=2; IntAct=EBI-356876, EBI-356553; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065, CC ECO:0000269|PubMed:20080638}. Melanosome {ECO:0000269|PubMed:17081065}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. Cytoplasm, CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P80315}. CC Note=Identified by mass spectrometry in melanosome fractions from stage CC I to stage IV. {ECO:0000269|PubMed:17081065}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P50991-1; Sequence=Displayed; CC Name=2; CC IsoId=P50991-2; Sequence=VSP_045537; CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U38846; AAC50384.1; -; mRNA. DR EMBL; AF026291; AAC96010.1; -; mRNA. DR EMBL; AK303082; BAH13897.1; -; mRNA. DR EMBL; AK312586; BAG35480.1; -; mRNA. DR EMBL; AC107081; AAY24140.1; -; Genomic_DNA. DR EMBL; BC014676; AAH14676.1; -; mRNA. DR EMBL; BC106934; AAI06935.1; -; mRNA. DR EMBL; BC106933; AAI06934.1; -; mRNA. DR CCDS; CCDS33206.1; -. [P50991-1] DR CCDS; CCDS58711.1; -. [P50991-2] DR RefSeq; NP_001243650.1; NM_001256721.1. [P50991-2] DR RefSeq; NP_006421.2; NM_006430.3. [P50991-1] DR PDB; 6NR8; EM; 7.80 A; D/L=26-539. DR PDB; 6NR9; EM; 8.50 A; D/L=26-539. DR PDB; 6NRA; EM; 7.70 A; D/L=26-539. DR PDB; 6NRB; EM; 8.70 A; D/L=26-539. DR PDB; 6NRC; EM; 8.30 A; D/L=26-539. DR PDB; 6NRD; EM; 8.20 A; D/L=26-539. DR PDB; 6QB8; EM; 3.97 A; D/d=1-539. DR PDB; 7LUM; EM; 4.50 A; F/N=1-539. DR PDB; 7LUP; EM; 6.20 A; F/N=1-539. DR PDB; 7NVL; EM; 2.50 A; D/d=1-539. DR PDB; 7NVM; EM; 3.10 A; D/d=1-539. DR PDB; 7NVN; EM; 3.00 A; D/d=1-539. DR PDB; 7NVO; EM; 3.50 A; D/d=1-539. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR PDBsum; 7LUM; -. DR PDBsum; 7LUP; -. DR PDBsum; 7NVL; -. DR PDBsum; 7NVM; -. DR PDBsum; 7NVN; -. DR PDBsum; 7NVO; -. DR AlphaFoldDB; P50991; -. DR SMR; P50991; -. DR BioGRID; 115826; 494. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P50991; -. DR DIP; DIP-32971N; -. DR IntAct; P50991; 220. DR MINT; P50991; -. DR STRING; 9606.ENSP00000377958; -. DR GlyGen; P50991; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P50991; -. DR MetOSite; P50991; -. DR PhosphoSitePlus; P50991; -. DR SwissPalm; P50991; -. DR BioMuta; CCT4; -. DR DMDM; 52001478; -. DR REPRODUCTION-2DPAGE; IPI00302927; -. DR UCD-2DPAGE; P50991; -. DR EPD; P50991; -. DR jPOST; P50991; -. DR MassIVE; P50991; -. DR MaxQB; P50991; -. DR PaxDb; P50991; -. DR PeptideAtlas; P50991; -. DR ProteomicsDB; 27004; -. DR ProteomicsDB; 56273; -. [P50991-1] DR TopDownProteomics; P50991-1; -. [P50991-1] DR Antibodypedia; 15920; 262 antibodies from 31 providers. DR DNASU; 10575; -. DR Ensembl; ENST00000394440.8; ENSP00000377958.3; ENSG00000115484.15. [P50991-1] DR Ensembl; ENST00000544079.2; ENSP00000443061.1; ENSG00000115484.15. [P50991-2] DR GeneID; 10575; -. DR KEGG; hsa:10575; -. DR MANE-Select; ENST00000394440.8; ENSP00000377958.3; NM_006430.4; NP_006421.2. DR UCSC; uc002sbo.5; human. [P50991-1] DR CTD; 10575; -. DR DisGeNET; 10575; -. DR GeneCards; CCT4; -. DR HGNC; HGNC:1617; CCT4. DR HPA; ENSG00000115484; Low tissue specificity. DR MIM; 605142; gene. DR neXtProt; NX_P50991; -. DR OpenTargets; ENSG00000115484; -. DR PharmGKB; PA26181; -. DR VEuPathDB; HostDB:ENSG00000115484; -. DR eggNOG; KOG0358; Eukaryota. DR GeneTree; ENSGT00550000074956; -. DR HOGENOM; CLU_008891_9_1_1; -. DR InParanoid; P50991; -. DR OMA; HPAANMI; -. DR OrthoDB; 511484at2759; -. DR PhylomeDB; P50991; -. DR TreeFam; TF106332; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P50991; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR SignaLink; P50991; -. DR BioGRID-ORCS; 10575; 766 hits in 1084 CRISPR screens. DR ChiTaRS; CCT4; human. DR GeneWiki; CCT4; -. DR GenomeRNAi; 10575; -. DR Pharos; P50991; Tbio. DR PRO; PR:P50991; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P50991; protein. DR Bgee; ENSG00000115484; Expressed in ventricular zone and 211 other tissues. DR Genevisible; P50991; HS. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005813; C:centrosome; IDA:MGI. DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL. DR GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:0090666; P:scaRNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:1901998; P:toxin transport; IEA:Ensembl. DR CDD; cd03338; TCP1_delta; 1. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR012717; Chap_CCT_delta. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR TIGRFAMs; TIGR02342; chap_CCT_delta; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. DR AGR; HGNC:1617; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cell projection; Chaperone; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Methylation; Nucleotide-binding; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 2..539 FT /note="T-complex protein 1 subunit delta" FT /id="PRO_0000128332" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 19 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 21 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P80315" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 202 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 288 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 302 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 319 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 326 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 444 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 60..89 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045537" FT VARIANT 112 FT /note="I -> V (in dbSNP:rs2272428)" FT /id="VAR_052266" FT CONFLICT 435 FT /note="R -> A (in Ref. 1; AAC50384)" FT /evidence="ECO:0000305" FT CONFLICT 531 FT /note="K -> R (in Ref. 3; BAH13897)" FT /evidence="ECO:0000305" FT HELIX 29..48 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 74..80 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 86..101 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 108..126 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 130..151 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 160..171 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 176..179 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 180..193 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 197..199 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 222..229 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:7NVN" FT STRAND 240..249 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 262..266 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 269..291 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 292..294 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 311..319 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 323..328 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 333..340 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 344..347 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 348..350 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 353..355 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 357..366 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 372..377 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 386..390 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 395..417 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 420..423 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 427..442 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 444..446 FT /evidence="ECO:0007829|PDB:7NVM" FT HELIX 447..458 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 460..469 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 473..486 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 491..494 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 495..498 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 499..502 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 503..507 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 509..511 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 512..530 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 532..535 FT /evidence="ECO:0007829|PDB:7NVL" SQ SEQUENCE 539 AA; 57924 MW; 39913C0D0735180D CRC64; MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM IQDGKGDVTI TNDGATILKQ MQVLHPAARM LVELSKAQDI EAGDGTTSVV IIAGSLLDSC TKLLQKGIHP TIISESFQKA LEKGIEILTD MSRPVELSDR ETLLNSATTS LNSKVVSQYS SLLSPMSVNA VMKVIDPATA TSVDLRDIKI VKKLGGTIDD CELVEGLVLT QKVSNSGITR VEKAKIGLIQ FCLSAPKTDM DNQIVVSDYA QMDRVLREER AYILNLVKQI KKTGCNVLLI QKSILRDALS DLALHFLNKM KIMVIKDIER EDIEFICKTI GTKPVAHIDQ FTADMLGSAE LAEEVNLNGS GKLLKITGCA SPGKTVTIVV RGSNKLVIEE AERSIHDALC VIRCLVKKRA LIAGGGAPEI ELALRLTEYS RTLSGMESYC VRAFADAMEV IPSTLAENAG LNPISTVTEL RNRHAQGEKT AGINVRKGGI SNILEELVVQ PLLVSVSALT LATETVRSIL KIDDVVNTR // ID TCPA_HUMAN Reviewed; 556 AA. AC P17987; E1P5B2; Q15556; Q5TCM3; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 14-DEC-2022, entry version 223. DE RecName: Full=T-complex protein 1 subunit alpha; DE Short=TCP-1-alpha; DE AltName: Full=CCT-alpha; GN Name=TCP1; Synonyms=CCT1, CCTA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX PubMed=2377466; DOI=10.1093/nar/18.14.4247; RA Kirchhoff C., Willison K.R.; RT "Nucleotide and amino-acid sequence of human testis-derived TCP1."; RL Nucleic Acids Res. 18:4247-4247(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 1-11, AND ACETYLATION AT MET-1. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 112-122; 131-145; 248-264; 469-480 AND 516-526, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 308-365 AND 462-516. RX PubMed=3653076; DOI=10.1002/j.1460-2075.1987.tb02459.x; RA Willison K., Kelly A., Dudley K., Goodfellow P., Spurr N., Groves V., RA Gorman P., Sheer D., Trowsdale J.; RT "The human homologue of the mouse T-complex gene, TCP1, is located on RT chromosome 6 but is not near the HLA region."; RL EMBO J. 6:1967-1974(1987). RN [9] RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=1630492; DOI=10.1038/358249a0; RA Lewis V.A., Hynes G.M., Zheng D., Saibil H., Willison K.R.; RT "T-complex polypeptide-1 is a subunit of a heteromeric particle in the RT eukaryotic cytosol."; RL Nature 358:249-252(1992). RN [10] RP INTERACTION WITH PACRG. RX PubMed=14532270; DOI=10.1074/jbc.m309655200; RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; RT "A product of the human gene adjacent to parkin is a component of Lewy RT bodies and suppresses Pael receptor-induced cell death."; RL J. Biol. Chem. 278:51901-51910(2003). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-181 AND SER-544, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-400, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE RP CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [19] RP INTERACTION WITH GBA1. RX PubMed=21098288; DOI=10.1073/pnas.1014376107; RA Lu J., Chiang J., Iyer R.R., Thompson E., Kaneski C.R., Xu D.S., Yang C., RA Chen M., Hodes R.J., Lonser R.R., Brady R.O., Zhuang Z.; RT "Decreased glucocerebrosidase activity in Gaucher disease parallels RT quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl."; RL Proc. Natl. Acad. Sci. U.S.A. 107:21665-21670(2010). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [25] RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059; RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J., RA Artandi S.E.; RT "Proteostatic control of telomerase function through TRiC-mediated folding RT of TCAB1."; RL Cell 159:1389-1403(2014). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-491; SER-544 AND RP SER-551, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [29] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). RN [30] RP VARIANT [LARGE SCALE ANALYSIS] LEU-7. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a CC molecular chaperone complex that assists the folding of proteins upon CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding CC of WRAP53/TCAB1, thereby regulating telomere maintenance CC (PubMed:25467444). As part of the TRiC complex may play a role in the CC assembly of BBSome, a complex involved in ciliogenesis regulating CC transports vesicles to the cilia (PubMed:20080638). The TRiC complex CC plays a role in the folding of actin and tubulin (Probable). CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000305}. CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked CC rings, 12 to 16 nm in diameter (PubMed:1630492, PubMed:20080638, CC PubMed:25467444). Interacts with PACRG (PubMed:14532270). Interacts CC with GBA1 (PubMed:21098288). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:1630492, CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:21098288, CC ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC P17987; Q9Y2Y0: ARL2BP; NbExp=3; IntAct=EBI-356553, EBI-3449344; CC P17987; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-356553, EBI-23662416; CC P17987; O43439: CBFA2T2; NbExp=3; IntAct=EBI-356553, EBI-748628; CC P17987; P78371: CCT2; NbExp=3; IntAct=EBI-356553, EBI-357407; CC P17987; P50991: CCT4; NbExp=2; IntAct=EBI-356553, EBI-356876; CC P17987; P50990: CCT8; NbExp=2; IntAct=EBI-356553, EBI-356507; CC P17987; P04062: GBA; NbExp=2; IntAct=EBI-356553, EBI-1564609; CC P17987; P83110: HTRA3; NbExp=5; IntAct=EBI-356553, EBI-2867394; CC P17987; P83110-1: HTRA3; NbExp=6; IntAct=EBI-356553, EBI-25469082; CC P17987; P83110-2: HTRA3; NbExp=7; IntAct=EBI-356553, EBI-22017714; CC P17987; P83105: HTRA4; NbExp=7; IntAct=EBI-356553, EBI-21776319; CC P17987; P42858: HTT; NbExp=3; IntAct=EBI-356553, EBI-466029; CC P17987; P78380: OLR1; NbExp=5; IntAct=EBI-356553, EBI-7151999; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1630492}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X52882; CAA37064.1; -; mRNA. DR EMBL; BT006969; AAP35615.1; -; mRNA. DR EMBL; AL135914; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47616.1; -; Genomic_DNA. DR EMBL; CH471051; EAW47618.1; -; Genomic_DNA. DR EMBL; BC000665; AAH00665.1; -; mRNA. DR EMBL; M26885; AAA61059.1; -; Genomic_DNA. DR EMBL; M27272; AAA61060.1; -; Genomic_DNA. DR EMBL; M26889; AAA61060.1; JOINED; Genomic_DNA. DR CCDS; CCDS5269.1; -. DR PIR; S10486; S10486. DR RefSeq; NP_110379.2; NM_030752.2. DR PDB; 6NR8; EM; 7.80 A; A/I=1-534. DR PDB; 6NR9; EM; 8.50 A; A/I=1-534. DR PDB; 6NRA; EM; 7.70 A; A/I=1-534. DR PDB; 6NRB; EM; 8.70 A; A/I=1-534. DR PDB; 6NRC; EM; 8.30 A; A/I=1-534. DR PDB; 6NRD; EM; 8.20 A; A/I=1-534. DR PDB; 6QB8; EM; 3.97 A; A/a=1-556. DR PDB; 7LUM; EM; 4.50 A; G/O=1-556. DR PDB; 7LUP; EM; 6.20 A; G/O=1-556. DR PDB; 7NVL; EM; 2.50 A; A/a=1-556. DR PDB; 7NVM; EM; 3.10 A; A/a=1-556. DR PDB; 7NVN; EM; 3.00 A; A/a=1-556. DR PDB; 7NVO; EM; 3.50 A; A/a=1-556. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR PDBsum; 7LUM; -. DR PDBsum; 7LUP; -. DR PDBsum; 7NVL; -. DR PDBsum; 7NVM; -. DR PDBsum; 7NVN; -. DR PDBsum; 7NVO; -. DR AlphaFoldDB; P17987; -. DR SMR; P17987; -. DR BioGRID; 112810; 538. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P17987; -. DR DIP; DIP-33676N; -. DR IntAct; P17987; 248. DR MINT; P17987; -. DR STRING; 9606.ENSP00000317334; -. DR GlyGen; P17987; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P17987; -. DR MetOSite; P17987; -. DR PhosphoSitePlus; P17987; -. DR SwissPalm; P17987; -. DR BioMuta; TCP1; -. DR DMDM; 135538; -. DR OGP; P17987; -. DR REPRODUCTION-2DPAGE; IPI00290566; -. DR REPRODUCTION-2DPAGE; P17987; -. DR UCD-2DPAGE; P17987; -. DR EPD; P17987; -. DR jPOST; P17987; -. DR MassIVE; P17987; -. DR MaxQB; P17987; -. DR PaxDb; P17987; -. DR PeptideAtlas; P17987; -. DR PRIDE; P17987; -. DR ProteomicsDB; 53538; -. DR Antibodypedia; 20023; 698 antibodies from 38 providers. DR DNASU; 6950; -. DR Ensembl; ENST00000321394.12; ENSP00000317334.7; ENSG00000120438.12. DR GeneID; 6950; -. DR KEGG; hsa:6950; -. DR MANE-Select; ENST00000321394.12; ENSP00000317334.7; NM_030752.3; NP_110379.2. DR UCSC; uc003qsr.4; human. DR CTD; 6950; -. DR DisGeNET; 6950; -. DR GeneCards; TCP1; -. DR HGNC; HGNC:11655; TCP1. DR HPA; ENSG00000120438; Low tissue specificity. DR MIM; 186980; gene. DR neXtProt; NX_P17987; -. DR OpenTargets; ENSG00000120438; -. DR PharmGKB; PA36406; -. DR VEuPathDB; HostDB:ENSG00000120438; -. DR eggNOG; KOG0360; Eukaryota. DR GeneTree; ENSGT00550000074878; -. DR InParanoid; P17987; -. DR OMA; KNYKNYG; -. DR OrthoDB; 335406at2759; -. DR PhylomeDB; P17987; -. DR TreeFam; TF106331; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P17987; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR SignaLink; P17987; -. DR SIGNOR; P17987; -. DR BioGRID-ORCS; 6950; 784 hits in 1085 CRISPR screens. DR ChiTaRS; TCP1; human. DR GeneWiki; T-complex_1; -. DR GenomeRNAi; 6950; -. DR Pharos; P17987; Tbio. DR PRO; PR:P17987; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P17987; protein. DR Bgee; ENSG00000120438; Expressed in cortical plate and 198 other tissues. DR ExpressionAtlas; P17987; baseline and differential. DR Genevisible; P17987; HS. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:MGI. DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0000242; C:pericentriolar material; IEA:Ensembl. DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL. DR GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:2000109; P:regulation of macrophage apoptotic process; IEA:Ensembl. DR GO; GO:0090666; P:scaRNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:1901998; P:toxin transport; IEA:Ensembl. DR GO; GO:0044053; P:translocation of peptides or proteins into host cell cytoplasm; IEA:Ensembl. DR GO; GO:0007021; P:tubulin complex assembly; NAS:UniProtKB. DR CDD; cd03335; TCP1_alpha; 1. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR012715; Chap_CCT_alpha. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR TIGRFAMs; TIGR02340; chap_CCT_alpha; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. DR AGR; HGNC:11655; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein; KW Reference proteome. FT CHAIN 1..556 FT /note="T-complex protein 1 subunit alpha" FT /id="PRO_0000128302" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 181 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 199 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 400 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 491 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 494 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P11983" FT MOD_RES 544 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 551 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VARIANT 7 FT /note="V -> L (in a breast cancer sample; somatic mutation; FT dbSNP:rs537218073)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036258" FT CONFLICT 480 FT /note="R -> S (in Ref. 8; AAA61060)" FT /evidence="ECO:0000305" FT CONFLICT 537..540 FT /note="SKDD -> ILRI (in Ref. 1; CAA37064)" FT /evidence="ECO:0000305" FT STRAND 8..13 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 15..32 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 33..35 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 70..85 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:7NVO" FT HELIX 90..109 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 114..135 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 140..143 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 146..156 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 165..178 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:7NVM" FT STRAND 194..199 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 227..239 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 260..280 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 285..290 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 294..303 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 313..323 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 328..331 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 346..356 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 359..370 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 373..377 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 382..404 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 407..410 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 411..413 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 414..426 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 433..445 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 447..456 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 460..476 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 478..485 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 486..489 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 490..493 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 494..497 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 498..501 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 507..525 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 527..533 FT /evidence="ECO:0007829|PDB:7NVL" SQ SEQUENCE 556 AA; 60344 MW; 486ECA836EA258A1 CRC64; MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGSYEDAVH SGALND // ID BBS5_HUMAN Reviewed; 341 AA. AC Q8N3I7; D3DPC3; Q6PKN0; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 14-DEC-2022, entry version 167. DE RecName: Full=Bardet-Biedl syndrome 5 protein; GN Name=BBS5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INVOLVEMENT IN BBS5, AND RP VARIANTS SER-184 AND HIS-207. RX PubMed=15137946; DOI=10.1016/s0092-8674(04)00450-7; RA Li J.B., Gerdes J.M., Haycraft C.J., Fan Y., Teslovich T.M., May-Simera H., RA Li H., Blacque O.E., Li L., Leitch C.C., Lewis R.A., Green J.S., RA Parfrey P.S., Leroux M.R., Davidson W.S., Beales P.L., Guay-Woodford L.M., RA Yoder B.K., Stormo G.D., Katsanis N., Dutcher S.K.; RT "Comparative genomics identifies a flagellar and basal body proteome that RT includes the BBS5 human disease gene."; RL Cell 117:541-552(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH CCDC28B. RX PubMed=16327777; DOI=10.1038/nature04370; RA Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S., RA Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.; RT "Dissection of epistasis in oligogenic Bardet-Biedl syndrome."; RL Nature 439:326-330(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, SUBCELLULAR RP LOCATION, AND BINDING TO PHOSPHOINOSITIDES. RX PubMed=17574030; DOI=10.1016/j.cell.2007.03.053; RA Nachury M.V., Loktev A.V., Zhang Q., Westlake C.J., Peraenen J., Merdes A., RA Slusarski D.C., Scheller R.H., Bazan J.F., Sheffield V.C., Jackson P.K.; RT "A core complex of BBS proteins cooperates with the GTPase Rab8 to promote RT ciliary membrane biogenesis."; RL Cell 129:1201-1213(2007). RN [8] RP FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME RP COMPLEX, INTERACTION WITH SMO, AND SUBCELLULAR LOCATION. RX PubMed=22072986; DOI=10.1371/journal.pgen.1002358; RA Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., RA Sheffield V.C.; RT "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and RT Smoothened."; RL PLoS Genet. 7:E1002358-E1002358(2011). RN [9] RP INTERACTION WITH PKD1. RX PubMed=24939912; DOI=10.1093/hmg/ddu267; RA Su X., Driscoll K., Yao G., Raed A., Wu M., Beales P.L., Zhou J.; RT "Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of RT polycystic kidney disease 1 protein."; RL Hum. Mol. Genet. 23:5441-5451(2014). RN [10] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). RN [11] RP VARIANTS BBS5 SER-72 AND ALA-183. RX PubMed=18203199; DOI=10.1002/ajmg.a.32136; RA Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Adeyemo A., RA Rotimi C.N., Sheffield V.C., Rosenberg T., Brondum-Nielsen K.; RT "Novel mutations in BBS5 highlight the importance of this gene in non- RT Caucasian Bardet-Biedl syndrome patients."; RL Am. J. Med. Genet. A 146A:517-520(2008). RN [12] RP VARIANT BBS5 SER-72, AND VARIANTS SER-184 AND ASP-251. RX PubMed=21344540; DOI=10.1002/humu.21480; RA Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A., RA Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A., RA Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D., RA Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K., Heon E.; RT "BBS genotype-phenotype assessment of a multiethnic patient cohort calls RT for a revision of the disease definition."; RL Hum. Mutat. 32:610-619(2011). CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex CC required for sorting of specific membrane proteins to the primary CC cilia. The BBSome complex is required for ciliogenesis but is CC dispensable for centriolar satellite function. This ciliogenic function CC is mediated in part by the Rab8 GDP/GTP exchange factor, which CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters CC the primary cilium and promotes extension of the ciliary membrane. CC Firstly the BBSome associates with the ciliary membrane and binds to CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the CC Rab8-GTP localizes to the cilium and promotes docking and fusion of CC carrier vesicles to the base of the ciliary membrane. The BBSome CC complex, together with the LTZL1, controls SMO ciliary trafficking and CC contributes to the sonic hedgehog (SHH) pathway regulation. Required CC for BBSome complex ciliary localization but not for the proper complex CC assembly. {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}. CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Binds to phosphoinositides. Interacts CC with CCDC28B. Interacts with SMO; the interaction is indicative for the CC association of SMO with the BBsome complex to facilitate ciliary CC localization of SMO. Interacts with PKD1 (PubMed:24939912). Interacts CC with DLEC1 (PubMed:33144677). {ECO:0000269|PubMed:16327777, CC ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986, CC ECO:0000269|PubMed:24939912, ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC Q8N3I7; Q3SYG4: BBS9; NbExp=6; IntAct=EBI-2892592, EBI-2826852; CC Q8N3I7; P78560: CRADD; NbExp=3; IntAct=EBI-2892592, EBI-520375; CC Q8N3I7; Q15051: IQCB1; NbExp=8; IntAct=EBI-2892592, EBI-2805823; CC Q8N3I7; Q6P597: KLC3; NbExp=3; IntAct=EBI-2892592, EBI-1643885; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane. Cytoplasm. CC Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome, centriolar CC satellite. Note=Localizes to basal bodies. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N3I7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N3I7-2; Sequence=VSP_017240; CC -!- DISEASE: Bardet-Biedl syndrome 5 (BBS5) [MIM:615983]: A syndrome CC characterized by usually severe pigmentary retinopathy, early-onset CC obesity, polydactyly, hypogenitalism, renal malformation and CC intellectual disability. Secondary features include diabetes mellitus, CC hypertension and congenital heart disease. Bardet-Biedl syndrome CC inheritance is autosomal recessive, but three mutated alleles (two at CC one locus, and a third at a second locus) may be required for clinical CC manifestation of some forms of the disease. CC {ECO:0000269|PubMed:15137946, ECO:0000269|PubMed:18203199, CC ECO:0000269|PubMed:21344540}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: BBS5 may interact genetically with BBS1. CC -!- SIMILARITY: Belongs to the BBS5 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY604003; AAT08182.1; -; mRNA. DR EMBL; AY604004; AAT08183.1; -; mRNA. DR EMBL; AL834305; CAD38975.1; -; mRNA. DR EMBL; AC093899; AAY24116.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11276.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11279.1; -; Genomic_DNA. DR EMBL; BC044593; AAH44593.1; -; mRNA. DR CCDS; CCDS2233.1; -. [Q8N3I7-1] DR RefSeq; NP_689597.1; NM_152384.2. [Q8N3I7-1] DR PDB; 6XTB; EM; 4.30 A; E=1-341. DR PDBsum; 6XTB; -. DR AlphaFoldDB; Q8N3I7; -. DR SMR; Q8N3I7; -. DR BioGRID; 126215; 17. DR ComplexPortal; CPX-1908; BBSome complex. DR CORUM; Q8N3I7; -. DR DIP; DIP-60357N; -. DR IntAct; Q8N3I7; 21. DR STRING; 9606.ENSP00000295240; -. DR iPTMnet; Q8N3I7; -. DR PhosphoSitePlus; Q8N3I7; -. DR BioMuta; BBS5; -. DR DMDM; 74750959; -. DR EPD; Q8N3I7; -. DR MassIVE; Q8N3I7; -. DR MaxQB; Q8N3I7; -. DR PaxDb; Q8N3I7; -. DR PeptideAtlas; Q8N3I7; -. DR ProteomicsDB; 71805; -. [Q8N3I7-1] DR ProteomicsDB; 71806; -. [Q8N3I7-2] DR ABCD; Q8N3I7; 1 sequenced antibody. DR Antibodypedia; 35007; 139 antibodies from 26 providers. DR DNASU; 129880; -. DR Ensembl; ENST00000295240.8; ENSP00000295240.3; ENSG00000163093.12. [Q8N3I7-1] DR Ensembl; ENST00000392663.6; ENSP00000376431.2; ENSG00000163093.12. [Q8N3I7-2] DR GeneID; 129880; -. DR KEGG; hsa:129880; -. DR MANE-Select; ENST00000295240.8; ENSP00000295240.3; NM_152384.3; NP_689597.1. DR UCSC; uc002uet.4; human. [Q8N3I7-1] DR CTD; 129880; -. DR DisGeNET; 129880; -. DR GeneCards; BBS5; -. DR GeneReviews; BBS5; -. DR HGNC; HGNC:970; BBS5. DR HPA; ENSG00000163093; Low tissue specificity. DR MalaCards; BBS5; -. DR MIM; 603650; gene. DR MIM; 615983; phenotype. DR neXtProt; NX_Q8N3I7; -. DR OpenTargets; ENSG00000163093; -. DR Orphanet; 110; Bardet-Biedl syndrome. DR PharmGKB; PA25279; -. DR VEuPathDB; HostDB:ENSG00000163093; -. DR eggNOG; ENOG502QR2Z; Eukaryota. DR GeneTree; ENSGT00390000002753; -. DR HOGENOM; CLU_052113_0_0_1; -. DR InParanoid; Q8N3I7; -. DR OMA; PNFGIQY; -. DR PhylomeDB; Q8N3I7; -. DR TreeFam; TF106129; -. DR PathwayCommons; Q8N3I7; -. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR SignaLink; Q8N3I7; -. DR SIGNOR; Q8N3I7; -. DR BioGRID-ORCS; 129880; 21 hits in 1039 CRISPR screens. DR ChiTaRS; BBS5; human. DR GeneWiki; BBS5; -. DR GenomeRNAi; 129880; -. DR Pharos; Q8N3I7; Tbio. DR PRO; PR:Q8N3I7; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8N3I7; protein. DR Bgee; ENSG00000163093; Expressed in right uterine tube and 103 other tissues. DR ExpressionAtlas; Q8N3I7; baseline and differential. DR Genevisible; Q8N3I7; HS. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0034464; C:BBSome; IDA:UniProtKB. DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl. DR GO; GO:0036064; C:ciliary basal body; ISS:BHF-UCL. DR GO; GO:0060170; C:ciliary membrane; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:BHF-UCL. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0060271; P:cilium assembly; IMP:BHF-UCL. DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL. DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central. DR GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL. DR GO; GO:0044458; P:motile cilium assembly; ISS:BHF-UCL. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR006606; BBL5. DR InterPro; IPR030804; BBS5/fem-3. DR InterPro; IPR014003; DM16_repeat. DR InterPro; IPR011993; PH-like_dom_sf. DR PANTHER; PTHR21351; BARDET-BIEDL SYNDROME PROTEIN 5; 1. DR Pfam; PF07289; BBL5; 1. DR PIRSF; PIRSF010072; DUF1448; 1. DR SMART; SM00683; DM16; 2. DR AGR; HGNC:970; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Bardet-Biedl syndrome; Cell membrane; KW Cell projection; Ciliopathy; Cilium; Cilium biogenesis/degradation; KW Cytoplasm; Cytoskeleton; Disease variant; Intellectual disability; KW Membrane; Obesity; Protein transport; Reference proteome; KW Sensory transduction; Transport; Vision. FT CHAIN 1..341 FT /note="Bardet-Biedl syndrome 5 protein" FT /id="PRO_0000223254" FT VAR_SEQ 207..227 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15137946" FT /id="VSP_017240" FT VARIANT 72 FT /note="G -> S (in BBS5; dbSNP:rs121908581)" FT /evidence="ECO:0000269|PubMed:18203199, FT ECO:0000269|PubMed:21344540" FT /id="VAR_066290" FT VARIANT 183 FT /note="T -> A (in BBS5; found in patient of Sri Lankan FT origin; not detected in patients of Northern European FT origin; dbSNP:rs121908582)" FT /evidence="ECO:0000269|PubMed:18203199" FT /id="VAR_072380" FT VARIANT 184 FT /note="N -> S (found in patients with Bardet-Biedl syndrome FT carrying homozygous mutations in other BBS genes; might FT have a modifying effect on disease phenotype; FT dbSNP:rs137853921)" FT /evidence="ECO:0000269|PubMed:15137946, FT ECO:0000269|PubMed:21344540" FT /id="VAR_025316" FT VARIANT 207 FT /note="R -> H (found as heterozygous variant in patients FT with Bardet-Biedl syndrome; might have a modifying effect FT on disease phenotype; dbSNP:rs35487251)" FT /evidence="ECO:0000269|PubMed:15137946" FT /id="VAR_025317" FT VARIANT 251 FT /note="N -> D (in dbSNP:rs143113298)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066291" SQ SEQUENCE 341 AA; 38755 MW; 63D67D877FDFD25B CRC64; MSVLDALWED RDVRFDLSAQ QMKTRPGEVL IDCLDSIEDT KGNNGDRGRL LVTNLRILWH SLALSRVNVS VGYNCILNIT TRTANSKLRG QTEALYILTK CNSTRFEFIF TNLVPGSPRL FTSVMAVHRA YETSKMYRDF KLRSALIQNK QLRLLPQEHV YDKINGVWNL SSDQGNLGTF FITNVRIVWH ANMNDSFNVS IPYLQIRSIK IRDSKFGLAL VIESSQQSGG YVLGFKIDPV EKLQESVKEI NSLHKVYSAS PIFGVDYEME EKPQPLEALT VEQIQDDVEI DSDGHTDAFV AYFADGNKQQ DREPVFSEEL GLAIEKLKDG FTLQGLWEVM S // ID TCPB_HUMAN Reviewed; 535 AA. AC P78371; A8K402; B5BTY7; B7Z243; B7Z7K4; B7ZAT2; Q14D36; Q6IAT3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 14-DEC-2022, entry version 209. DE RecName: Full=T-complex protein 1 subunit beta; DE Short=TCP-1-beta; DE AltName: Full=CCT-beta; GN Name=CCT2; Synonyms=99D8.1, CCTB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9819444; DOI=10.1128/mcb.18.12.7584; RA Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.; RT "Maturation of human cyclin E requires the function of eukaryotic RT chaperonin CCT."; RL Mol. Cell. Biol. 18:7584-7589(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Xin Y., Yu L., Bi A., Fan Y., Dai F., Zhang M., Zhang Q., Zhao S.; RT "Isolation and expression of a human novel cDNA homologous to the beta RT subunit of mouse CCT (chaperonin-containing TCP-1)."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217. RA Adams M.D., Loftus B.J., Zhou L., Phillips C., Brandon R., Fuhrmann J., RA Kim U.J., Kerlavage A.R., Venter J.C.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [11] RP PROTEIN SEQUENCE OF 2-20. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [12] RP PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V., Potts A., Quadroni M.; RL Submitted (MAY-2004) to UniProtKB. RN [13] RP PROTEIN SEQUENCE OF 26-40; 58-72; 83-131; 139-154; 157-170; 182-189; RP 192-203; 205-222; 237-250; 285-342; 348-354; 359-402; 406-427; 432-441; RP 445-466; 482-500 AND 502-516, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [14] RP INTERACTION WITH PACRG. RX PubMed=14532270; DOI=10.1074/jbc.m309655200; RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; RT "A product of the human gene adjacent to parkin is a component of Lewy RT bodies and suppresses Pael receptor-induced cell death."; RL J. Biol. Chem. 278:51901-51910(2003). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-154 AND LYS-181, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE RP CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-3; SER-260 AND THR-261, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, ACETYLATION [LARGE SCALE RP ANALYSIS] AT MET-1 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [24] RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059; RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J., RA Artandi S.E.; RT "Proteostatic control of telomerase function through TRiC-mediated folding RT of TCAB1."; RL Cell 159:1389-1403(2014). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-60, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [28] RP INTERACTION WITH FLCN. RX PubMed=27353360; DOI=10.1038/ncomms12037; RA Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D., RA Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W., RA Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W., RA Bratslavsky G., Mollapour M.; RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance RT drug binding."; RL Nat. Commun. 7:12037-12037(2016). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-248, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [30] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a CC molecular chaperone complex that assists the folding of proteins upon CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding CC of WRAP53/TCAB1, thereby regulating telomere maintenance CC (PubMed:25467444). As part of the TRiC complex may play a role in the CC assembly of BBSome, a complex involved in ciliogenesis regulating CC transports vesicles to the cilia (PubMed:20080638). The TRiC complex CC plays a role in the folding of actin and tubulin (Probable). CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000305}. CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked CC rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444). CC Interacts with PACRG (PubMed:14532270). Interacts with FLCN CC (PubMed:27353360). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:20080638, CC ECO:0000269|PubMed:25467444, ECO:0000269|PubMed:27353360, CC ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC P78371; Q8IWZ6: BBS7; NbExp=3; IntAct=EBI-357407, EBI-1806001; CC P78371; Q8TAB7: CCDC26; NbExp=3; IntAct=EBI-357407, EBI-10271580; CC P78371; P50991: CCT4; NbExp=4; IntAct=EBI-357407, EBI-356876; CC P78371; Q99832: CCT7; NbExp=2; IntAct=EBI-357407, EBI-357046; CC P78371; P42858: HTT; NbExp=6; IntAct=EBI-357407, EBI-466029; CC P78371; C9J082: NPHP1; NbExp=3; IntAct=EBI-357407, EBI-25830675; CC P78371; O14744: PRMT5; NbExp=3; IntAct=EBI-357407, EBI-351098; CC P78371; Q8TAS3: PRRG2; NbExp=3; IntAct=EBI-357407, EBI-10272071; CC P78371; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-357407, EBI-1752602; CC P78371; P17987: TCP1; NbExp=3; IntAct=EBI-357407, EBI-356553; CC P78371; O43493-5: TGOLN2; NbExp=3; IntAct=EBI-357407, EBI-25830716; CC P78371; Q8N0U8: VKORC1L1; NbExp=3; IntAct=EBI-357407, EBI-11337915; CC P78371; O76024: WFS1; NbExp=3; IntAct=EBI-357407, EBI-720609; CC P78371; O60232: ZNRD2; NbExp=6; IntAct=EBI-357407, EBI-741415; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P78371-1; Sequence=Displayed; CC Name=2; CC IsoId=P78371-2; Sequence=VSP_042648; CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF026293; AAC96012.1; -; mRNA. DR EMBL; AF026166; AAC98906.1; -; mRNA. DR EMBL; BT019966; AAV38769.1; -; mRNA. DR EMBL; AK290767; BAF83456.1; -; mRNA. DR EMBL; AK294307; BAH11729.1; -; mRNA. DR EMBL; AK302157; BAH13640.1; -; mRNA. DR EMBL; AK316397; BAH14768.1; -; mRNA. DR EMBL; AK316408; BAH14779.1; -; mRNA. DR EMBL; CR457071; CAG33352.1; -; mRNA. DR EMBL; AB451223; BAG70037.1; -; mRNA. DR EMBL; AB451346; BAG70160.1; -; mRNA. DR EMBL; AC018921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW97230.1; -; Genomic_DNA. DR EMBL; BC113514; AAI13515.1; -; mRNA. DR EMBL; BC113516; AAI13517.1; -; mRNA. DR EMBL; U91327; AAB67249.1; -; Genomic_DNA. DR CCDS; CCDS55843.1; -. [P78371-2] DR CCDS; CCDS8991.1; -. [P78371-1] DR RefSeq; NP_001185771.1; NM_001198842.1. [P78371-2] DR RefSeq; NP_006422.1; NM_006431.2. [P78371-1] DR PDB; 6NR8; EM; 7.80 A; B/J=16-524. DR PDB; 6NR9; EM; 8.50 A; B/J=16-524. DR PDB; 6NRA; EM; 7.70 A; B/J=16-524. DR PDB; 6NRB; EM; 8.70 A; B/J=16-524. DR PDB; 6NRC; EM; 8.30 A; B/J=16-524. DR PDB; 6NRD; EM; 8.20 A; B/J=16-524. DR PDB; 6QB8; EM; 3.97 A; B/b=1-535. DR PDB; 7LUM; EM; 4.50 A; E/M=1-535. DR PDB; 7LUP; EM; 6.20 A; E/M=1-535. DR PDB; 7NVL; EM; 2.50 A; B/b=1-535. DR PDB; 7NVM; EM; 3.10 A; B/b=1-535. DR PDB; 7NVN; EM; 3.00 A; B/b=1-535. DR PDB; 7NVO; EM; 3.50 A; B/b=1-535. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR PDBsum; 7LUM; -. DR PDBsum; 7LUP; -. DR PDBsum; 7NVL; -. DR PDBsum; 7NVM; -. DR PDBsum; 7NVN; -. DR PDBsum; 7NVO; -. DR AlphaFoldDB; P78371; -. DR SMR; P78371; -. DR BioGRID; 115827; 656. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P78371; -. DR DIP; DIP-38123N; -. DR IntAct; P78371; 279. DR MINT; P78371; -. DR STRING; 9606.ENSP00000299300; -. DR GlyGen; P78371; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P78371; -. DR MetOSite; P78371; -. DR PhosphoSitePlus; P78371; -. DR SwissPalm; P78371; -. DR BioMuta; CCT2; -. DR DMDM; 6094436; -. DR OGP; P78371; -. DR REPRODUCTION-2DPAGE; IPI00297779; -. DR SWISS-2DPAGE; P78371; -. DR UCD-2DPAGE; P78371; -. DR CPTAC; CPTAC-39; -. DR CPTAC; CPTAC-40; -. DR EPD; P78371; -. DR jPOST; P78371; -. DR MassIVE; P78371; -. DR MaxQB; P78371; -. DR PaxDb; P78371; -. DR PeptideAtlas; P78371; -. DR ProteomicsDB; 57599; -. [P78371-1] DR ProteomicsDB; 57600; -. [P78371-2] DR TopDownProteomics; P78371-1; -. [P78371-1] DR Antibodypedia; 762; 364 antibodies from 38 providers. DR DNASU; 10576; -. DR Ensembl; ENST00000299300.11; ENSP00000299300.6; ENSG00000166226.13. [P78371-1] DR Ensembl; ENST00000543146.2; ENSP00000445471.2; ENSG00000166226.13. [P78371-2] DR GeneID; 10576; -. DR KEGG; hsa:10576; -. DR MANE-Select; ENST00000299300.11; ENSP00000299300.6; NM_006431.3; NP_006422.1. DR UCSC; uc010stl.2; human. [P78371-1] DR CTD; 10576; -. DR DisGeNET; 10576; -. DR GeneCards; CCT2; -. DR HGNC; HGNC:1615; CCT2. DR HPA; ENSG00000166226; Low tissue specificity. DR MIM; 605139; gene. DR neXtProt; NX_P78371; -. DR OpenTargets; ENSG00000166226; -. DR PharmGKB; PA26179; -. DR VEuPathDB; HostDB:ENSG00000166226; -. DR eggNOG; KOG0363; Eukaryota. DR GeneTree; ENSGT00550000074930; -. DR InParanoid; P78371; -. DR OMA; YCTGGEI; -. DR PhylomeDB; P78371; -. DR TreeFam; TF105645; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P78371; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle. DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle. DR SignaLink; P78371; -. DR SIGNOR; P78371; -. DR BioGRID-ORCS; 10576; 778 hits in 1068 CRISPR screens. DR ChiTaRS; CCT2; human. DR GeneWiki; CCT2_(gene); -. DR GenomeRNAi; 10576; -. DR Pharos; P78371; Tbio. DR PRO; PR:P78371; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P78371; protein. DR Bgee; ENSG00000166226; Expressed in sperm and 203 other tissues. DR ExpressionAtlas; P78371; baseline and differential. DR Genevisible; P78371; HS. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0044183; F:protein folding chaperone; IDA:BHF-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. DR GO; GO:0051086; P:chaperone mediated protein folding independent of cofactor; IMP:BHF-UCL. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:MGI. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL. DR GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:0090666; P:scaRNA localization to Cajal body; IMP:BHF-UCL. DR GO; GO:1901998; P:toxin transport; IEA:Ensembl. DR CDD; cd03336; TCP1_beta; 1. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR012716; Chap_CCT_beta. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR PANTHER; PTHR11353:SF23; T-COMPLEX PROTEIN 1 SUBUNIT BETA; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR TIGRFAMs; TIGR02341; chap_CCT_beta; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. DR AGR; HGNC:1615; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.12, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..535 FT /note="T-complex protein 1 subunit beta" FT /id="PRO_0000128316" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 13 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 154 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 181 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 260 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 261 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT CROSSLNK 248 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..47 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042648" FT CONFLICT 51 FT /note="I -> T (in Ref. 4; BAH11729)" FT /evidence="ECO:0000305" FT CONFLICT 126 FT /note="I -> T (in Ref. 5; CAG33352)" FT /evidence="ECO:0000305" FT CONFLICT 354 FT /note="I -> T (in Ref. 4; BAF83456)" FT /evidence="ECO:0000305" FT CONFLICT 438 FT /note="S -> P (in Ref. 4; BAH13640)" FT /evidence="ECO:0000305" FT CONFLICT 444 FT /note="R -> K (in Ref. 6; BAG70037/BAG70160)" FT /evidence="ECO:0000305" FT CONFLICT 504 FT /note="L -> P (in Ref. 5; CAG33352)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 21..39 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 67..72 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 79..94 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 99..118 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 125..144 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 152..168 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 171..175 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 176..188 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 189..192 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 198..207 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 216..220 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 232..240 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 252..259 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 261..283 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 298..307 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 344..354 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 357..366 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 370..379 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 380..402 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 405..408 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 412..427 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 431..454 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 458..471 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 476..479 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 480..483 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 488..491 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 497..515 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 517..522 FT /evidence="ECO:0007829|PDB:7NVL" FT MOD_RES P78371-2:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 535 AA; 57488 MW; 57F9E1720D84A31F CRC64; MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT KLAVEAVLRL KGSGNLEAIH IIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDSRTVYGG GCSEMLMAHA VTQLANRTPG KEAVAMESYA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM REGTIGDMAI LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC // ID TCPE_HUMAN Reviewed; 541 AA. AC P48643; A8JZY8; A8K2X8; B4DYD8; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 14-DEC-2022, entry version 213. DE RecName: Full=T-complex protein 1 subunit epsilon; DE Short=TCP-1-epsilon; DE AltName: Full=CCT-epsilon; GN Name=CCT5; Synonyms=CCTE, KIAA0098 {ECO:0000303|PubMed:7788527}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7788527; DOI=10.1093/dnares/2.1.37; RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. III. The RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:37-43(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis, and Umbilical cord blood; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-24; 28-35; 50-59; 90-96; 133-170; 184-201; 203-214; RP 248-261; 264-275; 283-293; 324-340; 345-368; 382-388; 393-399; 401-410; RP 484-496; 514-525 AND 530-541, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RA Bienvenut W.V., Vousden K.H., Lukashchuk N.; RL Submitted (MAR-2008) to UniProtKB. RN [7] RP PROTEIN SEQUENCE OF 2-20; 97-126; 133-170; 184-201; 203-214; 266-275; RP 294-340; 345-368; 382-388 AND 401-410, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 203-210; 248-261; 324-340; 353-368 AND 515-525, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP INTERACTION WITH PACRG. RX PubMed=14532270; DOI=10.1074/jbc.m309655200; RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; RT "A product of the human gene adjacent to parkin is a component of Lewy RT bodies and suppresses Pael receptor-induced cell death."; RL J. Biol. Chem. 278:51901-51910(2003). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [11] RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x; RA Leong W.F., Chow V.T.; RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal RT differential cellular gene expression in response to enterovirus 71 RT infection."; RL Cell. Microbiol. 8:565-580(2006). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN CHAPERONIN-CONTAINING RP T-COMPLEX. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346 AND SER-539, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX. RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059; RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J., RA Artandi S.E.; RT "Proteostatic control of telomerase function through TRiC-mediated folding RT of TCAB1."; RL Cell 159:1389-1403(2014). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-210; LYS-214; LYS-265; RP LYS-275; LYS-279 AND LYS-392, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [23] RP UBIQUITINATION. RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028; RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.; RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C- RT terminal degrons."; RL Cell 173:1622-1635(2018). RN [24] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). RN [25] RP VARIANT HSNSP ARG-147. RX PubMed=16399879; DOI=10.1136/jmg.2005.039230; RA Bouhouche A., Benomar A., Bouslam N., Chkili T., Yahyaoui M.; RT "Mutation in the epsilon subunit of the cytosolic chaperonin-containing T- RT complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory RT neuropathy with spastic paraplegia."; RL J. Med. Genet. 43:441-443(2006). CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a CC molecular chaperone complex that assists the folding of proteins upon CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding CC of WRAP53/TCAB1, thereby regulating telomere maintenance CC (PubMed:25467444). As part of the TRiC complex may play a role in the CC assembly of BBSome, a complex involved in ciliogenesis regulating CC transports vesicles to the cilia (PubMed:20080638). The TRiC complex CC plays a role in the folding of actin and tubulin (Probable). CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000305}. CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked CC rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444). CC Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By CC similarity). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000250|UniProtKB:P80316, ECO:0000269|PubMed:14532270, CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444, CC ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC P48643; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-355710, EBI-2875816; CC P48643; P54253: ATXN1; NbExp=3; IntAct=EBI-355710, EBI-930964; CC P48643; O95817: BAG3; NbExp=3; IntAct=EBI-355710, EBI-747185; CC P48643; Q14457: BECN1; NbExp=3; IntAct=EBI-355710, EBI-949378; CC P48643; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-355710, EBI-350590; CC P48643; Q9H9Q2: COPS7B; NbExp=3; IntAct=EBI-355710, EBI-2510162; CC P48643; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-355710, EBI-10213520; CC P48643; Q9UKC9: FBXL2; NbExp=3; IntAct=EBI-355710, EBI-724253; CC P48643; Q9NXC2: GFOD1; NbExp=3; IntAct=EBI-355710, EBI-8799578; CC P48643; O75409: H2AP; NbExp=3; IntAct=EBI-355710, EBI-6447217; CC P48643; P52790: HK3; NbExp=3; IntAct=EBI-355710, EBI-2965780; CC P48643; P49639: HOXA1; NbExp=3; IntAct=EBI-355710, EBI-740785; CC P48643; P42858: HTT; NbExp=3; IntAct=EBI-355710, EBI-466029; CC P48643; Q14525: KRT33B; NbExp=3; IntAct=EBI-355710, EBI-1049638; CC P48643; Q68G74: LHX8; NbExp=3; IntAct=EBI-355710, EBI-8474075; CC P48643; A2RU56: LOC401296; NbExp=3; IntAct=EBI-355710, EBI-9088215; CC P48643; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-355710, EBI-2510853; CC P48643; O15130-2: NPFF; NbExp=3; IntAct=EBI-355710, EBI-25840002; CC P48643; Q96LB9: PGLYRP3; NbExp=3; IntAct=EBI-355710, EBI-12339509; CC P48643; O75925: PIAS1; NbExp=3; IntAct=EBI-355710, EBI-629434; CC P48643; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-355710, EBI-12891828; CC P48643; Q9H0F5-2: RNF38; NbExp=3; IntAct=EBI-355710, EBI-25866807; CC P48643; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-355710, EBI-9089805; CC P48643; O60902-3: SHOX2; NbExp=3; IntAct=EBI-355710, EBI-9092164; CC P48643; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-355710, EBI-11959123; CC P48643; O75886: STAM2; NbExp=3; IntAct=EBI-355710, EBI-373258; CC P48643; O95630: STAMBP; NbExp=3; IntAct=EBI-355710, EBI-396676; CC P48643; A1L378: STRC; NbExp=3; IntAct=EBI-355710, EBI-22013242; CC P48643; O60220: TIMM8A; NbExp=3; IntAct=EBI-355710, EBI-1049822; CC P48643; P04637: TP53; NbExp=3; IntAct=EBI-355710, EBI-366083; CC P48643; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-355710, EBI-10964469; CC P48643; Q96B02: UBE2W; NbExp=3; IntAct=EBI-355710, EBI-716589; CC P48643; P45880: VDAC2; NbExp=3; IntAct=EBI-355710, EBI-354022; CC P48643; O00308: WWP2; NbExp=6; IntAct=EBI-355710, EBI-743923; CC P48643; Q96N77-2: ZNF641; NbExp=3; IntAct=EBI-355710, EBI-12939666; CC P48643; O60232: ZNRD2; NbExp=4; IntAct=EBI-355710, EBI-741415; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P48643-1; Sequence=Displayed; CC Name=2; CC IsoId=P48643-2; Sequence=VSP_054005, VSP_054006; CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71) CC infection (at protein level). {ECO:0000269|PubMed:16548883}. CC -!- PTM: Ubiquitinated by the DCX(DCAF12) complex specifically recognizes CC the diglutamate (Glu-Glu) at the C-terminus, leading to its CC degradation. {ECO:0000269|PubMed:29779948}. CC -!- DISEASE: Neuropathy, hereditary sensory, with spastic paraplegia, CC autosomal recessive (HSNSP) [MIM:256840]: A disease characterized by CC spastic paraplegia and progressive distal sensory neuropathy leading to CC mutilating ulcerations of the upper and lower limbs. CC {ECO:0000269|PubMed:16399879}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA07894.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D43950; BAA07894.2; ALT_INIT; mRNA. DR EMBL; AK289353; BAF82042.1; -; mRNA. DR EMBL; AK290393; BAF83082.1; -; mRNA. DR EMBL; AK302383; BAG63700.1; -; mRNA. DR EMBL; AC012640; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471102; EAX08072.1; -; Genomic_DNA. DR EMBL; BC006543; AAH06543.1; -; mRNA. DR EMBL; BC035499; AAH35499.1; -; mRNA. DR CCDS; CCDS3877.1; -. [P48643-1] DR CCDS; CCDS82990.1; -. [P48643-2] DR RefSeq; NP_001293084.1; NM_001306155.1. [P48643-2] DR RefSeq; NP_036205.1; NM_012073.4. [P48643-1] DR PDB; 5UYX; X-ray; 3.50 A; A/B/C/D=1-541. DR PDB; 5UYZ; X-ray; 3.60 A; A/B/C/D=1-541. DR PDB; 6NR8; EM; 7.80 A; E/M=25-541. DR PDB; 6NR9; EM; 8.50 A; E/M=25-541. DR PDB; 6NRA; EM; 7.70 A; E/M=25-541. DR PDB; 6NRB; EM; 8.70 A; E/M=25-541. DR PDB; 6NRC; EM; 8.30 A; E/M=25-541. DR PDB; 6NRD; EM; 8.20 A; E/M=25-541. DR PDB; 6QB8; EM; 3.97 A; E/e=1-541. DR PDB; 7LUM; EM; 4.50 A; D/L=1-541. DR PDB; 7LUP; EM; 6.20 A; D/L=1-541. DR PDB; 7NVL; EM; 2.50 A; E/e=1-541. DR PDB; 7NVM; EM; 3.10 A; E/e=1-541. DR PDB; 7NVN; EM; 3.00 A; E/e=1-541. DR PDB; 7NVO; EM; 3.50 A; E/e=1-541. DR PDBsum; 5UYX; -. DR PDBsum; 5UYZ; -. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRA; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 6QB8; -. DR PDBsum; 7LUM; -. DR PDBsum; 7LUP; -. DR PDBsum; 7NVL; -. DR PDBsum; 7NVM; -. DR PDBsum; 7NVN; -. DR PDBsum; 7NVO; -. DR AlphaFoldDB; P48643; -. DR SMR; P48643; -. DR BioGRID; 116603; 480. DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex. DR CORUM; P48643; -. DR DIP; DIP-31181N; -. DR IntAct; P48643; 246. DR MINT; P48643; -. DR STRING; 9606.ENSP00000280326; -. DR ChEMBL; CHEMBL4295766; -. DR GlyGen; P48643; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P48643; -. DR MetOSite; P48643; -. DR PhosphoSitePlus; P48643; -. DR SwissPalm; P48643; -. DR BioMuta; CCT5; -. DR DMDM; 1351211; -. DR OGP; P48643; -. DR REPRODUCTION-2DPAGE; IPI00010720; -. DR SWISS-2DPAGE; P48643; -. DR EPD; P48643; -. DR jPOST; P48643; -. DR MassIVE; P48643; -. DR MaxQB; P48643; -. DR PaxDb; P48643; -. DR PeptideAtlas; P48643; -. DR PRIDE; P48643; -. DR ProteomicsDB; 5518; -. DR ProteomicsDB; 55918; -. [P48643-1] DR ABCD; P48643; 1 sequenced antibody. DR Antibodypedia; 1210; 341 antibodies from 33 providers. DR DNASU; 22948; -. DR Ensembl; ENST00000280326.9; ENSP00000280326.4; ENSG00000150753.12. [P48643-1] DR Ensembl; ENST00000506600.1; ENSP00000423052.1; ENSG00000150753.12. [P48643-2] DR GeneID; 22948; -. DR KEGG; hsa:22948; -. DR MANE-Select; ENST00000280326.9; ENSP00000280326.4; NM_012073.5; NP_036205.1. DR UCSC; uc011cmt.3; human. [P48643-1] DR CTD; 22948; -. DR DisGeNET; 22948; -. DR GeneCards; CCT5; -. DR HGNC; HGNC:1618; CCT5. DR HPA; ENSG00000150753; Low tissue specificity. DR MalaCards; CCT5; -. DR MIM; 256840; phenotype. DR MIM; 610150; gene. DR neXtProt; NX_P48643; -. DR OpenTargets; ENSG00000150753; -. DR Orphanet; 139578; Mutilating hereditary sensory neuropathy with spastic paraplegia. DR PharmGKB; PA26182; -. DR VEuPathDB; HostDB:ENSG00000150753; -. DR eggNOG; KOG0357; Eukaryota. DR GeneTree; ENSGT00550000074988; -. DR InParanoid; P48643; -. DR OMA; QTGSNDM; -. DR PhylomeDB; P48643; -. DR TreeFam; TF105638; -. DR BRENDA; 3.6.4.B10; 2681. DR PathwayCommons; P48643; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC. DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR SignaLink; P48643; -. DR BioGRID-ORCS; 22948; 756 hits in 1073 CRISPR screens. DR ChiTaRS; CCT5; human. DR GeneWiki; CCT5_(gene); -. DR GenomeRNAi; 22948; -. DR Pharos; P48643; Tbio. DR PRO; PR:P48643; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P48643; protein. DR Bgee; ENSG00000150753; Expressed in endometrium epithelium and 209 other tissues. DR ExpressionAtlas; P48643; baseline and differential. DR Genevisible; P48643; HS. DR GO; GO:0044297; C:cell body; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:MGI. DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005874; C:microtubule; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro. DR GO; GO:0048487; F:beta-tubulin binding; IPI:UniProtKB. DR GO; GO:0031681; F:G-protein beta-subunit binding; IPI:UniProtKB. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:CAFA. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA. DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase. DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal. DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL. DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL. DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. DR GO; GO:1901998; P:toxin transport; IEA:Ensembl. DR CDD; cd03339; TCP1_epsilon; 1. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR012718; Chap_CCT_epsi. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR PANTHER; PTHR11353; CHAPERONIN; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1. DR TIGRFAMs; TIGR02343; chap_CCT_epsi; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. DR AGR; HGNC:1618; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant; KW Isopeptide bond; Neuropathy; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT CHAIN 2..541 FT /note="T-complex protein 1 subunit epsilon" FT /id="PRO_0000128346" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 346 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 539 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 210 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 265 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 275 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 279 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 392 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..38 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054005" FT VAR_SEQ 56..110 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054006" FT VARIANT 146 FT /note="E -> V (in dbSNP:rs11557652)" FT /id="VAR_052267" FT VARIANT 147 FT /note="H -> R (in HSNSP; dbSNP:rs118203986)" FT /evidence="ECO:0000269|PubMed:16399879" FT /id="VAR_030658" FT CONFLICT 55 FT /note="N -> D (in Ref. 2; BAF83082)" FT /evidence="ECO:0000305" FT CONFLICT 512 FT /note="G -> D (in Ref. 2; BAF83082)" FT /evidence="ECO:0000305" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:7NVN" FT TURN 20..24 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 26..29 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 31..48 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:7NVO" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 74..80 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 86..101 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 108..125 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 130..151 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 158..161 FT /evidence="ECO:0007829|PDB:5UYX" FT HELIX 163..173 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 177..181 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 182..195 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 199..202 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 223..231 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 241..251 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 261..268 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 271..294 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 298..304 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 308..316 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 327..337 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 354..363 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 370..375 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 383..391 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 392..414 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 417..420 FT /evidence="ECO:0007829|PDB:7NVL" FT TURN 421..423 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 424..439 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 442..444 FT /evidence="ECO:0007829|PDB:7NVM" FT HELIX 445..455 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 457..465 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 470..483 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 501..504 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 507..509 FT /evidence="ECO:0007829|PDB:7NVL" FT HELIX 510..528 FT /evidence="ECO:0007829|PDB:7NVL" FT STRAND 530..535 FT /evidence="ECO:0007829|PDB:7NVL" SQ SEQUENCE 541 AA; 59671 MW; 164168BB80EF022A CRC64; MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA EQLLDRGIHP IRIADGYEQA ARVAIEHLDK ISDSVLVDIK DTEPLIQTAK TTLGSKVVNS CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP KKVEDAKIAI LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIQ QIKETGANLA ICQWGFDDEA NHLLLQNNLP AVRWVGGPEI ELIAIATGGR IVPRFSELTA EKLGFAGLVQ EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY GGGAAEISCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR QVKEMNPALG IDCLHKGTND MKQQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE E // ID HYDIN_HUMAN Reviewed; 5121 AA. AC Q4G0P3; A6NC70; A6NLZ0; B4DQY4; B4DRN4; F5H6V3; Q8N3H8; Q8N3P6; Q8TC08; AC Q96JG3; Q96SS4; Q9H5U3; Q9H9B8; Q9NTI0; Q9UBE5; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 3. DT 14-DEC-2022, entry version 150. DE RecName: Full=Hydrocephalus-inducing protein homolog; GN Name=HYDIN; Synonyms=HYDIN1, KIAA1864; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 6 AND 7), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4575-5121 (ISOFORM 1). RC TISSUE=Lung, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 715-5121 (ISOFORM 4), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4141-5121 (ISOFORM 1). RC TISSUE=Amygdala, and Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP IDENTIFICATION. RX PubMed=16938426; DOI=10.1016/j.ygeno.2006.07.012; RA Doggett N.A., Xie G., Meincke L.J., Sutherland R.D., Mundt M.O., RA Berbari N.S., Davy B.E., Robinson M.L., Rudd M.K., Weber J.L., RA Stallings R.L., Han C.; RT "A 360-kb interchromosomal duplication of the human HYDIN locus."; RL Genomics 88:762-771(2006). RN [6] RP REVIEW. RX PubMed=17296793; DOI=10.1083/jcb.200701113; RA Smith E.F.; RT "Hydin seek: finding a function in ciliary motility."; RL J. Cell Biol. 176:403-404(2007). RN [7] RP INVOLVEMENT IN CILD5. RX PubMed=23022101; DOI=10.1016/j.ajhg.2012.08.016; RA Olbrich H., Schmidts M., Werner C., Onoufriadis A., Loges N.T., Raidt J., RA Banki N.F., Shoemark A., Burgoyne T., Al Turki S., Hurles M.E., Kohler G., RA Schroeder J., Nurnberg G., Nurnberg P., Chung E.M., Reinhardt R., RA Marthin J.K., Nielsen K.G., Mitchison H.M., Omran H.; RT "Recessive HYDIN mutations cause primary ciliary dyskinesia without RT randomization of left-right body asymmetry."; RL Am. J. Hum. Genet. 91:672-684(2012). RN [8] RP INVOLVEMENT IN CILD5. RX PubMed=25186273; DOI=10.1183/09031936.00052014; RA Raidt J., Wallmeier J., Hjeij R., Onnebrink J.G., Pennekamp P., Loges N.T., RA Olbrich H., Haeffner K., Dougherty G.W., Omran H., Werner C.; RT "Ciliary beat pattern and frequency in genetic variants of primary ciliary RT dyskinesia."; RL Eur. Respir. J. 44:1579-1588(2014). RN [9] RP STRUCTURE BY NMR OF 458-563. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the C-terminal PAPD-like domain from human HYDIN RT protein."; RL Submitted (JUL-2007) to the PDB data bank. CC -!- FUNCTION: Required for ciliary motility. {ECO:0000250}. CC -!- SUBUNIT: Interacts with KIF9. {ECO:0000250|UniProtKB:Q80W93}. CC -!- INTERACTION: CC Q4G0P3-6; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-14748124, EBI-724639; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000305}. Cytoplasm, CC cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q80W93}. CC Note=Localizes in the cilium axoneme in a SPEF1-dependent manner. CC {ECO:0000250|UniProtKB:Q80W93}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q4G0P3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q4G0P3-2; Sequence=VSP_024684, VSP_024697, VSP_024698; CC Name=4; CC IsoId=Q4G0P3-5; Sequence=VSP_024691, VSP_024692; CC Name=5; CC IsoId=Q4G0P3-6; Sequence=VSP_024687, VSP_024688; CC Name=6; CC IsoId=Q4G0P3-8; Sequence=VSP_042692, VSP_042693, VSP_042694; CC Name=7; CC IsoId=Q4G0P3-10; Sequence=VSP_046818, VSP_042693, VSP_042694; CC -!- DISEASE: Ciliary dyskinesia, primary, 5 (CILD5) [MIM:608647]: An CC autosomal recessive form of primary dyskinesia, a disorder CC characterized by abnormalities of motile cilia. Respiratory infections CC leading to chronic inflammation and bronchiectasis are recurrent, due CC to defects in the respiratory cilia; reduced fertility is often CC observed in male patients due to abnormalities of sperm tails. Half of CC the patients exhibit randomization of left-right body asymmetry and CC situs inversus, due to dysfunction of monocilia at the embryonic node. CC Primary ciliary dyskinesia associated with situs inversus is referred CC to as Kartagener syndrome. CILD5 is characterized by early onset of a CC progressive decline in lung function due to an inability to clear mucus CC and particles from the airways. Affected individuals have recurrent CC infections of the sinuses, ears, airways, and lungs. Sperm motility is CC also decreased. Individuals with CILD5 do not have situs inversus. CC {ECO:0000269|PubMed:23022101, ECO:0000269|PubMed:25186273}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH28351.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15527.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK022933; BAB14314.1; -; mRNA. DR EMBL; AK026688; BAB15527.1; ALT_FRAME; mRNA. DR EMBL; AK299016; BAG61096.1; -; mRNA. DR EMBL; AK299348; BAG61346.1; -; mRNA. DR EMBL; AC027281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC028351; AAH28351.2; ALT_INIT; mRNA. DR EMBL; BC043273; AAH43273.1; -; mRNA. DR EMBL; AL122038; CAB59178.1; -; mRNA. DR EMBL; AL133042; CAB61370.1; -; mRNA. DR EMBL; AL137259; CAB70660.1; -; mRNA. DR CCDS; CCDS10897.1; -. [Q4G0P3-5] DR CCDS; CCDS56004.1; -. [Q4G0P3-8] DR CCDS; CCDS56005.1; -. [Q4G0P3-10] DR CCDS; CCDS59269.1; -. [Q4G0P3-1] DR PIR; T42699; T42699. DR PIR; T46330; T46330. DR RefSeq; NP_001185471.1; NM_001198542.1. [Q4G0P3-8] DR RefSeq; NP_001185472.1; NM_001198543.1. [Q4G0P3-10] DR RefSeq; NP_001257903.1; NM_001270974.2. [Q4G0P3-1] DR RefSeq; NP_060028.2; NM_017558.4. [Q4G0P3-5] DR PDB; 2E6J; NMR; -; A=459-563. DR PDB; 2YS4; NMR; -; A=182-296. DR PDBsum; 2E6J; -. DR PDBsum; 2YS4; -. DR BMRB; Q4G0P3; -. DR SMR; Q4G0P3; -. DR BioGRID; 120142; 11. DR IntAct; Q4G0P3; 5. DR STRING; 9606.ENSP00000377197; -. DR iPTMnet; Q4G0P3; -. DR PhosphoSitePlus; Q4G0P3; -. DR BioMuta; HYDIN; -. DR DMDM; 327478578; -. DR EPD; Q4G0P3; -. DR MassIVE; Q4G0P3; -. DR MaxQB; Q4G0P3; -. DR PaxDb; Q4G0P3; -. DR PeptideAtlas; Q4G0P3; -. DR ProteomicsDB; 27301; -. DR ProteomicsDB; 62119; -. [Q4G0P3-1] DR ProteomicsDB; 62120; -. [Q4G0P3-2] DR ProteomicsDB; 62121; -. [Q4G0P3-5] DR ProteomicsDB; 62122; -. [Q4G0P3-6] DR ProteomicsDB; 62123; -. [Q4G0P3-8] DR Antibodypedia; 66504; 48 antibodies from 12 providers. DR DNASU; 54768; -. DR Ensembl; ENST00000321489.9; ENSP00000314736.5; ENSG00000157423.18. [Q4G0P3-5] DR Ensembl; ENST00000393567.7; ENSP00000377197.2; ENSG00000157423.18. [Q4G0P3-1] DR Ensembl; ENST00000538248.5; ENSP00000444970.1; ENSG00000157423.18. [Q4G0P3-8] DR Ensembl; ENST00000541601.5; ENSP00000437341.1; ENSG00000157423.18. [Q4G0P3-10] DR Ensembl; ENST00000634268.1; ENSP00000489181.1; ENSG00000283022.2. [Q4G0P3-8] DR Ensembl; ENST00000634392.1; ENSP00000489221.1; ENSG00000283022.2. [Q4G0P3-10] DR Ensembl; ENST00000634745.1; ENSP00000489246.1; ENSG00000283022.2. [Q4G0P3-5] DR Ensembl; ENST00000635381.2; ENSP00000489526.1; ENSG00000283022.2. [Q4G0P3-1] DR GeneID; 54768; -. DR KEGG; hsa:54768; -. DR MANE-Select; ENST00000393567.7; ENSP00000377197.2; NM_001270974.2; NP_001257903.1. DR UCSC; uc010vmc.3; human. [Q4G0P3-1] DR CTD; 54768; -. DR DisGeNET; 54768; -. DR GeneCards; HYDIN; -. DR GeneReviews; HYDIN; -. DR HGNC; HGNC:19368; HYDIN. DR HPA; ENSG00000157423; Tissue enhanced (brain, choroid plexus). DR MalaCards; HYDIN; -. DR MIM; 608647; phenotype. DR MIM; 610812; gene. DR neXtProt; NX_Q4G0P3; -. DR OpenTargets; ENSG00000157423; -. DR Orphanet; 244; Primary ciliary dyskinesia. DR PharmGKB; PA134866950; -. DR VEuPathDB; HostDB:ENSG00000157423; -. DR eggNOG; ENOG502QQ4F; Eukaryota. DR GeneTree; ENSGT00610000086095; -. DR HOGENOM; CLU_000116_1_0_1; -. DR InParanoid; Q4G0P3; -. DR OMA; AHLQMEV; -. DR OrthoDB; 3322at2759; -. DR PhylomeDB; Q4G0P3; -. DR TreeFam; TF340616; -. DR PathwayCommons; Q4G0P3; -. DR SignaLink; Q4G0P3; -. DR SIGNOR; Q4G0P3; -. DR BioGRID-ORCS; 54768; 46 hits in 1056 CRISPR screens. DR ChiTaRS; HYDIN; human. DR EvolutionaryTrace; Q4G0P3; -. DR GenomeRNAi; 54768; -. DR Pharos; Q4G0P3; Tbio. DR PRO; PR:Q4G0P3; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q4G0P3; protein. DR Bgee; ENSG00000157423; Expressed in right uterine tube and 101 other tissues. DR ExpressionAtlas; Q4G0P3; baseline and differential. DR Genevisible; Q4G0P3; HS. DR GO; GO:1990716; C:axonemal central apparatus; ISS:UniProtKB. DR GO; GO:1990718; C:axonemal central pair projection; IEA:Ensembl. DR GO; GO:0005930; C:axoneme; IBA:GO_Central. DR GO; GO:1904158; P:axonemal central apparatus assembly; IBA:GO_Central. DR GO; GO:0003341; P:cilium movement; IBA:GO_Central. DR GO; GO:0002064; P:epithelial cell development; IEA:Ensembl. DR GO; GO:0060438; P:trachea development; IEA:Ensembl. DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 22. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR031549; ASH. DR InterPro; IPR033305; Hydin-like. DR InterPro; IPR033768; Hydin_ADK. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23053; DLEC1 DELETED IN LUNG AND ESOPHAGEAL CANCER 1; 1. DR Pfam; PF15780; ASH; 1. DR Pfam; PF17213; Hydin_ADK; 1. DR AGR; HGNC:19368; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; KW Coiled coil; Cytoplasm; Cytoskeleton; Kartagener syndrome; KW Primary ciliary dyskinesia; Reference proteome. FT CHAIN 1..5121 FT /note="Hydrocephalus-inducing protein homolog" FT /id="PRO_0000284844" FT REGION 363..754 FT /note="Interaction with KIF9" FT /evidence="ECO:0000250|UniProtKB:Q80W93" FT REGION 956..987 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1925..1951 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2155..2186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2333..2459 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2482..2534 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2664..2684 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3852..3874 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1908..1933 FT /evidence="ECO:0000255" FT COILED 2267..2365 FT /evidence="ECO:0000255" FT COILED 2504..2549 FT /evidence="ECO:0000255" FT COMPBIAS 1936..1951 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2333..2374 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2395..2426 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2440..2455 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2489..2534 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3856..3874 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..3823 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024684" FT VAR_SEQ 1 FT /note="M -> MESAGGFKLGMEPLSGGGVCEKKKLLKM (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042692" FT VAR_SEQ 1 FT /note="M -> MESAGGFKLGEKKKLLKM (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046818" FT VAR_SEQ 693..708 FT /note="CVVPALHLVNTEVDFG -> YCSPACSSPESPPSLQ (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024687" FT VAR_SEQ 709..5121 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024688" FT VAR_SEQ 923 FT /note="S -> R (in isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042693" FT VAR_SEQ 924..5121 FT /note="Missing (in isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042694" FT VAR_SEQ 1015..1017 FT /note="IVK -> VRG (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005" FT /id="VSP_024691" FT VAR_SEQ 1018..5121 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005" FT /id="VSP_024692" FT VAR_SEQ 3824 FT /note="E -> M (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024697" FT VAR_SEQ 4887..5121 FT /note="GTFSFEFQPLKAGETFGRLTLHNTDLGYYQYELYLKATPALPEKPVHFQTVL FT GSSQIILVKFINYTRQRTEYYCRTDCTDFHAEKLINAAPGGQGGTEASVEVLFEPSHLG FT ETKGILILSSLAGGEYIIPLFGMALPPKPQGPFSIRAGYSIIIPFKNVFYHMVTFSIIV FT DNPAFTIRAGESVRPKKINNITVSFEGNPSGSKTPITTKLTVSCPPGEGSETGVKWVYY FT LKGITL -> RWGLTASSRLECSGMIIAPCSLKLLQSRPPPASAS (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_024698" FT VARIANT 451 FT /note="R -> P (in dbSNP:rs7200485)" FT /id="VAR_031837" FT VARIANT 584 FT /note="T -> N (in dbSNP:rs7200126)" FT /id="VAR_031838" FT VARIANT 690 FT /note="T -> A (in dbSNP:rs10744982)" FT /id="VAR_031839" FT VARIANT 724 FT /note="N -> D (in dbSNP:rs3817211)" FT /id="VAR_031840" FT VARIANT 1077 FT /note="I -> V (in dbSNP:rs6416709)" FT /id="VAR_059667" FT VARIANT 1228 FT /note="V -> L (in dbSNP:rs1774513)" FT /id="VAR_059668" FT VARIANT 1534 FT /note="I -> V (in dbSNP:rs1774303)" FT /id="VAR_059669" FT VARIANT 1718 FT /note="V -> M (in dbSNP:rs783762)" FT /id="VAR_051036" FT VARIANT 1892 FT /note="R -> H (in dbSNP:rs783732)" FT /id="VAR_051037" FT VARIANT 1952 FT /note="R -> Q (in dbSNP:rs17321570)" FT /id="VAR_051038" FT VARIANT 2087 FT /note="R -> C (in dbSNP:rs1774541)" FT /id="VAR_059670" FT VARIANT 2099 FT /note="V -> M (in dbSNP:rs1798337)" FT /id="VAR_051039" FT VARIANT 2242 FT /note="Q -> R (in dbSNP:rs2258307)" FT /id="VAR_059671" FT VARIANT 2276 FT /note="Q -> R (in dbSNP:rs1815707)" FT /id="VAR_051040" FT VARIANT 2298 FT /note="R -> G (in dbSNP:rs1774360)" FT /id="VAR_059672" FT VARIANT 2306 FT /note="E -> G (in dbSNP:rs2502726)" FT /id="VAR_051041" FT VARIANT 2445 FT /note="N -> I (in dbSNP:rs1798532)" FT /id="VAR_051042" FT VARIANT 2455 FT /note="P -> Q (in dbSNP:rs1798531)" FT /id="VAR_061666" FT VARIANT 2502 FT /note="L -> S (in dbSNP:rs1798529)" FT /id="VAR_051043" FT VARIANT 2530 FT /note="K -> E (in dbSNP:rs1798528)" FT /id="VAR_059673" FT VARIANT 2558 FT /note="G -> E (in dbSNP:rs8044142)" FT /id="VAR_051044" FT VARIANT 2570 FT /note="D -> N (in dbSNP:rs8044001)" FT /id="VAR_059674" FT VARIANT 2589 FT /note="K -> R (in dbSNP:rs1774395)" FT /id="VAR_051045" FT VARIANT 2694 FT /note="I -> S (in dbSNP:rs1774449)" FT /id="VAR_059675" FT VARIANT 2932 FT /note="P -> L (in dbSNP:rs11075812)" FT /id="VAR_051046" FT VARIANT 2937 FT /note="E -> K (in dbSNP:rs8047935)" FT /id="VAR_051047" FT VARIANT 2939 FT /note="R -> K (in dbSNP:rs7188837)" FT /id="VAR_051048" FT VARIANT 2994 FT /note="E -> G (in dbSNP:rs12102425)" FT /id="VAR_051049" FT VARIANT 3116 FT /note="T -> R (in dbSNP:rs1774423)" FT /id="VAR_051050" FT VARIANT 3269 FT /note="Y -> D (in dbSNP:rs7197263)" FT /id="VAR_051051" FT VARIANT 3291 FT /note="A -> P (in dbSNP:rs1798440)" FT /id="VAR_059676" FT VARIANT 3316 FT /note="L -> P (in dbSNP:rs1774331)" FT /id="VAR_059677" FT VARIANT 3739 FT /note="A -> T (in dbSNP:rs1774504)" FT /id="VAR_059678" FT VARIANT 3742 FT /note="V -> I (in dbSNP:rs1798413)" FT /id="VAR_059679" FT VARIANT 3811 FT /note="R -> H (in dbSNP:rs13338821)" FT /id="VAR_051052" FT VARIANT 3840 FT /note="V -> L (in dbSNP:rs1798325)" FT /id="VAR_059680" FT VARIANT 3869 FT /note="M -> R (in dbSNP:rs7192347)" FT /id="VAR_059681" FT VARIANT 3899 FT /note="V -> M (in dbSNP:rs1626593)" FT /id="VAR_051053" FT VARIANT 4005 FT /note="T -> A (in dbSNP:rs1539302)" FT /id="VAR_059682" FT VARIANT 4026 FT /note="A -> T (in dbSNP:rs11075798)" FT /id="VAR_051054" FT VARIANT 4088 FT /note="K -> R (in dbSNP:rs1774416)" FT /id="VAR_051055" FT VARIANT 4160 FT /note="E -> Q (in dbSNP:rs1798314)" FT /id="VAR_059683" FT VARIANT 4270 FT /note="H -> Y (in dbSNP:rs1891343)" FT /id="VAR_051056" FT VARIANT 4363 FT /note="S -> C (in dbSNP:rs1770434)" FT /id="VAR_059684" FT VARIANT 4412 FT /note="K -> E (in dbSNP:rs1774480)" FT /id="VAR_059685" FT VARIANT 4552 FT /note="M -> L (in dbSNP:rs1770442)" FT /id="VAR_059686" FT VARIANT 4606 FT /note="N -> K (in dbSNP:rs783898)" FT /id="VAR_051058" FT VARIANT 4869 FT /note="R -> Q (in dbSNP:rs2795652)" FT /id="VAR_059687" FT CONFLICT 299 FT /note="L -> P (in Ref. 1; BAB14314)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="L -> M (in Ref. 3; AAH28351)" FT /evidence="ECO:0000305" FT CONFLICT 460 FT /note="K -> T (in Ref. 1; BAB14314)" FT /evidence="ECO:0000305" FT CONFLICT 532 FT /note="T -> I (in Ref. 3; AAH28351)" FT /evidence="ECO:0000305" FT CONFLICT 584 FT /note="T -> I (in Ref. 1; BAG61096)" FT /evidence="ECO:0000305" FT CONFLICT 881 FT /note="D -> N (in Ref. 1; BAG61096)" FT /evidence="ECO:0000305" FT CONFLICT 3945 FT /note="S -> N (in Ref. 3; AAH43273)" FT /evidence="ECO:0000305" FT CONFLICT 4663 FT /note="P -> T (in Ref. 3; AAH43273)" FT /evidence="ECO:0000305" FT CONFLICT 4667 FT /note="G -> V (in Ref. 1; BAB15527)" FT /evidence="ECO:0000305" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 210..215 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 217..224 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 231..236 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 241..250 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 255..262 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 275..281 FT /evidence="ECO:0007829|PDB:2YS4" FT STRAND 460..464 FT /evidence="ECO:0007829|PDB:2E6J" FT STRAND 466..476 FT /evidence="ECO:0007829|PDB:2E6J" FT STRAND 479..487 FT /evidence="ECO:0007829|PDB:2E6J" FT STRAND 493..497 FT /evidence="ECO:0007829|PDB:2E6J" FT HELIX 503..507 FT /evidence="ECO:0007829|PDB:2E6J" FT STRAND 509..517 FT /evidence="ECO:0007829|PDB:2E6J" FT STRAND 524..529 FT /evidence="ECO:0007829|PDB:2E6J" FT STRAND 535..541 FT /evidence="ECO:0007829|PDB:2E6J" FT STRAND 543..547 FT /evidence="ECO:0007829|PDB:2E6J" FT STRAND 554..561 FT /evidence="ECO:0007829|PDB:2E6J" SQ SEQUENCE 5121 AA; 575892 MW; 47FB2A11C7E50A4F CRC64; MTSRRLEESM GAVQMGLVNM FKGFQSKVLP PLSPKVVTEE EVNRMLTPSE FLKEMSLTTE QRLAKTRLMC RPQIIELLDM GETTHQKFSG IDLDQALFQP FPSEIIFQNY TPCEVYEVPL ILRNNDKIPR LVKVVEESSP YFKVISPKDI GHKVAPGVPS IFRILFTPEE NKDYAHTLTC VTEREKFIVP IKARGARAIL DFPDKLNFST CPVKYSTQKI LLVRNIGNKN AVFHIKTCRP FSIEPAIGTL NVGESMQLEV EFEPQSVGDH SGRLIVCYDT GEKVFVSLYG AAIDMNIRLD KNSLTIEKTY ISLANQRTIT IHNRSNIIAH FLWKVFATQQ EEDREKYRAC DDLIKEEKDE TDEFFEECIT DPLLREHLSV LSRTFANQRR LVQGDSKLFF NNVFTVEPLE GDVWPNSSAE ITVYFNPLEA KLYQQTIYCD ILGREIRLPL RIKGEGMGPK IHFNFELLDI GKVFTGSAHC YEAILYNKGS IDALFNMTPP TSALGACFVF SPKEGIIEPS GVQAIQISFS STILGNFEEE FLVNVNGSPE PVKLTIRGCV IGPTFHFNVP ALHFGDVSFG FPHTLICSLN NTSLIPMTYK LRIPGDGLGH KSISYCEQHV DYKRPSWTKE EISSMKPKEF TISPDCGTIR PQGFAAIRVT LCSNTVQKYE LALVVDVEGI GEEVLALLIT ARCVVPALHL VNTEVDFGHC FLKYPYEKTL QLANQDDLPG FYEVQPQVCE EVPTVLFSSP TPSGVISPSS TIHIPLVLET QVTGEHRSTV YISIFGSQDP PLVCHLKSAG EGPVIYVHPN QVDFGNIYVL KDSSRILNLC NQSFIPAFFQ AHMAHKKSLW TIEPNEGMVP PETDVQLALT ANLNDTLTFK DCVILDIENS STYRIPVQAS GTGSTIVSDK PFAPELNLGA HFSLDTHYYH FKLINKGRRI QQLFWMNDSF RPQAKLSKKG RVKKGHAHVQ PQPSGSQEPR DPQSPVFHLH PASMELYPGQ AIDVILEGYS ATPRIVKEKL VCHAIIGAQK GKSLVMAVNI TCEFVAPLIQ LSTKQLIYRL EKKPNSILKP DYQPLAIKNI STLPVNLLLS TSGPFFICET DKSLLPATPE PIKLEIDEEK NLLIKFDPSY RNDLNNWVAE EILAIKYVEH PQIDSLDLRG EVHYPNLSFE TKELDFGCIL NDTELIRYVT ITNCSPLVVK FRWFFLVNDE ENQIRFVTLP KKPYSAPVSQ MESIPATSEA ASPPAILVTV ESPEMDLNDF VKTVLVDEDA RPEEKELRKT KASSVISDEI KISSTEIERI YSSQSQVEDQ ESLQTCEQNE MLSIGIEEVF DILPLFGVLQ PHSSHQISFT FYGHANIIAQ AKALCEVEEG PTYEITLKGE ASLVNYSFDT KDIHYGLQLF DHVTEREITL TNMGKVGFEF KVLTDHQSSP DNLLPGVPLI LPVSGFISSH QEQVLKVYYL PGVPEVFKRS FQIQIAHLDP ENITLSGEGI FPQICLDLPR NLTANEKYEM FLNQARKNTD KEYNKCEMLD HFDIITEEVP EDEPAEVSAH LQMEVERLIV QSYVLEHQKT TTPDPMDDPC FSHRSRRKLA KIQLPEYILD FGYIILGEVR THIIKIINTS HFPVSFHADK RVLHETGFST ELDRVKNLPH CETEIFEVRF DPQGANLPVG SKEVILPIKV VGGPTVHICL QAKVTIPTMT LSRGKVDFAT IQCGQCLVET IQLSNHLQVP CEWFVQSQKP VDKLEKHMPK YLRQKLRAEL KPKTRIFEIQ PISGVLDPGE KSNVQVKFMP KEEKFYSQTL VFQIAQSAQK LTLLARGQGL EPRLEFSPSV LDLGPLLLCA PGDEAEVIVK NPCNFPIEFY SLEFDQQYLI EEKILRKLKG YDSYNTLLLP PRNPGEKLPP ELYEYFKEIK KSKEEQMRAK YLENLAQENE EEDITSSDQG TSNSTKRTSL SRGISVTSNL EEWHALLVES KTYLEEEEDE ESLEKIIFQT DKLQSIDSHS MEEVGEVENN PVSKAIARHL GIDISAEGRL AKNRKGIAII IHGTPLSGKS ANAVSVAKYY NAACLSIDSI VLEAVANSNN IPGIRARELC IRAAIEQSVK EGEEAAQEAA VGQNVIGQGR LSTDTLGKLA SEMTLVAPEI KPGKSVRGSV VITKSKADSH GSGSQKQHHS HQSETPQISS SPLPPGPIHR WLSVSPSVGG ETGLMSCVLP DELLVQILAE RIQLSDCYRG VVFDGLDTLF AQNAAAALLC LLKAIGSREH IYILNMAQDY AAMKAQEKAK KEQEERKHKG ALEKEKERLQ NMDEEEYDAL TEEEKLTFDR GIQQALRERK KREQERLAKE MQEKKLQQEL ERQKEEDELK RRVKKGKQGP IKEEPPMKKS QAANKQVPPL TKVDVKMETI ERKISVREQT MSEKEELNKK KRNMGDVSMH GLPLVQDQED SEGDNSKDPD KQLAPKFKTY ELTLKDVQNI LMYWDRKQGV QLPPAGMEEA PHEPDDQRQV PLGGRRGRKD RERERLEKER TEKERLEREK AERERLEKLR ALEERSDWEG EGEEDHEGKK EKDLGVPFLD IQTPDFEGLS WKQALESDKL PKGEQILDIL GLGASGPPIP PPALFSIVSY PVKRPPLTMT DDLEHFVFVI PPSEDISLDE KKEMEIESDF LATTNTTKAQ EEQTSSSKGG KQKMKEKIDQ VFEIQKDKRH MALNRKVLSG EPAGTISQLS DTDLDNFNGQ HSQEKFTRLN HFRWIVPANG EVTLQVHFSS DEFGNFDQTF NFEILGTCCQ YQLYCRGICT YPYICQDPKV VFPQRKMDMK TNEVIFKKYV MSTETYYFGP LLCGKSRDKY KSSLFPGNME TLTILNTSLM VVEASFYFQN DVKANTYFLE PNTMVLKPNE KQILNVWAYP TSVGVFEDSI VCCINDNPEP AIFQLSCQGI RPELELEPRQ LHFDRLLLHR QESRVVLLRN VTLLPVAWRI TSLEHLGDDF TVSLMQGTIP PEAEYGLHLY FQPTKPVNIK KAIRLEVLDA ENLLGVVQIE NIMVFAEAYD IALDITFPKG AEGGLDFGIV RVTEEAKQPL QLKNRGKYEI AFSFSVDSVG ISTPNINSMI SVQPKKGSLT PTEKPTNVQV FFHAKKEVKI EHQPVLRCQI IEPNISEGGE IIASIPIKFS ANAVYSKYNI TPSSVINFGA LICGTRKSTT FTIENQGVTD FKFALYKLTG ESPIHQKKAA SHVRHARSRE SESFYKTGSS RAAKFSDTIQ KEVTTTGQAR FAHGMFTVYP GFGSIPSGGQ QVINVDCVAD AMGKCEEFIA IDISGRDPAV HPAGILYTLL AEACLPAFVT ENNALIFEEH QICTSANLHH ILQTIESGGL FVEDENKFIF CNVLVGRQAK ARFKISNVGK ITCDVNIVVR PISNKPFARI VDIFEVEPSK MCIASHSHAF ATVSFTPQIM QNYQCIFEAT LDGLPSTLAK SRGLVFDIAG EGNLPRVTVV RPVLHNQYGN PLLLFKRLLL GHSEKLPLIL KNNGVLPAQL HVDLQDELGV FSLKGRPTTA YIYITEENKP HVKAKKAHTA SLVVSPGDTA EFDVVFHSQK VGRMRGIIHL SVINNQYEET SIHMVGEGYE DDITLDNIHG LVAPTSQEDI SISEFTEIIE DNDMEDLVAA ALVDHIQFGD CHIGHSYNAS FTVTNHSQVN LIRFEWPVSA TIAFSPQMGH LHPGCAKDIV VTMKSDVPIN LKNMRIRCKL SRIMFQLPAD QVPDWDDRMH TVKWVDVPRN MPGTFTTKRK VIETDPEPAH SVLEENYQEL QLQISANVDF ASYHCQARDV RFKETLVYQT RVFEFDVINS GRVQLEFSWV SEDTSKAVSF AKPDHQGSAQ KDQLSQGTMH TGSTLDSTMD HWAEGSPQPF SVEPSSGIVP VGKIQKFKVK FSPLDIGDFE SNLFCQIPNL PPGEQGPVLV AKGRSTLPIC HFDLKDSDYI SGHQRNPELR GSSGGALDPN TRVIEFTTVG IGGKNLRTFT ILNPTNSTYS FCWISEEIES LQNPAAFTCL TEKGFIHPEK KAEIVFQFTP FHLGITESSW TFLIPEHNIT VPFLLVGKTT EPLISLNKSH LNFSSLLIGR EARETVQIIN KEEQGFDFSF QDNSRYSEGF SNSLLVCPME GWIPPLSRFP IDIFFTPKQE GDVNFNLICN VEKKVHPVTL NVKAEGYTMN VEIKCKDRTG SITLLTPNQT NIINFYEVEL NECVQCEFNF INTGKFTFSF QAQLCGSKTL LQYLEFSPID STVDVGQSVH ATLSFQPLKK CVLTDLELII KISHGPTFMC NISGCAVSPA IHFSFTSYNF GTCFIYQAGM PPYKQTLVIT NKEETPMSID CLYTNTTHLE VNSRVDVVKP GNTLEIPITF YPRESINYQE LIPFEINGLS QQTVEIKGKG TKMKILVLDP ANRIVKLGAV LPGQVVKRTV SIMNNSLAQL TFNQSILFTI PELQEPKVLT LAPFHNITLK PKEVCKLEVI FAPKKRVPPF SEEVFMECMG LLRPLFLLSG CCQALEISLD QEHIPFGPVV YQTQATRRIL MMNTGDVGAR FKWDIKKFEP HFSISPEEGY ITSGMEVSFE VTYHPTEVGK ESLCKNILCY IQGGSPLSLT LSGVCVGPPA VKEVVNFTCQ VRSKHTQTIL LSNRTNQTWN LHPIFEGEHW EGPEFITLEA HQQNKPYEIT YRPRTMNLEN RKHQGTLFFP LPDGTGWLYA LHGTSELPKA VANIYREVPC KTPYTELLPI TNWLNKPQRF RVIVEILKPE KPDLSITMKG LDYIDVLSGS KKDYKLNFFS HKEGTYAAKV IFRNEVTNEF LYYNVSFRVI PSGIIKTIEM VTPVRQVASA SIKLENPLPY SVTFSTECRM PDIALPSQFV VPANSEGTFS FEFQPLKAGE TFGRLTLHNT DLGYYQYELY LKATPALPEK PVHFQTVLGS SQIILVKFIN YTRQRTEYYC RTDCTDFHAE KLINAAPGGQ GGTEASVEVL FEPSHLGETK GILILSSLAG GEYIIPLFGM ALPPKPQGPF SIRAGYSIII PFKNVFYHMV TFSIIVDNPA FTIRAGESVR PKKINNITVS FEGNPSGSKT PITTKLTVSC PPGEGSETGV KWVYYLKGIT L // ID BBS2_HUMAN Reviewed; 721 AA. AC Q9BXC9; Q96CM0; Q96SN9; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 2. DT 14-DEC-2022, entry version 179. DE RecName: Full=Bardet-Biedl syndrome 2 protein {ECO:0000305}; GN Name=BBS2 {ECO:0000312|HGNC:HGNC:967}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT BBS2 GLY-75, AND VARIANTS ASN-70 AND RP VAL-123. RX PubMed=11285252; DOI=10.1093/hmg/10.8.865; RA Nishimura D.Y., Searby C.C., Carmi R., Elbedour K., Van Maldergem L., RA Fulton A.B., Lam B.L., Powell B.R., Swiderski R.E., Bugge K.E., RA Haider N.B., Kwitek-Black A.E., Ying L., Duhl D.M., Gorman S.M., Heon E., RA Iannaccone A., Bonneau D., Biesecker L.G., Jacobson S.G., Stone E.M., RA Sheffield V.C.; RT "Positional cloning of a novel gene on chromosome 16q causing Bardet-Biedl RT syndrome (BBS2)."; RL Hum. Mol. Genet. 10:865-874(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-70. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-70 AND VAL-122. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INVOLVEMENT IN BBS2, AND VARIANT BBS2 VAL-139. RX PubMed=16823392; DOI=10.1038/sj.ejhg.5201688; RA Laurier V., Stoetzel C., Muller J., Thibault C., Corbani S., Jalkh N., RA Salem N., Chouery E., Poch O., Licaire S., Danse J.M., Amati-Bonneau P., RA Bonneau D., Megarbane A., Mandel J.L., Dollfus H.; RT "Pitfalls of homozygosity mapping: an extended consanguineous Bardet-Biedl RT syndrome family with two mutant genes (BBS2, BBS10), three mutations, but RT no triallelism."; RL Eur. J. Hum. Genet. 14:1195-1203(2006). RN [5] RP INTERACTION WITH CCDC28B. RX PubMed=16327777; DOI=10.1038/nature04370; RA Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S., RA Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.; RT "Dissection of epistasis in oligogenic Bardet-Biedl syndrome."; RL Nature 439:326-330(2006). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=17574030; DOI=10.1016/j.cell.2007.03.053; RA Nachury M.V., Loktev A.V., Zhang Q., Westlake C.J., Peraenen J., Merdes A., RA Slusarski D.C., Scheller R.H., Bazan J.F., Sheffield V.C., Jackson P.K.; RT "A core complex of BBS proteins cooperates with the GTPase Rab8 to promote RT ciliary membrane biogenesis."; RL Cell 129:1201-1213(2007). RN [7] RP INTERACTION WITH ALDOB. RX PubMed=18000879; DOI=10.1002/cm.20250; RA Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.; RT "Novel interaction partners of Bardet-Biedl syndrome proteins."; RL Cell Motil. Cytoskeleton 65:143-155(2008). RN [8] RP INTERACTION WITH BBS7 AND MKKS. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [9] RP FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME RP COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=22072986; DOI=10.1371/journal.pgen.1002358; RA Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., RA Sheffield V.C.; RT "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and RT Smoothened."; RL PLoS Genet. 7:E1002358-E1002358(2011). RN [10] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). RN [11] RP INVOLVEMENT IN RP74, AND VARIANTS RP74 ASP-33; ALA-104; ARG-134 AND RP PRO-632. RX PubMed=25541840; DOI=10.1001/jamaophthalmol.2014.5251; RA Shevach E., Ali M., Mizrahi-Meissonnier L., McKibbin M., El-Asrag M., RA Watson C.M., Inglehearn C.F., Ben-Yosef T., Blumenfeld A., Jalas C., RA Banin E., Sharon D.; RT "Association between missense mutations in the BBS2 gene and nonsyndromic RT retinitis pigmentosa."; RL JAMA Ophthalmol. 133:312-318(2015). RN [12] RP VARIANTS BBS2 ALA-104; GLN-315; TRP-315; ILE-558 AND PRO-632. RX PubMed=11567139; DOI=10.1126/science.1063525; RA Katsanis N., Ansley S.J., Badano J.L., Eichers E.R., Lewis R.A., RA Hoskins B.E., Scambler P.J., Davidson W.S., Beales P.L., Lupski J.R.; RT "Triallelic inheritance in Bardet-Biedl syndrome, a Mendelian recessive RT disorder."; RL Science 293:2256-2259(2001). RN [13] RP VARIANTS BBS2 GLN-315 AND TRP-349. RX PubMed=12677556; DOI=10.1086/375178; RA Beales P.L., Badano J.L., Ross A.J., Ansley S.J., Hoskins B.E., Kirsten B., RA Mein C.A., Froguel P., Scambler P.J., Lewis R.A., Lupski J.R., Katsanis N.; RT "Genetic interaction of BBS1 mutations with alleles at other BBS loci can RT result in non-Mendelian Bardet-Biedl syndrome."; RL Am. J. Hum. Genet. 72:1187-1199(2003). RN [14] RP VARIANT BBS2 GLU-174. RX PubMed=12872256; DOI=10.1002/humu.10241; RA Hoskins B.E., Thorn A., Scambler P.J., Beales P.L.; RT "Evaluation of multiplex capillary heteroduplex analysis: a rapid and RT sensitive mutation screening technique."; RL Hum. Mutat. 22:151-157(2003). RN [15] RP VARIANT BBS2 HIS-643. RX PubMed=12920096; DOI=10.1136/jmg.40.8.e104; RA Fauser S., Munz M., Besch D.; RT "Further support for digenic inheritance in Bardet-Biedl syndrome."; RL J. Med. Genet. 40:E104-E104(2003). RN [16] RP VARIANT BBS2 PRO-23, AND VARIANT VAL-123. RX PubMed=15666242; DOI=10.1086/428679; RA Karmous-Benailly H., Martinovic J., Gubler M.-C., Sirot Y., Clech L., RA Ozilou C., Auge J., Brahimi N., Etchevers H., Detrait E., Esculpavit C., RA Audollent S., Goudefroye G., Gonzales M., Tantau J., Loget P., Joubert M., RA Gaillard D., Jeanne-Pasquier C., Delezoide A.-L., Peter M.-O., Plessis G., RA Simon-Bouy B., Dollfus H., Le Merrer M., Munnich A., Encha-Razavi F., RA Vekemans M., Attie-Bitach T.; RT "Antenatal presentation of Bardet-Biedl syndrome may mimic Meckel RT syndrome."; RL Am. J. Hum. Genet. 76:493-504(2005). RN [17] RP VARIANT VAL-123. RX PubMed=15770229; DOI=10.1038/sj.ejhg.5201372; RA Hichri H., Stoetzel C., Laurier V., Caron S., Sigaudy S., Sarda P., RA Hamel C., Martin-Coignard D., Gilles M., Leheup B., Holder M., Kaplan J., RA Bitoun P., Lacombe D., Verloes A., Bonneau D., Perrin-Schmitt F., RA Brandt C., Besancon A.-F., Mandel J.-L., Cossee M., Dollfus H.; RT "Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl RT syndrome family cohort."; RL Eur. J. Hum. Genet. 13:607-616(2005). RN [18] RP VARIANT LYS-629. RX PubMed=20120035; DOI=10.1002/humu.21204; RA Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Riise R., RA Sheffield V.C., Rosenberg T., Brondum-Nielsen K.; RT "Bardet-Biedl syndrome in Denmark -- report of 13 novel sequence variations RT in six genes."; RL Hum. Mutat. 31:429-436(2010). RN [19] RP VARIANTS BBS2 CYS-81; ALA-104; ARG-125; PRO-136; TRP-307; CYS-317 AND RP PRO-632. RX PubMed=21344540; DOI=10.1002/humu.21480; RA Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A., RA Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A., RA Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D., RA Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K., Heon E.; RT "BBS genotype-phenotype assessment of a multiethnic patient cohort calls RT for a revision of the disease definition."; RL Hum. Mutat. 32:610-619(2011). CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex CC required for sorting of specific membrane proteins to the primary CC cilia. The BBSome complex is required for ciliogenesis but is CC dispensable for centriolar satellite function. This ciliogenic function CC is mediated in part by the Rab8 GDP/GTP exchange factor, which CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters CC the primary cilium and promotes extension of the ciliary membrane. CC Firstly the BBSome associates with the ciliary membrane and binds to CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the CC Rab8-GTP localizes to the cilium and promotes docking and fusion of CC carrier vesicles to the base of the ciliary membrane. The BBSome CC complex, together with the LTZL1, controls SMO ciliary trafficking and CC contributes to the sonic hedgehog (SHH) pathway regulation. Required CC for proper BBSome complex assembly and its ciliary localization. CC {ECO:0000269|PubMed:17574030, ECO:0000269|PubMed:22072986}. CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (via C-terminus) with BBS7. CC Interacts (via coiled coil domain) with MKKS. Interacts with CCDC28B CC and ALDOB. Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000269|PubMed:16327777, ECO:0000269|PubMed:17574030, CC ECO:0000269|PubMed:18000879, ECO:0000269|PubMed:20080638, CC ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC Q9BXC9; P05062: ALDOB; NbExp=4; IntAct=EBI-748297, EBI-1045507; CC Q9BXC9; Q8NFJ9: BBS1; NbExp=8; IntAct=EBI-748297, EBI-1805484; CC Q9BXC9; Q8IWZ6: BBS7; NbExp=14; IntAct=EBI-748297, EBI-1806001; CC Q9BXC9; Q8IWZ6-2: BBS7; NbExp=6; IntAct=EBI-748297, EBI-20947190; CC Q9BXC9; Q3SYG4: BBS9; NbExp=15; IntAct=EBI-748297, EBI-2826852; CC Q9BXC9; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-748297, EBI-10242151; CC Q9BXC9; P52597: HNRNPF; NbExp=3; IntAct=EBI-748297, EBI-352986; CC Q9BXC9; Q15051: IQCB1; NbExp=8; IntAct=EBI-748297, EBI-2805823; CC Q9BXC9; P61968: LMO4; NbExp=3; IntAct=EBI-748297, EBI-2798728; CC Q9BXC9; Q99750: MDFI; NbExp=7; IntAct=EBI-748297, EBI-724076; CC Q9BXC9; Q9NPJ1: MKKS; NbExp=4; IntAct=EBI-748297, EBI-721319; CC Q9BXC9; Q16656-4: NRF1; NbExp=3; IntAct=EBI-748297, EBI-11742836; CC Q9BXC9; P61289: PSME3; NbExp=7; IntAct=EBI-748297, EBI-355546; CC Q9BXC9; Q93062: RBPMS; NbExp=3; IntAct=EBI-748297, EBI-740322; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane. Cytoplasm. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, CC centriolar satellite. CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DISEASE: Bardet-Biedl syndrome 2 (BBS2) [MIM:615981]: A syndrome CC characterized by usually severe pigmentary retinopathy, early-onset CC obesity, polydactyly, hypogenitalism, renal malformation and CC intellectual disability. Secondary features include diabetes mellitus, CC hypertension and congenital heart disease. Bardet-Biedl syndrome CC inheritance is autosomal recessive, but three mutated alleles (two at CC one locus, and a third at a second locus) may be required for clinical CC manifestation of some forms of the disease. CC {ECO:0000269|PubMed:11285252, ECO:0000269|PubMed:11567139, CC ECO:0000269|PubMed:12677556, ECO:0000269|PubMed:12872256, CC ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15666242, CC ECO:0000269|PubMed:16823392, ECO:0000269|PubMed:21344540}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Retinitis pigmentosa 74 (RP74) [MIM:616562]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. {ECO:0000269|PubMed:25541840}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- WEB RESOURCE: Name=Mutations of the BBS2 gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/bbs2mut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF342736; AAK28552.1; -; mRNA. DR EMBL; AK027635; BAB55252.1; -; mRNA. DR EMBL; BC014140; AAH14140.1; -; mRNA. DR CCDS; CCDS32451.1; -. DR RefSeq; NP_114091.3; NM_031885.3. DR RefSeq; XP_005256137.1; XM_005256080.2. DR AlphaFoldDB; Q9BXC9; -. DR SMR; Q9BXC9; -. DR BioGRID; 107059; 74. DR ComplexPortal; CPX-1908; BBSome complex. DR CORUM; Q9BXC9; -. DR DIP; DIP-46563N; -. DR IntAct; Q9BXC9; 47. DR STRING; 9606.ENSP00000245157; -. DR GlyGen; Q9BXC9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BXC9; -. DR MetOSite; Q9BXC9; -. DR PhosphoSitePlus; Q9BXC9; -. DR BioMuta; BBS2; -. DR DMDM; 20454827; -. DR EPD; Q9BXC9; -. DR jPOST; Q9BXC9; -. DR MassIVE; Q9BXC9; -. DR MaxQB; Q9BXC9; -. DR PaxDb; Q9BXC9; -. DR PeptideAtlas; Q9BXC9; -. DR ProteomicsDB; 79404; -. DR Antibodypedia; 28577; 116 antibodies from 22 providers. DR DNASU; 583; -. DR Ensembl; ENST00000245157.11; ENSP00000245157.5; ENSG00000125124.14. DR Ensembl; ENST00000682047.1; ENSP00000507699.1; ENSG00000125124.14. DR Ensembl; ENST00000682205.1; ENSP00000508377.1; ENSG00000125124.14. DR Ensembl; ENST00000682470.1; ENSP00000507654.1; ENSG00000125124.14. DR Ensembl; ENST00000682855.1; ENSP00000507027.1; ENSG00000125124.14. DR GeneID; 583; -. DR KEGG; hsa:583; -. DR MANE-Select; ENST00000245157.11; ENSP00000245157.5; NM_031885.5; NP_114091.4. DR UCSC; uc002ejd.3; human. DR CTD; 583; -. DR DisGeNET; 583; -. DR GeneCards; BBS2; -. DR GeneReviews; BBS2; -. DR HGNC; HGNC:967; BBS2. DR HPA; ENSG00000125124; Low tissue specificity. DR MalaCards; BBS2; -. DR MIM; 606151; gene. DR MIM; 615981; phenotype. DR MIM; 616562; phenotype. DR neXtProt; NX_Q9BXC9; -. DR OpenTargets; ENSG00000125124; -. DR Orphanet; 110; Bardet-Biedl syndrome. DR Orphanet; 791; Retinitis pigmentosa. DR PharmGKB; PA25276; -. DR VEuPathDB; HostDB:ENSG00000125124; -. DR eggNOG; ENOG502QPWU; Eukaryota. DR GeneTree; ENSGT00390000017113; -. DR InParanoid; Q9BXC9; -. DR OrthoDB; 327831at2759; -. DR PhylomeDB; Q9BXC9; -. DR TreeFam; TF313236; -. DR PathwayCommons; Q9BXC9; -. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR SignaLink; Q9BXC9; -. DR SIGNOR; Q9BXC9; -. DR BioGRID-ORCS; 583; 13 hits in 1076 CRISPR screens. DR ChiTaRS; BBS2; human. DR GeneWiki; BBS2; -. DR GenomeRNAi; 583; -. DR Pharos; Q9BXC9; Tbio. DR PRO; PR:Q9BXC9; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9BXC9; protein. DR Bgee; ENSG00000125124; Expressed in adrenal tissue and 177 other tissues. DR ExpressionAtlas; Q9BXC9; baseline and differential. DR Genevisible; Q9BXC9; HS. DR GO; GO:0034464; C:BBSome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL. DR GO; GO:0060170; C:ciliary membrane; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0032420; C:stereocilium; IEA:Ensembl. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0030534; P:adult behavior; ISS:BHF-UCL. DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl. DR GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL. DR GO; GO:0060271; P:cilium assembly; ISS:BHF-UCL. DR GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI. DR GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL. DR GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL. DR GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:BHF-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISS:BHF-UCL. DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:BHF-UCL. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; ISS:BHF-UCL. DR GO; GO:0033365; P:protein localization to organelle; ISS:BHF-UCL. DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISS:BHF-UCL. DR GO; GO:0007288; P:sperm axoneme assembly; ISS:BHF-UCL. DR GO; GO:0021756; P:striatum development; ISS:BHF-UCL. DR GO; GO:0042311; P:vasodilation; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IMP:UniProtKB. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR016616; Bardet-Biedl_syndrome_2_prot. DR InterPro; IPR029333; BBS2_C. DR InterPro; IPR029429; BBS2_Mid. DR InterPro; IPR029430; BBS2_N. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR PANTHER; PTHR32465; BARDET-BIEDL SYNDROME 2 PROTEIN; 1. DR Pfam; PF14782; BBS2_C; 1. DR Pfam; PF14783; BBS2_Mid; 1. DR Pfam; PF14781; BBS2_N; 1. DR PIRSF; PIRSF013684; BBS2; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR AGR; HGNC:967; -. PE 1: Evidence at protein level; KW Bardet-Biedl syndrome; Cell membrane; Cell projection; Ciliopathy; Cilium; KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton; KW Disease variant; Intellectual disability; Membrane; Obesity; KW Protein transport; Reference proteome; Retinitis pigmentosa; KW Sensory transduction; Transport; Vision. FT CHAIN 1..721 FT /note="Bardet-Biedl syndrome 2 protein" FT /id="PRO_0000064843" FT COILED 325..369 FT /evidence="ECO:0000255" FT VARIANT 23 FT /note="R -> P (in BBS2)" FT /evidence="ECO:0000269|PubMed:15666242" FT /id="VAR_038889" FT VARIANT 33 FT /note="A -> D (in RP74; dbSNP:rs797045155)" FT /evidence="ECO:0000269|PubMed:25541840" FT /id="VAR_075726" FT VARIANT 70 FT /note="S -> N (in dbSNP:rs4784677)" FT /evidence="ECO:0000269|PubMed:11285252, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334" FT /id="VAR_013162" FT VARIANT 75 FT /note="V -> G (in BBS2; in linkage disequilibrium with FT V-123 in a Bedouin kindred; dbSNP:rs121908174)" FT /evidence="ECO:0000269|PubMed:11285252" FT /id="VAR_013163" FT VARIANT 81 FT /note="G -> C (in BBS2; dbSNP:rs750506474)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066280" FT VARIANT 104 FT /note="D -> A (in BBS2 and RP74; dbSNP:rs121908179)" FT /evidence="ECO:0000269|PubMed:11567139, FT ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:25541840" FT /id="VAR_013164" FT VARIANT 122 FT /note="A -> V (in dbSNP:rs17856449)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_029747" FT VARIANT 123 FT /note="I -> V (in dbSNP:rs11373)" FT /evidence="ECO:0000269|PubMed:11285252, FT ECO:0000269|PubMed:15666242, ECO:0000269|PubMed:15770229" FT /id="VAR_013165" FT VARIANT 125 FT /note="L -> R (in BBS2)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066281" FT VARIANT 134 FT /note="P -> R (in RP74; dbSNP:rs376306240)" FT /evidence="ECO:0000269|PubMed:25541840" FT /id="VAR_075727" FT VARIANT 136 FT /note="A -> P (in BBS2)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066282" FT VARIANT 139 FT /note="G -> V (in BBS2; dbSNP:rs121908181)" FT /evidence="ECO:0000269|PubMed:16823392" FT /id="VAR_075728" FT VARIANT 174 FT /note="D -> E (in BBS2; dbSNP:rs767373822)" FT /evidence="ECO:0000269|PubMed:12872256" FT /id="VAR_038890" FT VARIANT 307 FT /note="C -> W (in BBS2)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066283" FT VARIANT 315 FT /note="R -> Q (in BBS2; dbSNP:rs544773389)" FT /evidence="ECO:0000269|PubMed:11567139, FT ECO:0000269|PubMed:12677556" FT /id="VAR_013166" FT VARIANT 315 FT /note="R -> W (in BBS2; dbSNP:rs121908178)" FT /evidence="ECO:0000269|PubMed:11567139" FT /id="VAR_013167" FT VARIANT 317 FT /note="Y -> C (in BBS2; dbSNP:rs1597016660)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066284" FT VARIANT 349 FT /note="L -> W (in BBS2; has a modifier effect on BBS; FT dbSNP:rs752280639)" FT /evidence="ECO:0000269|PubMed:12677556" FT /id="VAR_038891" FT VARIANT 504 FT /note="A -> V (in dbSNP:rs16957538)" FT /id="VAR_029748" FT VARIANT 558 FT /note="T -> I (in BBS2; dbSNP:rs370581600)" FT /evidence="ECO:0000269|PubMed:11567139" FT /id="VAR_013168" FT VARIANT 629 FT /note="E -> K (in a patient with Bardet-Biedl syndrome FT compound heterozygote for mutations in BBS10; uncertain FT pathological role; dbSNP:rs746505864)" FT /evidence="ECO:0000269|PubMed:20120035" FT /id="VAR_066285" FT VARIANT 632 FT /note="R -> P (in BBS2 and RP74; dbSNP:rs138043021)" FT /evidence="ECO:0000269|PubMed:11567139, FT ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:25541840" FT /id="VAR_013169" FT VARIANT 643 FT /note="R -> H (in BBS2; dbSNP:rs532361142)" FT /evidence="ECO:0000269|PubMed:12920096" FT /id="VAR_038892" FT CONFLICT 63 FT /note="E -> G (in Ref. 2; BAB55252)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="C -> R (in Ref. 2; BAB55252)" FT /evidence="ECO:0000305" FT CONFLICT 457 FT /note="L -> S (in Ref. 2; BAB55252)" FT /evidence="ECO:0000305" FT CONFLICT 648 FT /note="Y -> H (in Ref. 2; BAB55252)" FT /evidence="ECO:0000305" SQ SEQUENCE 721 AA; 79844 MW; EF97CAA28709A089 CRC64; MLLPVFTLKL RHKISPRMVA IGRYDGTHPC LAAATQTGKV FIHNPHTRNQ HVSASRVFQS PLESDVSLLS INQAVSCLTA GVLNPELGYD ALLVGTQTNL LAYDVYNNSD LFYREVADGA NAIVLGTLGD ISSPLAIIGG NCALQGFNHE GSDLFWTVTG DNVNSLALCD FDGDGKKELL VGSEDFDIRV FKEDEIVAEM TETEIVTSLC PMYGSRFGYA LSNGTVGVYD KTSRYWRIKS KNHAMSIHAF DLNSDGVNEL ITGWSNGKVD ARSDRTGEVI FKDNFSSAIA GVVEGDYRMD GHIQLICCSV DGEIRGYLPG TAEMRGNLMD TSAEQDLIRE LSQKKQNLLL ELRNYEENAK AELASPLNEA DGHRGIIPAN TRLHTTLSVS LGNETQTAHT ELRISTSNDT IIRAVLIFAE GIFTGESHVV HPSIHNLSSS ICIPIVPPKD VPVDLHLKAF VGYRSSTQFH VFESTRQLPR FSMYALTSLD PASEPISYVN FTIAERAQRV VVWLGQNFLL PEDTHIQNAP FQVCFTSLRN GGHLHIKIKL SGEITINTDD IDLAGDIIQS MASFFAIEDL QVEADFPVYF EELRKVLVKV DEYHSVHQKL SADMADHSNL IRSLLVGAED ARLMRDMKTM KSRYMELYDL NRDLLNGYKI RCNNHTELLG NLKAVNQAIQ RAGRLRVGKP KNQVITACRD AIRSNNINTL FKIMRVGTAS S // ID MKKS_HUMAN Reviewed; 570 AA. AC Q9NPJ1; A8K7B0; D3DW18; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-DEC-2022, entry version 193. DE RecName: Full=Molecular chaperone MKKS {ECO:0000305}; DE AltName: Full=Bardet-Biedl syndrome 6 protein; DE AltName: Full=McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin; GN Name=MKKS {ECO:0000312|HGNC:HGNC:7108}; GN Synonyms=BBS6 {ECO:0000303|PubMed:28753627}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MKKS CYS-37; TYR-84 AND SER-242, AND RP VARIANTS VAL-49 AND CYS-517. RX PubMed=10802661; DOI=10.1038/75637; RA Stone D.L., Slavotinek A.M., Bouffard G.G., Banerjee-Basu S., RA Baxevanis A.D., Barr M., Biesecker L.G.; RT "Mutation of a gene encoding a putative chaperonin causes McKusick-Kaufman RT syndrome."; RL Nat. Genet. 25:79-82(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS BBS6 ASP-52; LEU-155; RP ALA-286; GLU-345 AND SER-499, AND CHARACTERIZATION OF VARIANT PRO-325. RX PubMed=15731008; DOI=10.1242/jcs.01676; RA Kim J.C., Ou Y.Y., Badano J.L., Esmail M.A., Leitch C.C., Fiedrich E., RA Beales P.L., Archibald J.M., Katsanis N., Rattner J.B., Leroux M.R.; RT "MKKS/BBS6, a divergent chaperonin-like protein linked to the obesity RT disorder Bardet-Biedl syndrome, is a novel centrosomal component required RT for cytokinesis."; RL J. Cell Sci. 118:1007-1020(2005). RN [7] RP INTERACTION WITH CCDC28B. RX PubMed=16327777; DOI=10.1038/nature04370; RA Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S., RA Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.; RT "Dissection of epistasis in oligogenic Bardet-Biedl syndrome."; RL Nature 439:326-330(2006). RN [8] RP SUBCELLULAR LOCATION, INTERACTION WITH STUB1, AND CHARACTERIZATION OF RP VARIANTS BBS6 CYS-37; ALA-57; SER-242; GLU-345 AND SER-499. RX PubMed=18094050; DOI=10.1091/mbc.e07-07-0631; RA Hirayama S., Yamazaki Y., Kitamura A., Oda Y., Morito D., Okawa K., RA Kimura H., Cyr D.M., Kubota H., Nagata K.; RT "MKKS is a centrosome-shuttling protein degraded by disease-causing RT mutations via CHIP-mediated ubiquitination."; RL Mol. Biol. Cell 19:899-911(2008). RN [9] RP FUNCTION, IDENTIFICATION IN A MULTIPROTEIN COMPLEX, INTERACTION WITH BBS2, RP AND CHARACTERIZATION OF VARIANTS BBS6 CYS-37; ASP-52; ALA-57; TYR-84; RP PRO-236 AND PRO-277. RX PubMed=20080638; DOI=10.1073/pnas.0910268107; RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., RA Sheffield V.C.; RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and RT mediate BBSome assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010). RN [10] RP INTERACTION WITH BBS12, VARIANT BBS6 ARG-395, AND CHARACTERIZATION OF RP VARIANT BBS6 ARG-395. RX PubMed=26900326; RA Hulleman J.D., Nguyen A., Ramprasad V.L., Murugan S., Gupta R., RA Mahindrakar A., Angara R., Sankurathri C., Mootha V.V.; RT "A novel H395R mutation in MKKS/BBS6 causes retinitis pigmentosa and RT polydactyly without other findings of Bardet-Biedl or McKusick-Kaufman RT syndrome."; RL Mol. Vis. 22:73-81(2016). RN [11] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). RN [12] RP VARIANT BBS6 ASP-52. RX PubMed=10973238; DOI=10.1038/79116; RA Slavotinek A.M., Stone E.M., Mykytyn K., Heckenlively J.R., Green J.S., RA Heon E., Musarella M.A., Parfrey P.S., Sheffield V.C., Biesecker L.G.; RT "Mutations in MKKS cause Bardet-Biedl syndrome."; RL Nat. Genet. 26:15-16(2000). RN [13] RP VARIANTS BBS6 CYS-37; ALA-57 AND PRO-277. RC TISSUE=Peripheral blood lymphocyte; RX PubMed=10973251; DOI=10.1038/79201; RA Katsanis N., Beales P.L., Woods M.O., Lewis R.A., Green J.S., Parfrey P.S., RA Ansley S.J., Davidson W.S., Lupski J.R.; RT "Mutations in MKKS cause obesity, retinal dystrophy and renal malformations RT associated with Bardet-Biedl syndrome."; RL Nat. Genet. 26:67-70(2000). RN [14] RP VARIANTS BBS6 MET-32; ALA-57; PRO-236; ALA-286; SER-499; ALA-511 AND RP HIS-518, AND VARIANT SER-242. RX PubMed=11179009; DOI=10.1086/318794; RA Beales P.L., Katsanis N., Lewis R.A., Ansley S.J., Elcioglu N., Raza J., RA Woods M.O., Green J.S., Parfrey P.S., Davidson W.S., Lupski J.R.; RT "Genetic and mutational analyses of a large multiethnic Bardet-Biedl cohort RT reveal a minor involvement of BBS6 and delineate the critical intervals of RT other loci."; RL Am. J. Hum. Genet. 68:606-616(2001). RN [15] RP VARIANTS BBS6 CYS-37; SER-242 AND SER-499. RX PubMed=11567139; DOI=10.1126/science.1063525; RA Katsanis N., Ansley S.J., Badano J.L., Eichers E.R., Lewis R.A., RA Hoskins B.E., Scambler P.J., Davidson W.S., Beales P.L., Lupski J.R.; RT "Triallelic inheritance in Bardet-Biedl syndrome, a Mendelian recessive RT disorder."; RL Science 293:2256-2259(2001). RN [16] RP VARIANTS BBS6 LEU-155; SER-242 AND GLU-345, AND VARIANT VAL-339. RX PubMed=12107442; DOI=10.1007/s00439-002-0733-3; RA Slavotinek A.M., Searby C., Al-Gazali L., Hennekam R.C.M., RA Schrander-Stumpel C., Orcana-Losa M., Pardo-Reoyo S., Cantani A., Kumar D., RA Capellini Q., Neri G., Zackai E., Biesecker L.G.; RT "Mutation analysis of the MKKS gene in McKusick-Kaufman syndrome and RT selected Bardet-Biedl syndrome patients."; RL Hum. Genet. 110:561-567(2002). RN [17] RP VARIANT BBS6 PRO-236, AND VARIANT PRO-325. RX PubMed=12677556; DOI=10.1086/375178; RA Beales P.L., Badano J.L., Ross A.J., Ansley S.J., Hoskins B.E., Kirsten B., RA Mein C.A., Froguel P., Scambler P.J., Lewis R.A., Lupski J.R., Katsanis N.; RT "Genetic interaction of BBS1 mutations with alleles at other BBS loci can RT result in non-Mendelian Bardet-Biedl syndrome."; RL Am. J. Hum. Genet. 72:1187-1199(2003). RN [18] RP VARIANT PRO-325, AND CHARACTERIZATION OF VARIANT PRO-325. RX PubMed=12837689; DOI=10.1093/hmg/ddg188; RA Badano J.L., Kim J.C., Hoskins B.E., Lewis R.A., Ansley S.J., Cutler D.J., RA Castellan C., Beales P.L., Leroux M.R., Katsanis N.; RT "Heterozygous mutations in BBS1, BBS2 and BBS6 have a potential epistatic RT effect on Bardet-Biedl patients with two mutations at a second BBS locus."; RL Hum. Mol. Genet. 12:1651-1659(2003). RN [19] RP VARIANTS BBS6 PRO-181 AND ASN-492. RX PubMed=12920096; DOI=10.1136/jmg.40.8.e104; RA Fauser S., Munz M., Besch D.; RT "Further support for digenic inheritance in Bardet-Biedl syndrome."; RL J. Med. Genet. 40:E104-E104(2003). RN [20] RP VARIANTS BBS6 PRO-237 AND PRO-460, AND VARIANTS VAL-339; CYS-517 AND RP VAL-532. RX PubMed=15666242; DOI=10.1086/428679; RA Karmous-Benailly H., Martinovic J., Gubler M.-C., Sirot Y., Clech L., RA Ozilou C., Auge J., Brahimi N., Etchevers H., Detrait E., Esculpavit C., RA Audollent S., Goudefroye G., Gonzales M., Tantau J., Loget P., Joubert M., RA Gaillard D., Jeanne-Pasquier C., Delezoide A.-L., Peter M.-O., Plessis G., RA Simon-Bouy B., Dollfus H., Le Merrer M., Munnich A., Encha-Razavi F., RA Vekemans M., Attie-Bitach T.; RT "Antenatal presentation of Bardet-Biedl syndrome may mimic Meckel RT syndrome."; RL Am. J. Hum. Genet. 76:493-504(2005). RN [21] RP VARIANTS BBS6 ALA-237 AND PRO-237, AND VARIANTS VAL-339; CYS-517 AND RP VAL-532. RX PubMed=15770229; DOI=10.1038/sj.ejhg.5201372; RA Hichri H., Stoetzel C., Laurier V., Caron S., Sigaudy S., Sarda P., RA Hamel C., Martin-Coignard D., Gilles M., Leheup B., Holder M., Kaplan J., RA Bitoun P., Lacombe D., Verloes A., Bonneau D., Perrin-Schmitt F., RA Brandt C., Besancon A.-F., Mandel J.-L., Cossee M., Dollfus H.; RT "Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl RT syndrome family cohort."; RL Eur. J. Hum. Genet. 13:607-616(2005). RN [22] RP VARIANTS SER-242; CYS-517 AND VAL-532. RX PubMed=15483080; DOI=10.1210/jc.2004-0465; RA Andersen K.L., Echwald S.M., Larsen L.H., Hamid Y.H., Glumer C., RA Jorgensen T., Borch-Johnsen K., Andersen T., Sorensen T.I., Hansen T., RA Pedersen O.; RT "Variation of the McKusick-Kaufman gene and studies of relationships with RT common forms of obesity."; RL J. Clin. Endocrinol. Metab. 90:225-230(2005). RN [23] RP VARIANT SER-242, AND DISCUSSION OF THE PATHOLOGICAL ROLE OF VARIANT RP SER-242. RX PubMed=20120035; DOI=10.1002/humu.21204; RA Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Riise R., RA Sheffield V.C., Rosenberg T., Brondum-Nielsen K.; RT "Bardet-Biedl syndrome in Denmark -- report of 13 novel sequence variations RT in six genes."; RL Hum. Mutat. 31:429-436(2010). RN [24] RP VARIANTS BBS6 ARG-41; ARG-99 AND LEU-299, AND VARIANT THR-488. RX PubMed=21344540; DOI=10.1002/humu.21480; RA Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A., RA Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A., RA Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D., RA Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K., Heon E.; RT "BBS genotype-phenotype assessment of a multiethnic patient cohort calls RT for a revision of the disease definition."; RL Hum. Mutat. 32:610-619(2011). RN [25] RP VARIANT BBS6 ALA-57. RX PubMed=22152675; DOI=10.1016/j.ajhg.2011.11.005; RA Huang L., Szymanska K., Jensen V.L., Janecke A.R., Innes A.M., Davis E.E., RA Frosk P., Li C., Willer J.R., Chodirker B.N., Greenberg C.R., McLeod D.R., RA Bernier F.P., Chudley A.E., Muller T., Shboul M., Logan C.V., Loucks C.M., RA Beaulieu C.L., Bowie R.V., Bell S.M., Adkins J., Zuniga F.I., Ross K.D., RA Wang J., Ban M.R., Becker C., Nurnberg P., Douglas S., Craft C.M., RA Akimenko M.A., Hegele R.A., Ober C., Utermann G., Bolz H.J., Bulman D.E., RA Katsanis N., Blacque O.E., Doherty D., Parboosingh J.S., Leroux M.R., RA Johnson C.A., Boycott K.M.; RT "TMEM237 is mutated in individuals with a Joubert syndrome related disorder RT and expands the role of the TMEM family at the ciliary transition zone."; RL Am. J. Hum. Genet. 89:713-730(2011). RN [26] RP VARIANT BBS6 40-SER--ASN-570 DEL. RX PubMed=28761321; RA Ullah A., Umair M., Yousaf M., Khan S.A., Nazim-Ud-Din M., Shah K., RA Ahmad F., Azeem Z., Ali G., Alhaddad B., Rafique A., Jan A., Haack T.B., RA Strom T.M., Meitinger T., Ghous T., Ahmad W.; RT "Sequence variants in four genes underlying Bardet-Biedl syndrome in RT consanguineous families."; RL Mol. Vis. 23:482-494(2017). RN [27] RP CHARACTERIZATION OF VARIANTS MKKS CYS-37; TYR-84 AND SER-242, SUBCELLULAR RP LOCATION, FUNCTION, MUTAGENESIS OF LEU-454, CHARACTERIZATION OF VARIANT RP BBS6 CYS-37, AND INTERACTION WITH SMARCC1. RX PubMed=28753627; DOI=10.1371/journal.pgen.1006936; RA Scott C.A., Marsden A.N., Rebagliati M.R., Zhang Q., Chamling X., RA Searby C.C., Baye L.M., Sheffield V.C., Slusarski D.C.; RT "Nuclear/cytoplasmic transport defects in BBS6 underlie congenital heart RT disease through perturbation of a chromatin remodeling protein."; RL PLoS Genet. 13:E1006936-E1006936(2017). CC -!- FUNCTION: Probable molecular chaperone that assists the folding of CC proteins upon ATP hydrolysis (PubMed:20080638). Plays a role in the CC assembly of BBSome, a complex involved in ciliogenesis regulating CC transports vesicles to the cilia (PubMed:20080638). May play a role in CC protein processing in limb, cardiac and reproductive system CC development. May play a role in cytokinesis (PubMed:28753627). CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:28753627}. CC -!- SUBUNIT: Component of a complex composed at least of MKKS, BBS10, CC BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 and CCT8 (PubMed:20080638). CC Interacts with STUB1 (PubMed:18094050). Interacts with BBS2 (via coiled CC coil domain) (PubMed:20080638). Interacts with CCDC28B CC (PubMed:16327777). Interacts with BBS12 (PubMed:26900326). Interacts CC with SMARCC1, a component of the SWI/SNF complexes; the interaction CC takes place predominantly in the cytoplasm and may modulate SMARCC1 CC location (PubMed:28753627). Interacts with DLEC1 (PubMed:33144677). CC {ECO:0000269|PubMed:16327777, ECO:0000269|PubMed:18094050, CC ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:26900326, CC ECO:0000269|PubMed:28753627, ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC Q9NPJ1; Q6ZW61: BBS12; NbExp=14; IntAct=EBI-721319, EBI-6128352; CC Q9NPJ1; Q9BXC9: BBS2; NbExp=4; IntAct=EBI-721319, EBI-748297; CC Q9NPJ1; Q01850: CDR2; NbExp=3; IntAct=EBI-721319, EBI-1181367; CC Q9NPJ1; O96006: ZBED1; NbExp=3; IntAct=EBI-721319, EBI-740037; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome. Cytoplasm, cytosol {ECO:0000269|PubMed:28753627}. CC Nucleus {ECO:0000269|PubMed:28753627}. Note=The majority of the protein CC resides within the pericentriolar material (PCM), a proteinaceous tube CC surrounding centrioles. During interphase, the protein is confined to CC the lateral surfaces of the PCM but during mitosis it relocalizes CC throughout the PCM and is found at the intercellular bridge. The MKSS CC protein is highly mobile and rapidly shuttles between the cytosol and CC centrosome. CC -!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues. CC -!- DOMAIN: The substrate-binding apical domain region is sufficient for CC centrosomal association. CC -!- DISEASE: McKusick-Kaufman syndrome (MKKS) [MIM:236700]: Autosomal CC recessive developmental disorder. It is characterized by CC hydrometrocolpos, postaxial polydactyly and congenital heart defects. CC {ECO:0000269|PubMed:10802661, ECO:0000269|PubMed:28753627}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Bardet-Biedl syndrome 6 (BBS6) [MIM:605231]: A syndrome CC characterized by usually severe pigmentary retinopathy, early-onset CC obesity, polydactyly, hypogenitalism, renal malformation and CC intellectual disability. Secondary features include diabetes mellitus, CC hypertension and congenital heart disease. Bardet-Biedl syndrome CC inheritance is autosomal recessive, but three mutated alleles (two at CC one locus, and a third at a second locus) may be required for clinical CC manifestation of some forms of the disease. CC {ECO:0000269|PubMed:10973238, ECO:0000269|PubMed:10973251, CC ECO:0000269|PubMed:11179009, ECO:0000269|PubMed:11567139, CC ECO:0000269|PubMed:12107442, ECO:0000269|PubMed:12677556, CC ECO:0000269|PubMed:12920096, ECO:0000269|PubMed:15666242, CC ECO:0000269|PubMed:15731008, ECO:0000269|PubMed:15770229, CC ECO:0000269|PubMed:18094050, ECO:0000269|PubMed:20080638, CC ECO:0000269|PubMed:21344540, ECO:0000269|PubMed:22152675, CC ECO:0000269|PubMed:26900326, ECO:0000269|PubMed:28753627, CC ECO:0000269|PubMed:28761321}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Mutations of the MKKS gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/mkksmut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF221992; AAF73872.1; -; mRNA. DR EMBL; AF221993; AAF73873.1; -; mRNA. DR EMBL; AK291925; BAF84614.1; -; mRNA. DR EMBL; AL157427; CAB75652.1; -; mRNA. DR EMBL; AL034430; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10344.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10345.1; -; Genomic_DNA. DR CCDS; CCDS13111.1; -. DR PIR; T46911; T46911. DR RefSeq; NP_061336.1; NM_018848.3. DR RefSeq; NP_740754.1; NM_170784.2. DR AlphaFoldDB; Q9NPJ1; -. DR SMR; Q9NPJ1; -. DR BioGRID; 113837; 15. DR CORUM; Q9NPJ1; -. DR DIP; DIP-60349N; -. DR IntAct; Q9NPJ1; 11. DR STRING; 9606.ENSP00000246062; -. DR iPTMnet; Q9NPJ1; -. DR PhosphoSitePlus; Q9NPJ1; -. DR BioMuta; MKKS; -. DR DMDM; 11133565; -. DR EPD; Q9NPJ1; -. DR MassIVE; Q9NPJ1; -. DR PaxDb; Q9NPJ1; -. DR PeptideAtlas; Q9NPJ1; -. DR ProteomicsDB; 82024; -. DR Antibodypedia; 24160; 148 antibodies from 23 providers. DR DNASU; 8195; -. DR Ensembl; ENST00000347364.7; ENSP00000246062.4; ENSG00000125863.20. DR Ensembl; ENST00000399054.6; ENSP00000382008.2; ENSG00000125863.20. DR Ensembl; ENST00000651692.1; ENSP00000498849.1; ENSG00000125863.20. DR GeneID; 8195; -. DR KEGG; hsa:8195; -. DR MANE-Select; ENST00000347364.7; ENSP00000246062.4; NM_170784.3; NP_740754.1. DR UCSC; uc002wnt.3; human. DR CTD; 8195; -. DR DisGeNET; 8195; -. DR GeneCards; MKKS; -. DR GeneReviews; MKKS; -. DR HGNC; HGNC:7108; MKKS. DR HPA; ENSG00000125863; Low tissue specificity. DR MalaCards; MKKS; -. DR MIM; 236700; phenotype. DR MIM; 604896; gene. DR MIM; 605231; phenotype. DR neXtProt; NX_Q9NPJ1; -. DR OpenTargets; ENSG00000125863; -. DR Orphanet; 110; Bardet-Biedl syndrome. DR Orphanet; 2473; McKusick-Kaufman syndrome. DR PharmGKB; PA30826; -. DR VEuPathDB; HostDB:ENSG00000125863; -. DR eggNOG; KOG0360; Eukaryota. DR GeneTree; ENSGT00390000007214; -. DR HOGENOM; CLU_478131_0_0_1; -. DR InParanoid; Q9NPJ1; -. DR OMA; FVCQKVI; -. DR OrthoDB; 1539473at2759; -. DR PhylomeDB; Q9NPJ1; -. DR TreeFam; TF329106; -. DR PathwayCommons; Q9NPJ1; -. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR SignaLink; Q9NPJ1; -. DR BioGRID-ORCS; 8195; 12 hits in 1078 CRISPR screens. DR ChiTaRS; MKKS; human. DR GeneWiki; MKKS; -. DR GenomeRNAi; 8195; -. DR Pharos; Q9NPJ1; Tbio. DR PRO; PR:Q9NPJ1; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9NPJ1; protein. DR Bgee; ENSG00000125863; Expressed in middle temporal gyrus and 188 other tissues. DR Genevisible; Q9NPJ1; HS. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:1902636; C:kinociliary basal body; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; ISS:BHF-UCL. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc. DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl. DR GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central. DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB. DR GO; GO:0060027; P:convergent extension involved in gastrulation; ISS:BHF-UCL. DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:BHF-UCL. DR GO; GO:0007368; P:determination of left/right symmetry; ISS:BHF-UCL. DR GO; GO:0032502; P:developmental process; IBA:GO_Central. DR GO; GO:0060324; P:face development; IEA:Ensembl. DR GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0008406; P:gonad development; TAS:ProtInc. DR GO; GO:0007507; P:heart development; TAS:ProtInc. DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL. DR GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL. DR GO; GO:0046907; P:intracellular transport; ISS:BHF-UCL. DR GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL. DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl. DR GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:BHF-UCL. DR GO; GO:0045776; P:negative regulation of blood pressure; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl. DR GO; GO:1905515; P:non-motile cilium assembly; IEA:Ensembl. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:BHF-UCL. DR GO; GO:0051877; P:pigment granule aggregation in cell center; ISS:BHF-UCL. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0006457; P:protein folding; TAS:ProtInc. DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISS:BHF-UCL. DR GO; GO:0051492; P:regulation of stress fiber assembly; IEA:Ensembl. DR GO; GO:0007608; P:sensory perception of smell; ISS:BHF-UCL. DR GO; GO:0035176; P:social behavior; ISS:BHF-UCL. DR GO; GO:0007286; P:spermatid development; ISS:BHF-UCL. DR GO; GO:0021756; P:striatum development; ISS:BHF-UCL. DR GO; GO:0042311; P:vasodilation; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 1.10.560.10; -; 1. DR Gene3D; 3.30.260.10; -; 1. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR002423; Cpn60/GroEL/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom_sf. DR InterPro; IPR027413; GROEL-like_equatorial_sf. DR InterPro; IPR028790; MKKS. DR InterPro; IPR027410; TCP-1-like_intermed_sf. DR PANTHER; PTHR46787; SYNDROMES PUTATIVE CHAPERONIN-RELATED; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR SUPFAM; SSF52029; GroEL apical domain-like; 1. DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1. DR AGR; HGNC:7108; -. PE 1: Evidence at protein level; KW ATP-binding; Bardet-Biedl syndrome; Chaperone; Ciliopathy; Cytoplasm; KW Cytoskeleton; Disease variant; Intellectual disability; Nucleotide-binding; KW Nucleus; Obesity; Reference proteome; Sensory transduction; Vision. FT CHAIN 1..570 FT /note="Molecular chaperone MKKS" FT /id="PRO_0000128415" FT REGION 198..370 FT /note="Substrate-binding apical domain" FT BINDING 192..199 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT VARIANT 32 FT /note="I -> M (in BBS6)" FT /evidence="ECO:0000269|PubMed:11179009" FT /id="VAR_017035" FT VARIANT 37 FT /note="Y -> C (in MKKS and BBS6; causes both increased MKKS FT protein degradation and reduced solubility relative to FT wild-type and Tyr-84 mutant; the mutant is immobilized at FT the centrosome even in the absence of proteasome FT inhibition; the mutant is also highly polyubiquitinated; no FT effect on import to the nucleus; dbSNP:rs74315396)" FT /evidence="ECO:0000269|PubMed:10802661, FT ECO:0000269|PubMed:10973251, ECO:0000269|PubMed:11567139, FT ECO:0000269|PubMed:18094050, ECO:0000269|PubMed:20080638, FT ECO:0000269|PubMed:28753627" FT /id="VAR_009864" FT VARIANT 40..570 FT /note="Missing (in BBS6)" FT /evidence="ECO:0000269|PubMed:28761321" FT /id="VAR_080223" FT VARIANT 41 FT /note="G -> R (in BBS6; dbSNP:rs766132697)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066262" FT VARIANT 49 FT /note="G -> V (in dbSNP:rs528833454)" FT /evidence="ECO:0000269|PubMed:10802661" FT /id="VAR_009865" FT VARIANT 52 FT /note="G -> D (in BBS6; fails to associate with centrosome; FT dbSNP:rs28937875)" FT /evidence="ECO:0000269|PubMed:10973238, FT ECO:0000269|PubMed:15731008, ECO:0000269|PubMed:20080638" FT /id="VAR_009882" FT VARIANT 57 FT /note="T -> A (in BBS6; found in a patient also carrying FT A-155 in TMEM237; causes both increased MKKS protein FT degradation and reduced solubility relative to wild-type FT and Y-84 mutant; greatly reduces the ability to interact FT with BBS12; dbSNP:rs74315399)" FT /evidence="ECO:0000269|PubMed:10973251, FT ECO:0000269|PubMed:11179009, ECO:0000269|PubMed:18094050, FT ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:22152675" FT /id="VAR_009883" FT VARIANT 84 FT /note="H -> Y (in MKKS; associated with S-242; decreased FT interaction with BBS12; no effect on ciliogenesis; disrupts FT import to the nucleus; no effect on interaction with FT SMARCC1; may affect modulation of SMARCC1 subcellular FT location; dbSNP:rs281797258)" FT /evidence="ECO:0000269|PubMed:10802661, FT ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:28753627" FT /id="VAR_009866" FT VARIANT 99 FT /note="C -> R (in BBS6; dbSNP:rs1297985227)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066263" FT VARIANT 155 FT /note="R -> L (in BBS6; increases MKKS protein degradation; FT localizes properly to the centrosome; dbSNP:rs138111422)" FT /evidence="ECO:0000269|PubMed:12107442, FT ECO:0000269|PubMed:15731008" FT /id="VAR_017040" FT VARIANT 181 FT /note="A -> P (in BBS6)" FT /evidence="ECO:0000269|PubMed:12920096" FT /id="VAR_038898" FT VARIANT 236 FT /note="S -> P (in BBS6)" FT /evidence="ECO:0000269|PubMed:11179009, FT ECO:0000269|PubMed:12677556, ECO:0000269|PubMed:20080638" FT /id="VAR_017036" FT VARIANT 237 FT /note="T -> A (in BBS6; dbSNP:rs760185677)" FT /evidence="ECO:0000269|PubMed:15770229" FT /id="VAR_038899" FT VARIANT 237 FT /note="T -> P (in BBS6)" FT /evidence="ECO:0000269|PubMed:15666242, FT ECO:0000269|PubMed:15770229" FT /id="VAR_038900" FT VARIANT 242 FT /note="A -> S (in MKKS and BBS6; associated with Y-84 in FT MKKS; unknown pathological significance; increases MKKS FT protein degradation; no effect on ciliogenesis; disrupts FT import to the nucleus; no effect on interaction with FT SMARCC1; may affect modulation of SMARCC1 subcellular FT location; dbSNP:rs74315394)" FT /evidence="ECO:0000269|PubMed:10802661, FT ECO:0000269|PubMed:11179009, ECO:0000269|PubMed:11567139, FT ECO:0000269|PubMed:12107442, ECO:0000269|PubMed:15483080, FT ECO:0000269|PubMed:18094050, ECO:0000269|PubMed:20120035, FT ECO:0000269|PubMed:28753627" FT /id="VAR_009867" FT VARIANT 277 FT /note="L -> P (in BBS6; moderately affects interaction with FT BBS2; greatly reduces the ability to interact with BBS12; FT dbSNP:rs74315398)" FT /evidence="ECO:0000269|PubMed:10973251, FT ECO:0000269|PubMed:20080638" FT /id="VAR_009884" FT VARIANT 286 FT /note="D -> A (in BBS6; fails to associate with FT centrosome)" FT /evidence="ECO:0000269|PubMed:11179009, FT ECO:0000269|PubMed:15731008" FT /id="VAR_017037" FT VARIANT 299 FT /note="P -> L (in BBS6; dbSNP:rs756083063)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066264" FT VARIANT 325 FT /note="T -> P (has a modifier effect on BBS; causes a FT mislocalization of the protein; fails to associate with FT centrosome; dbSNP:rs137853156)" FT /evidence="ECO:0000269|PubMed:12677556, FT ECO:0000269|PubMed:12837689, ECO:0000269|PubMed:15731008" FT /id="VAR_038901" FT VARIANT 339 FT /note="I -> V (in dbSNP:rs137853909)" FT /evidence="ECO:0000269|PubMed:12107442, FT ECO:0000269|PubMed:15666242, ECO:0000269|PubMed:15770229" FT /id="VAR_017041" FT VARIANT 345 FT /note="G -> E (in BBS6; increases MKKS protein degradation; FT fails to associate with centrosome; the mutant is highly FT polyubiquitinated and rapidly degraded by the FT ubiquitin-proteasome protein degradation pathway; FT dbSNP:rs779116830)" FT /evidence="ECO:0000269|PubMed:12107442, FT ECO:0000269|PubMed:15731008, ECO:0000269|PubMed:18094050" FT /id="VAR_017042" FT VARIANT 395 FT /note="H -> R (in BBS6; atypical mild phenotype consisting FT of retinitis pigmentosa and polydactyly without other signs FT of Bardet-Biedl syndrome; results in decreased interaction FT with BBS12; dbSNP:rs912923677)" FT /evidence="ECO:0000269|PubMed:26900326" FT /id="VAR_077208" FT VARIANT 460 FT /note="S -> P (in BBS6)" FT /evidence="ECO:0000269|PubMed:15666242" FT /id="VAR_038902" FT VARIANT 488 FT /note="A -> T (in a patient with Bardet-Biedl syndrome FT compound heterozygote for mutations in BBS12; uncertain FT pathological role; dbSNP:rs61734546)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066265" FT VARIANT 492 FT /note="D -> N (in BBS6; unknown pathological significance; FT dbSNP:rs142327258)" FT /evidence="ECO:0000269|PubMed:12920096" FT /id="VAR_038903" FT VARIANT 499 FT /note="C -> S (in BBS6; causes both increased MKKS protein FT degradation and reduced solubility relative to wild-type FT and Tyr-84 mutant; localizes properly to the centrosome; FT dbSNP:rs281797259 and dbSNP:rs137853155)" FT /evidence="ECO:0000269|PubMed:11179009, FT ECO:0000269|PubMed:11567139, ECO:0000269|PubMed:15731008, FT ECO:0000269|PubMed:18094050" FT /id="VAR_013161" FT VARIANT 511 FT /note="S -> A (in BBS6)" FT /evidence="ECO:0000269|PubMed:11179009" FT /id="VAR_017038" FT VARIANT 517 FT /note="R -> C (in dbSNP:rs1547)" FT /evidence="ECO:0000269|PubMed:10802661, FT ECO:0000269|PubMed:15483080, ECO:0000269|PubMed:15666242, FT ECO:0000269|PubMed:15770229" FT /id="VAR_009868" FT VARIANT 518 FT /note="R -> H (in BBS6; dbSNP:rs149051148)" FT /evidence="ECO:0000269|PubMed:11179009" FT /id="VAR_017039" FT VARIANT 532 FT /note="G -> V (in dbSNP:rs1545)" FT /evidence="ECO:0000269|PubMed:15483080, FT ECO:0000269|PubMed:15666242, ECO:0000269|PubMed:15770229" FT /id="VAR_009869" FT MUTAGEN 454 FT /note="L->P: No effect on import to the nucleus." FT /evidence="ECO:0000269|PubMed:28753627" SQ SEQUENCE 570 AA; 62342 MW; 14BA57FF8AEA0AF7 CRC64; MSRLEAKKPS LCKSEPLTTE RVRTTLSVLK RIVTSCYGPS GRLKQLHNGF GGYVCTTSQS SALLSHLLVT HPILKILTAS IQNHVSSFSD CGLFTAILCC NLIENVQRLG LTPTTVIRLN KHLLSLCISY LKSETCGCRI PVDFSSTQIL LCLVRSILTS KPACMLTRKE TEHVSALILR AFLLTIPENA EGHIILGKSL IVPLKGQRVI DSTVLPGILI EMSEVQLMRL LPIKKSTALK VALFCTTLSG DTSDTGEGTV VVSYGVSLEN AVLDQLLNLG RQLISDHVDL VLCQKVIHPS LKQFLNMHRI IAIDRIGVTL MEPLTKMTGT QPIGSLGSIC PNSYGSVKDV CTAKFGSKHF FHLIPNEATI CSLLLCNRND TAWDELKLTC QTALHVLQLT LKEPWALLGG GCTETHLAAY IRHKTHNDPE SILKDDECTQ TELQLIAEAF CSALESVVGS LEHDGGEILT DMKYGHLWSV QADSPCVANW PDLLSQCGCG LYNSQEELNW SFLRSTRRPF VPQSCLPHEA VGSASNLTLD CLTAKLSGLQ VAVETANLIL DLSYVIEDKN // ID BBS4_HUMAN Reviewed; 519 AA. AC Q96RK4; B4E178; Q53DZ5; Q8NHU9; Q96H45; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 14-DEC-2022, entry version 199. DE RecName: Full=Bardet-Biedl syndrome 4 protein; GN Name=BBS4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT BBS4 PRO-295. RX PubMed=11381270; DOI=10.1038/88925; RA Mykytyn K., Braun T., Carmi R., Haider N.B., Searby C.C., Shastri M., RA Beck G., Wright A.F., Iannaccone A., Elbedour K., Riise R., Baldi A., RA Raas-Rothschild A., Gorman S.W., Duhl D.M., Jacobson S.G., Casavant T., RA Stone E.M., Sheffield V.C.; RT "Identification of the gene that, when mutated, causes the human obesity RT syndrome BBS4."; RL Nat. Genet. 28:188-191(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=15497446; DOI=10.1080/10425170410001679165; RA Ye X., Dai J., Fang W., Jin W., Guo Y., Song J., Ji C., Gu S., Xie Y., RA Mao Y.; RT "Cloning and characterization of a splice variant of human Bardet-Biedl RT syndrome 4 gene (BBS4)."; RL DNA Seq. 15:213-218(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP THR-354. RC TISSUE=Kidney; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-393. RC TISSUE=Testis, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH CCDC28B. RX PubMed=16327777; DOI=10.1038/nature04370; RA Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S., RA Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.; RT "Dissection of epistasis in oligogenic Bardet-Biedl syndrome."; RL Nature 439:326-330(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=17574030; DOI=10.1016/j.cell.2007.03.053; RA Nachury M.V., Loktev A.V., Zhang Q., Westlake C.J., Peraenen J., Merdes A., RA Slusarski D.C., Scheller R.H., Bazan J.F., Sheffield V.C., Jackson P.K.; RT "A core complex of BBS proteins cooperates with the GTPase Rab8 to promote RT ciliary membrane biogenesis."; RL Cell 129:1201-1213(2007). RN [8] RP INTERACTION WITH ALDOB. RX PubMed=18000879; DOI=10.1002/cm.20250; RA Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.; RT "Novel interaction partners of Bardet-Biedl syndrome proteins."; RL Cell Motil. Cytoskeleton 65:143-155(2008). RN [9] RP INTERACTION WITH CEP290. RX PubMed=23943788; DOI=10.1093/hmg/ddt394; RA Zhang Y., Seo S., Bhattarai S., Bugge K., Searby C.C., Zhang Q., RA Drack A.V., Stone E.M., Sheffield V.C.; RT "BBS mutations modify phenotypic expression of CEP290-related RT ciliopathies."; RL Hum. Mol. Genet. 23:40-51(2014). RN [10] RP INTERACTION WITH PKD1. RX PubMed=24939912; DOI=10.1093/hmg/ddu267; RA Su X., Driscoll K., Yao G., Raed A., Wu M., Beales P.L., Zhou J.; RT "Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of RT polycystic kidney disease 1 protein."; RL Hum. Mol. Genet. 23:5441-5451(2014). RN [11] RP FUNCTION, INTERACTION WITH DCTN1 AND PCM1, AND SUBCELLULAR LOCATION. RX PubMed=15107855; DOI=10.1038/ng1352; RA Kim J.C., Badano J.L., Sibold S., Esmail M.A., Hill J., Hoskins B.E., RA Leitch C.C., Venner K., Ansley S.J., Ross A.J., Leroux M.R., Katsanis N., RA Beales P.L.; RT "The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region RT and is required for microtubule anchoring and cell cycle progression."; RL Nat. Genet. 36:462-470(2004). RN [12] RP FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME RP COMPLEX, AND INTERACTION WITH LZTL1. RX PubMed=22072986; DOI=10.1371/journal.pgen.1002358; RA Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., RA Sheffield V.C.; RT "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and RT Smoothened."; RL PLoS Genet. 7:E1002358-E1002358(2011). RN [13] RP INTERACTION WITH DLEC1. RX PubMed=33144677; DOI=10.1038/s41598-020-75957-y; RA Okitsu Y., Nagano M., Yamagata T., Ito C., Toshimori K., Dohra H., RA Fujii W., Yogo K.; RT "Dlec1 is required for spermatogenesis and male fertility in mice."; RL Sci. Rep. 10:18883-18883(2020). RN [14] RP VARIANTS BBS4 HIS-165; PRO-327; GLU-364 AND ILE-457. RX PubMed=12016587; DOI=10.1086/341031; RA Katsanis N., Eichers E.R., Ansley S.J., Lewis R.A., Kayserili H., RA Hoskins B.E., Scambler P.J., Beales P.L., Lupski J.R.; RT "BBS4 is a minor contributor to Bardet-Biedl syndrome and may also RT participate in triallelic inheritance."; RL Am. J. Hum. Genet. 71:22-29(2002). RN [15] RP VARIANT BBS4 VAL-472. RX PubMed=12677556; DOI=10.1086/375178; RA Beales P.L., Badano J.L., Ross A.J., Ansley S.J., Hoskins B.E., Kirsten B., RA Mein C.A., Froguel P., Scambler P.J., Lewis R.A., Lupski J.R., Katsanis N.; RT "Genetic interaction of BBS1 mutations with alleles at other BBS loci can RT result in non-Mendelian Bardet-Biedl syndrome."; RL Am. J. Hum. Genet. 72:1187-1199(2003). RN [16] RP VARIANT BBS4 VAL-472. RX PubMed=12872256; DOI=10.1002/humu.10241; RA Hoskins B.E., Thorn A., Scambler P.J., Beales P.L.; RT "Evaluation of multiplex capillary heteroduplex analysis: a rapid and RT sensitive mutation screening technique."; RL Hum. Mutat. 22:151-157(2003). RN [17] RP VARIANT BBS4 GLY-368, AND VARIANTS ARG-46 AND THR-354. RX PubMed=15666242; DOI=10.1086/428679; RA Karmous-Benailly H., Martinovic J., Gubler M.-C., Sirot Y., Clech L., RA Ozilou C., Auge J., Brahimi N., Etchevers H., Detrait E., Esculpavit C., RA Audollent S., Goudefroye G., Gonzales M., Tantau J., Loget P., Joubert M., RA Gaillard D., Jeanne-Pasquier C., Delezoide A.-L., Peter M.-O., Plessis G., RA Simon-Bouy B., Dollfus H., Le Merrer M., Munnich A., Encha-Razavi F., RA Vekemans M., Attie-Bitach T.; RT "Antenatal presentation of Bardet-Biedl syndrome may mimic Meckel RT syndrome."; RL Am. J. Hum. Genet. 76:493-504(2005). RN [18] RP VARIANT BBS4 ARG-351, AND VARIANT THR-354. RX PubMed=15770229; DOI=10.1038/sj.ejhg.5201372; RA Hichri H., Stoetzel C., Laurier V., Caron S., Sigaudy S., Sarda P., RA Hamel C., Martin-Coignard D., Gilles M., Leheup B., Holder M., Kaplan J., RA Bitoun P., Lacombe D., Verloes A., Bonneau D., Perrin-Schmitt F., RA Brandt C., Besancon A.-F., Mandel J.-L., Cossee M., Dollfus H.; RT "Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl RT syndrome family cohort."; RL Eur. J. Hum. Genet. 13:607-616(2005). RN [19] RP VARIANTS ARG-46; LYS-61; ASP-412 AND LYS-488. RX PubMed=21344540; DOI=10.1002/humu.21480; RA Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A., RA Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A., RA Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D., RA Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K., Heon E.; RT "BBS genotype-phenotype assessment of a multiethnic patient cohort calls RT for a revision of the disease definition."; RL Hum. Mutat. 32:610-619(2011). CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex CC required for sorting of specific membrane proteins to the primary CC cilia. The BBSome complex is required for ciliogenesis but is CC dispensable for centriolar satellite function. This ciliogenic function CC is mediated in part by the Rab8 GDP/GTP exchange factor, which CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters CC the primary cilium and promotes extension of the ciliary membrane. CC Firstly the BBSome associates with the ciliary membrane and binds to CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the CC Rab8-GTP localizes to the cilium and promotes docking and fusion of CC carrier vesicles to the base of the ciliary membrane. The BBSome CC complex, together with the LTZL1, controls SMO ciliary trafficking and CC contributes to the sonic hedgehog (SHH) pathway regulation. Required CC for proper BBSome complex assembly and its ciliary localization. CC Required for microtubule anchoring at the centrosome but not for CC microtubule nucleation. May be required for the dynein-mediated CC transport of pericentriolar proteins to the centrosome. CC {ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:17574030, CC ECO:0000269|PubMed:22072986}. CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts with PCM1 and DCTN1. CC Interacts with DC28B. Interacts with ALDOB and C2CD3. Interacts with CC PKD1 (PubMed:24939912). Interacts with CEP290 (PubMed:23943788). CC Interacts with DLEC1 (PubMed:33144677). {ECO:0000269|PubMed:15107855, CC ECO:0000269|PubMed:16327777, ECO:0000269|PubMed:17574030, CC ECO:0000269|PubMed:18000879, ECO:0000269|PubMed:22072986, CC ECO:0000269|PubMed:23943788, ECO:0000269|PubMed:24939912, CC ECO:0000269|PubMed:33144677}. CC -!- INTERACTION: CC Q96RK4; P05062: ALDOB; NbExp=4; IntAct=EBI-1805814, EBI-1045507; CC Q96RK4; A8MTZ0: BBIP1; NbExp=14; IntAct=EBI-1805814, EBI-2892417; CC Q96RK4; Q8NFJ9: BBS1; NbExp=8; IntAct=EBI-1805814, EBI-1805484; CC Q96RK4; Q3SYG4: BBS9; NbExp=6; IntAct=EBI-1805814, EBI-2826852; CC Q96RK4; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-1805814, EBI-739879; CC Q96RK4; Q9BUN5: CCDC28B; NbExp=3; IntAct=EBI-1805814, EBI-10299032; CC Q96RK4; Q14203: DCTN1; NbExp=3; IntAct=EBI-1805814, EBI-724352; CC Q96RK4; Q99814: EPAS1; NbExp=2; IntAct=EBI-1805814, EBI-447470; CC Q96RK4; Q15051: IQCB1; NbExp=5; IntAct=EBI-1805814, EBI-2805823; CC Q96RK4; P15173: MYOG; NbExp=3; IntAct=EBI-1805814, EBI-3906629; CC Q96RK4; P00973-2: OAS1; NbExp=5; IntAct=EBI-1805814, EBI-12081862; CC Q96RK4; P07237: P4HB; NbExp=3; IntAct=EBI-1805814, EBI-395883; CC Q96RK4; Q15154: PCM1; NbExp=17; IntAct=EBI-1805814, EBI-741421; CC Q96RK4; P60201-2: PLP1; NbExp=3; IntAct=EBI-1805814, EBI-12188331; CC Q96RK4; P10276: RARA; NbExp=3; IntAct=EBI-1805814, EBI-413374; CC Q96RK4; P13631: RARG; NbExp=5; IntAct=EBI-1805814, EBI-2568901; CC Q96RK4; Q04864-2: REL; NbExp=3; IntAct=EBI-1805814, EBI-10829018; CC Q96RK4; Q08AE8: SPIRE1; NbExp=3; IntAct=EBI-1805814, EBI-1055655; CC Q96RK4; Q15915: ZIC1; NbExp=3; IntAct=EBI-1805814, EBI-11963196; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000250}. Cell projection, cilium membrane CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome, centriolar satellite CC {ECO:0000250}. Cell projection, cilium, flagellum CC {ECO:0000250|UniProtKB:Q8C1Z7}. Cell projection, cilium CC {ECO:0000250|UniProtKB:Q8C1Z7}. Note=Localizes to the pericentriolar CC material. Centrosomal localization requires dynein (By similarity). CC Localizes to the connecting cilium of photoreceptor cells (By CC similarity). {ECO:0000250|UniProtKB:Q8C1Z7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96RK4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96RK4-2; Sequence=VSP_024410; CC Name=3; CC IsoId=Q96RK4-3; Sequence=VSP_047507; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. The highest level of CC expression is found in the kidney. CC -!- DISEASE: Bardet-Biedl syndrome 4 (BBS4) [MIM:615982]: A syndrome CC characterized by usually severe pigmentary retinopathy, early-onset CC obesity, polydactyly, hypogenitalism, renal malformation and CC intellectual disability. Secondary features include diabetes mellitus, CC hypertension and congenital heart disease. Bardet-Biedl syndrome CC inheritance is autosomal recessive, but three mutated alleles (two at CC one locus, and a third at a second locus) may be required for clinical CC manifestation of some forms of the disease. CC {ECO:0000269|PubMed:11381270, ECO:0000269|PubMed:12016587, CC ECO:0000269|PubMed:12677556, ECO:0000269|PubMed:12872256, CC ECO:0000269|PubMed:15666242, ECO:0000269|PubMed:15770229}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the BBS4 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Mutations of the BBS4 gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/bbs4mut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF359281; AAK58868.1; -; mRNA. DR EMBL; AY457143; AAS13441.1; -; mRNA. DR EMBL; AK075321; BAC11547.1; -; mRNA. DR EMBL; AK303706; BAG64690.1; -; mRNA. DR EMBL; AC009712; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008923; AAH08923.2; -; mRNA. DR EMBL; BC027624; AAH27624.1; -; mRNA. DR CCDS; CCDS10246.1; -. [Q96RK4-1] DR CCDS; CCDS58377.1; -. [Q96RK4-3] DR RefSeq; NP_001239607.1; NM_001252678.1. [Q96RK4-3] DR RefSeq; NP_001307594.1; NM_001320665.1. DR RefSeq; NP_149017.2; NM_033028.4. [Q96RK4-1] DR RefSeq; XP_011520150.1; XM_011521848.1. [Q96RK4-3] DR RefSeq; XP_011520151.1; XM_011521849.1. [Q96RK4-3] DR RefSeq; XP_016877940.1; XM_017022451.1. DR RefSeq; XP_016877941.1; XM_017022452.1. [Q96RK4-3] DR RefSeq; XP_016877942.1; XM_017022453.1. [Q96RK4-3] DR RefSeq; XP_016877943.1; XM_017022454.1. [Q96RK4-3] DR PDB; 6XT9; EM; 3.80 A; D=1-519. DR PDBsum; 6XT9; -. DR AlphaFoldDB; Q96RK4; -. DR SMR; Q96RK4; -. DR BioGRID; 107060; 46. DR ComplexPortal; CPX-1908; BBSome complex. DR CORUM; Q96RK4; -. DR DIP; DIP-46540N; -. DR IntAct; Q96RK4; 65. DR STRING; 9606.ENSP00000268057; -. DR iPTMnet; Q96RK4; -. DR PhosphoSitePlus; Q96RK4; -. DR BioMuta; BBS4; -. DR DMDM; 160359000; -. DR EPD; Q96RK4; -. DR MassIVE; Q96RK4; -. DR MaxQB; Q96RK4; -. DR PaxDb; Q96RK4; -. DR PeptideAtlas; Q96RK4; -. DR ProteomicsDB; 5732; -. DR ProteomicsDB; 77975; -. [Q96RK4-1] DR ProteomicsDB; 77976; -. [Q96RK4-2] DR Antibodypedia; 26730; 286 antibodies from 31 providers. DR DNASU; 585; -. DR Ensembl; ENST00000268057.9; ENSP00000268057.4; ENSG00000140463.14. [Q96RK4-1] DR Ensembl; ENST00000395205.6; ENSP00000378631.3; ENSG00000140463.14. [Q96RK4-3] DR GeneID; 585; -. DR KEGG; hsa:585; -. DR MANE-Select; ENST00000268057.9; ENSP00000268057.4; NM_033028.5; NP_149017.2. DR UCSC; uc002avb.4; human. [Q96RK4-1] DR CTD; 585; -. DR DisGeNET; 585; -. DR GeneCards; BBS4; -. DR GeneReviews; BBS4; -. DR HGNC; HGNC:969; BBS4. DR HPA; ENSG00000140463; Low tissue specificity. DR MalaCards; BBS4; -. DR MIM; 600374; gene. DR MIM; 615982; phenotype. DR neXtProt; NX_Q96RK4; -. DR OpenTargets; ENSG00000140463; -. DR Orphanet; 110; Bardet-Biedl syndrome. DR PharmGKB; PA25278; -. DR VEuPathDB; HostDB:ENSG00000140463; -. DR eggNOG; KOG1124; Eukaryota. DR GeneTree; ENSGT00940000158166; -. DR HOGENOM; CLU_033477_1_0_1; -. DR InParanoid; Q96RK4; -. DR OMA; WNNIGAC; -. DR PhylomeDB; Q96RK4; -. DR TreeFam; TF324966; -. DR PathwayCommons; Q96RK4; -. DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium. DR SignaLink; Q96RK4; -. DR SIGNOR; Q96RK4; -. DR BioGRID-ORCS; 585; 5 hits in 1069 CRISPR screens. DR ChiTaRS; BBS4; human. DR GeneWiki; BBS4; -. DR GenomeRNAi; 585; -. DR Pharos; Q96RK4; Tbio. DR PRO; PR:Q96RK4; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q96RK4; protein. DR Bgee; ENSG00000140463; Expressed in right uterine tube and 188 other tissues. DR ExpressionAtlas; Q96RK4; baseline and differential. DR Genevisible; Q96RK4; HS. DR GO; GO:0034464; C:BBSome; IDA:UniProtKB. DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB. DR GO; GO:0005814; C:centriole; IDA:BHF-UCL. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL. DR GO; GO:0060170; C:ciliary membrane; IDA:BHF-UCL. DR GO; GO:0035869; C:ciliary transition zone; IDA:GO_Central. DR GO; GO:0005929; C:cilium; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL. DR GO; GO:0097730; C:non-motile cilium; IDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; IEA:GOC. DR GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB. DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl. DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl. DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl. DR GO; GO:0043014; F:alpha-tubulin binding; IDA:BHF-UCL. DR GO; GO:0048487; F:beta-tubulin binding; IDA:BHF-UCL. DR GO; GO:0034452; F:dynactin binding; IDA:BHF-UCL. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:UniProtKB. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0030534; P:adult behavior; ISS:BHF-UCL. DR GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL. DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB. DR GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL. DR GO; GO:0060271; P:cilium assembly; ISS:BHF-UCL. DR GO; GO:0016358; P:dendrite development; ISS:BHF-UCL. DR GO; GO:0060324; P:face development; IEA:Ensembl. DR GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL. DR GO; GO:0060613; P:fat pad development; IEA:Ensembl. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0001947; P:heart looping; ISS:BHF-UCL. DR GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL. DR GO; GO:0046907; P:intracellular transport; ISS:BHF-UCL. DR GO; GO:0051457; P:maintenance of protein location in nucleus; IGI:BHF-UCL. DR GO; GO:0032402; P:melanosome transport; ISS:BHF-UCL. DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:BHF-UCL. DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:BHF-UCL. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:BHF-UCL. DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl. DR GO; GO:0038108; P:negative regulation of appetite by leptin-mediated signaling pathway; ISS:BHF-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl. DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IEA:Ensembl. DR GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:1905515; P:non-motile cilium assembly; ISS:BHF-UCL. DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:BHF-UCL. DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl. DR GO; GO:0045724; P:positive regulation of cilium assembly; ISS:BHF-UCL. DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0071539; P:protein localization to centrosome; IMP:BHF-UCL. DR GO; GO:0061512; P:protein localization to cilium; IMP:GO_Central. DR GO; GO:0033365; P:protein localization to organelle; ISS:BHF-UCL. DR GO; GO:1903546; P:protein localization to photoreceptor outer segment; IEA:Ensembl. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISS:BHF-UCL. DR GO; GO:0032465; P:regulation of cytokinesis; IMP:BHF-UCL. DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:BHF-UCL. DR GO; GO:1902855; P:regulation of non-motile cilium assembly; IEA:Ensembl. DR GO; GO:0051492; P:regulation of stress fiber assembly; IEA:Ensembl. DR GO; GO:0001895; P:retina homeostasis; ISS:BHF-UCL. DR GO; GO:0046548; P:retinal rod cell development; ISS:BHF-UCL. DR GO; GO:0007608; P:sensory perception of smell; ISS:BHF-UCL. DR GO; GO:0050893; P:sensory processing; TAS:BHF-UCL. DR GO; GO:0035176; P:social behavior; IEA:Ensembl. DR GO; GO:0007286; P:spermatid development; ISS:BHF-UCL. DR GO; GO:0021756; P:striatum development; ISS:BHF-UCL. DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR028786; BBS4. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR44186; -; 1. DR Pfam; PF13181; TPR_8; 2. DR SMART; SM00028; TPR; 8. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS50005; TPR; 8. DR PROSITE; PS50293; TPR_REGION; 1. DR AGR; HGNC:969; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Bardet-Biedl syndrome; Cell membrane; KW Cell projection; Ciliopathy; Cilium; Cilium biogenesis/degradation; KW Cytoplasm; Cytoskeleton; Disease variant; Flagellum; KW Intellectual disability; Membrane; Obesity; Protein transport; KW Reference proteome; Repeat; Sensory transduction; TPR repeat; Transport; KW Vision. FT CHAIN 1..519 FT /note="Bardet-Biedl syndrome 4 protein" FT /id="PRO_0000106263" FT REPEAT 67..100 FT /note="TPR 1" FT REPEAT 101..134 FT /note="TPR 2" FT REPEAT 135..168 FT /note="TPR 3" FT REPEAT 169..201 FT /note="TPR 4" FT REPEAT 203..235 FT /note="TPR 5" FT REPEAT 237..269 FT /note="TPR 6" FT REPEAT 270..303 FT /note="TPR 7" FT REPEAT 304..337 FT /note="TPR 8" FT REPEAT 339..371 FT /note="TPR 9" FT REPEAT 373..408 FT /note="TPR 10" FT REGION 1..66 FT /note="Required for localization to centrosomes" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 101..337 FT /note="Interaction with PCM1" FT /evidence="ECO:0000269|PubMed:15107855" FT REGION 338..519 FT /note="Required for localization to centrosomes" FT REGION 440..519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 449..495 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..172 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047507" FT VAR_SEQ 1..8 FT /note="MAEERVAT -> MALTVVPSFSVSGVWK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15497446" FT /id="VSP_024410" FT VARIANT 46 FT /note="K -> R (in dbSNP:rs75295839)" FT /evidence="ECO:0000269|PubMed:15666242, FT ECO:0000269|PubMed:21344540" FT /id="VAR_038894" FT VARIANT 61 FT /note="E -> K (found in patients with Bardet-Biedl syndrome FT carrying mutations in other BBS genes; uncertain FT pathological role; dbSNP:rs1251827333)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066287" FT VARIANT 165 FT /note="N -> H (in BBS4)" FT /evidence="ECO:0000269|PubMed:12016587" FT /id="VAR_017049" FT VARIANT 268 FT /note="E -> K (in dbSNP:rs11638283)" FT /id="VAR_028722" FT VARIANT 295 FT /note="R -> P (in BBS4; dbSNP:rs121434632)" FT /evidence="ECO:0000269|PubMed:11381270" FT /id="VAR_013170" FT VARIANT 327 FT /note="L -> P (in BBS4)" FT /evidence="ECO:0000269|PubMed:12016587" FT /id="VAR_017050" FT VARIANT 351 FT /note="L -> R (in BBS4)" FT /evidence="ECO:0000269|PubMed:15770229" FT /id="VAR_038895" FT VARIANT 354 FT /note="I -> T (in dbSNP:rs2277598)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15666242, ECO:0000269|PubMed:15770229" FT /id="VAR_017054" FT VARIANT 364 FT /note="A -> E (in BBS4; dbSNP:rs28938468)" FT /evidence="ECO:0000269|PubMed:12016587" FT /id="VAR_017051" FT VARIANT 368 FT /note="D -> G (in BBS4; dbSNP:rs772548770)" FT /evidence="ECO:0000269|PubMed:15666242" FT /id="VAR_038896" FT VARIANT 393 FT /note="A -> V (in dbSNP:rs17852452)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_028723" FT VARIANT 412 FT /note="E -> D (in a patient with Bardet-Biedl syndrome FT compound heterozygote for mutations in BBS1; uncertain FT pathological role; dbSNP:rs147202164)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066288" FT VARIANT 457 FT /note="S -> I (in BBS4)" FT /evidence="ECO:0000269|PubMed:12016587" FT /id="VAR_017052" FT VARIANT 472 FT /note="M -> V (in BBS4; dbSNP:rs2277596)" FT /evidence="ECO:0000269|PubMed:12677556, FT ECO:0000269|PubMed:12872256" FT /id="VAR_017053" FT VARIANT 488 FT /note="T -> K (in a patient with Bardet-Biedl syndrome FT homozygous for a mutation in BBS12; uncertain pathological FT role; dbSNP:rs561284402)" FT /evidence="ECO:0000269|PubMed:21344540" FT /id="VAR_066289" FT VARIANT 503 FT /note="P -> L (in BBS4; dbSNP:rs756419611)" FT /id="VAR_038897" SQ SEQUENCE 519 AA; 58282 MW; 59BC9B29355C8E3C CRC64; MAEERVATRT QFPVSTESQK PRQKKAPEFP ILEKQNWLIH LHYIRKDYEA CKAVIKEQLQ ETQGLCEYAI YVQALIFRLE GNIQESLELF QTCAVLSPQS ADNLKQVARS LFLLGKHKAA IEVYNEAAKL NQKDWEISHN LGVCYIYLKQ FNKAQDQLHN ALNLNRHDLT YIMLGKIHLL EGDLDKAIEV YKKAVEFSPE NTELLTTLGL LYLQLGIYQK AFEHLGNALT YDPTNYKAIL AAGSMMQTHG DFDVALTKYR VVACAVPESP PLWNNIGMCF FGKKKYVAAI SCLKRANYLA PFDWKILYNL GLVHLTMQQY ASAFHFLSAA INFQPKMGEL YMLLAVALTN LEDIENAKRA YAEAVHLDKC NPLVNLNYAV LLYNQGEKKN ALAQYQEMEK KVSLLKDNSS LEFDSEMVEM AQKLGAALQV GEALVWTKPV KDPKSKHQTT STSKPASFQQ PLGSNQALGQ AMSSAAAYRT LPSGAGGTSQ FTKPPSLPLE PEPAVESSPT ETSEQIREK // ID K0A1M3_HUMAN Unreviewed; 180 AA. AC K0A1M3; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 14-DEC-2022, entry version 28. DE SubName: Full=HYDIN {ECO:0000313|EMBL:AFS65326.1}; DE Flags: Fragment; GN Name=HYDIN {ECO:0000313|EMBL:AFS65326.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AFS65326.1}; RN [1] {ECO:0000313|EMBL:AFS65326.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23022101; DOI=10.1016/j.ajhg.2012.08.016; RG UK10K Consortium; RA Olbrich H., Schmidts M., Werner C., Onoufriadis A., Loges N.T., Raidt J., RA Banki N.F., Shoemark A., Burgoyne T., Al Turki S., Hurles M.E., Kohler G., RA Schroeder J., Nurnberg G., Nurnberg P., Chung E.M.K., Reinhardt R., RA Marthin J.K., Nielsen K.G., Mitchison H.M., Omran H.; RT "Recessive HYDIN mutations cause primary ciliary dyskinesia without RT randomization of left-right body asymmetry."; RL Am. J. Hum. Genet. 91:672-684(2012). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JX501991; AFS65326.1; -; mRNA. DR AlphaFoldDB; K0A1M3; -. DR PeptideAtlas; K0A1M3; -. DR ChiTaRS; HYDIN; human. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR033305; Hydin-like. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR23053; DLEC1 DELETED IN LUNG AND ESOPHAGEAL CANCER 1; 1. PE 2: Evidence at transcript level; FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AFS65326.1" FT NON_TER 180 FT /evidence="ECO:0000313|EMBL:AFS65326.1" SQ SEQUENCE 180 AA; 20380 MW; BBC0069FE43AEFF0 CRC64; TVESPEMDLN DFVKTVLVDE DARPEEKELR KTKASSVISD EIKISSTEIE RIYSSQSQVE DQESLQTCEQ NEMLSIGIEE VFDILPLFGV LQPHSSHQIS FTFYGHANII AQAKALCEVE EGPTYEITLK GEASLVNYSF DTKDIHYGLQ LFDHVTEREI TLTNMGKVGF EFKVLTDHQS // ID Q32W78_HUMAN Unreviewed; 76 AA. AC Q32W78; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-DEC-2022, entry version 24. DE SubName: Full=Deleted in lung and esophageal cancer 1 transcript variant 1 {ECO:0000313|EMBL:AAX18633.1}; DE Flags: Fragment; GN Name=DLEC1 {ECO:0000313|EMBL:AAX18633.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAX18633.1}; RN [1] {ECO:0000313|EMBL:AAX18633.1} RP NUCLEOTIDE SEQUENCE. RA Qiu G.-H., Ying J., Srivastava G., Tao Q.; RT "The tumor suppressor gene DLEC1 at 3p21.3 is frequently silenced by RT epigenetic mechanisms in multiple human tumors and induces cell-cycle RT arrest in G1 phase."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY789462; AAX18633.1; -; mRNA. DR AlphaFoldDB; Q32W78; -. DR ChiTaRS; DLEC1; human. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro. DR InterPro; IPR033304; DLEC1. DR PANTHER; PTHR46348; DELETED IN LUNG AND ESOPHAGEAL CANCER PROTEIN 1; 1. PE 2: Evidence at transcript level; FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAX18633.1" FT NON_TER 76 FT /evidence="ECO:0000313|EMBL:AAX18633.1" SQ SEQUENCE 76 AA; 8355 MW; F3E0EFE857DDD85B CRC64; GEFQSTEPEQ SCADTPVFLA KPPIGFFTDY EIGPVYEMVI ALQNTTTTSR YLRVLPPSTP YFALGLVSPV LDCGYC // ID A1L305_HUMAN Unreviewed; 711 AA. AC A1L305; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 14-DEC-2022, entry version 59. DE SubName: Full=DLEC1 protein {ECO:0000313|EMBL:AAI29825.1}; GN Name=DLEC1 {ECO:0000313|EMBL:AAI29825.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI29825.1}; RN [1] {ECO:0000313|EMBL:AAI29825.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC129824; AAI29825.1; -; mRNA. DR AlphaFoldDB; A1L305; -. DR PeptideAtlas; A1L305; -. DR ChiTaRS; DLEC1; human. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR033304; DLEC1. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR46348; DELETED IN LUNG AND ESOPHAGEAL CANCER PROTEIN 1; 1. PE 2: Evidence at transcript level; FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 711 AA; 80354 MW; 0B5E2295FBFB4135 CRC64; METRSSKTRR SLASRTNECQ GTMWAPTSPP AGSSSPSQPT WKSSLYSSLA YSEAFHYSFA ARPRRLTQLA LAQRPEPQLL RLRPSSLRTQ DISHLLTGVF RNLYSAEVIG DEVSASLIKA RGSENERHEE FVDQLQQIRE LYKQRLDEFE MLERHITQAQ ARAIAENERV MSQAGVQDLE SLVRLPPVKS VSRWCIDSEL LRKHHLISPE DYYTDTVPFH SAPKGISLPG CSKLTFSCEK RSVQKKELNK KLEDSCRKKL AEFEDELDHT VDSLTWNLTP KAKERTREPL KKASQPRNKN WMNHLRVPQR ELDRLLLARM ESRNHFLKNP RFFPPNTRYG GKSLVFPPKK PAPIGEFQST EPEQSCADTP VFLAKPPIGF FTDYEIGPVY EMVIALQNTT TTSRYLRVLP PSTPYFALGL GMFPGKGGMV APGMTCQYIV QFFPDCLGDF DDFILVETQS AHTLLIPLQA RRPPPVLTLS PVLDCGYCLI GGVKMTRFIC KNVGFSVGRF CIMPKTSWPP LSFKAIATVG FVEQPPFGIL PSVFELAPGH AILVEVLFSP KSLGKAEQTF IIMCDNCQIK ELVTIGIGQL IALDLIYISG EKSQPDPGEL TDLTAQHFIR FEPENLRSTA RKQLIIRNAT HVELAFYWQI MKPNLQPLMP GETFSMDSIK CYPDKETAFS IMPRKGVLSP HTDHEFILSF SPHEVQMVSS Q // ID A2VDF1_HUMAN Unreviewed; 873 AA. AC A2VDF1; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 14-DEC-2022, entry version 56. DE SubName: Full=DLEC1 protein {ECO:0000313|EMBL:AAI29826.1}; DE Flags: Fragment; GN Name=DLEC1 {ECO:0000313|EMBL:AAI29826.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI29826.1}; RN [1] {ECO:0000313|EMBL:AAI29826.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC129825; AAI29826.1; -; mRNA. DR AlphaFoldDB; A2VDF1; -. DR PeptideAtlas; A2VDF1; -. DR ChiTaRS; DLEC1; human. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR033304; DLEC1. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR46348; DELETED IN LUNG AND ESOPHAGEAL CANCER PROTEIN 1; 1. PE 2: Evidence at transcript level; FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 873 FT /evidence="ECO:0000313|EMBL:AAI29826.1" SQ SEQUENCE 873 AA; 98088 MW; 878A5486FD9CE470 CRC64; METRSSKTRR SLASRTNECQ GTMWAPTSPP AGSSSPSQPT WKSSLYSSLA YSEAFHYSFA ARPRRLTQLA LAQRPEPQLL RLRPSSLRTQ DISHLLTGVF RNLYSAEVIG DEVSASLIKA RGSENERHEE FVDQLQQIRE LYKQRLDEFE MLERHITQAQ ARAIAENERV MSQAGVQDLE SLVRLPPVKS VSRWCIDSEL LRKHHLISPE DYYTDTVPFH SAPKGISLPG CSKLTFSCEK RSVQKKELNK KLEDSCRKKL AEFEDELDHT VDSLTWNLTP KAKERTREPL KKASQPRNKN WMNHLRVPQR ELDRLLLARM ESRNHFLKNP RFFPPNTRYG GKSPVFPPKK PAPIGEFQST EPEQSCADTP VFLAKPPIGF FTDYEIGPVY EMVIALQNTT TTSRYLRVLP PSTPYFALGL GMFPGKGGMV APGMTCQYIV QFFPDCLGDF DDFILVETQS AHTLLIPLQA RRPPPVLTLS PVLDCGYCLI GGVKMTRFIC KNVGFSVGRF CIMPKTSWPP LSFKAIATVG FVEQPPFGIL PSVFELAPGH AILVEVLFSP KSLGKAEQTF IIMCDNCQIK ELVTIGIGQL IALDLIYISG EKSQPDPGEL TDLTAQHFIR FEPENLRSTA RKQLIIRNAT HVELAFYWQI MKPNLQPLMP GETFSMDSIK CYPDKETAFS IMPRKGVLSP HTDHEFILSF SPHELRDFHS VLQMVLEEVP EPVSSEAESL GHSSYSVDDV IVLEIEVKGS VEPFQVLLEP YALIIPGENY IGINVKKAFK MWNNSKSPIR YLWGKISDCH IIEVEPGTGV IEPSEVGDFE LNFTGGVPGP TSQDLLCEIE DSPSPVVLHI EAVFKGPALI INVSALQFGL LRL // ID B7ZW06_HUMAN Unreviewed; 1755 AA. AC B7ZW06; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 14-DEC-2022, entry version 49. DE SubName: Full=Deleted in lung and esophageal cancer 1 {ECO:0000313|EMBL:AAI71799.1}; GN Name=DLEC1 {ECO:0000313|EMBL:AAI71799.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAI71799.1}; RN [1] {ECO:0000313|EMBL:AAI71799.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC171799; AAI71799.1; -; mRNA. DR PeptideAtlas; B7ZW06; -. DR ChiTaRS; DLEC1; human. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 7. DR InterPro; IPR033304; DLEC1. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR46348; DELETED IN LUNG AND ESOPHAGEAL CANCER PROTEIN 1; 1. PE 2: Evidence at transcript level; FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1339..1360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1529..1553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1755 AA; 195710 MW; 40FF95FDC651A723 CRC64; METRSSKTRR SLASRTNECQ GTMWAPTSPP AGSSSPSQPT WKSSLYSSLA YSEAFHYSFA ARPRRLTQLA LAQRPEPQLL RLRPSSLRTQ DISHLLTGVF RNLYSAEVIG DEVSASLIKA RGSENERHEE FVDQLQQIRE LYKQRLDEFE MLERHITQAQ ARAIAENERV MSQAGVQDLE SLVRLPPVKS VSRWCIDSEL LRKHHLISPE DYYTDTVPFH SAPKGISLPG CSKLTFSCEK RSVQKKELNK KLEDSCRKKL AEFEDELDHT VDSLTWNLTP KAKERTREPL KKASQPRNKN WMNHLRVPQR ELDRLLLARM ESRNHFLKNP RFFPPNTRYG GKSLVFPPKK PAPIGEFQST EPEQSCADTP VFLAKPPIGF FTDYEIGPVY EMVIALQNTT TTSRYLRVLP PSTPYFALGL GMFPGKGGMV APGMTCQYIV QFFPDCLGDF DDFILVETQS AHTLLIPLQA RRPPPVLTLS PVLDCGYCLI GGVKMTRFIC KNVGFSVGRF CIMPKTSWPP LSFKAIATVG FVEQPPFGIL PSVFELAPGH AILVEVLFSP KSLGKAEQTF IIMCDNCQIK ELVTIGIGQL IALDLIYISG EKSQPDPGEL TDLTAQHFIR FEPENLRSTA RKQLIIRNAT HVELAFYWQI MKPNLQPLMP GETFSMDSIK CYPDKETAFS IMPRKGVLSP HTDHEFILSF SPHELRDFHS VLQMVLEEVP EPVSSEAESL GHSSYSVDDV IVLEIEVKGS VEPFQVLLEP YALIIPGENY IGINVKKAFK MWNNSKSPIR YLWGKISDCH IIEVEPGTGV IEPSEVGDFE LNFTGGVPGP TSQDLLCEIE DSPSPVVLHI EAVFKGPPLI INVSALQFGL LRLGQKATNS IQIRNVSQLP ATWRMKESPV SLQERPEDVS PFDIEPSSGQ LHSLGECRVD ITLEALHCQH LETVLELEVE NGAWSYLPVY AEVQKPHVYL QSSQVEVRNL YLGVPTKTTI TLINGTLLPT QFHWGKLLGH QAEFCMVTVS PKHGLLGPSE ECQLKLELTA HTQEELTHLA LPCHVSGMKK PLVLGISGKP QGLQVAITIS KESSDCSTEQ WPGHPKELRL DFGSAVPLRT RVTRQLILTN RSPIRTRFSL KFEYFGSPQN SLSKKTSLPN MPPALLKTVR MQEHLAKREQ LDFMESMLSH GKGAAFFPHF SQGMLGPYQQ LCIDITGCAN MWGEYWDNLI CTVGDLLPEV IPVHMAAVGC PISSLRTTSY TIDQAQKEPA MRFGTQVSGG DTVTRTLRLN NSSPCDIRLD WETYVPEDKE DRLVELLVFY GPPFPLRDQA GNELVCPDTP EGGCLLWSPG PSSSSEFSHE TDSSVEGSSS ASNRVAQKLI SVILQAHEGV PSGHLYCISP KQVVVPAGGS STIYISFTPM VLSPEILHKV ECTGYALGFM SLDSKVEREI PGKRHRLQDF AVGPLKLDLH SYVRPAQLSV ELDYGGSMEF QCQASDLIPE QPCSGVLSEL VTTHHLKLTN TTEIPHYFRL MVSRPFSVSQ DGASQDHRAP GPGQKQECEE ETASADKQLV LQAQENMLVN VSFSLSLELL SYQKLPADQT LPGVDIQQSA SGEREMVFTQ NLLLEYTNQT TQVVPLRAVV AVPELQLSTS WVDFGTCFVS QQRVREVYLM NLSGCRSYWT MLMGQQEPAK AAVAFRVSPN SGLLEARSAN APPTSIALQV FFTARSSELY ESTMVVEGVL GEKSCTLRLR GQGSYDERYM LPHQP // ID J3KRJ6_HUMAN Unreviewed; 113 AA. AC J3KRJ6; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 14-DEC-2022, entry version 49. DE SubName: Full=Hydrocephalus-inducing protein homolog {ECO:0000313|Ensembl:ENSP00000462031.1}; DE Flags: Fragment; GN Name=HYDIN {ECO:0000313|Ensembl:ENSP00000462031.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000462031.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000462031.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000462031.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC009136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; J3KRJ6; -. DR Ensembl; ENST00000538568.5; ENSP00000462031.1; ENSG00000157423.18. DR Ensembl; ENST00000634827.1; ENSP00000489274.1; ENSG00000283022.2. DR UCSC; uc059wsk.1; human. DR HGNC; HGNC:19368; HYDIN. DR VEuPathDB; HostDB:ENSG00000157423; -. DR GeneTree; ENSGT00610000086095; -. DR HOGENOM; CLU_2151446_0_0_1; -. DR ChiTaRS; HYDIN; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000157423; Expressed in right uterine tube and 101 other tissues. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR033305; Hydin-like. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR23053; DLEC1 DELETED IN LUNG AND ESOPHAGEAL CANCER 1; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|PeptideAtlas:J3KRJ6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000462031.1" SQ SEQUENCE 113 AA; 12490 MW; 50B590318B60B0AF CRC64; XIYVLKDSSR ILNLCNQSFI PAFFQAHMAH KKSLWTIEPN EGMVPPETDV QLALTANLND TLTFKDCVIL DIENSSTYRI PVQASGTGST IVSDKPFAPE LNLGAHFRNL TVS // ID J3KTP9_HUMAN Unreviewed; 151 AA. AC J3KTP9; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 14-DEC-2022, entry version 51. DE SubName: Full=Hydrocephalus-inducing protein homolog {ECO:0000313|Ensembl:ENSP00000463093.1}; DE Flags: Fragment; GN Name=HYDIN {ECO:0000313|Ensembl:ENSP00000463093.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000463093.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000463093.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000463093.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC009136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; J3KTP9; -. DR Ensembl; ENST00000539447.5; ENSP00000463093.1; ENSG00000157423.18. DR Ensembl; ENST00000635365.1; ENSP00000488915.1; ENSG00000283022.2. DR UCSC; uc059wsl.1; human. DR HGNC; HGNC:19368; HYDIN. DR VEuPathDB; HostDB:ENSG00000157423; -. DR GeneTree; ENSGT00610000086095; -. DR HOGENOM; CLU_1744652_0_0_1; -. DR ChiTaRS; HYDIN; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000157423; Expressed in right uterine tube and 101 other tissues. DR InterPro; IPR033305; Hydin-like. DR PANTHER; PTHR23053; DLEC1 DELETED IN LUNG AND ESOPHAGEAL CANCER 1; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|PeptideAtlas:J3KTP9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000463093.1" SQ SEQUENCE 151 AA; 17534 MW; D8C7DAAEEDB99E7E CRC64; XPKVVTEEEV NRMLTPSEFL KEMSLTTEQR LAKTRLMCRP QIIELLDMGE TTHQKFSGID LDQALFQPFP SEIIFQNYTP CEVYEVPLIL RNNDKIPRLV KVVEESSPYF KVISPKDIGH KVAPGVPSIF RILFTPEENK AFLYRTSYWN S // ID Q32W76_HUMAN Unreviewed; 82 AA. AC Q32W76; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 14-DEC-2022, entry version 100. DE SubName: Full=Deleted in lung and esophageal cancer 1 transcript variant 3 {ECO:0000313|EMBL:AAX18635.1}; DE SubName: Full=Deleted in lung and esophageal cancer protein 1 {ECO:0000313|Ensembl:ENSP00000404261.1}; DE Flags: Fragment; GN Name=DLEC1 {ECO:0000313|EMBL:AAX18635.1, GN ECO:0000313|Ensembl:ENSP00000404261.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAX18635.1}; RN [1] {ECO:0000313|EMBL:AAX18635.1} RP NUCLEOTIDE SEQUENCE. RA Qiu G.-H., Ying J., Srivastava G., Tao Q.; RT "The tumor suppressor gene DLEC1 at 3p21.3 is frequently silenced by RT epigenetic mechanisms in multiple human tumors and induces cell-cycle RT arrest in G1 phase."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSP00000404261.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] {ECO:0000313|Ensembl:ENSP00000404261.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC144536; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP006309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY789464; AAX18635.1; -; mRNA. DR Ensembl; ENST00000447130.1; ENSP00000404261.1; ENSG00000008226.20. DR UCSC; uc062iey.1; human. DR HGNC; HGNC:2899; DLEC1. DR VEuPathDB; HostDB:ENSG00000008226; -. DR GeneTree; ENSGT00390000006098; -. DR HOGENOM; CLU_2564353_0_0_1; -. DR ChiTaRS; DLEC1; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000008226; Expressed in right uterine tube and 142 other tissues. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro. DR InterPro; IPR033304; DLEC1. DR PANTHER; PTHR46348; DELETED IN LUNG AND ESOPHAGEAL CANCER PROTEIN 1; 1. PE 2: Evidence at transcript level; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAX18635.1" SQ SEQUENCE 82 AA; 9086 MW; 8D2D8936C7E362B4 CRC64; PPKKPAPIGE FQSTEPEQSC ADTPVFLAKP PIGFFTDYEI GPVYEMVIAL QNTTTTSRYL RVLPPSTPYF ALGLGHCNRR LC // ID B1B5Y4_HUMAN Unreviewed; 1755 AA. AC B1B5Y4; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 14-DEC-2022, entry version 71. DE SubName: Full=Deleted in lung and esophageal cancer protein 1 {ECO:0000313|EMBL:BAG11659.1}; DE Flags: Fragment; GN Name=DLEC1 {ECO:0000313|EMBL:BAG11659.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG11659.1}; RN [1] {ECO:0000313|EMBL:BAG11659.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Spleen {ECO:0000313|EMBL:BAG11659.1}; RA Nagase T., Kikuno R.F., Yamakawa H., Ohara O.; RT "Homo sapiens mRNA for large protein."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB425198; BAG11659.1; -; mRNA. DR RefSeq; NP_001308082.1; NM_001321153.1. DR PeptideAtlas; B1B5Y4; -. DR DNASU; 9940; -. DR GeneID; 9940; -. DR CTD; 9940; -. DR OrthoDB; 373519at2759; -. DR BioGRID-ORCS; 9940; 9 hits in 1062 CRISPR screens. DR ChiTaRS; DLEC1; human. DR GenomeRNAi; 9940; -. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 7. DR InterPro; IPR033304; DLEC1. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR46348; DELETED IN LUNG AND ESOPHAGEAL CANCER PROTEIN 1; 1. PE 2: Evidence at transcript level; FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1339..1360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1529..1553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAG11659.1" SQ SEQUENCE 1755 AA; 195656 MW; F04FE94174BA504D CRC64; RSSKTRRSLA SRTNECQGTM WAPTSPPAGS SSPSQPTWKS SLYSSLAYSE AFHYSFAARP RRLTQLALAQ RPEPQLLRLR PSSLRTQDIS HLLTGVFRNL YSAEVIGDEV SASLIKARGS ENERHEEFVD QLQQIRELYK QRLDEFEMLE RHITQAQARA IAENERVMSQ AGVQDLESLV RLPPVKSVSR WCIDSELLRK HHLISPEDYY TDTVPFHSAP KGISLPGCSK LTFSCEKRSV QKKELNKKLE DSCRKKLAEF EDELDHTVDS LTWNLTPKAK ERTREPLKKA SQPRNKNWMN HLRVPQRELD RLLLARMESR NHFLKNPRFF PPNTRYGGKS LVFPPKKPAP IGEFQSTEPE QSCADTPVFL AKPPIGFFTD YEIGPVYEMV IALQNTTTTS RYLRVLPPST PYFALGLGMF PGKGGMVAPG MTCQYIVQFF PDCLGDFDDF ILVETQSAHT LLIPLQARRP PPVLTLSPVL DCGYCLIGGV KMTRFICKNV GFSVGRFCIM PKTSWPPLSF KAIATVGFVE QPPFGILPSV FELAPGHAIL VEVLFSPKSL GKAEQTFIIM CDNCQIKELV TIGIGQLIAL DLIYISGEKS QPDPGELTDL TAQHFIRFEP ENLRSTARKQ LIIRNATHVE LAFYWQIMKP NLQPLMPGET FSMDSIKCYP DKETAFSIMP RKGVLSPHTD HEFILSFSPH ELRDFHSVLQ MVLEEVPEPV SSEAESLGHS SYSVDDVIVL EIEVKGSVEP FQVLLEPYAL IIPGENYIGI NVKKAFKMWN NSKSPIRYLW GKISDCHIIE VEPGTGVIEP SEVGDFELNF TGGVPGPTSQ DLLCEIEDSP SPVVLHIEAV FKGPALIINV SALQFGLLRL GQKATNSIQI RNVSQLPATW RMKESPVSLQ ERPEDVSPFD IEPSSGQLHS LGECRVDITL EALHCQHLET VLELEVENGA WSYLPVYAEV QKPHVYLQSS QVEVRNLYLG VPTKTTITLI NGTLLPTQFH WGKLLGHQAE FCMVTVSPKH GLLGPSEECQ LKLELTAHTQ EELTHLALPC HVSGMKKPLV LGISGKPQGL QVAITISKES SDCSVFSTEQ WPGHPKELRL DFGSAVPLRT RVTRQLILTN RSPIRTRFSL KFEYFGSPQN SLSKKTSLPN MPPALLKTVR MQEHLAKREQ LDFMESMLSH GKGAAFFPHF SQGMLGPYQQ LCIDITGCAN MWGEYWDNLI CTVGDLLPEV IPVHMAAVGC PISSLRTTSY TIDQAQKEPA MRFGTQVSGG DTVTRTLRLN NSSPCDIRLD WETYVPEDKE DRLVELLVFY GPPFPLRDQA GNELVCPDTP EGGCLLWSPG PSSSSEFSHE TDSSVEGSSS ASNRVAQKLI SVILQAHEGV PSGHLYCISP KQVVVPAGGS STIYISFTPM VLSPEILHKV ECTGYALGFM SLDSKVEREI PGKRHRLQDF AVGPLKLDLH SYVRPAQLSV ELDYGGSMEF QCQASDLIPE QPCSGVLSEL VTTHHLKLTN TTEIPHYFRL MVSRPFSVSQ DGASQDHRAP GPGQKQECEE ETASADKQLV LQAQENMLVN VSFSLSLELL SYQKLPADQT LPGVDIQQSA SGEREMVFTQ NLLLEYTNQT TQVVPLRAVV AVPELQLSTS WVDFGTCFVS QQRVREVYLM NLSGCRSYWT MLMGQQEPAK AAVAFRVSPN SGLLEARSAN APPTSIALQV FFTARSSELY ESTMVVEGVL GEKSCTLRLR GQGSYDERYM LPHQP // ID J3QL79_HUMAN Unreviewed; 528 AA. AC J3QL79; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 14-DEC-2022, entry version 58. DE SubName: Full=Hydrocephalus-inducing protein homolog {ECO:0000313|Ensembl:ENSP00000463422.1}; DE Flags: Fragment; GN Name=HYDIN {ECO:0000313|Ensembl:ENSP00000463422.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000463422.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000463422.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000463422.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC009136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; J3QL79; -. DR PeptideAtlas; J3QL79; -. DR Ensembl; ENST00000545230.5; ENSP00000463422.1; ENSG00000157423.18. DR Ensembl; ENST00000634415.1; ENSP00000489101.1; ENSG00000283022.2. DR UCSC; uc059wsm.1; human. DR HGNC; HGNC:19368; HYDIN. DR VEuPathDB; HostDB:ENSG00000157423; -. DR GeneTree; ENSGT00610000086095; -. DR ChiTaRS; HYDIN; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000157423; Expressed in right uterine tube and 101 other tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 4. DR InterPro; IPR031549; ASH. DR InterPro; IPR033305; Hydin-like. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR23053; DLEC1 DELETED IN LUNG AND ESOPHAGEAL CANCER 1; 1. DR Pfam; PF15780; ASH; 1. PE 1: Evidence at protein level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Proteomics identification {ECO:0007829|PeptideAtlas:J3QL79}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 302..368 FT /note="ASH" FT /evidence="ECO:0000259|Pfam:PF15780" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000463422.1" SQ SEQUENCE 528 AA; 59465 MW; 44AA1982DA697FEA CRC64; VKYSTQKILL VRNIGNKNAV FHIKTCRPFS IEPAIGTLNV GESMQLEVEF EPQSVGDHSG RLIVCYDTGE KVFVSLYGAA IDMNIRLDKN SLTIEKTYIS LANQRTITIH NRSNIIAHFL WKVFATQQEE DREKYRACDD LIKEEKDETD EFFEECITDP LLREHLSVLS RTFANQRRLV QGDSKLFFNN VFTVEPLEGD VWPNSSAEIT VYFNPLEAKL YQQTIYCDIL GREIRLPLRI KGEGMGPKIH FNFELLDIGK VFTGSAHCYE AILYNKGSID ALFNMTPPTS ALGACFVFSP KEGIIEPSGV QAIQISFSST ILGNFEEEFL VNVNGSPEPV KLTIRGCVIG PTFHFNVPAL HFGDVSFATQ ELRDPQVLIP FQRFPHTLIC SLNNTSLIPM TYKLRIPGDG LGHKSISYCE QHVDYKRPSW TKEEISSMKP KEFTISPDCG TIRPQGFAAI RVTLCSNTVQ KYELALVVDV EGIGEEVLAL LITASAPELC NRKVMLSVLQ WKIHRAKRSL PRDTVAVT // ID H0YH52_HUMAN Unreviewed; 127 AA. AC H0YH52; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 14-DEC-2022, entry version 56. DE SubName: Full=Hydrocephalus-inducing protein homolog {ECO:0000313|Ensembl:ENSP00000446122.1}; DE Flags: Fragment; GN Name=HYDIN {ECO:0000313|Ensembl:ENSP00000446122.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000446122.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000446122.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000446122.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC009136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; H0YH52; -. DR ProteomicsDB; 38600; -. DR Antibodypedia; 66504; 48 antibodies from 12 providers. DR Ensembl; ENST00000542890.1; ENSP00000446122.1; ENSG00000157423.18. DR Ensembl; ENST00000635523.1; ENSP00000489503.1; ENSG00000283022.2. DR UCSC; uc059wso.1; human. DR HGNC; HGNC:19368; HYDIN. DR VEuPathDB; HostDB:ENSG00000157423; -. DR GeneTree; ENSGT00610000086095; -. DR HOGENOM; CLU_1986593_0_0_1; -. DR ChiTaRS; HYDIN; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000157423; Expressed in right uterine tube and 101 other tissues. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR033305; Hydin-like. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR23053; DLEC1 DELETED IN LUNG AND ESOPHAGEAL CANCER 1; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|PeptideAtlas:H0YH52}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000446122.1" SQ SEQUENCE 127 AA; 14176 MW; D34C05A41810CE98 CRC64; XKLRIPGDGL GHKSISYCEQ HVDYKRPSWT KEEISSMKPK EFTISPDCGT IRPQGFAAIR VTLCSNTVQK YELALVVDVE GIGEEVLALL ITASAPELCN RKVMLSVLQW KIHRAKRSLP RDTVAVT // ID J3QQJ7_HUMAN Unreviewed; 833 AA. AC J3QQJ7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 14-DEC-2022, entry version 62. DE SubName: Full=Hydrocephalus-inducing protein homolog {ECO:0000313|Ensembl:ENSP00000463767.1}; DE Flags: Fragment; GN Name=HYDIN {ECO:0000313|Ensembl:ENSP00000463767.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000463767.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000463767.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000463767.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC009136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; J3QQJ7; -. DR PeptideAtlas; J3QQJ7; -. DR Ensembl; ENST00000393552.6; ENSP00000463767.1; ENSG00000157423.18. DR Ensembl; ENST00000635262.1; ENSP00000489173.1; ENSG00000283022.2. DR UCSC; uc059wsj.1; human. DR HGNC; HGNC:19368; HYDIN. DR VEuPathDB; HostDB:ENSG00000157423; -. DR GeneTree; ENSGT00610000086095; -. DR HOGENOM; CLU_369583_0_0_1; -. DR ChiTaRS; HYDIN; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000157423; Expressed in right uterine tube and 101 other tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 5. DR InterPro; IPR031549; ASH. DR InterPro; IPR033305; Hydin-like. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR23053; DLEC1 DELETED IN LUNG AND ESOPHAGEAL CANCER 1; 1. DR Pfam; PF15780; ASH; 1. PE 1: Evidence at protein level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Proteomics identification {ECO:0007829|PeptideAtlas:J3QQJ7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 132..231 FT /note="ASH" FT /evidence="ECO:0000259|Pfam:PF15780" FT REGION 574..606 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000463767.1" SQ SEQUENCE 833 AA; 93021 MW; 5DA3DE8E6B643D2C CRC64; RTFANQRRLV QGDSKLFFNN VFTVEPLEGD VWPNSSAEIT VYFNPLEAKL YQQTIYCDIL GREIRLPLRI KGEGMGPKIH FNFELLDIGK VFTGSAHCYE AILYNKGSID ALFNMTPPTS ALGACFVFSP KEGIIEPSGV QAIQISFSST ILGNFEEEFL VNVNGSPEPV KLTIRGCVIG PTFHFNVPAL HFGDVSFGFP HTLICSLNNT SLIPMTYKLR IPGDGLGHKS ISYCEQHVDY KRPSWTKEEI SSMKPKEFTI SPDCGTIRPQ GFAAIRVTLC SNTVQKYELA LVVDVEGIGE EVLALLITAR CVVPALHLVN TEVDFGHCFL KYPYEKTLQL ANQDDLPGFY EVQPQVCEEV PTVLFSSPTP SGVISPSSTI HIPLVLETQV TGEHRSTVYI SIFGSQDPPL VCHLKSAGEG PVIYVHPNQV DFGNIYVLKD SSRILNLCNQ SFIPAFFQAH MAHKKSLWTI EPNEGMVPPE TDVQLALTAN LNDTLTFKDC VILDIENSST YRIPVQASGT GSTIVSDKPF APELNLGAHF SLDTHYYHFK LINKGRRIQQ LFWMNDSFRP QAKLSKKGRV KKGHAHVQPQ PSGSQEPRDP QSPVFHLHPA SMELYPGQAI DVILEGYSAT PRKPNSILKP DYQPLAIKNI STLPVNLLLS TSGPFFICET DKSLLPATPE PIKLEIDEEK NLLIKFDPSY RNDLNNWVAE EILAIKYVEH PQIDSLDLRG EVHYPNLSFE TKELDFGCIL NDTELIRYVT ITNCSPLVVK FRWFFLVNDE ENQIRFVTLP KKPYSAPVSQ MESIPATSEA ASPPAILVTV ESPEMDLNDF VKK // ID B4DZ93_HUMAN Unreviewed; 424 AA. AC B4DZ93; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-DEC-2022, entry version 33. DE SubName: Full=cDNA FLJ60984, highly similar to Deleted in lung and esophageal cancer protein1 {ECO:0000313|EMBL:BAG64005.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG64005.1}; RN [1] {ECO:0000313|EMBL:BAG64005.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Testis {ECO:0000313|EMBL:BAG64005.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., RA Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK302803; BAG64005.1; -; mRNA. DR AlphaFoldDB; B4DZ93; -. DR PeptideAtlas; B4DZ93; -. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro. DR InterPro; IPR033304; DLEC1. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR PANTHER; PTHR46348; DELETED IN LUNG AND ESOPHAGEAL CANCER PROTEIN 1; 1. DR PROSITE; PS50096; IQ; 1. PE 2: Evidence at transcript level; FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 282..309 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 424 AA; 48085 MW; D15B99C08DC6AC72 CRC64; METRSSKTRR SLASRTNECQ GTMWAPTSPP AGSSSPSQPT WKSSLYSSLA YSEAFHYSFA ARPRRLTQLA LAQRPEPQLL RLRPSSLRTQ DISHLLTGVF RNLYSAEVIG DEVSASLIKA RGSENERHEE FVDQLQQIRE LYKQRLDEFE MLERHITQAQ ARAIAENERV MSQAGVQDLE SLVRLPPVKS VSRWCIDSEL LRKHHLISPE DYYTDTVPFH SAPKGISLPG CSKLTFSCEK RSVQKKELNK KLEDSCRKKL AEFEDELDHT VDSLTWNLTP KAKERTREPL KKASQPTCEQ KASKRPGTVK RPRCWRFSIG SAPLTSITKI DAQVRGGETR QDYKDTRRFP LEAPSCALLF RPCRLPDTCP PFSLREAWRF LIAHAVGISV RCRSFAPSWA VCTNPPFSPT AAPYPVTIVL SPTR //