ID   HOP_HUMAN               Reviewed;          73 AA.
AC   Q9BPY8; A8K0Z2; E9PB55; G3V294; Q8N0V6; Q96CI1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   18-JUL-2018, entry version 136.
DE   RecName: Full=Homeodomain-only protein;
DE   AltName: Full=Lung cancer-associated Y protein;
DE   AltName: Full=Not expressed in choriocarcinoma protein 1;
DE   AltName: Full=Odd homeobox protein 1;
GN   Name=HOPX; Synonyms=HOD, HOP, LAGY, NECC1, OB1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Heart;
RX   PubMed=14516659; DOI=10.1016/S0925-4773(03)00090-X;
RA   Adu J., Leong F.T., Smith N.R., Leek J.P., Markham A.F.,
RA   Robinson P.A., Mighell A.J.;
RT   "Expression of mOb1, a novel atypical 73 amino acid K50-homeodomain
RT   protein, during mouse development.";
RL   Mech. Dev. 119:S43-S47(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   POSSIBLE INVOLVEMENT IN CHORIOCARCINOMA.
RX   PubMed=12573257; DOI=10.1016/S0888-7543(02)00011-3;
RA   Asanoma K., Matsuda T., Kondo H., Kato K., Kishino T., Niikawa N.,
RA   Wake N., Kato H.;
RT   "NECC1, a candidate choriocarcinoma suppressor gene that encodes a
RT   homeodomain consensus motif.";
RL   Genomics 81:15-25(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   POSSIBLE INVOLVEMENT IN LUNG CANCER.
RX   PubMed=12759545; DOI=10.1159/000070306;
RA   Chen Y., Petersen S., Pacyna-Gengelbach M., Pietas A., Petersen I.;
RT   "Identification of a novel homeobox-containing gene, LAGY, which is
RT   downregulated in lung cancer.";
RL   Oncology 64:450-458(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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 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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=B-cell;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INVOLVEMENT IN HEAD AND NECK SQUAMOUS CELL CARCINOMA.
RX   PubMed=15213722; DOI=10.1038/sj.bjc.6601952;
RA   Lemaire F., Millon R., Muller D., Rabouel Y., Bracco L., Abecassis J.,
RA   Wasylyk B.;
RT   "Loss of HOP tumour suppressor expression in head and neck squamous
RT   cell carcinoma.";
RL   Br. J. Cancer 91:258-261(2004).
RN   [8]
RP   INVOLVEMENT IN ORAL SQUAMOUS CELL CARCINOMA.
RX   PubMed=15381369; DOI=10.1016/j.cancergencyto.2004.01.026;
RA   Toruner G.A., Ulger C., Alkan M., Galante A.T., Rinaggio J., Wilk R.,
RA   Tian B., Soteropoulos P., Hameed M.R., Schwalb M.N., Dermody J.J.;
RT   "Association between gene expression profile and tumor invasion in
RT   oral squamous cell carcinoma.";
RL   Cancer Genet. Cytogenet. 154:27-35(2004).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH HSPA1A; HSPA1B AND HSPA8.
RX   PubMed=27708256; DOI=10.1038/ncomms12882;
RA   Seo J.H., Park J.H., Lee E.J., Vo T.T., Choi H., Kim J.Y., Jang J.K.,
RA   Wee H.J., Lee H.S., Jang S.H., Park Z.Y., Jeong J., Lee K.J.,
RA   Seok S.H., Park J.Y., Lee B.J., Lee M.N., Oh G.T., Kim K.W.;
RT   "ARD1-mediated Hsp70 acetylation balances stress-induced protein
RT   refolding and degradation.";
RL   Nat. Commun. 7:12882-12882(2016).
CC   -!- FUNCTION: Atypical homeodomain protein which does not bind DNA and
CC       is required to modulate cardiac growth and development. Acts via
CC       its interaction with SRF, thereby modulating the expression of
CC       SRF-dependent cardiac-specific genes and cardiac development.
CC       Prevents SRF-dependent transcription either by inhibiting SRF
CC       binding to DNA or by recruiting histone deacetylase (HDAC)
CC       proteins that prevent transcription by SRF. Overexpression causes
CC       cardiac hypertrophy (By similarity). May act as a tumor
CC       suppressor. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone
CC       proteins and assists in chaperone-mediated protein refolding
CC       (PubMed:27708256). {ECO:0000250|UniProtKB:Q8R1H0,
CC       ECO:0000269|PubMed:27708256}.
CC   -!- SUBUNIT: Interacts with serum response factor (SRF). Component of
CC       a large complex containing histone deacetylases such as HDAC2 (By
CC       similarity). Interacts with the acetylated forms of HSPA1A and
CC       HSPA1B. Interacts with HSPA8 (PubMed:27708256).
CC       {ECO:0000250|UniProtKB:Q8R1H0, ECO:0000269|PubMed:27708256}.
CC   -!- INTERACTION:
CC       Q99081:TCF12; NbExp=3; IntAct=EBI-10295883, EBI-722877;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8R1H0}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q8R1H0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=A;
CC         IsoId=Q9BPY8-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=Q9BPY8-2; Sequence=VSP_012659;
CC         Note=Ref.1 (AAM46830/AAM46831) sequences are in conflict in
CC         position: 76:P->L. {ECO:0000305};
CC       Name=3;
CC         IsoId=Q9BPY8-3; Sequence=VSP_047290;
CC         Note=Gene prediction based on EST data.;
CC       Name=4;
CC         IsoId=Q9BPY8-4; Sequence=VSP_047290, VSP_012659;
CC         Note=Gene prediction based on EST data.;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the heart,
CC       brain, placenta, lung, skeletal and smooth muscles, uterus,
CC       urinary bladder, kidney and spleen. Down-regulated in some types
CC       of cancer such as lung cancer, choriocarcinoma, head and neck
CC       squamous cell carcinoma and oral squamous cell carcinoma.
CC       {ECO:0000269|PubMed:12573257, ECO:0000269|PubMed:12759545}.
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DR   EMBL; AF492675; AAM46827.1; -; mRNA.
DR   EMBL; AF492676; AAM46828.1; -; mRNA.
DR   EMBL; AF492677; AAM46829.1; -; mRNA.
DR   EMBL; AF492678; AAM46830.1; -; mRNA.
DR   EMBL; AF492679; AAM46831.1; -; mRNA.
DR   EMBL; AF492680; AAM46832.1; -; mRNA.
DR   EMBL; AF492681; AAM46833.1; -; mRNA.
DR   EMBL; AB059408; BAB40926.1; -; mRNA.
DR   EMBL; AB059409; BAB40927.1; -; mRNA.
DR   EMBL; AB059410; BAB40928.1; -; mRNA.
DR   EMBL; AF454763; AAL56613.1; -; mRNA.
DR   EMBL; AK289707; BAF82396.1; -; mRNA.
DR   EMBL; AC108215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014225; AAH14225.1; -; mRNA.
DR   CCDS; CCDS3507.1; -. [Q9BPY8-1]
DR   CCDS; CCDS47062.1; -. [Q9BPY8-3]
DR   CCDS; CCDS54767.1; -. [Q9BPY8-4]
DR   RefSeq; NP_001138931.1; NM_001145459.1. [Q9BPY8-1]
DR   RefSeq; NP_001138932.1; NM_001145460.1. [Q9BPY8-4]
DR   RefSeq; NP_115884.4; NM_032495.5. [Q9BPY8-3]
DR   RefSeq; NP_631957.1; NM_139211.4. [Q9BPY8-1]
DR   RefSeq; NP_631958.1; NM_139212.3. [Q9BPY8-1]
DR   RefSeq; XP_016864218.1; XM_017008729.1.
DR   RefSeq; XP_016864219.1; XM_017008730.1. [Q9BPY8-1]
DR   RefSeq; XP_016864220.1; XM_017008731.1. [Q9BPY8-1]
DR   RefSeq; XP_016864221.1; XM_017008732.1. [Q9BPY8-1]
DR   RefSeq; XP_016864222.1; XM_017008733.1. [Q9BPY8-1]
DR   RefSeq; XP_016864223.1; XM_017008734.1. [Q9BPY8-1]
DR   UniGene; Hs.619396; -.
DR   ProteinModelPortal; Q9BPY8; -.
DR   SMR; Q9BPY8; -.
DR   BioGrid; 124117; 11.
DR   IntAct; Q9BPY8; 2.
DR   STRING; 9606.ENSP00000450527; -.
DR   iPTMnet; Q9BPY8; -.
DR   PhosphoSitePlus; Q9BPY8; -.
DR   BioMuta; HOPX; -.
DR   DMDM; 60392394; -.
DR   PaxDb; Q9BPY8; -.
DR   PeptideAtlas; Q9BPY8; -.
DR   PRIDE; Q9BPY8; -.
DR   ProteomicsDB; 78595; -.
DR   ProteomicsDB; 78596; -. [Q9BPY8-2]
DR   DNASU; 84525; -.
DR   Ensembl; ENST00000317745; ENSP00000315198; ENSG00000171476. [Q9BPY8-1]
DR   Ensembl; ENST00000337881; ENSP00000337330; ENSG00000171476. [Q9BPY8-1]
DR   Ensembl; ENST00000381255; ENSP00000370654; ENSG00000171476. [Q9BPY8-1]
DR   Ensembl; ENST00000381260; ENSP00000370659; ENSG00000171476. [Q9BPY8-2]
DR   Ensembl; ENST00000420433; ENSP00000396275; ENSG00000171476. [Q9BPY8-3]
DR   Ensembl; ENST00000503639; ENSP00000424101; ENSG00000171476. [Q9BPY8-1]
DR   Ensembl; ENST00000508121; ENSP00000422175; ENSG00000171476. [Q9BPY8-1]
DR   Ensembl; ENST00000553379; ENSP00000452340; ENSG00000171476. [Q9BPY8-1]
DR   Ensembl; ENST00000554144; ENSP00000450527; ENSG00000171476. [Q9BPY8-4]
DR   Ensembl; ENST00000555760; ENSP00000452098; ENSG00000171476. [Q9BPY8-1]
DR   Ensembl; ENST00000556376; ENSP00000451794; ENSG00000171476. [Q9BPY8-1]
DR   Ensembl; ENST00000556614; ENSP00000452003; ENSG00000171476. [Q9BPY8-1]
DR   GeneID; 84525; -.
DR   KEGG; hsa:84525; -.
DR   UCSC; uc003hbz.3; human. [Q9BPY8-1]
DR   CTD; 84525; -.
DR   DisGeNET; 84525; -.
DR   EuPathDB; HostDB:ENSG00000171476.21; -.
DR   GeneCards; HOPX; -.
DR   HGNC; HGNC:24961; HOPX.
DR   HPA; CAB018632; -.
DR   HPA; HPA030180; -.
DR   MIM; 607275; gene.
DR   neXtProt; NX_Q9BPY8; -.
DR   OpenTargets; ENSG00000171476; -.
DR   PharmGKB; PA162391564; -.
DR   eggNOG; KOG0490; Eukaryota.
DR   eggNOG; ENOG410YIJ3; LUCA.
DR   GeneTree; ENSGT00390000017143; -.
DR   HOGENOM; HOG000112932; -.
DR   HOVERGEN; HBG051921; -.
DR   InParanoid; Q9BPY8; -.
DR   OMA; KVSKHPD; -.
DR   OrthoDB; EOG091G1BXE; -.
DR   PhylomeDB; Q9BPY8; -.
DR   SIGNOR; Q9BPY8; -.
DR   ChiTaRS; HOPX; human.
DR   GeneWiki; HOPX; -.
DR   GenomeRNAi; 84525; -.
DR   PRO; PR:Q9BPY8; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000171476; -.
DR   CleanEx; HS_HOPX; -.
DR   Genevisible; Q9BPY8; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:CAFA.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0001829; P:trophectodermal cell differentiation; IDA:MGI.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR039162; HOPX.
DR   PANTHER; PTHR21408; PTHR21408; 1.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Cytoplasm;
KW   Developmental protein; Homeobox; Nucleus; Proto-oncogene;
KW   Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1     73       Homeodomain-only protein.
FT                                /FTId=PRO_0000049129.
FT   DNA_BIND      3     62       Homeobox; atypical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00108}.
FT   VAR_SEQ       1      1       M -> MLIFLGCYRRRLEERAGTM (in isoform 3
FT                                and isoform 4). {ECO:0000305}.
FT                                /FTId=VSP_047290.
FT   VAR_SEQ      49     73       KWFKQRLAKWRRSEGLPSECRSVTD -> GSDLISRSKIWH
FT                                PESSPQREGYPHDSLPCLAFDYFSLLPPQCKEMV (in
FT                                isoform 2 and isoform 4).
FT                                {ECO:0000303|PubMed:14516659}.
FT                                /FTId=VSP_012659.
FT   CONFLICT     72     72       T -> I (in Ref. 6; AAH14225).
FT                                {ECO:0000305}.
SQ   SEQUENCE   73 AA;  8260 MW;  CE65E4D2A8972022 CRC64;
     MSAETASGPT EDQVEILEYN FNKVDKHPDS TTLCLIAAEA GLSEEETQKW FKQRLAKWRR
     SEGLPSECRS VTD
//