ID NADAP_HUMAN Reviewed; 742 AA. AC Q9BWU0; A0A087X0M4; A6NJ39; Q4KMT1; Q4KMX0; Q7Z5Q9; Q9NVN2; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Kanadaptin; DE AltName: Full=Human lung cancer oncogene 3 protein; DE Short=HLC-3; DE AltName: Full=Kidney anion exchanger adapter protein; DE AltName: Full=Solute carrier family 4 anion exchanger member 1 adapter protein; GN Name=SLC4A1AP; ORFNames=HLC3; 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), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=15764369; DOI=10.1080/09687860400011365; RA Kittanakom S., Keskanokwong T., Akkarapatumwong V., Yenchitsomanus P.-T., RA Reithmeier R.A.F.; RT "Human kanadaptin and kidney anion exchanger 1 (kAE1) do not interact in RT transfected HEK 293 cells."; RL Mol. Membr. Biol. 21:395-402(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-85. 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=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), AND VARIANT THR-85. 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-742. RA Kim J.W.; RT "Identification of a new oncogene in human lung cancer."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-412 AND SER-476, AND RP IDENTIFICATION BY 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 [10] RP IDENTIFICATION BY MASS 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-412, VARIANT RP [LARGE SCALE ANALYSIS] THR-85, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-258; SER-412 AND RP SER-658, 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-412, 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-90; SER-258; SER-412; RP SER-655 AND SER-658, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-90 AND SER-412, AND 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 [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-441, 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 [18] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 95-222. RG Joint center for structural genomics (JCSG); RT "Crystal structure of a FHA domain of kanadaptin (SLC4A1AP) from Homo RT sapiens at 1.55 A resolution."; RL Submitted (OCT-2012) to the PDB data bank. CC -!- INTERACTION: CC Q9BWU0; Q13418: ILK; NbExp=8; IntAct=EBI-1999704, EBI-747644; CC Q9BWU0; P15884: TCF4; NbExp=3; IntAct=EBI-1999704, EBI-533224; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15764369}. Cytoplasm CC {ECO:0000269|PubMed:15764369}. Note=Mainly nuclear. Small amounts are CC found in the cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=2; CC IsoId=Q9BWU0-2; Sequence=Displayed; CC Name=1; CC IsoId=Q9BWU0-1; Sequence=VSP_062158; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:15764369}. CC -!- MISCELLANEOUS: Isoform 2 is a prediction based on conservation with CC orthologs. {ECO:0000305}. CC -!- CAUTION: PubMed:15764369 initially suggested a role in targeting SLC4A1 CC (kidney anion exchanger 1) to the plasma membrane; it does not seem to CC do so as it does not interact with SLC4A1 and has no effect on SLC4A1 CC trafficking. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAN12269.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Band 3 entry; CC URL="https://en.wikipedia.org/wiki/Band_3"; 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; AY028435; AAK29177.1; -; mRNA. DR EMBL; AK001486; BAA91718.1; -; mRNA. DR EMBL; AC074091; AAX93203.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00555.1; -; Genomic_DNA. DR EMBL; BC098302; AAH98302.1; -; mRNA. DR EMBL; BC098358; AAH98358.1; -; mRNA. DR EMBL; BC099711; AAH99711.1; -; mRNA. DR EMBL; BC099739; AAH99739.1; -; mRNA. DR EMBL; AY117688; AAN12269.1; ALT_INIT; mRNA. DR RefSeq; NP_060628.2; NM_018158.2. [Q9BWU0-2] DR PDB; 4H87; X-ray; 1.55 A; A/B=95-222. DR PDBsum; 4H87; -. DR AlphaFoldDB; Q9BWU0; -. DR SMR; Q9BWU0; -. DR BioGRID; 116605; 128. DR IntAct; Q9BWU0; 35. DR MINT; Q9BWU0; -. DR STRING; 9606.ENSP00000479964; -. DR GlyCosmos; Q9BWU0; 1 site, 1 glycan. DR GlyGen; Q9BWU0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BWU0; -. DR MetOSite; Q9BWU0; -. DR PhosphoSitePlus; Q9BWU0; -. DR BioMuta; SLC4A1AP; -. DR DMDM; 74724887; -. DR EPD; Q9BWU0; -. DR jPOST; Q9BWU0; -. DR MassIVE; Q9BWU0; -. DR MaxQB; Q9BWU0; -. DR PaxDb; 9606-ENSP00000479964; -. DR PeptideAtlas; Q9BWU0; -. DR ProteomicsDB; 79316; -. DR Pumba; Q9BWU0; -. DR Antibodypedia; 28720; 148 antibodies from 25 providers. DR DNASU; 22950; -. DR Ensembl; ENST00000326019.11; ENSP00000323837.7; ENSG00000163798.14. [Q9BWU0-2] DR Ensembl; ENST00000618046.4; ENSP00000483501.1; ENSG00000163798.14. [Q9BWU0-2] DR GeneID; 22950; -. DR KEGG; hsa:22950; -. DR MANE-Select; ENST00000326019.11; ENSP00000323837.7; NM_018158.3; NP_060628.3. DR UCSC; uc002rlk.5; human. [Q9BWU0-2] DR AGR; HGNC:13813; -. DR CTD; 22950; -. DR DisGeNET; 22950; -. DR GeneCards; SLC4A1AP; -. DR HGNC; HGNC:13813; SLC4A1AP. DR HPA; ENSG00000163798; Low tissue specificity. DR MIM; 602655; gene. DR neXtProt; NX_Q9BWU0; -. DR OpenTargets; ENSG00000163798; -. DR PharmGKB; PA37811; -. DR VEuPathDB; HostDB:ENSG00000163798; -. DR eggNOG; KOG1881; Eukaryota. DR GeneTree; ENSGT00940000155320; -. DR HOGENOM; CLU_015909_2_1_1; -. DR InParanoid; Q9BWU0; -. DR OMA; QQAIWTF; -. DR OrthoDB; 126345at2759; -. DR PhylomeDB; Q9BWU0; -. DR TreeFam; TF314854; -. DR PathwayCommons; Q9BWU0; -. DR SignaLink; Q9BWU0; -. DR BioGRID-ORCS; 22950; 18 hits in 1167 CRISPR screens. DR ChiTaRS; SLC4A1AP; human. DR GenomeRNAi; 22950; -. DR Pharos; Q9BWU0; Tdark. DR PRO; PR:Q9BWU0; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9BWU0; Protein. DR Bgee; ENSG00000163798; Expressed in calcaneal tendon and 108 other cell types or tissues. DR ExpressionAtlas; Q9BWU0; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR CDD; cd19856; DSRM_Kanadaptin; 1. DR CDD; cd22677; FHA_Kanadaptin; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 3.30.160.20; -; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR23308:SF53; KANADAPTIN-RELATED; 1. DR PANTHER; PTHR23308; NUCLEAR INHIBITOR OF PROTEIN PHOSPHATASE-1; 1. DR Pfam; PF00035; dsrm; 1. DR Pfam; PF00498; FHA; 1. DR SMART; SM00240; FHA; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR Genevisible; Q9BWU0; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Coiled coil; Cytoplasm; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..742 FT /note="Kanadaptin" FT /id="PRO_0000076268" FT DOMAIN 135..195 FT /note="FHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086" FT REGION 1..112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 254..282 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 565..742 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 443..476 FT /evidence="ECO:0000255" FT COMPBIAS 1..15 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..61 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 591..605 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 606..623 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 640..667 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 685..699 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 28 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 258 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 MOD_RES 412 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 476 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 655 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 658 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 441 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1 FT /note="M -> MLAPLRNAPGREGATSPSPPTDATGSLGEWDVDRNVKTEGWVSKERI FT SKLHRLRM (in isoform 1)" FT /id="VSP_062158" FT VARIANT 85 FT /note="P -> T (in dbSNP:rs9678851)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:19690332" FT /id="VAR_024748" FT VARIANT 127 FT /note="R -> C (in dbSNP:rs9679004)" FT /id="VAR_051219" FT CONFLICT 57..61 FT /note="SNSGE -> PIAKP (in Ref. 6; AAN12269)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="G -> R (in Ref. 2; AAK29177)" FT /evidence="ECO:0000305" FT CONFLICT 305 FT /note="Q -> R (in Ref. 5; AAH98358)" FT /evidence="ECO:0000305" FT CONFLICT 319 FT /note="A -> V (in Ref. 2; AAK29177)" FT /evidence="ECO:0000305" FT CONFLICT 390 FT /note="L -> I (in Ref. 6; AAN12269)" FT /evidence="ECO:0000305" FT STRAND 168..173 FT /evidence="ECO:0007829|PDB:4H87" FT STRAND 176..182 FT /evidence="ECO:0007829|PDB:4H87" FT STRAND 187..194 FT /evidence="ECO:0007829|PDB:4H87" FT STRAND 197..200 FT /evidence="ECO:0007829|PDB:4H87" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:4H87" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:4H87" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:4H87" FT STRAND 262..265 FT /evidence="ECO:0007829|PDB:4H87" FT STRAND 269..275 FT /evidence="ECO:0007829|PDB:4H87" SQ SEQUENCE 742 AA; 82890 MW; C668F8F365575AC1 CRC64; MADILSQSET LASQDLSGDF KKPALPVSPA ARSKAPASSS SNPEEVQKEG PTALQDSNSG EPDIPPPQPD CGDFRSLQEE QSRPPTAVSS PGGPARAPPY QEPPWGGPAT APYSLETLKG GTILGTRSLK GTSYCLFGRL SGCDVCLEHP SVSRYHAVLQ HRASGPDGEC DSNGPGFYLY DLGSTHGTFL NKTRIPPRTY CRVHVGHVVR FGGSTRLFIL QGPEEDREAE SELTVTQLKE LRKQQQILLE KKMLGEDSDE EEEMDTSERK INAGSQDDEM GCTWGMGEDA VEDDAEENPI VLEFQQEREA FYIKDPKKAL QGFFDREGEE LEYEFDEQGH STWLCRVRLP VDDSTGKQLV AEAIHSGKKK EAMIQCSLEA CRILDTLGLL RQEAVSRKRK AKNWEDEDFY DSDDDTFLDR TGLIEKKRLN RMKKAGKIDE KPETFESLVA KLNDAERELS EISERLKASS QVLSESPSQD SLDAFMSEMK SGSTLDGVSR KKLHLRTFEL RKEQQRLKGL IKIVKPAEIP ELKKTETQTT GAENKAKKLT LPLFGAMKGG SKFKLKTGTV GKLPPKRPEL PPTLMRMKDE PEVEEEEEEE EEEEKEKEEH EKKKLEDGSL SRPQPEIEPE AAVQEMRPPT DLTHFKETQT HENMSQLSEE EQNKDYQDCS KTTSLCAGPS ASKNEYEKSR GELKKKKTPG PGKLPPTLSS KYPEDDPDYC VWVPPEGQSG DGRTHLNDKY GY //