ID Z280D_HUMAN Reviewed; 979 AA. AC Q6N043; A1L495; B2RMT6; Q6MZM6; Q6N085; Q6P2R6; Q7Z6J5; Q9H0U5; Q9HCI8; AC Q9NXS0; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 3. DT 27-MAR-2024, entry version 165. DE RecName: Full=Zinc finger protein 280D; DE AltName: Full=Suppressor of hairy wing homolog 4; DE AltName: Full=Zinc finger protein 634; GN Name=ZNF280D; Synonyms=KIAA1584, SUHW4, ZNF634; 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), AND VARIANT ILE-568. RC TISSUE=Brain; RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT ILE-568. RC TISSUE=Colon; 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 MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT RP ILE-568. RC TISSUE=Colon endothelium, Liver, and Uterine endothelium; 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 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND VARIANT RP ILE-568. RC TISSUE=Brain, Liver, Skin, 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND IDENTIFICATION BY RP 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 [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-74; LYS-126; LYS-210 AND RP LYS-292, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-126 AND LYS-210, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-740, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-34; LYS-74; LYS-87; RP LYS-126; LYS-140; LYS-189; LYS-210; LYS-223; LYS-233; LYS-275; LYS-284; RP LYS-550; LYS-740 AND LYS-976, 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). CC -!- FUNCTION: May function as a transcription factor. CC -!- INTERACTION: CC Q6N043-2; Q13185: CBX3; NbExp=3; IntAct=EBI-12027202, EBI-78176; CC Q6N043-2; P45973: CBX5; NbExp=3; IntAct=EBI-12027202, EBI-78219; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q6N043-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6N043-2; Sequence=VSP_017624; CC Name=3; CC IsoId=Q6N043-3; Sequence=VSP_017625, VSP_017626; CC Name=4; CC IsoId=Q6N043-4; Sequence=VSP_017623, VSP_017627, VSP_017628; CC Name=5; CC IsoId=Q6N043-5; Sequence=VSP_017622; CC Name=6; CC IsoId=Q6N043-6; Sequence=VSP_054317, VSP_054318; CC -!- SEQUENCE CAUTION: CC Sequence=BAB13410.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAE46003.1; Type=Erroneous initiation; Note=Extended 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; AB046804; BAB13410.1; ALT_INIT; mRNA. DR EMBL; AK000093; BAA90940.1; -; mRNA. DR EMBL; AL136634; CAB66569.1; -; mRNA. DR EMBL; BX640637; CAE45785.1; -; mRNA. DR EMBL; BX640707; CAE45827.1; -; mRNA. DR EMBL; BX641000; CAE46003.1; ALT_INIT; mRNA. DR EMBL; AC010999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090517; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090518; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015382; AAH15382.2; -; mRNA. DR EMBL; BC053649; AAH53649.2; -; mRNA. DR EMBL; BC064359; AAH64359.1; -; mRNA. DR EMBL; BC130451; AAI30452.1; -; mRNA. DR EMBL; BC136412; AAI36413.1; -; mRNA. DR CCDS; CCDS32245.1; -. [Q6N043-1] DR CCDS; CCDS42041.1; -. [Q6N043-2] DR CCDS; CCDS58364.1; -. [Q6N043-6] DR RefSeq; NP_001002843.1; NM_001002843.2. [Q6N043-2] DR RefSeq; NP_001002844.1; NM_001002844.2. [Q6N043-6] DR RefSeq; NP_001275517.1; NM_001288588.1. [Q6N043-1] DR RefSeq; NP_001275518.1; NM_001288589.1. [Q6N043-6] DR RefSeq; NP_060131.2; NM_017661.3. [Q6N043-1] DR RefSeq; XP_011520004.1; XM_011521702.1. DR RefSeq; XP_016877833.1; XM_017022344.1. DR RefSeq; XP_016877834.1; XM_017022345.1. DR AlphaFoldDB; Q6N043; -. DR BioGRID; 120173; 22. DR IntAct; Q6N043; 3. DR MINT; Q6N043; -. DR STRING; 9606.ENSP00000267807; -. DR GlyGen; Q6N043; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q6N043; -. DR PhosphoSitePlus; Q6N043; -. DR SwissPalm; Q6N043; -. DR BioMuta; ZNF280D; -. DR DMDM; 223634726; -. DR EPD; Q6N043; -. DR jPOST; Q6N043; -. DR MassIVE; Q6N043; -. DR MaxQB; Q6N043; -. DR PaxDb; 9606-ENSP00000267807; -. DR PeptideAtlas; Q6N043; -. DR ProteomicsDB; 66603; -. [Q6N043-1] DR ProteomicsDB; 66604; -. [Q6N043-2] DR ProteomicsDB; 66605; -. [Q6N043-3] DR ProteomicsDB; 66606; -. [Q6N043-4] DR ProteomicsDB; 66607; -. [Q6N043-5] DR ProteomicsDB; 69425; -. DR Pumba; Q6N043; -. DR Antibodypedia; 25170; 84 antibodies from 21 providers. DR DNASU; 54816; -. DR Ensembl; ENST00000267807.12; ENSP00000267807.7; ENSG00000137871.21. [Q6N043-1] DR Ensembl; ENST00000558067.5; ENSP00000454173.1; ENSG00000137871.21. [Q6N043-4] DR Ensembl; ENST00000558320.5; ENSP00000453706.1; ENSG00000137871.21. [Q6N043-6] DR Ensembl; ENST00000559237.5; ENSP00000454111.1; ENSG00000137871.21. [Q6N043-2] DR Ensembl; ENST00000560002.5; ENSP00000453636.1; ENSG00000137871.21. [Q6N043-3] DR GeneID; 54816; -. DR KEGG; hsa:54816; -. DR MANE-Select; ENST00000267807.12; ENSP00000267807.7; NM_017661.4; NP_060131.2. DR UCSC; uc002adu.5; human. [Q6N043-1] DR AGR; HGNC:25953; -. DR CTD; 54816; -. DR GeneCards; ZNF280D; -. DR HGNC; HGNC:25953; ZNF280D. DR HPA; ENSG00000137871; Low tissue specificity. DR neXtProt; NX_Q6N043; -. DR OpenTargets; ENSG00000137871; -. DR PharmGKB; PA162410004; -. DR VEuPathDB; HostDB:ENSG00000137871; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000158889; -. DR HOGENOM; CLU_010097_2_0_1; -. DR InParanoid; Q6N043; -. DR OMA; GDLMSKH; -. DR OrthoDB; 2883180at2759; -. DR PhylomeDB; Q6N043; -. DR TreeFam; TF331707; -. DR PathwayCommons; Q6N043; -. DR SignaLink; Q6N043; -. DR BioGRID-ORCS; 54816; 7 hits in 1181 CRISPR screens. DR ChiTaRS; ZNF280D; human. DR GeneWiki; SUHW4; -. DR GenomeRNAi; 54816; -. DR Pharos; Q6N043; Tdark. DR PRO; PR:Q6N043; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q6N043; Protein. DR Bgee; ENSG00000137871; Expressed in calcaneal tendon and 196 other cell types or tissues. DR ExpressionAtlas; Q6N043; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR InterPro; IPR025243; DUF4195. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24388; ZINC FINGER PROTEIN; 1. DR PANTHER; PTHR24388:SF34; ZINC FINGER PROTEIN 280D; 1. DR Pfam; PF13836; DUF4195; 1. DR SMART; SM00355; ZnF_C2H2; 9. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. DR Genevisible; Q6N043; HS. PE 1: Evidence at protein level; KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..979 FT /note="Zinc finger protein 280D" FT /id="PRO_0000227977" FT ZN_FING 321..343 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 358..381 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 388..412 FT /note="C2H2-type 3; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 418..441 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 449..469 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 89..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 157..236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 523..608 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 739..809 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 896..979 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 739..780 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 781..801 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 545 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 908 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q68FE8" FT MOD_RES 911 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q68FE8" FT CROSSLNK 32 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 34 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 74 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 87 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 126 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 140 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 189 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:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 223 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 233 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 284 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 292 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 550 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 740 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 976 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..759 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_017622" FT VAR_SEQ 1..296 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017623" FT VAR_SEQ 1..13 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10997877, FT ECO:0000303|PubMed:17974005" FT /id="VSP_017624" FT VAR_SEQ 128..158 FT /note="GYITNSSRVVSNKSSELLFDLTQDTGLSHYQ -> VSVSKTIRPAQGSIGCC FT LSISTVPSYNSGLS (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054317" FT VAR_SEQ 159..979 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054318" FT VAR_SEQ 579..592 FT /note="KPNGSKSKYKPKIS -> IVGAFTNALSVVPK (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_017625" FT VAR_SEQ 593..979 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_017626" FT VAR_SEQ 687..717 FT /note="GITLVCLNCDFLSDVSGLDNMATHLSQHKTH -> CVGGQIECDLPKLHKLV FT VEPRLTLGLLTPNF (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017627" FT VAR_SEQ 718..979 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017628" FT VARIANT 568 FT /note="V -> I (in dbSNP:rs28620278)" FT /evidence="ECO:0000269|PubMed:10997877, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17974005" FT /id="VAR_054314" FT VARIANT 778 FT /note="A -> V (in dbSNP:rs12900993)" FT /id="VAR_054315" FT VARIANT 781 FT /note="K -> I (in dbSNP:rs12901843)" FT /id="VAR_054316" FT VARIANT 785 FT /note="G -> A (in dbSNP:rs12900729)" FT /id="VAR_054317" FT CONFLICT 229 FT /note="S -> P (in Ref. 4; CAE46003)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="L -> W (in Ref. 4; CAE45785)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="A -> T (in Ref. 4; CAE45785)" FT /evidence="ECO:0000305" FT CONFLICT 544 FT /note="L -> P (in Ref. 3; BAA90940)" FT /evidence="ECO:0000305" FT CONFLICT 742 FT /note="E -> R (in Ref. 4; CAE45827)" FT /evidence="ECO:0000305" SQ SEQUENCE 979 AA; 109285 MW; 9B11A04F21298503 CRC64; MGDNPFQPKS NSKMAELFME CEEEELEPWQ KKVKEVEDDD DDEPIFVGEI SSSKPAISNI LNRVNPSSYS RGLKNGALSR GITAAFKPTS QHYTNPTSNP VPASPINFHP ESRSSDSSVI VQPFSKPGYI TNSSRVVSNK SSELLFDLTQ DTGLSHYQGG PTLSMAGMSE SSFLSKRPST SEVNNVNPKK PKPSESVSGA NSSAVLPSVK SPSVTSSQAM LAKGTNTSSN QSKNGTPFPR ACPKCNIHFN LLDPLKNHMK YCCPDMINNF LGLAKTEFSS TVNKNTTIDS EKGKLIMLVN DFYYGKHEGD VQEEQKTHTT FKCFSCLKIL KNNIRFMNHM KHHLELEKQS SESWENHTTC QHCYRQFPTP FQLQCHIEST HTPHEFSTIC KICELSFETE HVLLQHMKDN HKPGEMPYVC QVCNYRSSSF SDVETHFRTS HENTKNLLCP FCLKVIKIAT PYMHHYMKHQ KKGIHRCTKC RLQFLTCKEK MDHKTQHHRT FIKPKQLEGL PPGTKVTIRA SVGPLQSGAS PTPSISASAS TLQLSPPRTK NITAKNPAKS NTSKPNTVKS NASKPNTSKP NGSKSKYKPK ISNMQKKQST LASSNKKSKV NTALRNLRYR RGIHKCIECC SEIKDFANHF PTYVHCSFCR YNTSCSKAYV NHMMSFHSNR PSKRFCIFKK HSENLRGITL VCLNCDFLSD VSGLDNMATH LSQHKTHTCQ VVMQKVSVCI PTSEHLSELK KEAPAKEQEP VSKEIARPNM AERETETSNS ESKQDKAASS KEKNGCNANS FEGSSTTKSE ESITVSDKEN ETCLADQETG SKNIVSCDSN IGADKVEKKK QIQHVCQEME LKMCQSSENI ILSDQIKDHN SSEARFSSKN IKDLRLASDN VSIDQFLRKR HEPESVSSDV SEQGSIHLEP LTPSEVLEYE ATEILQKGSG DPSAKTDEVV SDQTDDIPGG NNPSTTEATV DLEDEKERS //