ID JHD2C_HUMAN Reviewed; 2540 AA. AC Q15652; A0T124; Q5SQZ8; Q5SQZ9; Q5SR00; Q7Z3E7; Q8N3U0; Q96KB9; Q9P2G7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 27-MAR-2024, entry version 178. DE RecName: Full=Probable JmjC domain-containing histone demethylation protein 2C; DE EC=1.14.11.-; DE AltName: Full=Jumonji domain-containing protein 1C; DE AltName: Full=Thyroid receptor-interacting protein 8; DE Short=TR-interacting protein 8; DE Short=TRIP-8; GN Name=JMJD1C; Synonyms=JHDM2C, KIAA1380, TRIP8; 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 3). RX PubMed=17353003; DOI=10.1016/j.abb.2007.01.017; RA Wolf S.S., Patchev V.K., Obendorf M.; RT "A novel variant of the putative demethylase gene, s-JMJD1C, is a RT coactivator of the AR."; RL Arch. Biochem. Biophys. 460:56-66(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 379-2540, AND VARIANTS THR-464 AND ASP-2535. RC TISSUE=Amygdala, and Cervix; 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=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-427. RC TISSUE=Embryo; 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] OF 1275-2540. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2030-2212, AND INTERACTION WITH THYROID RP RECEPTOR. RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974; RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.; RT "Two classes of proteins dependent on either the presence or absence of RT thyroid hormone for interaction with the thyroid hormone receptor."; RL Mol. Endocrinol. 9:243-254(1995). RN [7] RP IDENTIFICATION OF THE GENE. RX PubMed=14533015; RA Katoh M., Katoh M.; RT "Identification and characterization of TRIP8 gene in silico."; RL Int. J. Mol. Med. 12:817-821(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-376 AND SER-641, 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 [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; SER-373; SER-617; RP SER-638; SER-641; SER-652 AND SER-1989, AND IDENTIFICATION BY MASS RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501; THR-505; SER-601; RP SER-639; SER-641 AND SER-943, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, 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 [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2132 AND LYS-2136, 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). CC -!- FUNCTION: Probable histone demethylase that specifically demethylates CC 'Lys-9' of histone H3, thereby playing a central role in histone code. CC Demethylation of Lys residue generates formaldehyde and succinate. May CC be involved in hormone-dependent transcriptional activation, by CC participating in recruitment to androgen-receptor target genes (By CC similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Interacts specifically with the ligand-binding domain of the CC thyroid receptor (TR). Requires the presence of thyroid hormone for its CC interaction. {ECO:0000269|PubMed:7776974}. CC -!- INTERACTION: CC Q15652; P10275: AR; NbExp=4; IntAct=EBI-1224969, EBI-608057; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q15652-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15652-2; Sequence=VSP_018303, VSP_018304, VSP_018305; CC Name=3; Synonyms=s-JMJD1C; CC IsoId=Q15652-3; Sequence=VSP_043909; CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the CC association with nuclear receptors. {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 3]: May function as a tumor suppressor, reduced CC expression in breast cancer tumors. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC41741.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAD97921.1; 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; EF068222; ABK64187.1; -; mRNA. DR EMBL; BX537954; CAD97921.1; ALT_FRAME; mRNA. DR EMBL; AC022022; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL607128; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL713895; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK027280; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL831917; CAD38578.1; -; mRNA. DR EMBL; AB037801; BAA92618.1; -; mRNA. DR EMBL; L40411; AAC41741.1; ALT_FRAME; mRNA. DR CCDS; CCDS41532.1; -. [Q15652-1] DR CCDS; CCDS60538.1; -. [Q15652-3] DR RefSeq; NP_001269877.1; NM_001282948.1. [Q15652-3] DR RefSeq; NP_001305082.1; NM_001318153.1. DR RefSeq; NP_001305083.1; NM_001318154.1. [Q15652-3] DR RefSeq; NP_001309181.1; NM_001322252.1. DR RefSeq; NP_001309183.1; NM_001322254.1. DR RefSeq; NP_001309187.1; NM_001322258.1. DR RefSeq; NP_116165.1; NM_032776.2. [Q15652-1] DR RefSeq; XP_016871386.1; XM_017015897.1. [Q15652-3] DR RefSeq; XP_016871387.1; XM_017015898.1. [Q15652-3] DR PDB; 2YPD; X-ray; 2.10 A; A/B=2157-2540. DR PDB; 5FZO; X-ray; 1.84 A; A/B=2157-2500. DR PDBsum; 2YPD; -. DR PDBsum; 5FZO; -. DR AlphaFoldDB; Q15652; -. DR SMR; Q15652; -. DR BioGRID; 128677; 72. DR DIP; DIP-38114N; -. DR IntAct; Q15652; 23. DR MINT; Q15652; -. DR STRING; 9606.ENSP00000382204; -. DR BindingDB; Q15652; -. DR ChEMBL; CHEMBL3792271; -. DR GlyCosmos; Q15652; 18 sites, 2 glycans. DR GlyGen; Q15652; 35 sites, 2 O-linked glycans (35 sites). DR iPTMnet; Q15652; -. DR PhosphoSitePlus; Q15652; -. DR BioMuta; JMJD1C; -. DR DMDM; 85541650; -. DR EPD; Q15652; -. DR jPOST; Q15652; -. DR MassIVE; Q15652; -. DR MaxQB; Q15652; -. DR PaxDb; 9606-ENSP00000382204; -. DR PeptideAtlas; Q15652; -. DR ProteomicsDB; 60691; -. [Q15652-1] DR ProteomicsDB; 60692; -. [Q15652-2] DR ProteomicsDB; 60693; -. [Q15652-3] DR Pumba; Q15652; -. DR Antibodypedia; 28318; 165 antibodies from 28 providers. DR DNASU; 221037; -. DR Ensembl; ENST00000399262.7; ENSP00000382204.2; ENSG00000171988.20. [Q15652-1] DR Ensembl; ENST00000542921.5; ENSP00000444682.1; ENSG00000171988.20. [Q15652-3] DR GeneID; 221037; -. DR KEGG; hsa:221037; -. DR MANE-Select; ENST00000399262.7; ENSP00000382204.2; NM_032776.3; NP_116165.1. DR UCSC; uc001jmn.5; human. [Q15652-1] DR AGR; HGNC:12313; -. DR CTD; 221037; -. DR DisGeNET; 221037; -. DR GeneCards; JMJD1C; -. DR HGNC; HGNC:12313; JMJD1C. DR HPA; ENSG00000171988; Low tissue specificity. DR MalaCards; JMJD1C; -. DR MIM; 604503; gene. DR neXtProt; NX_Q15652; -. DR OpenTargets; ENSG00000171988; -. DR Orphanet; 567; 22q11.2 deletion syndrome. DR Orphanet; 91352; Germinoma of the central nervous system. DR PharmGKB; PA128394767; -. DR VEuPathDB; HostDB:ENSG00000171988; -. DR eggNOG; KOG1356; Eukaryota. DR GeneTree; ENSGT00940000158210; -. DR HOGENOM; CLU_228251_0_0_1; -. DR InParanoid; Q15652; -. DR OMA; PNKTSKM; -. DR OrthoDB; 3473445at2759; -. DR PhylomeDB; Q15652; -. DR TreeFam; TF324723; -. DR BioCyc; MetaCyc:ENSG00000171988-MONOMER; -. DR BRENDA; 1.14.11.65; 2681. DR PathwayCommons; Q15652; -. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; Q15652; -. DR SIGNOR; Q15652; -. DR BioGRID-ORCS; 221037; 34 hits in 1183 CRISPR screens. DR ChiTaRS; JMJD1C; human. DR GenomeRNAi; 221037; -. DR Pharos; Q15652; Tbio. DR PRO; PR:Q15652; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q15652; Protein. DR Bgee; ENSG00000171988; Expressed in calcaneal tendon and 202 other cell types or tissues. DR ExpressionAtlas; Q15652; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central. DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; TAS:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 2.60.120.650; Cupin; 1. DR InterPro; IPR045109; JHDM2-like. DR InterPro; IPR003347; JmjC_dom. DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1. DR PANTHER; PTHR12549:SF6; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 2C-RELATED; 1. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51184; JMJC; 1. DR Genevisible; Q15652; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; Dioxygenase; Iron; KW Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..2540 FT /note="Probable JmjC domain-containing histone FT demethylation protein 2C" FT /id="PRO_0000084284" FT DOMAIN 2274..2498 FT /note="JmjC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT ZN_FING 1846..1871 FT /note="C6-type" FT /evidence="ECO:0000255" FT REGION 278..478 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 631..656 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1242..1263 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1614..1692 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1971..2064 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 2066..2070 FT /note="LXXLL motif" FT COMPBIAS 278..310 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 311..424 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 435..456 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 457..478 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1614..1683 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1971..2005 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2015..2046 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2047..2064 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 2336 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT BINDING 2338 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT BINDING 2466 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT MOD_RES 317 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q69ZK6" FT MOD_RES 373 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 376 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 475 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q69ZK6" FT MOD_RES 501 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 505 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 601 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 617 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 638 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 639 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 652 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 943 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1989 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CROSSLNK 2132 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 2136 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..219 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_018303" FT VAR_SEQ 1..182 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17353003" FT /id="VSP_043909" FT VAR_SEQ 1692..1699 FT /note="TGIPRSVL -> SCHLVKTE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_018304" FT VAR_SEQ 1700..2540 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_018305" FT VARIANT 272 FT /note="A -> T (in dbSNP:rs34798625)" FT /id="VAR_049654" FT VARIANT 394 FT /note="E -> D (in dbSNP:rs35380596)" FT /id="VAR_049655" FT VARIANT 464 FT /note="S -> T (in dbSNP:rs10761725)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_049656" FT VARIANT 591 FT /note="M -> V (in dbSNP:rs41274072)" FT /id="VAR_061277" FT VARIANT 1393 FT /note="N -> Y (in dbSNP:rs9703886)" FT /id="VAR_049657" FT VARIANT 2400 FT /note="D -> E (in dbSNP:rs34491125)" FT /id="VAR_049658" FT VARIANT 2535 FT /note="E -> D (in dbSNP:rs1935)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_049659" FT CONFLICT 488 FT /note="T -> A (in Ref. 2; CAD97921)" FT /evidence="ECO:0000305" FT CONFLICT 779 FT /note="T -> A (in Ref. 2; CAD97921)" FT /evidence="ECO:0000305" FT CONFLICT 783 FT /note="T -> P (in Ref. 2; CAD97921)" FT /evidence="ECO:0000305" FT CONFLICT 2093 FT /note="S -> A (in Ref. 6; AAC41741)" FT /evidence="ECO:0000305" FT CONFLICT 2148 FT /note="Missing (in Ref. 5; BAA92618)" FT /evidence="ECO:0000305" FT STRAND 2159..2162 FT /evidence="ECO:0007829|PDB:5FZO" FT TURN 2163..2166 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2167..2170 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2178..2186 FT /evidence="ECO:0007829|PDB:5FZO" FT TURN 2187..2189 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2192..2194 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2197..2199 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2203..2206 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2208..2215 FT /evidence="ECO:0007829|PDB:5FZO" FT TURN 2225..2227 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2235..2243 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2245..2247 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2259..2261 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2264..2266 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2268..2273 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2275..2284 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2288..2291 FT /evidence="ECO:0007829|PDB:5FZO" FT TURN 2300..2302 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2305..2307 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2315..2319 FT /evidence="ECO:0007829|PDB:5FZO" FT TURN 2323..2326 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2332..2337 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2339..2350 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2360..2368 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2374..2381 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2387..2394 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2396..2398 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2399..2412 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2423..2426 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2433..2443 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2448..2453 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2457..2460 FT /evidence="ECO:0007829|PDB:5FZO" FT STRAND 2465..2481 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2484..2486 FT /evidence="ECO:0007829|PDB:5FZO" FT HELIX 2487..2496 FT /evidence="ECO:0007829|PDB:5FZO" SQ SEQUENCE 2540 AA; 284525 MW; 8B1727414D6B677F CRC64; MAVETRAELV GKRFLCVAVG DEARSERWES GRGWRSWRAG VIRAVSHRDS RNPDLAVYVE FDDLEWDKRE WVKVYEDFST FLVEYHLIWA KRNDPSQTQG SKSKQIQWPA LTFKPLVERN IPSSVTAVEF LVDKQLDFLT EDSAFQPYQD DIDSLNPVLR DNPQLHEEVK VWVKEQKVQE IFMQGPYSLN GYRVRVYRQD SATQWFTGII THHDLFTRTM IVMNDQVLEP QNVDPSMVQM TFLDDVVHSL LKGENIGITS RRRSRANQNV NAVHSHYTRA QANSPRPAMN SQAAVPKQNT HQQQQQRSIR PNKRKGSDSS IPDEEKMKEE KYDYISRGEN PKGKNKHLMN KRRKPEEDEK KLNMKRLRTD NVSDFSESSD SENSNKRIID NSSEQKPENE LKNKNTSKIN GEEGKPHNNE KAGEETLKNS QPPWDQIQED KKHEEAEKRK SVDTQLQEDM IIHSSEQSTV SDHNSNDLLP QECNMDKTHT MELLPKEKFV SRPPTPKCVI DITNDTNLEK VAQENSSTFG LQTLQKMDPN VSDSKHSIAN AKFLETAKKD SDQSWVSDVV KVDLTQSSVT NASSGNDHLN MEKEKYVSYI SPLSAVSVME DKLHKRSPPP ETIKSKLNTS VDTHKIKSSP SPEVVKPKIT HSPDSVKSKA TYVNSQATGE RRLANKIEHE LSRCSFHPIP TRSSTLETTK SPLIIDKNEH FTVYRDPALI GSETGANHIS PFLSQHPFPL HSSSHRTCLN PGTHHPALTP APHLLAGSSS QTPLPTINTH PLTSGPHHAV HHPHLLPTVL PGVPTASLLG GHPRLESAHA SSLSHLALAH QQQQQLLQHQ SPHLLGQAHP SASYNQLGLY PIIWQYPNGT HAYSGLGLPS SKWVHPENAV NAEASLRRNS PSPWLHQPTP VTSADGIGLL SHIPVRPSSA EPHRPLKITA HSSPPLTKTL VDHHKEELER KAFMEPLRSV ASTSAKNDLD LNRSQTGKDC HLHRHFVDPV LNQLQRPPQE TGERLNKYKE EHRRILQESI DVAPFTTKIK GLEGERENYS RVASSSSSPK SHIIKQDMDV ERSVSDLYKM KHSVPQSLPQ SNYFTTLSNS VVNEPPRSYP SKEVSNIYGD KQSNALAAAA ANPQTLTSFI TSLSKPPPLI KHQPESEGLV GKIPEHLPHQ IASHSVTTFR NDCRSPTHLT VSSTNTLRSM PALHRAPVFH PPIHHSLERK EGSYSSLSPP TLTPVMPVNA GGKVQESQKP PTLIPEPKDS QANFKSSSEQ SLTEMWRPNN NLSKEKTEWH VEKSSGKLQA AMASVIVRPS SSTKTDSMPA MQLASKDRVS ERSSAGAHKT DCLKLAEAGE TGRIILPNVN SDSVHTKSEK NFQAVSQGSV PSSVMSAVNT MCNTKTDVIT SAADTTSVSS WGGSEVISSL SNTILASTSS ECVSSKSVSQ PVAQKQECKV STTAPVTLAS SKTGSVVQPS SGFSGTTDFI HLKKHKAALA AAQYKSSNAS ETEPNAIKNQ TLSASLPLDS TVICSTINKA NSVGNGQASQ TSQPNYHTKL KKAWLTRHSE EDKNTNKMEN SGNSVSEIIK PCSVNLIAST SSDIQNSVDS KIIVDKYVKD DKVNRRKAKR TYESGSESGD SDESESKSEQ RTKRQPKPTY KKKQNDLQKR KGEIEEDLKP NGVLSRSAKE RSKLKLQSNS NTGIPRSVLK DWRKVKKLKQ TGESFLQDDS CCEIGPNLQK CRECRLIRSK KGEEPAHSPV FCRFYYFRRL SFSKNGVVRI DGFSSPDQYD DEAMSLWTHE NFEDDELDIE TSKYILDIIG DKFCQLVTSE KTALSWVKKD AKIAWKRAVR GVREMCDACE ATLFNIHWVC QKCGFVVCLD CYKAKERKSS RDKELYAWMK CVKGQPHDHK HLMPTQIIPG SVLTDLLDAM HTLREKYGIK SHCHCTNKQN LQVGNFPTMN GVSQVLQNVL NHSNKISLCM PESQQQNTPP KSEKNGGSSP ESDVGTDNKL TPPESQSPLH WLADLAEQKA REEKKENKEL TLENQIKEER EQDNSESPNG RTSPLVSQNN EQGSTLRDLL TTTAGKLRVG STDAGIAFAP VYSMGAPSSK SGRTMPNILD DIIASVVENK IPPSKTSKIN VKPELKEEPE ESIISAVDEN NKLYSDIPHS WICEKHILWL KDYKNSSNWK LFKECWKQGQ PAVVSGVHKK MNISLWKAES ISLDFGDHQA DLLNCKDSII SNANVKEFWD GFEEVSKRQK NKSGETVVLK LKDWPSGEDF KTMMPARYED LLKSLPLPEY CNPEGKFNLA SHLPGFFVRP DLGPRLCSAY GVVAAKDHDI GTTNLHIEVS DVVNILVYVG IAKGNGILSK AGILKKFEEE DLDDILRKRL KDSSEIPGAL WHIYAGKDVD KIREFLQKIS KEQGLEVLPE HDPIRDQSWY VNKKLRQRLL EEYGVRTCTL IQFLGDAIVL PAGALHQVQN FHSCIQVTED FVSPEHLVES FHLTQELRLL KEEINYDDKL QVKNILYHAV KEMVRALKIH EDEVEDMEEN //