JHD2C_HUMAN
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 03-AUG-2022, entry version 169.
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};
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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; 50.
DR DIP; DIP-38114N; -.
DR IntAct; Q15652; 21.
DR MINT; Q15652; -.
DR STRING; 9606.ENSP00000382204; -.
DR BindingDB; Q15652; -.
DR ChEMBL; CHEMBL3792271; -.
DR GlyGen; Q15652; 18 sites, 2 O-linked glycans (18 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; Q15652; -.
DR PeptideAtlas; Q15652; -.
DR PRIDE; Q15652; -.
DR ProteomicsDB; 60691; -. [Q15652-1]
DR ProteomicsDB; 60692; -. [Q15652-2]
DR ProteomicsDB; 60693; -. [Q15652-3]
DR Antibodypedia; 28318; 143 antibodies from 27 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 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; DDKINRR; -.
DR OrthoDB; 1185631at2759; -.
DR PhylomeDB; Q15652; -.
DR TreeFam; TF324723; -.
DR BioCyc; MetaCyc:ENSG00000171988-MON; -.
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; 24 hits in 1097 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 200 other tissues.
DR ExpressionAtlas; Q15652; baseline and differential.
DR Genevisible; Q15652; HS.
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 H3-methyl-lysine-9 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
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
