PRD10_HUMAN
ID PRD10_HUMAN Reviewed; 1147 AA.
AC Q9NQV6; B7ZL71; G3XAE5; J3KP23; Q17R90; Q2KHR4; Q863Z2; Q9NXI4; Q9ULI9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=PR domain zinc finger protein 10;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 10;
DE AltName: Full=Tristanin;
GN Name=PRDM10; Synonyms=KIAA1231, PFM7, TRIS;
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 2).
RC TISSUE=Brain;
RX PubMed=12175877; DOI=10.1016/s0736-5748(02)00055-2;
RA Siegel D.A., Huang M.K., Becker S.F.;
RT "Ectopic dendrite initiation: CNS pathogenesis as a model of CNS
RT development.";
RL Int. J. Dev. Neurosci. 20:373-389(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10668202; DOI=10.14670/hh-15.109;
RA Jiang G.L., Huang S.;
RT "The yin-yang of PR-domain family genes in tumorigenesis.";
RL Histol. Histopathol. 15:109-117(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND VARIANT ALA-573.
RC TISSUE=Amygdala;
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
RP ALA-573.
RC TISSUE=Brain, 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 268-1147 (ISOFORM 6), AND VARIANT
RP ALA-573.
RC TISSUE=Colon mucosa;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424 AND THR-428, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-380, 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 188-339.
RG Structural genomics consortium (SGC);
RT "Methyltransferase domain of human PR domain-containing protein 10.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NQV6; Q04864: REL; NbExp=3; IntAct=EBI-10312448, EBI-307352;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=3;
CC IsoId=Q9NQV6-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQV6-2; Sequence=VSP_036351, VSP_035655, VSP_035656;
CC Name=1;
CC IsoId=Q9NQV6-1; Sequence=VSP_036351;
CC Name=4;
CC IsoId=Q9NQV6-4; Sequence=VSP_035655, VSP_036352;
CC Name=5;
CC IsoId=Q9NQV6-5; Sequence=VSP_036351, VSP_036352;
CC Name=6;
CC IsoId=Q9NQV6-6; Sequence=VSP_035655, VSP_036352, VSP_036353;
CC Name=7;
CC IsoId=Q9NQV6-7; Sequence=VSP_036352;
CC -!- DOMAIN: The SET domain is degenerated, suggesting that it has lost
CC methyltransferase activity.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF503171; AAP30847.1; -; mRNA.
DR EMBL; AF275817; AAF87243.1; -; mRNA.
DR EMBL; AB033057; BAA86545.2; -; mRNA.
DR EMBL; BX648944; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AP003041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67761.1; -; Genomic_DNA.
DR EMBL; BC112934; AAI12935.1; -; mRNA.
DR EMBL; BC117415; AAI17416.1; -; mRNA.
DR EMBL; BC143612; AAI43613.1; -; mRNA.
DR EMBL; AK000234; BAA91026.1; ALT_INIT; mRNA.
DR CCDS; CCDS44771.1; -. [Q9NQV6-7]
DR CCDS; CCDS44772.1; -. [Q9NQV6-1]
DR CCDS; CCDS8484.1; -. [Q9NQV6-4]
DR CCDS; CCDS8485.1; -. [Q9NQV6-2]
DR RefSeq; NP_064613.2; NM_020228.2. [Q9NQV6-7]
DR RefSeq; NP_955469.1; NM_199437.1. [Q9NQV6-4]
DR RefSeq; NP_955470.1; NM_199438.1. [Q9NQV6-1]
DR RefSeq; NP_955471.1; NM_199439.1. [Q9NQV6-2]
DR PDB; 3IHX; X-ray; 2.50 A; A/B/C/D=188-339.
DR PDBsum; 3IHX; -.
DR AlphaFoldDB; Q9NQV6; -.
DR SMR; Q9NQV6; -.
DR BioGRID; 121298; 67.
DR IntAct; Q9NQV6; 23.
DR MINT; Q9NQV6; -.
DR STRING; 9606.ENSP00000351686; -.
DR GlyGen; Q9NQV6; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; Q9NQV6; -.
DR PhosphoSitePlus; Q9NQV6; -.
DR BioMuta; PRDM10; -.
DR DMDM; 442570289; -.
DR EPD; Q9NQV6; -.
DR jPOST; Q9NQV6; -.
DR MassIVE; Q9NQV6; -.
DR MaxQB; Q9NQV6; -.
DR PaxDb; Q9NQV6; -.
DR PeptideAtlas; Q9NQV6; -.
DR PRIDE; Q9NQV6; -.
DR ProteomicsDB; 33727; -.
DR ProteomicsDB; 82192; -. [Q9NQV6-3]
DR ProteomicsDB; 82193; -. [Q9NQV6-1]
DR ProteomicsDB; 82194; -. [Q9NQV6-2]
DR ProteomicsDB; 82195; -. [Q9NQV6-4]
DR ProteomicsDB; 82196; -. [Q9NQV6-5]
DR ProteomicsDB; 82197; -. [Q9NQV6-6]
DR ABCD; Q9NQV6; 1 sequenced antibody.
DR Antibodypedia; 19222; 239 antibodies from 33 providers.
DR DNASU; 56980; -.
DR Ensembl; ENST00000304538.10; ENSP00000302669.6; ENSG00000170325.16. [Q9NQV6-2]
DR Ensembl; ENST00000358825.9; ENSP00000351686.5; ENSG00000170325.16. [Q9NQV6-7]
DR Ensembl; ENST00000360871.8; ENSP00000354118.3; ENSG00000170325.16. [Q9NQV6-4]
DR Ensembl; ENST00000423662.6; ENSP00000398431.2; ENSG00000170325.16. [Q9NQV6-1]
DR Ensembl; ENST00000526082.5; ENSP00000432237.1; ENSG00000170325.16. [Q9NQV6-5]
DR GeneID; 56980; -.
DR KEGG; hsa:56980; -.
DR MANE-Select; ENST00000360871.8; ENSP00000354118.3; NM_199437.2; NP_955469.1. [Q9NQV6-4]
DR UCSC; uc001qfj.4; human. [Q9NQV6-3]
DR CTD; 56980; -.
DR DisGeNET; 56980; -.
DR GeneCards; PRDM10; -.
DR HGNC; HGNC:13995; PRDM10.
DR HPA; ENSG00000170325; Low tissue specificity.
DR MIM; 618319; gene.
DR neXtProt; NX_Q9NQV6; -.
DR OpenTargets; ENSG00000170325; -.
DR PharmGKB; PA33708; -.
DR VEuPathDB; HostDB:ENSG00000170325; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158740; -.
DR InParanoid; Q9NQV6; -.
DR OMA; IRVIFQN; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF350894; -.
DR PathwayCommons; Q9NQV6; -.
DR SignaLink; Q9NQV6; -.
DR BioGRID-ORCS; 56980; 339 hits in 1083 CRISPR screens.
DR ChiTaRS; PRDM10; human.
DR EvolutionaryTrace; Q9NQV6; -.
DR GenomeRNAi; 56980; -.
DR Pharos; Q9NQV6; Tbio.
DR PRO; PR:Q9NQV6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NQV6; protein.
DR Bgee; ENSG00000170325; Expressed in secondary oocyte and 180 other tissues.
DR ExpressionAtlas; Q9NQV6; baseline and differential.
DR Genevisible; Q9NQV6; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; IDA:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd19194; PR-SET_PRDM10; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044403; PRDM10_PR/SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 4.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1147
FT /note="PR domain zinc finger protein 10"
FT /id="PRO_0000047767"
FT DOMAIN 208..326
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 355..377
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 530..552
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 560..582
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 588..610
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 616..639
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 644..666
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 672..695
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 727..750
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 772..795
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 834..857
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 380
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..97
FT /note="MDSKDESSHVWPTSAEHEQNAAQVHFVPDTGTVAQIVYTDDQVRPPQQVVYT
FT ADGASYTSVDGPEHTLVYIHPVEAAQTLFTDPGQVAYVQQDATAQ -> MSAYSVPSTF
FT A (in isoform 1, isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:10668202, ECO:0000303|PubMed:12175877,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036351"
FT VAR_SEQ 511..514
FT /note="Missing (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12175877,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_035655"
FT VAR_SEQ 952..985
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12175877"
FT /id="VSP_035656"
FT VAR_SEQ 984
FT /note="I -> IQVSEPTASAPSSA (in isoform 4, isoform 5,
FT isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_036352"
FT VAR_SEQ 1132..1147
FT /note="TTTNGNGSSEVHITKP -> AGSKVIQNEFTVGEECELETMTGEKVKTVVQL
FT EGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036353"
FT VARIANT 22
FT /note="A -> T (in dbSNP:rs11221912)"
FT /id="VAR_054418"
FT VARIANT 573
FT /note="T -> A (in dbSNP:rs2241571)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_019984"
FT CONFLICT 46
FT /note="P -> S (in Ref. 6; AAI12935)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="T -> A (in Ref. 8; BAA91026)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="F -> L (in Ref. 4; BX648944)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="C -> Y (in Ref. 4; BX648944)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112
FT /note="S -> N (in Ref. 4; BX648944)"
FT /evidence="ECO:0000305"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:3IHX"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3IHX"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:3IHX"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3IHX"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:3IHX"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3IHX"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:3IHX"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:3IHX"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3IHX"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:3IHX"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3IHX"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:3IHX"
SQ SEQUENCE 1147 AA; 130136 MW; E565CA8822CB2934 CRC64;
MDSKDESSHV WPTSAEHEQN AAQVHFVPDT GTVAQIVYTD DQVRPPQQVV YTADGASYTS
VDGPEHTLVY IHPVEAAQTL FTDPGQVAYV QQDATAQQAS LPVHNQVLPS IESVDGSDPL
ATLQTPLGRL EAKEEEDEDE DEDTEEDEEE DGEDTDLDDW EPDPPRPFDP HDLWCEECNN
AHASVCPKHG PLHPIPNRPV LTRARASLPL VLYIDRFLGG VFSKRRIPKR TQFGPVEGPL
VRGSELKDCY IHLKVSLDKG DRKERDLHED LWFELSDETL CNWMMFVRPA QNHLEQNLVA
YQYGHHVYYT TIKNVEPKQE LKVWYAASYA EFVNQKIHDI SEEERKVLRE QEKNWPCYEC
NRRFISSEQL QQHLNSHDEK LDVFSRTRGR GRGRGKRRFG PGRRPGRPPK FIRLEITSEN
GEKSDDGTQD LLHFPTKEQF DEAEPATLNG LDQPEQTTIP IPQLPQETQS SLEHEPETHT
LHLQPQHEES VVPTQSTLTA DDMRRAKRIR LELQNAALQH LFIRKSFRPF KCLQCGKAFR
EKDKLDQHLR FHGREGNCPL TCDLCNKGFI SSTSLESHMK LHSDQKTYSC IFCPESFDRL
DLLKDHVAIH INDGYFTCPT CKKRFPDFIQ VKKHVRSFHS EKIYQCTECD KAFCRPDKLR
LHMLRHSDRK DFLCSTCGKQ FKRKDKLREH MQRMHNPERE AKKADRISRS KTFKPRITST
DYDSFTFKCR LCMMGFRRRG MLVNHLSKRH PDMKIEEVPE LTLPIIKPNR DYFCQYCDKV
YKSASKRKAH ILKNHPGAEL PPSIRKLRPA GPGEPDPMLS THTQLTGTIA TPPVCCPHCS
KQYSSKTKMV QHIRKKHPEF AQLSNTIHTP LTTAVISATP AVLTTDSATG ETVVTTDLLT
QAMTELSQTL TTDYRTPQGD YQRIQYIPVS QSASGLQQPQ HIQLQVVQVA SATSPHQSQQ
STVDVGQLHD PQPYPQHAIQ VQHIQVSGQP LSPSAQQAQQ GLSPSHIQGS SSTQGQALQQ
QQQQQQNSSV QHTYLPSAWN SFRGYSSEIQ MMTLPPGQFV ITDSGVATPV TTGQVKAVTS
GHYVLSESQS ELEEKQTSAL SGGVQVEPPA HSDSLDPQTN SQQQTTQYII TTTTNGNGSS
EVHITKP
