ZBT10_HUMAN
ID ZBT10_HUMAN Reviewed; 871 AA.
AC Q96DT7; A4FVD0; Q86W96; Q8IXI9; Q96MH9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Zinc finger and BTB domain-containing protein 10;
DE AltName: Full=Zinc finger protein RIN ZF;
GN Name=ZBTB10; Synonyms=RINZF, RINZFC;
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), AND VARIANTS THR-50 AND ILE-174.
RC TISSUE=Brain;
RA Kashuba V.I., Protopopov A.I., Zabarovsky E.R.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RA Rakhmanaliev E.R.;
RT "Identification of four genes on human chromosome 3 homologous to the known
RT genes on other chromosomes by in silico analysis.";
RL Thesis (2002), Novosibirsk Institute of Cytology and Genetics, Russia.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Prostate;
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 GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 368-871 (ISOFORMS 1/3/4).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP 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 [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-126, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-468, AND IDENTIFICATION BY MASS
RP 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-468 AND LYS-684, 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-468, 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-245; LYS-468; LYS-483; LYS-497;
RP LYS-573; LYS-672; LYS-684; LYS-696 AND LYS-706, 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).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q96DT7; Q9Y4Z0: LSM4; NbExp=3; IntAct=EBI-10235384, EBI-372521;
CC Q96DT7; Q70IA8: MOB3C; NbExp=4; IntAct=EBI-10235384, EBI-9679267;
CC Q96DT7; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-10235384, EBI-399246;
CC Q96DT7; Q15014: MORF4L2; NbExp=3; IntAct=EBI-10235384, EBI-399257;
CC Q96DT7; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-10235384, EBI-740727;
CC Q96DT7-3; O00311: CDC7; NbExp=3; IntAct=EBI-12017160, EBI-374980;
CC Q96DT7-3; Q96LK0: CEP19; NbExp=3; IntAct=EBI-12017160, EBI-741885;
CC Q96DT7-3; O43602-2: DCX; NbExp=3; IntAct=EBI-12017160, EBI-14148644;
CC Q96DT7-3; P26196: DDX6; NbExp=3; IntAct=EBI-12017160, EBI-351257;
CC Q96DT7-3; Q08426: EHHADH; NbExp=3; IntAct=EBI-12017160, EBI-2339219;
CC Q96DT7-3; Q9BYC5: FUT8; NbExp=3; IntAct=EBI-12017160, EBI-2869363;
CC Q96DT7-3; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-12017160, EBI-14103818;
CC Q96DT7-3; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-12017160, EBI-746778;
CC Q96DT7-3; Q8N7B6-2: PACRGL; NbExp=3; IntAct=EBI-12017160, EBI-10694433;
CC Q96DT7-3; O43189: PHF1; NbExp=3; IntAct=EBI-12017160, EBI-530034;
CC Q96DT7-3; Q96IZ5: RBM41; NbExp=3; IntAct=EBI-12017160, EBI-740773;
CC Q96DT7-3; O76064: RNF8; NbExp=3; IntAct=EBI-12017160, EBI-373337;
CC Q96DT7-3; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-12017160, EBI-14096082;
CC Q96DT7-3; Q68CQ4: UTP25; NbExp=3; IntAct=EBI-12017160, EBI-747711;
CC Q96DT7-3; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-12017160, EBI-740727;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96DT7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DT7-2; Sequence=VSP_040319;
CC Name=3;
CC IsoId=Q96DT7-3; Sequence=VSP_040317;
CC Name=4;
CC IsoId=Q96DT7-4; Sequence=VSP_040316, VSP_040318;
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DR EMBL; AJ319673; CAC40989.1; -; mRNA.
DR EMBL; AJ507398; CAD45447.1; -; Genomic_DNA.
DR EMBL; AK056913; BAB71309.1; -; mRNA.
DR EMBL; AC009812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050061; AAH50061.1; -; mRNA.
DR EMBL; BC127098; AAI27099.1; -; mRNA.
DR CCDS; CCDS47880.1; -. [Q96DT7-1]
DR CCDS; CCDS64920.1; -. [Q96DT7-4]
DR RefSeq; NP_001099009.1; NM_001105539.2. [Q96DT7-1]
DR RefSeq; NP_001264074.1; NM_001277145.1. [Q96DT7-4]
DR RefSeq; NP_076418.3; NM_023929.4. [Q96DT7-2]
DR AlphaFoldDB; Q96DT7; -.
DR SMR; Q96DT7; -.
DR BioGRID; 122435; 134.
DR IntAct; Q96DT7; 54.
DR MINT; Q96DT7; -.
DR STRING; 9606.ENSP00000387462; -.
DR iPTMnet; Q96DT7; -.
DR PhosphoSitePlus; Q96DT7; -.
DR BioMuta; ZBTB10; -.
DR DMDM; 317373300; -.
DR EPD; Q96DT7; -.
DR jPOST; Q96DT7; -.
DR MassIVE; Q96DT7; -.
DR MaxQB; Q96DT7; -.
DR PaxDb; Q96DT7; -.
DR PeptideAtlas; Q96DT7; -.
DR PRIDE; Q96DT7; -.
DR ProteomicsDB; 76321; -. [Q96DT7-1]
DR ProteomicsDB; 76322; -. [Q96DT7-2]
DR ProteomicsDB; 76323; -. [Q96DT7-3]
DR ProteomicsDB; 76324; -. [Q96DT7-4]
DR Antibodypedia; 6507; 129 antibodies from 23 providers.
DR DNASU; 65986; -.
DR Ensembl; ENST00000379091.8; ENSP00000368384.4; ENSG00000205189.12. [Q96DT7-4]
DR Ensembl; ENST00000426744.5; ENSP00000416134.2; ENSG00000205189.12. [Q96DT7-2]
DR Ensembl; ENST00000430430.5; ENSP00000387462.1; ENSG00000205189.12. [Q96DT7-1]
DR Ensembl; ENST00000455036.8; ENSP00000412036.3; ENSG00000205189.12. [Q96DT7-1]
DR Ensembl; ENST00000610895.2; ENSP00000484716.1; ENSG00000205189.12. [Q96DT7-3]
DR GeneID; 65986; -.
DR KEGG; hsa:65986; -.
DR MANE-Select; ENST00000455036.8; ENSP00000412036.3; NM_001105539.3; NP_001099009.1.
DR UCSC; uc003ybv.6; human. [Q96DT7-1]
DR CTD; 65986; -.
DR DisGeNET; 65986; -.
DR GeneCards; ZBTB10; -.
DR HGNC; HGNC:30953; ZBTB10.
DR HPA; ENSG00000205189; Low tissue specificity.
DR MIM; 618576; gene.
DR neXtProt; NX_Q96DT7; -.
DR OpenTargets; ENSG00000205189; -.
DR PharmGKB; PA134883318; -.
DR VEuPathDB; HostDB:ENSG00000205189; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157988; -.
DR HOGENOM; CLU_022356_1_1_1; -.
DR InParanoid; Q96DT7; -.
DR OMA; WATQNLT; -.
DR OrthoDB; 755439at2759; -.
DR PhylomeDB; Q96DT7; -.
DR TreeFam; TF330979; -.
DR PathwayCommons; Q96DT7; -.
DR SignaLink; Q96DT7; -.
DR BioGRID-ORCS; 65986; 43 hits in 1142 CRISPR screens.
DR ChiTaRS; ZBTB10; human.
DR GenomeRNAi; 65986; -.
DR Pharos; Q96DT7; Tbio.
DR PRO; PR:Q96DT7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96DT7; protein.
DR Bgee; ENSG00000205189; Expressed in secondary oocyte and 192 other tissues.
DR Genevisible; Q96DT7; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISS:ARUK-UCL.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..871
FT /note="Zinc finger and BTB domain-containing protein 10"
FT /id="PRO_0000047725"
FT DOMAIN 364..433
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 722..744
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 750..772
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..851
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 468
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 672
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 684
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 696
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 706
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..292
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040316"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040317"
FT VAR_SEQ 293..324
FT /note="DELSRGTRNYKKTLLLRHHVSTEHKLHEANAQ -> MTRLERSSHRTVICKV
FT PGELVAREGKCASRAR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040318"
FT VAR_SEQ 665..688
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040319"
FT VARIANT 50
FT /note="P -> T (in dbSNP:rs591989)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_018384"
FT VARIANT 174
FT /note="M -> I (in dbSNP:rs593747)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_018385"
FT CONFLICT 324
FT /note="Q -> P (in Ref. 1; CAC40989)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="C -> W (in Ref. 1; CAC40989)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="S -> R (in Ref. 1; CAC40989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 871 AA; 94894 MW; A823948FDC3D6AC1 CRC64;
MSFSEMNRRT LAFRGGGLVT ASGGGSTNNN AGGEASAWPP QPQPRQPPPP APPALQPPNG
RGADEEVELE GLEPQDLEAS AGPAAGAAEE AKELLLPQDA GGPTSLGGGA GGPLLAERNR
RTLAFRGGGG GGLGNNGSSR GRPETSVWPL RHFNGRGPAT VDLELDALEG KELMQDGASL
SDSTEDEEEG ASLGDGSGAE GGSCSSSRRS GGDGGDEVEG SGVGAGEGET VQHFPLARPK
SLMQKLQCSF QTSWLKDFPW LRYSKDTGLM SCGWCQKTPA DGGSVDLPPV GHDELSRGTR
NYKKTLLLRH HVSTEHKLHE ANAQESEIPS EEGYCDFNSR PNENSYCYQL LRQLNEQRKK
GILCDVSIVV SGKIFKAHKN ILVAGSRFFK TLYCFSNKES PNQNNTTHLD IAAVQGFSVI
LDFLYSGNLV LTSQNAIEVM TVASYLQMSE VVQTCRNFIK DALNISIKSE APESVVVDYN
NRKPVNRDGL SSSRDQKIAS FWATRNLTNL ASNVKIENDG CNVDEGQIEN YQMNDSSWVQ
DGSPEMAENE SEGQTKVFIW NNMGSQGIQE TGKTRRKNQT TKRFIYNIPP NNETNLEDCS
VMQPPVAYPE ENTLLIKEEP DLDGALLSGP DGDRNVNANL LAEAGTSQDG GDAGTSHDFK
YGLMPGPSND FKYGLIPGTS NDFKYGLIPG ASNDFKYGLL PESWPKQETW ENGESSLIMN
KLKCPHCSYV AKYRRTLKRH LLIHTGVRSF SCDICGKLFT RREHVKRHSL VHKKDKKYKC
MVCKKIFMLA ASVGIRHGSR RYGVCVDCAD KSQPGGQEGV DQGQDTEFPR DEEYEENEVG
EADEELVDDG EDQNDPSRWD ESGEVCMSLD D
