ZBT21_HUMAN
ID ZBT21_HUMAN Reviewed; 1066 AA.
AC Q9ULJ3; Q5R2W1; Q5R2W2; Q6P4R0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Zinc finger and BTB domain-containing protein 21;
DE AltName: Full=Zinc finger protein 295;
GN Name=ZBTB21; Synonyms=KIAA1227, ZNF295;
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] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP ZBTB14, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal kidney, and Testis;
RX PubMed=15629158; DOI=10.1016/j.bbrc.2004.12.048;
RA Wang J., Kudoh J., Takayanagi A., Shimizu N.;
RT "Novel human BTB/POZ domain-containing zinc finger protein ZNF295 is
RT directly associated with ZFP161.";
RL Biochem. Biophys. Res. Commun. 327:615-627(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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-714, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381 AND SER-422, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-422; THR-431;
RP SER-434; SER-435; SER-438; SER-605 AND SER-1003, AND IDENTIFICATION BY MASS
RP 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].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; THR-431; SER-435 AND
RP SER-1003, AND 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-605 AND SER-714, AND
RP IDENTIFICATION BY 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 THR-431 AND SER-434, 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-345; SER-411; SER-422;
RP THR-431; SER-435; SER-605; SER-714 AND SER-1003, AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-430; LYS-469; LYS-617 AND
RP LYS-879, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40 AND LYS-879, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-430; LYS-469 AND LYS-879,
RP AND 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40, 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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-255; LYS-266; LYS-273;
RP LYS-312; LYS-337; LYS-383; LYS-430; LYS-469; LYS-475; LYS-617; LYS-643;
RP LYS-659; LYS-702; LYS-763; LYS-785; LYS-875; LYS-879 AND LYS-935, 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).
RN [20]
RP STRUCTURE BY NMR OF 713-806.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of ZF-C2H2 domains from human zinc finger protein
RT 295.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Acts as a transcription repressor.
CC {ECO:0000269|PubMed:15629158}.
CC -!- SUBUNIT: Homodimer. Interacts with ZBTB14.
CC {ECO:0000269|PubMed:15629158}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15629158}.
CC Note=Colocalizes with ZBTB14 in nucleus in HEK293 cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ZNF295L;
CC IsoId=Q9ULJ3-1; Sequence=Displayed;
CC Name=2; Synonyms=ZNF295S;
CC IsoId=Q9ULJ3-2; Sequence=VSP_041349;
CC -!- TISSUE SPECIFICITY: Ubiquitous in fetal and adult tissues.
CC {ECO:0000269|PubMed:15629158}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86541.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB041014; BAD74063.1; -; mRNA.
DR EMBL; AB041015; BAD74064.1; -; mRNA.
DR EMBL; AB033053; BAA86541.1; ALT_INIT; mRNA.
DR EMBL; AP001745; BAA95529.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09579.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09580.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09581.1; -; Genomic_DNA.
DR EMBL; BC063290; AAH63290.1; -; mRNA.
DR CCDS; CCDS13678.1; -. [Q9ULJ3-1]
DR CCDS; CCDS42934.1; -. [Q9ULJ3-2]
DR RefSeq; NP_001091872.1; NM_001098402.1. [Q9ULJ3-1]
DR RefSeq; NP_001091873.1; NM_001098403.1. [Q9ULJ3-2]
DR RefSeq; NP_001307658.1; NM_001320729.1. [Q9ULJ3-2]
DR RefSeq; NP_001307660.1; NM_001320731.1. [Q9ULJ3-1]
DR RefSeq; NP_065778.3; NM_020727.4. [Q9ULJ3-1]
DR RefSeq; XP_005261178.1; XM_005261121.3. [Q9ULJ3-1]
DR RefSeq; XP_011527890.1; XM_011529588.2. [Q9ULJ3-1]
DR RefSeq; XP_011527892.1; XM_011529590.2. [Q9ULJ3-1]
DR RefSeq; XP_016883849.1; XM_017028360.1. [Q9ULJ3-1]
DR RefSeq; XP_016883850.1; XM_017028361.1. [Q9ULJ3-1]
DR PDB; 1WJP; NMR; -; A=713-806.
DR PDBsum; 1WJP; -.
DR AlphaFoldDB; Q9ULJ3; -.
DR BMRB; Q9ULJ3; -.
DR SMR; Q9ULJ3; -.
DR BioGRID; 119066; 145.
DR IntAct; Q9ULJ3; 26.
DR MINT; Q9ULJ3; -.
DR STRING; 9606.ENSP00000308759; -.
DR GlyGen; Q9ULJ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULJ3; -.
DR PhosphoSitePlus; Q9ULJ3; -.
DR SwissPalm; Q9ULJ3; -.
DR BioMuta; ZBTB21; -.
DR DMDM; 9979550; -.
DR EPD; Q9ULJ3; -.
DR jPOST; Q9ULJ3; -.
DR MassIVE; Q9ULJ3; -.
DR MaxQB; Q9ULJ3; -.
DR PaxDb; Q9ULJ3; -.
DR PeptideAtlas; Q9ULJ3; -.
DR PRIDE; Q9ULJ3; -.
DR ProteomicsDB; 85046; -. [Q9ULJ3-1]
DR ProteomicsDB; 85047; -. [Q9ULJ3-2]
DR ABCD; Q9ULJ3; 3 sequenced antibodies.
DR Antibodypedia; 9340; 96 antibodies from 24 providers.
DR DNASU; 49854; -.
DR Ensembl; ENST00000310826.10; ENSP00000308759.5; ENSG00000173276.14. [Q9ULJ3-1]
DR Ensembl; ENST00000398499.5; ENSP00000381512.1; ENSG00000173276.14. [Q9ULJ3-1]
DR Ensembl; ENST00000398505.7; ENSP00000381517.3; ENSG00000173276.14. [Q9ULJ3-2]
DR Ensembl; ENST00000398511.3; ENSP00000381523.3; ENSG00000173276.14. [Q9ULJ3-1]
DR GeneID; 49854; -.
DR KEGG; hsa:49854; -.
DR MANE-Select; ENST00000310826.10; ENSP00000308759.5; NM_001098402.2; NP_001091872.1.
DR UCSC; uc002yzy.5; human. [Q9ULJ3-1]
DR CTD; 49854; -.
DR DisGeNET; 49854; -.
DR GeneCards; ZBTB21; -.
DR HGNC; HGNC:13083; ZBTB21.
DR HPA; ENSG00000173276; Tissue enhanced (bone).
DR MIM; 616485; gene.
DR neXtProt; NX_Q9ULJ3; -.
DR OpenTargets; ENSG00000173276; -.
DR PharmGKB; PA37659; -.
DR VEuPathDB; HostDB:ENSG00000173276; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161028; -.
DR HOGENOM; CLU_014382_0_0_1; -.
DR InParanoid; Q9ULJ3; -.
DR OMA; RSVIVCR; -.
DR PhylomeDB; Q9ULJ3; -.
DR TreeFam; TF331184; -.
DR PathwayCommons; Q9ULJ3; -.
DR SignaLink; Q9ULJ3; -.
DR BioGRID-ORCS; 49854; 10 hits in 1143 CRISPR screens.
DR ChiTaRS; ZBTB21; human.
DR EvolutionaryTrace; Q9ULJ3; -.
DR GeneWiki; ZNF295; -.
DR GenomeRNAi; 49854; -.
DR Pharos; Q9ULJ3; Tbio.
DR PRO; PR:Q9ULJ3; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9ULJ3; protein.
DR Bgee; ENSG00000173276; Expressed in cauda epididymis and 183 other tissues.
DR ExpressionAtlas; Q9ULJ3; baseline and differential.
DR Genevisible; Q9ULJ3; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0031208; F:POZ domain binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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; IPR041011; Znf_C2H2_6.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF18450; zf_C2H2_6; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1066
FT /note="Zinc finger and BTB domain-containing protein 21"
FT /id="PRO_0000047515"
FT DOMAIN 30..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 546..569
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 575..598
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 670..692
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 748..770
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 775..798
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 909..932
FT /note="C2H2-type 6; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 937..959
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1043..1065
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 30..96
FT /note="Mediates homodimerization"
FT REGION 154..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 383
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 475
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 617
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 643
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 702
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 763
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 785
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 875
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 935
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 535..735
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15629158"
FT /id="VSP_041349"
FT VARIANT 185
FT /note="N -> S (in dbSNP:rs871545)"
FT /id="VAR_052807"
FT VARIANT 218
FT /note="K -> Q (in dbSNP:rs871546)"
FT /id="VAR_052808"
FT CONFLICT 961
FT /note="S -> P (in Ref. 5; AAH63290)"
FT /evidence="ECO:0000305"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:1WJP"
FT HELIX 734..746
FT /evidence="ECO:0007829|PDB:1WJP"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:1WJP"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:1WJP"
FT HELIX 760..769
FT /evidence="ECO:0007829|PDB:1WJP"
FT HELIX 773..775
FT /evidence="ECO:0007829|PDB:1WJP"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:1WJP"
FT HELIX 787..796
FT /evidence="ECO:0007829|PDB:1WJP"
SQ SEQUENCE 1066 AA; 118870 MW; E1779E26943FDAC8 CRC64;
MEGLLHYINP AHAISLLSAL NEERLKGQLC DVLLIVGDQK FRAHKNVLAA SSEYFQSLFT
NKENESQTVF QLDFCEPDAF DNVLNYIYSS SLFVEKSSLA AVQELGYSLG ISFLTNIVSK
TPQAPFPTCP NRKKVFVEDD ENSSQKRSVI VCQSRNEAQG KTVSQNQPDV SHTSRPSPSI
AVKANTNKPH VPKPIEPLHN LSLTEKSWPK DSSVVYAKSL EHSGSLDDPN RISLVKRNAV
LPSKPLQDRE AMDDKPGVSG QLPKGKALEL ALKRPRPPVL SVCSSSETPY LLKETNKGNG
QGEDRNLLYY SKLGLVIPSS GSGSGNQSID RSGPLVKSLL RRSLSMDSQV PVYSPSIDLK
SSQGSSSVSS DAPGNVLCAL SQKSSLKDCS EKTALDDRPQ VLQPHRLRSF SASQSTDREG
ASPVTEVRIK TEPSSPLSDP SDIIRVTVGD AATTAAASSS SVTRDLSLKT EDDQKDMSRL
PAKRRFQADR RLPFKKLKVN EHGSPVSEDN FEEGSSPTLL DADFPDSDLN KDEFGELEGT
RPNKKFKCKH CLKIFRSTAG LHRHVNMYHN PEKPYACDIC HKRFHTNFKV WTHCQTQHGI
VKNPSPASSS HAVLDEKFQR KLIDIVRERE IKKALIIKLR RGKPGFQGQS SSQAQQVIKR
NLRSRAKGAY ICTYCGKAYR FLSQFKQHIK MHPGEKPLGV NKVAKPKEHA PLASPVENKE
VYQCRLCNAK LSSLLEQGSH ERLCRNAAVC PYCSLRFFSP ELKQEHESKC EYKKLTCLEC
MRTFKSSFSI WRHQVEVHNQ NNMAPTENFS LPVLDHNGDV TGSSRPQSQP EPNKVNHIVT
TKDDNVFSDS SEQVNFDSED SSCLPEDLSL SKQLKIQVKE EPVEEAEEEA PEASTAPKEA
GPSKEASLWP CEKCGKMFTV HKQLERHQEL LCSVKPFICH VCNKAFRTNF RLWSHFQSHM
SQASEESAHK ESEVCPVPTN SPSPPPLPPP PPLPKIQPLE PDSPTGLSEN PTPATEKLFV
PQESDTLFYH APPLSAITFK RQFMCKLCHR TFKTAFSLWS HEQTHN
