ZBTB1_HUMAN
ID ZBTB1_HUMAN Reviewed; 713 AA.
AC Q9Y2K1; A8K6S8; Q86SW8;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Zinc finger and BTB domain-containing protein 1;
GN Name=ZBTB1; Synonyms=KIAA0997;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-417.
RC TISSUE=Cervix carcinoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND THR-356, 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 [7]
RP FUNCTION, SUBUNIT, SUMOYLATION AT LYS-265 AND LYS-328, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF LYS-265 AND LYS-328, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20797634; DOI=10.1016/j.molcel.2010.07.026;
RA Matic I., Schimmel J., Hendriks I.A., van Santen M.A., van de Rijke F.,
RA van Dam H., Gnad F., Mann M., Vertegaal A.C.;
RT "Site-specific identification of SUMO-2 targets in cells reveals an
RT inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.";
RL Mol. Cell 39:641-652(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21706167; DOI=10.1007/s11010-011-0911-5;
RA Liu Q., Yao F., Wang M., Zhou B., Cheng H., Wang W., Jin L., Lin Q.,
RA Wang J.C.;
RT "Novel human BTB/POZ domain-containing zinc finger protein ZBTB1 inhibits
RT transcriptional activities of CRE.";
RL Mol. Cell. Biochem. 357:405-414(2011).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22753936; DOI=10.4049/jimmunol.1200623;
RA Punwani D., Simon K., Choi Y., Dutra A., Gonzalez-Espinosa D., Pak E.,
RA Naradikian M., Song C.H., Zhang J., Bodine D.M., Puck J.M.;
RT "Transcription factor zinc finger and BTB domain 1 is essential for
RT lymphocyte development.";
RL J. Immunol. 189:1253-1264(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP IDENTIFICATION BY 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 [12]
RP FUNCTION, INTERACTION WITH TRIM28, MUTAGENESIS OF CYS-536 AND CYS-539, AND
RP DOMAIN UBZ-TYPE.
RX PubMed=24657165; DOI=10.1016/j.molcel.2014.02.017;
RA Kim H., Dejsuphong D., Adelmant G., Ceccaldi R., Yang K., Marto J.A.,
RA D'Andrea A.D.;
RT "Transcriptional repressor ZBTB1 promotes chromatin remodeling and
RT translesion DNA synthesis.";
RL Mol. Cell 54:107-118(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-275 AND LYS-328, AND
RP 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-328, 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-328, AND
RP IDENTIFICATION BY MASS 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-200; LYS-205; LYS-260;
RP LYS-265; LYS-283; LYS-303; LYS-316; LYS-328; LYS-340; LYS-346; LYS-381;
RP LYS-528 AND LYS-563, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Acts as a transcriptional repressor (PubMed:20797634).
CC Represses cAMP-responsive element (CRE)-mediated transcriptional
CC activation (PubMed:21706167). In addition, has a role in translesion
CC DNA synthesis. Requires for UV-inducible RAD18 loading, PCNA
CC monoubiquitination, POLH recruitment to replication factories and
CC efficient translesion DNA synthesis (PubMed:24657165). Plays a key role
CC in the transcriptional regulation of T lymphocyte development (By
CC similarity). {ECO:0000250|UniProtKB:Q91VL9,
CC ECO:0000269|PubMed:20797634, ECO:0000269|PubMed:21706167,
CC ECO:0000269|PubMed:24657165}.
CC -!- SUBUNIT: Homodimer. Homooligomer. Isoform 1 and isoform 2 can
CC homodimerize. Heterodimer of isoform 1 and isoform 2. Interacts (via
CC BTB domain) with TRIM28 (unphosphorylated or phosphorylated form)
CC (PubMed:24657165). {ECO:0000269|PubMed:20797634,
CC ECO:0000269|PubMed:22753936, ECO:0000269|PubMed:24657165}.
CC -!- INTERACTION:
CC Q9Y2K1; O43488: AKR7A2; NbExp=4; IntAct=EBI-2682961, EBI-748855;
CC Q9Y2K1; Q3B820: FAM161A; NbExp=6; IntAct=EBI-2682961, EBI-719941;
CC Q9Y2K1; Q92993: KAT5; NbExp=3; IntAct=EBI-2682961, EBI-399080;
CC Q9Y2K1; P55081: MFAP1; NbExp=3; IntAct=EBI-2682961, EBI-1048159;
CC Q9Y2K1; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-2682961, EBI-10232538;
CC Q9Y2K1; P11309: PIM1; NbExp=3; IntAct=EBI-2682961, EBI-696621;
CC Q9Y2K1; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-2682961, EBI-748391;
CC Q9Y2K1; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-2682961, EBI-5235829;
CC Q9Y2K1; P24278: ZBTB25; NbExp=4; IntAct=EBI-2682961, EBI-739899;
CC Q9Y2K1; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-2682961, EBI-740727;
CC Q9Y2K1; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-2682961, EBI-10172590;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21706167}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:20797634}. Note=Localized in dot-like
CC structures in the nucleus (PubMed:21706167). Colocalized with SMRT in
CC nuclear bodies (PubMed:20797634). The sumoylated form is preferentially
CC located in the nucleoplasm outside the nuclear bodies(PubMed:20797634).
CC {ECO:0000269|PubMed:20797634, ECO:0000269|PubMed:21706167}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2K1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2K1-2; Sequence=VSP_040976;
CC -!- DOMAIN: Both the BTB domain and C2H2-type motifs are necessary for
CC transcriptional repression activity. The BTB domain is also necessary
CC for oligomerization and efficient sumoylation. The hydrophobic cluster
CC preceding Lys-328 enhanced sumoylation efficiency (PubMed:20797634).
CC {ECO:0000269|PubMed:20797634}.
CC -!- DOMAIN: The UBZ-type zinc finger domain is required for targeting ZBTB1
CC to UV damage sites and for PCNA monoubiquitination. UBZ-type zinc
CC finger domain mediates binding to 'Lys-63'-linked polyubiquitin chains
CC (in vitro). {ECO:0000269|PubMed:24657165}.
CC -!- PTM: Sumoylated with SUMO2 at Lys-328 and to a lesser extent at Lys-
CC 265. Sumoylation inhibits its transcriptional repression activity and
CC regulates its subcellular localization. {ECO:0000269|PubMed:20797634}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76841.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK291743; BAF84432.1; -; mRNA.
DR EMBL; AB023214; BAA76841.2; ALT_INIT; mRNA.
DR EMBL; AL049869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050719; AAH50719.1; -; mRNA.
DR EMBL; BX248777; CAD66584.1; -; mRNA.
DR CCDS; CCDS32097.1; -. [Q9Y2K1-2]
DR CCDS; CCDS45126.1; -. [Q9Y2K1-1]
DR RefSeq; NP_001116801.1; NM_001123329.1. [Q9Y2K1-1]
DR RefSeq; NP_055765.2; NM_014950.2. [Q9Y2K1-2]
DR RefSeq; XP_005267467.1; XM_005267410.1. [Q9Y2K1-1]
DR RefSeq; XP_011534868.1; XM_011536566.2. [Q9Y2K1-1]
DR RefSeq; XP_011534870.1; XM_011536568.2. [Q9Y2K1-2]
DR RefSeq; XP_016876583.1; XM_017021094.1.
DR RefSeq; XP_016876584.1; XM_017021095.1. [Q9Y2K1-1]
DR AlphaFoldDB; Q9Y2K1; -.
DR BioGRID; 116556; 129.
DR IntAct; Q9Y2K1; 39.
DR MINT; Q9Y2K1; -.
DR STRING; 9606.ENSP00000451000; -.
DR GlyGen; Q9Y2K1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2K1; -.
DR PhosphoSitePlus; Q9Y2K1; -.
DR BioMuta; ZBTB1; -.
DR DMDM; 46577710; -.
DR EPD; Q9Y2K1; -.
DR jPOST; Q9Y2K1; -.
DR MassIVE; Q9Y2K1; -.
DR MaxQB; Q9Y2K1; -.
DR PaxDb; Q9Y2K1; -.
DR PeptideAtlas; Q9Y2K1; -.
DR PRIDE; Q9Y2K1; -.
DR ProteomicsDB; 85818; -. [Q9Y2K1-1]
DR ProteomicsDB; 85819; -. [Q9Y2K1-2]
DR Antibodypedia; 24644; 78 antibodies from 23 providers.
DR DNASU; 22890; -.
DR Ensembl; ENST00000358738.3; ENSP00000351587.3; ENSG00000126804.14. [Q9Y2K1-2]
DR Ensembl; ENST00000554015.5; ENSP00000451000.1; ENSG00000126804.14. [Q9Y2K1-1]
DR Ensembl; ENST00000683701.1; ENSP00000506911.1; ENSG00000126804.14. [Q9Y2K1-1]
DR GeneID; 22890; -.
DR KEGG; hsa:22890; -.
DR MANE-Select; ENST00000683701.1; ENSP00000506911.1; NM_001123329.2; NP_001116801.1.
DR UCSC; uc001xhh.5; human. [Q9Y2K1-1]
DR CTD; 22890; -.
DR DisGeNET; 22890; -.
DR GeneCards; ZBTB1; -.
DR HGNC; HGNC:20259; ZBTB1.
DR HPA; ENSG00000126804; Low tissue specificity.
DR MIM; 616578; gene.
DR neXtProt; NX_Q9Y2K1; -.
DR OpenTargets; ENSG00000126804; -.
DR PharmGKB; PA128395769; -.
DR VEuPathDB; HostDB:ENSG00000126804; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157501; -.
DR HOGENOM; CLU_028599_0_0_1; -.
DR InParanoid; Q9Y2K1; -.
DR OMA; EGGEPDH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Y2K1; -.
DR TreeFam; TF332229; -.
DR PathwayCommons; Q9Y2K1; -.
DR SignaLink; Q9Y2K1; -.
DR BioGRID-ORCS; 22890; 20 hits in 1132 CRISPR screens.
DR ChiTaRS; ZBTB1; human.
DR GenomeRNAi; 22890; -.
DR Pharos; Q9Y2K1; Tbio.
DR PRO; PR:Q9Y2K1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9Y2K1; protein.
DR Bgee; ENSG00000126804; Expressed in sperm and 199 other tissues.
DR ExpressionAtlas; Q9Y2K1; baseline and differential.
DR Genevisible; Q9Y2K1; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; ISS:UniProtKB.
DR GO; GO:2000176; P:positive regulation of pro-T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; ISS:UniProtKB.
DR GO; GO:0002711; P:positive regulation of T cell mediated immunity; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; ISS:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; IMP:UniProtKB.
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; 8.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Differentiation; DNA damage; DNA repair; DNA-binding;
KW Immunity; Innate immunity; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..713
FT /note="Zinc finger and BTB domain-containing protein 1"
FT /id="PRO_0000047707"
FT DOMAIN 24..91
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 216..242
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..470
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 533..558
FT /note="UBZ-type"
FT /evidence="ECO:0000305|PubMed:24657165"
FT ZN_FING 578..600
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 686..709
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 265
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 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 328
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 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 563
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 633..713
FT /note="RYVCSICDQGNFRKHDHVRHMISHLSAGETICQVCFQIFPNNEQLEQHMDVH
FT LYTCGICGAKFNLRKDMRSHYNAKHLKRT -> SGEIGPSKPVEK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_040976"
FT MUTAGEN 265
FT /note="K->R: Reduces sumoylation. Inhibits transcriptional
FT repressive activity. Inhibits sumoylation and reduces
FT transcriptional repressive activity; when associated with
FT R-328."
FT /evidence="ECO:0000269|PubMed:20797634"
FT MUTAGEN 325
FT /note="I->S: Reduces sumoylation of Lys-328."
FT MUTAGEN 326
FT /note="I->N: Reduces sumoylation of Lys-328."
FT MUTAGEN 328
FT /note="K->R: Reduces sumoylation. Does not reduce
FT transcriptional repressive activity. Inhibits sumoylation
FT but does not reduce transcriptional repressive activity;
FT when associated with R-265."
FT /evidence="ECO:0000269|PubMed:20797634"
FT MUTAGEN 536
FT /note="C->A: Abolishes binding to ubiquitin; Abolishes
FT recruitment to DNA lesion sites."
FT /evidence="ECO:0000269|PubMed:24657165"
FT MUTAGEN 539
FT /note="C->A: Abolishes binding to ubiquitin; Abolishes
FT recruitment to DNA lesion sites."
FT /evidence="ECO:0000269|PubMed:24657165"
FT CONFLICT 203
FT /note="T -> N (in Ref. 2; BAA76841)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="I -> T (in Ref. 4; AAH50719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 713 AA; 82016 MW; 4B120DD45FA14305 CRC64;
MAKPSHSSYV LQQLNNQREW GFLCDCCIAI DDIYFQAHKA VLAACSSYFR MFFMNHQHST
AQLNLSNMKI SAECFDLILQ FMYLGKIMTA PSSFEQFKVA MNYLQLYNVP DCLEDIQDAD
CSSSKCSSSA SSKQNSKMIF GVRMYEDTVA RNGNEANRWC AEPSSTVNTP HNREADEESL
QLGNFPEPLF DVCKKSSVSK LSTPKERVSR RFGRSFTCDS CGFGFSCEKL LDEHVLTCTN
RHLYQNTRSY HRIVDIRDGK DSNIKAEFGE KDSSKTFSAQ TDKYRGDTSQ AADDSASTTG
SRKSSTVESE IASEEKSRAA ERKRIIIKME PEDIPTDELK DFNIIKVTDK DCNESTDNDE
LEDEPEEPFY RYYVEEDVSI KKSGRKTLKP RMSVSADERG GLENMRPPNN SSPVQEDAEN
ASCELCGLTI TEEDLSSHYL AKHIENICAC GKCGQILVKG RQLQEHAQRC GEPQDLTMNG
LGNTEEKMDL EENPDEQSEI RDMFVEMLDD FRDNHYQINS IQKKQLFKHS ACPFRCPNCG
QRFETENLVV EHMSSCLDQD MFKSAIMEEN ERDHRRKHFC NLCGKGFYQR CHLREHYTVH
TKEKQFVCQT CGKQFLRERQ LRLHNDMHKG MARYVCSICD QGNFRKHDHV RHMISHLSAG
ETICQVCFQI FPNNEQLEQH MDVHLYTCGI CGAKFNLRKD MRSHYNAKHL KRT
