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   27-MAR-2024, entry version 205.
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.
DR   RefSeq; XP_016883849.1; XM_017028360.1. [Q9ULJ3-1]
DR   RefSeq; XP_016883850.1; XM_017028361.1.
DR   PDB; 1WJP; NMR; -; A=713-806.
DR   PDBsum; 1WJP; -.
DR   AlphaFoldDB; Q9ULJ3; -.
DR   BMRB; Q9ULJ3; -.
DR   SMR; Q9ULJ3; -.
DR   BioGRID; 119066; 163.
DR   IntAct; Q9ULJ3; 30.
DR   MINT; Q9ULJ3; -.
DR   STRING; 9606.ENSP00000308759; -.
DR   ChEMBL; CHEMBL5069368; -.
DR   GlyGen; Q9ULJ3; 4 sites, 1 O-linked glycan (4 sites).
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; 9606-ENSP00000308759; -.
DR   PeptideAtlas; Q9ULJ3; -.
DR   ProteomicsDB; 85046; -. [Q9ULJ3-1]
DR   ProteomicsDB; 85047; -. [Q9ULJ3-2]
DR   Pumba; Q9ULJ3; -.
DR   ABCD; Q9ULJ3; 3 sequenced antibodies.
DR   Antibodypedia; 9340; 112 antibodies from 25 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   AGR; HGNC:13083; -.
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; PMDIIRI; -.
DR   OrthoDB; 783166at2759; -.
DR   PhylomeDB; Q9ULJ3; -.
DR   TreeFam; TF331184; -.
DR   PathwayCommons; Q9ULJ3; -.
DR   SignaLink; Q9ULJ3; -.
DR   BioGRID-ORCS; 49854; 15 hits in 1222 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 184 other cell types or tissues.
DR   ExpressionAtlas; Q9ULJ3; baseline and differential.
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:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd18209; BTB_POZ_ZBTB21_ZNF295; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
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   PANTHER; PTHR24394:SF15; ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 21; 1.
DR   PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   Pfam; PF18450; zf_C2H2_6; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
DR   Genevisible; Q9ULJ3; HS.
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
//