ZBT32_HUMAN
ID ZBT32_HUMAN Reviewed; 487 AA.
AC Q9Y2Y4; Q8WVP2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Zinc finger and BTB domain-containing protein 32;
DE AltName: Full=FANCC-interacting protein;
DE AltName: Full=Fanconi anemia zinc finger protein;
DE AltName: Full=Testis zinc finger protein;
DE AltName: Full=Zinc finger protein 538;
GN Name=ZBTB32; Synonyms=FAZF, TZFP, ZNF538;
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], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10544010; DOI=10.1006/bbrc.1999.1594;
RA Lin W.-C., Lai C.-H., Tang C.J., Huang C.-J., Tang T.K.;
RT "Identification and gene structure of a novel human PLZF-related
RT transcription factor gene, TZFP.";
RL Biochem. Biophys. Res. Commun. 264:789-795(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE
RP SPLICING, AND INTERACTION WITH ZBTB16 AND FANCC.
RC TISSUE=B-cell;
RX PubMed=10572087;
RA Hoatlin M.E., Zhi Y., Ball H., Silvey K., Melnick A., Stone S., Arai S.,
RA Hawe N., Owen G., Zelent A., Licht J.D.;
RT "A novel BTB/POZ transcriptional repressor protein interacts with the
RT Fanconi anemia group C protein and PLZF.";
RL Blood 94:3737-3747(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-294.
RC TISSUE=Lymph;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-117, AND SUBUNIT.
RX PubMed=20493880; DOI=10.1016/j.jmb.2010.05.028;
RA Stogios P.J., Cuesta-Seijo J.A., Chen L., Pomroy N.C., Prive G.G.;
RT "Insights into strand exchange in BTB domain dimers from the crystal
RT structures of FAZF and Miz1.";
RL J. Mol. Biol. 400:983-997(2010).
CC -!- FUNCTION: DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3'
CC core sequence. May function as a transcriptional transactivator and
CC transcriptional repressor. Probably exerts its repressor effect by
CC preventing GATA3 from binding to DNA. May play a role in regulating the
CC differentiation and activation of helper T-cells (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10572087}.
CC -!- SUBUNIT: Homodimer (via PTB domain). Interacts with the N-terminal of
CC FANCC. Interacts with ZBTB16. Interacts with GATA3 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y2Y4; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-954098, EBI-372094;
CC Q9Y2Y4; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-954098, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10572087}.
CC Note=Located in nuclear speckles.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Some isoforms
CC are ubiquitously expressed. {ECO:0000269|PubMed:10544010}.
CC -!- DOMAIN: The C-terminal zinc finger domain functions as a
CC transcriptional transactivator. {ECO:0000250}.
CC -!- DOMAIN: The BTB (POZ) domain possesses repressor activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF130255; AAD27708.1; -; mRNA.
DR EMBL; AF165097; AAD48448.1; -; mRNA.
DR EMBL; BC017700; AAH17700.1; ALT_TERM; mRNA.
DR CCDS; CCDS12471.1; -.
DR PIR; JC7126; JC7126.
DR RefSeq; NP_001303831.1; NM_001316902.1.
DR RefSeq; NP_001303832.1; NM_001316903.1.
DR RefSeq; NP_055198.1; NM_014383.2.
DR RefSeq; XP_011525020.1; XM_011526718.2.
DR RefSeq; XP_016882078.1; XM_017026589.1.
DR PDB; 3M5B; X-ray; 2.00 A; A/B=1-117.
DR PDBsum; 3M5B; -.
DR AlphaFoldDB; Q9Y2Y4; -.
DR BMRB; Q9Y2Y4; -.
DR SMR; Q9Y2Y4; -.
DR BioGRID; 117964; 66.
DR IntAct; Q9Y2Y4; 8.
DR MINT; Q9Y2Y4; -.
DR STRING; 9606.ENSP00000376035; -.
DR iPTMnet; Q9Y2Y4; -.
DR PhosphoSitePlus; Q9Y2Y4; -.
DR BioMuta; ZBTB32; -.
DR DMDM; 74762048; -.
DR MassIVE; Q9Y2Y4; -.
DR PaxDb; Q9Y2Y4; -.
DR PeptideAtlas; Q9Y2Y4; -.
DR PRIDE; Q9Y2Y4; -.
DR ProteomicsDB; 85936; -.
DR Antibodypedia; 35117; 183 antibodies from 25 providers.
DR DNASU; 27033; -.
DR Ensembl; ENST00000262630.7; ENSP00000262630.3; ENSG00000011590.14.
DR Ensembl; ENST00000392197.7; ENSP00000376035.1; ENSG00000011590.14.
DR GeneID; 27033; -.
DR KEGG; hsa:27033; -.
DR MANE-Select; ENST00000392197.7; ENSP00000376035.1; NM_014383.3; NP_055198.1.
DR UCSC; uc002oay.3; human.
DR CTD; 27033; -.
DR DisGeNET; 27033; -.
DR GeneCards; ZBTB32; -.
DR HGNC; HGNC:16763; ZBTB32.
DR HPA; ENSG00000011590; Tissue enriched (testis).
DR MIM; 605859; gene.
DR neXtProt; NX_Q9Y2Y4; -.
DR OpenTargets; ENSG00000011590; -.
DR PharmGKB; PA142670541; -.
DR VEuPathDB; HostDB:ENSG00000011590; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162716; -.
DR HOGENOM; CLU_600733_0_0_1; -.
DR InParanoid; Q9Y2Y4; -.
DR OMA; VWRDQRI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9Y2Y4; -.
DR TreeFam; TF350825; -.
DR PathwayCommons; Q9Y2Y4; -.
DR SignaLink; Q9Y2Y4; -.
DR SIGNOR; Q9Y2Y4; -.
DR BioGRID-ORCS; 27033; 11 hits in 1131 CRISPR screens.
DR ChiTaRS; ZBTB32; human.
DR EvolutionaryTrace; Q9Y2Y4; -.
DR GeneWiki; ZBTB32; -.
DR GenomeRNAi; 27033; -.
DR Pharos; Q9Y2Y4; Tbio.
DR PRO; PR:Q9Y2Y4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y2Y4; protein.
DR Bgee; ENSG00000011590; Expressed in left testis and 95 other tissues.
DR ExpressionAtlas; Q9Y2Y4; baseline and differential.
DR Genevisible; Q9Y2Y4; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA: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; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..487
FT /note="Zinc finger and BTB domain-containing protein 32"
FT /id="PRO_0000273417"
FT DOMAIN 29..87
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 373..395
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 401..423
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 112..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 174
FT /note="R -> S (in dbSNP:rs2227278)"
FT /id="VAR_030145"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:3M5B"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:3M5B"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:3M5B"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:3M5B"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3M5B"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3M5B"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:3M5B"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3M5B"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:3M5B"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:3M5B"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:3M5B"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3M5B"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:3M5B"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:3M5B"
SQ SEQUENCE 487 AA; 52963 MW; B528F3C2AFFC4838 CRC64;
MSLPPIRLPS PYGSDRLVQL AARLRPALCD TLITVGSQEF PAHSLVLAGV SQQLGRRGQW
ALGEGISPST FAQLLNFVYG ESVELQPGEL RPLQEAARAL GVQSLEEACW RARGDRAKKP
DPGLKKHQEE PEKPSRNPER ELGDPGEKQK PEQVSRTGGR EQEMLHKHSP PRGRPEMAGA
TQEAQQEQTR SKEKRLQAPV GQRGADGKHG VLTWLRENPG GSEESLRKLP GPLPPAGSLQ
TSVTPRPSWA EAPWLVGGQP ALWSILLMPP RYGIPFYHST PTTGAWQEVW REQRIPLSLN
APKGLWSQNQ LASSSPTPGS LPQGPAQLSP GEMEESDQGH TGALATCAGH EDKAGCPPRP
HPPPAPPARS RPYACSVCGK RFSLKHQMET HYRVHTGEKP FSCSLCPQRS RDFSAMTKHL
RTHGAAPYRC SLCGAGCPSL ASMQAHMRGH SPSQLPPGWT IRSTFLYSSS RPSRPSTSPC
CPSSSTT
