ZBT16_HUMAN
ID ZBT16_HUMAN Reviewed; 673 AA.
AC Q05516; Q8TAL4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Zinc finger and BTB domain-containing protein 16;
DE AltName: Full=Promyelocytic leukemia zinc finger protein;
DE AltName: Full=Zinc finger protein 145;
DE AltName: Full=Zinc finger protein PLZF;
GN Name=ZBTB16; Synonyms=PLZF, ZNF145;
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 PLZFB), ALTERNATIVE SPLICING, AND
RP CHROMOSOMAL TRANSLOCATION WITH RARA.
RC TISSUE=Heart ventricle;
RX PubMed=8384553; DOI=10.1002/j.1460-2075.1993.tb05757.x;
RA Chen Z., Brand N.J., Chen A., Chen S.-J., Tong J.-H., Wang Z.-Y.,
RA Waxman S., Zelent A.;
RT "Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid
RT receptor-alpha locus due to a variant t(11;17) translocation associated
RT with acute promyelocytic leukaemia.";
RL EMBO J. 12:1161-1167(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10500192; DOI=10.1073/pnas.96.20.11422;
RA Zhang T., Xiong H., Kan L.-X., Zhang C.-K., Jiao X.-F., Fu G., Zhang Q.-H.,
RA Lu L., Tong J.-H., Gu B.-W., Yu M., Liu J.-X., Licht J., Waxman S.,
RA Zelent A., Chen E., Chen S.-J.;
RT "Genomic sequence, structural organization, molecular evolution, and
RT aberrant rearrangement of promyelocytic leukemia zinc finger gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11422-11427(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PLZFB).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-455.
RX PubMed=8387545; DOI=10.1172/jci116453;
RA Chen S.-J., Zelent A., Tong J.-H., Yu H.-Q., Wang Z.-Y., Derre J.,
RA Berger R., Waxman S., Chen Z.;
RT "Rearrangements of the retinoic acid receptor alpha and promyelocytic
RT leukemia zinc finger genes resulting from t(11;17)(q23;q21) in a patient
RT with acute promyelocytic leukemia.";
RL J. Clin. Invest. 91:2260-2267(1993).
RN [5]
RP INTERACTION WITH ZBTB32.
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 [6]
RP FUNCTION, AND INTERACTION WITH RUNX1T1.
RX PubMed=10688654; DOI=10.1128/mcb.20.6.2075-2086.2000;
RA Melnick A.M., Westendorf J.J., Polinger A., Carlile G.W., Arai S.,
RA Ball H.J., Lutterbach B., Hiebert S.W., Licht J.D.;
RT "The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is
RT a corepressor for the promyelocytic leukemia zinc finger protein.";
RL Mol. Cell. Biol. 20:2075-2086(2000).
RN [7]
RP INTERACTION WITH EPN1.
RX PubMed=11161217; DOI=10.1126/science.291.5506.1047;
RA Itoh T., Koshiba S., Kigawa T., Kikuchi A., Yokoyama S., Takenawa T.;
RT "Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding
RT and endocytosis.";
RL Science 291:1047-1051(2001).
RN [8]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL3.
RX PubMed=14528312; DOI=10.1038/ncb1056;
RA Furukawa M., He Y.J., Borchers C., Xiong Y.;
RT "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
RT ligases.";
RL Nat. Cell Biol. 5:1001-1007(2003).
RN [9]
RP INTERACTION WITH ATP7B.
RX PubMed=16676348; DOI=10.1002/jcb.20980;
RA Ko J.H., Son W., Bae G.Y., Kang J.H., Oh W., Yoo O.J.;
RT "A new hepatocytic isoform of PLZF lacking the BTB domain interacts with
RT ATP7B, the Wilson disease protein, and positively regulates ERK signal
RT transduction.";
RL J. Cell. Biochem. 99:719-734(2006).
RN [10]
RP FUNCTION, INTERACTION WITH RNF112, AND SUBCELLULAR LOCATION.
RX PubMed=24359566; DOI=10.1186/1423-0127-20-98;
RA Lin D.Y., Huang C.C., Hsieh Y.T., Lin H.C., Pao P.C., Tsou J.H., Lai C.Y.,
RA Hung L.Y., Wang J.M., Chang W.C., Lee Y.C.;
RT "Analysis of the interaction between Zinc finger protein 179 (Znf179) and
RT promyelocytic leukemia zinc finger (Plzf).";
RL J. Biomed. Sci. 20:98-98(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 6-126.
RX PubMed=9770450; DOI=10.1073/pnas.95.21.12123;
RA Ahmad K.F., Engel C.K., Prive G.G.;
RT "Crystal structure of the BTB domain from PLZF.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12123-12128(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 7-122.
RX PubMed=10537309;
RA Li X., Peng H., Schultz D.C., Lopez-Guisa J.M., Rauscher F.J. III,
RA Marmorstein R.;
RT "Structure-function studies of the BTB/POZ transcriptional repression
RT domain from the promyelocytic leukemia zinc finger oncoprotein.";
RL Cancer Res. 59:5275-5282(1999).
RN [13]
RP VARIANT SGYMR VAL-617.
RX PubMed=18611983; DOI=10.1136/jmg.2008.059451;
RA Fischer S., Kohlhase J., Boehm D., Schweiger B., Hoffmann D., Heitmann M.,
RA Horsthemke B., Wieczorek D.;
RT "Biallelic loss of function of the promyelocytic leukaemia zinc finger
RT (PLZF) gene causes severe skeletal defects and genital hypoplasia.";
RL J. Med. Genet. 45:731-737(2008).
CC -!- FUNCTION: Acts as a transcriptional repressor (PubMed:10688654,
CC PubMed:24359566). Transcriptional repression may be mediated through
CC recruitment of histone deacetylases to target promoters
CC (PubMed:10688654). May play a role in myeloid maturation and in the
CC development and/or maintenance of other differentiated tissues.
CC Probable substrate-recognition component of an E3 ubiquitin-protein
CC ligase complex which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins (PubMed:14528312).
CC {ECO:0000269|PubMed:10688654, ECO:0000269|PubMed:14528312,
CC ECO:0000269|PubMed:24359566}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Binds EPN1 (PubMed:11161217). Interacts with ZBTB32 and CUL3
CC (PubMed:10572087, PubMed:14528312). Interacts with ATP7B
CC (PubMed:16676348). Interacts with transcriptional corepressor RUNX1T1
CC (via its N-terminus); the interaction increases the transcription
CC repression activity of ZBTB16 (PubMed:10688654). Interacts (via C2H2-
CC type zinc finger domains 1 and 2) with RNF112 (PubMed:24359566).
CC {ECO:0000269|PubMed:10572087, ECO:0000269|PubMed:10688654,
CC ECO:0000269|PubMed:11161217, ECO:0000269|PubMed:14528312,
CC ECO:0000269|PubMed:16676348, ECO:0000269|PubMed:24359566}.
CC -!- INTERACTION:
CC Q05516; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-711925, EBI-746752;
CC Q05516; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-711925, EBI-2548012;
CC Q05516; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-711925, EBI-11530605;
CC Q05516; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-711925, EBI-10175300;
CC Q05516; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-711925, EBI-739624;
CC Q05516; Q9Y2V7: COG6; NbExp=5; IntAct=EBI-711925, EBI-3866319;
CC Q05516; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-711925, EBI-751587;
CC Q05516; P68104: EEF1A1; NbExp=4; IntAct=EBI-711925, EBI-352162;
CC Q05516; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-711925, EBI-2349927;
CC Q05516; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-711925, EBI-19153639;
CC Q05516; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-711925, EBI-6658203;
CC Q05516; Q5TD97: FHL5; NbExp=3; IntAct=EBI-711925, EBI-750641;
CC Q05516; Q08379: GOLGA2; NbExp=8; IntAct=EBI-711925, EBI-618309;
CC Q05516; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-711925, EBI-5916454;
CC Q05516; O95872: GPANK1; NbExp=3; IntAct=EBI-711925, EBI-751540;
CC Q05516; Q13547: HDAC1; NbExp=2; IntAct=EBI-711925, EBI-301834;
CC Q05516; P07686: HEXB; NbExp=3; IntAct=EBI-711925, EBI-7133736;
CC Q05516; P49639: HOXA1; NbExp=3; IntAct=EBI-711925, EBI-740785;
CC Q05516; Q00444: HOXC5; NbExp=3; IntAct=EBI-711925, EBI-11955357;
CC Q05516; O75031: HSF2BP; NbExp=3; IntAct=EBI-711925, EBI-7116203;
CC Q05516; P42858: HTT; NbExp=4; IntAct=EBI-711925, EBI-466029;
CC Q05516; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-711925, EBI-14069005;
CC Q05516; Q6A162: KRT40; NbExp=9; IntAct=EBI-711925, EBI-10171697;
CC Q05516; A0A0C4DGV4: LAMTOR5; NbExp=6; IntAct=EBI-711925, EBI-10173304;
CC Q05516; O95751: LDOC1; NbExp=4; IntAct=EBI-711925, EBI-740738;
CC Q05516; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-711925, EBI-16439278;
CC Q05516; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-711925, EBI-10172526;
CC Q05516; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-711925, EBI-11522433;
CC Q05516; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-711925, EBI-6952711;
CC Q05516; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-711925, EBI-10271199;
CC Q05516; O00746: NME4; NbExp=3; IntAct=EBI-711925, EBI-744871;
CC Q05516; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-711925, EBI-1051317;
CC Q05516; O43189: PHF1; NbExp=3; IntAct=EBI-711925, EBI-530034;
CC Q05516; O75928-2: PIAS2; NbExp=3; IntAct=EBI-711925, EBI-348567;
CC Q05516; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-711925, EBI-14066006;
CC Q05516; P29590: PML; NbExp=7; IntAct=EBI-711925, EBI-295890;
CC Q05516; P29590-5: PML; NbExp=2; IntAct=EBI-711925, EBI-304008;
CC Q05516; P31321: PRKAR1B; NbExp=3; IntAct=EBI-711925, EBI-2805516;
CC Q05516; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-711925, EBI-11984839;
CC Q05516; Q04864-2: REL; NbExp=3; IntAct=EBI-711925, EBI-10829018;
CC Q05516; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-711925, EBI-726876;
CC Q05516; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-711925, EBI-10308083;
CC Q05516; Q9NYJ8: TAB2; NbExp=3; IntAct=EBI-711925, EBI-358708;
CC Q05516; Q08117-2: TLE5; NbExp=3; IntAct=EBI-711925, EBI-11741437;
CC Q05516; Q13077: TRAF1; NbExp=5; IntAct=EBI-711925, EBI-359224;
CC Q05516; Q12933: TRAF2; NbExp=5; IntAct=EBI-711925, EBI-355744;
CC Q05516; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-711925, EBI-3650647;
CC Q05516; P19474: TRIM21; NbExp=3; IntAct=EBI-711925, EBI-81290;
CC Q05516; P36406: TRIM23; NbExp=3; IntAct=EBI-711925, EBI-740098;
CC Q05516; P14373: TRIM27; NbExp=5; IntAct=EBI-711925, EBI-719493;
CC Q05516; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-711925, EBI-2130429;
CC Q05516; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-711925, EBI-9090990;
CC Q05516; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-711925, EBI-10180829;
CC Q05516; Q9NP79: VTA1; NbExp=4; IntAct=EBI-711925, EBI-740160;
CC Q05516; Q05516: ZBTB16; NbExp=8; IntAct=EBI-711925, EBI-711925;
CC Q05516; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-711925, EBI-12287587;
CC Q05516; Q9H707: ZNF552; NbExp=3; IntAct=EBI-711925, EBI-2555731;
CC Q05516; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-711925, EBI-4395669;
CC Q05516; Q8N720: ZNF655; NbExp=3; IntAct=EBI-711925, EBI-625509;
CC Q05516; O35826: Gne; Xeno; NbExp=2; IntAct=EBI-711925, EBI-7109445;
CC Q05516; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-711925, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24359566}. Nucleus,
CC nuclear body {ECO:0000269|PubMed:24359566}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=PLZFB;
CC IsoId=Q05516-1; Sequence=Displayed;
CC Name=PLZFA;
CC IsoId=Q05516-2; Sequence=VSP_006896;
CC -!- TISSUE SPECIFICITY: Within the hematopoietic system, PLZF is expressed
CC in bone marrow, early myeloid cell lines and peripheral blood
CC mononuclear cells. Also expressed in the ovary, and at lower levels, in
CC the kidney and lung.
CC -!- INDUCTION: By retinoic acid.
CC -!- DISEASE: Skeletal defects, genital hypoplasia, and impaired
CC intellectual development (SGYMR) [MIM:612447]: A disorder characterized
CC by intellectual disability, craniofacial dysmorphism, microcephaly and
CC short stature. Additional features include absence of the thumbs,
CC hypoplasia of the radii and ulnae, additional vertebrae and ribs,
CC retarded bone age and genital hypoplasia.
CC {ECO:0000269|PubMed:18611983}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving ZBTB16 may be a cause
CC of acute promyelocytic leukemia (APL). Translocation t(11;17)(q32;q21)
CC with RARA. {ECO:0000269|PubMed:8384553}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PLZFID37.html";
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DR EMBL; Z19002; CAA79489.1; -; mRNA.
DR EMBL; AF060568; AAD03619.1; -; Genomic_DNA.
DR EMBL; BC026902; AAH26902.1; -; mRNA.
DR EMBL; BC029812; AAH29812.1; -; mRNA.
DR EMBL; S60093; AAC60590.2; -; Genomic_DNA.
DR CCDS; CCDS8367.1; -. [Q05516-1]
DR PIR; S36336; S36336.
DR RefSeq; NP_001018011.1; NM_001018011.1. [Q05516-1]
DR RefSeq; NP_005997.2; NM_006006.4. [Q05516-1]
DR RefSeq; XP_016873746.1; XM_017018257.1.
DR RefSeq; XP_016873747.1; XM_017018258.1.
DR RefSeq; XP_016873748.1; XM_017018259.1. [Q05516-1]
DR PDB; 1BUO; X-ray; 1.90 A; A=6-126.
DR PDB; 1CS3; X-ray; 2.00 A; A=7-122.
DR PDBsum; 1BUO; -.
DR PDBsum; 1CS3; -.
DR AlphaFoldDB; Q05516; -.
DR SMR; Q05516; -.
DR BioGRID; 113498; 171.
DR DIP; DIP-2654N; -.
DR IntAct; Q05516; 124.
DR MINT; Q05516; -.
DR STRING; 9606.ENSP00000338157; -.
DR BindingDB; Q05516; -.
DR ChEMBL; CHEMBL4105726; -.
DR MoonDB; Q05516; Predicted.
DR iPTMnet; Q05516; -.
DR PhosphoSitePlus; Q05516; -.
DR BioMuta; ZBTB16; -.
DR DMDM; 90109930; -.
DR EPD; Q05516; -.
DR MassIVE; Q05516; -.
DR PaxDb; Q05516; -.
DR PeptideAtlas; Q05516; -.
DR PRIDE; Q05516; -.
DR ProteomicsDB; 58332; -. [Q05516-1]
DR ProteomicsDB; 58333; -. [Q05516-2]
DR ABCD; Q05516; 3 sequenced antibodies.
DR Antibodypedia; 897; 403 antibodies from 38 providers.
DR DNASU; 7704; -.
DR Ensembl; ENST00000335953.9; ENSP00000338157.4; ENSG00000109906.15. [Q05516-1]
DR Ensembl; ENST00000392996.2; ENSP00000376721.2; ENSG00000109906.15. [Q05516-1]
DR Ensembl; ENST00000682278.1; ENSP00000506794.1; ENSG00000109906.15. [Q05516-1]
DR Ensembl; ENST00000682697.1; ENSP00000506924.1; ENSG00000109906.15. [Q05516-1]
DR Ensembl; ENST00000682971.1; ENSP00000506894.1; ENSG00000109906.15. [Q05516-1]
DR Ensembl; ENST00000683318.1; ENSP00000508351.1; ENSG00000109906.15. [Q05516-1]
DR Ensembl; ENST00000683554.1; ENSP00000506953.1; ENSG00000109906.15. [Q05516-1]
DR Ensembl; ENST00000684295.1; ENSP00000507788.1; ENSG00000109906.15. [Q05516-1]
DR GeneID; 7704; -.
DR KEGG; hsa:7704; -.
DR MANE-Select; ENST00000335953.9; ENSP00000338157.4; NM_006006.6; NP_005997.2.
DR UCSC; uc001pop.4; human. [Q05516-1]
DR CTD; 7704; -.
DR DisGeNET; 7704; -.
DR GeneCards; ZBTB16; -.
DR HGNC; HGNC:12930; ZBTB16.
DR HPA; ENSG00000109906; Tissue enhanced (tongue).
DR MalaCards; ZBTB16; -.
DR MIM; 176797; gene.
DR MIM; 612447; phenotype.
DR neXtProt; NX_Q05516; -.
DR OpenTargets; ENSG00000109906; -.
DR Orphanet; 520; Acute promyelocytic leukemia.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA37517; -.
DR VEuPathDB; HostDB:ENSG00000109906; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154616; -.
DR HOGENOM; CLU_026420_0_0_1; -.
DR InParanoid; Q05516; -.
DR OMA; MGLIQLQ; -.
DR PhylomeDB; Q05516; -.
DR TreeFam; TF350825; -.
DR PathwayCommons; Q05516; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q05516; -.
DR SIGNOR; Q05516; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7704; 11 hits in 1135 CRISPR screens.
DR ChiTaRS; ZBTB16; human.
DR EvolutionaryTrace; Q05516; -.
DR GeneWiki; Zinc_finger_and_BTB_domain-containing_protein_16; -.
DR GenomeRNAi; 7704; -.
DR Pharos; Q05516; Tbio.
DR PRO; PR:Q05516; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q05516; protein.
DR Bgee; ENSG00000109906; Expressed in skin of hip and 203 other tissues.
DR ExpressionAtlas; Q05516; baseline and differential.
DR Genevisible; Q05516; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
DR GO; GO:0035136; P:forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IDA:UniProtKB.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; IEA:Ensembl.
DR GO; GO:0001823; P:mesonephros development; ISS:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; TAS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0061036; P:positive regulation of cartilage development; IDA:UniProtKB.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0051138; P:positive regulation of NK T cell differentiation; IEA:Ensembl.
DR GO; GO:0045778; P:positive regulation of ossification; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; 3.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement;
KW Disease variant; DNA-binding; Intellectual disability; Metal-binding;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..673
FT /note="Zinc finger and BTB domain-containing protein 16"
FT /id="PRO_0000047729"
FT DOMAIN 34..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 404..426
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 490..512
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 518..540
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..568
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 574..596
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 602..624
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 630..652
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 200..300
FT /note="Interaction with RUNX1T1"
FT /evidence="ECO:0000269|PubMed:10688654"
FT REGION 215..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 394..395
FT /note="Breakpoint for translocation to form PLZF-RAR-alpha
FT oncogene"
FT MOD_RES 76
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000255"
FT MOD_RES 184
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000255"
FT MOD_RES 197
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000255"
FT MOD_RES 256
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000255"
FT MOD_RES 282
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000255"
FT MOD_RES 628
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000255"
FT VAR_SEQ 255..377
FT /note="Missing (in isoform PLZFA)"
FT /evidence="ECO:0000305"
FT /id="VSP_006896"
FT VARIANT 617
FT /note="M -> V (in SGYMR; dbSNP:rs121434606)"
FT /evidence="ECO:0000269|PubMed:18611983"
FT /id="VAR_054912"
FT CONFLICT 580
FT /note="G -> D (in Ref. 1; CAA79489)"
FT /evidence="ECO:0000305"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:1BUO"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1BUO"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1BUO"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1BUO"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1BUO"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1BUO"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1CS3"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1BUO"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1BUO"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1BUO"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:1BUO"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:1BUO"
SQ SEQUENCE 673 AA; 74274 MW; 51F8E361FA31239E CRC64;
MDLTKMGMIQ LQNPSHPTGL LCKANQMRLA GTLCDVVIMV DSQEFHAHRT VLACTSKMFE
ILFHRNSQHY TLDFLSPKTF QQILEYAYTA TLQAKAEDLD DLLYAAEILE IEYLEEQCLK
MLETIQASDD NDTEATMADG GAEEEEDRKA RYLKNIFISK HSSEESGYAS VAGQSLPGPM
VDQSPSVSTS FGLSAMSPTK AAVDSLMTIG QSLLQGTLQP PAGPEEPTLA GGGRHPGVAE
VKTEMMQVDE VPSQDSPGAA ESSISGGMGD KVEERGKEGP GTPTRSSVIT SARELHYGRE
ESAEQVPPPA EAGQAPTGRP EHPAPPPEKH LGIYSVLPNH KADAVLSMPS SVTSGLHVQP
ALAVSMDFST YGGLLPQGFI QRELFSKLGE LAVGMKSESR TIGEQCSVCG VELPDNEAVE
QHRKLHSGMK TYGCELCGKR FLDSLRLRMH LLAHSAGAKA FVCDQCGAQF SKEDALETHR
QTHTGTDMAV FCLLCGKRFQ AQSALQQHME VHAGVRSYIC SECNRTFPSH TALKRHLRSH
TGDHPYECEF CGSCFRDEST LKSHKRIHTG EKPYECNGCG KKFSLKHQLE THYRVHTGEK
PFECKLCHQR SRDYSAMIKH LRTHNGASPY QCTICTEYCP SLSSMQKHMK GHKPEEIPPD
WRIEKTYLYL CYV
