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 27-MAR-2024, entry version 236. 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; O43504: LAMTOR5; NbExp=8; IntAct=EBI-711925, EBI-713382; 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; P62258: YWHAE; NbExp=2; IntAct=EBI-711925, EBI-356498; 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="https://atlasgeneticsoncology.org/gene/37/PLZF"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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; 173. DR DIP; DIP-2654N; -. DR IntAct; Q05516; 125. 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; 9606-ENSP00000338157; -. DR PeptideAtlas; Q05516; -. DR ProteomicsDB; 58332; -. [Q05516-1] DR ProteomicsDB; 58333; -. [Q05516-2] DR ABCD; Q05516; 3 sequenced antibodies. DR Antibodypedia; 897; 443 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 AGR; HGNC:12930; -. DR CTD; 7704; -. DR DisGeNET; 7704; -. DR GeneCards; ZBTB16; -. DR HGNC; HGNC:12930; ZBTB16. DR HPA; ENSG00000109906; Low tissue specificity. 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; SDAIMSM; -. DR OrthoDB; 3044976at2759; -. 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; 12 hits in 1214 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 205 other cell types or tissues. DR ExpressionAtlas; Q05516; baseline and differential. 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: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: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:0031703; F:type 2 angiotensin receptor binding; IEA:Ensembl. 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:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. 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: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:0045893; P:positive regulation of DNA-templated transcription; IDA: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: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 CDD; cd18205; BTB_POZ_ZBTB16_PLZF; 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; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24390:SF197; GH18834P-RELATED; 1. DR PANTHER; PTHR24390; ZINC FINGER PROTEIN; 1. DR Pfam; PF00651; BTB; 1. DR Pfam; PF00096; zf-C2H2; 3. DR Pfam; PF13912; zf-C2H2_6; 2. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 9. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9. DR Genevisible; Q05516; HS. 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 //