ID   ZBT7B_HUMAN             Reviewed;         539 AA.
AC   O15156; B4E3K5; D3DV83; J3KQQ3; Q68DR2; Q96EP2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 7B {ECO:0000305};
DE   AltName: Full=Krueppel-related zinc finger protein cKrox;
DE            Short=hcKrox;
DE   AltName: Full=T-helper-inducing POZ/Krueppel-like factor;
DE   AltName: Full=Zinc finger and BTB domain-containing protein 15;
DE   AltName: Full=Zinc finger protein 67 homolog;
DE            Short=Zfp-67;
DE   AltName: Full=Zinc finger protein 857B;
DE   AltName: Full=Zinc finger protein Th-POK;
GN   Name=ZBTB7B {ECO:0000312|HGNC:HGNC:18668};
GN   Synonyms=ZBTB15, ZFP67, ZNF857B;
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 1), AND FUNCTION.
RC   TISSUE=Skin fibroblast;
RX   PubMed=9370309; DOI=10.1016/s0378-1119(97)00360-0;
RA   Widom R.L., Culic I., Lee J.Y., Korn J.H.;
RT   "Cloning and characterization of hcKrox, a transcriptional regulator of
RT   extracellular matrix gene expression.";
RL   Gene 198:407-420(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Salivary gland;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-369, AND IDENTIFICATION BY
RP   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   [8]
RP   ACETYLATION BY EP300, AND UBIQUITINATION.
RX   PubMed=20810990; DOI=10.4049/jimmunol.1001462;
RA   Zhang M., Zhang J., Rui J., Liu X.;
RT   "p300-mediated acetylation stabilizes the Th-inducing POK factor.";
RL   J. Immunol. 185:3960-3969(2010).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, 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).
CC   -!- FUNCTION: Transcription regulator that acts as a key regulator of
CC       lineage commitment of immature T-cell precursors. Exerts distinct
CC       biological functions in the mammary epithelial cells and T cells in a
CC       tissue-specific manner. Necessary and sufficient for commitment of CD4
CC       lineage, while its absence causes CD8 commitment. Development of
CC       immature T-cell precursors (thymocytes) to either the CD4 helper or CD8
CC       killer T-cell lineages correlates precisely with their T-cell receptor
CC       specificity for major histocompatibility complex class II or class I
CC       molecules, respectively. Cross-antagonism between ZBTB7B and CBF
CC       complexes are determinative to CD4 versus CD8 cell fate decision.
CC       Suppresses RUNX3 expression and imposes CD4+ lineage fate by inducing
CC       the SOCS suppressors of cytokine signaling. induces, as a
CC       transcriptional activator, SOCS genes expression which represses RUNX3
CC       expression and promotes the CD4+ lineage fate. During CD4 lineage
CC       commitment, associates with multiple sites at the CD8 locus, acting as
CC       a negative regulator of the CD8 promoter and enhancers by epigenetic
CC       silencing through the recruitment of class II histone deacetylases,
CC       such as HDAC4 and HDAC5, to these loci. Regulates the development of
CC       IL17-producing CD1d-restricted naural killer (NK) T cells. Also
CC       functions as an important metabolic regulator in the lactating mammary
CC       glands. Critical feed-forward regulator of insulin signaling in mammary
CC       gland lactation, directly regulates expression of insulin receptor
CC       substrate-1 (IRS-1) and insulin-induced Akt-mTOR-SREBP signaling (By
CC       similarity). Transcriptional repressor of the collagen COL1A1 and
CC       COL1A2 genes. May also function as a repressor of fibronectin and
CC       possibly other extracellular matrix genes (PubMed:9370309). Potent
CC       driver of brown fat development, thermogenesis and cold-induced beige
CC       fat formation. Recruits the brown fat lncRNA 1 (Blnc1):HNRNPU
CC       ribonucleoprotein complex to activate thermogenic gene expression in
CC       brown and beige adipocytes (By similarity).
CC       {ECO:0000250|UniProtKB:Q64321, ECO:0000269|PubMed:9370309}.
CC   -!- SUBUNIT: Homodimerizes. Interacts with NCL, NEDD4 and YBX1. Interacts
CC       with HNRNPU (via RNA-binding RGG-box region); the interaction
CC       facilitates the recruitment of long non-coding RNA Blnc1 by ZBTB7B.
CC       Interacts with HDAC4 and HDAC5; the interaction allows the recruitment
CC       of HDAC4 and HDAC5 on CD8 loci for deacetylation and possible
CC       inhibition of CD8 genes expression. {ECO:0000250|UniProtKB:Q64321}.
CC   -!- INTERACTION:
CC       O15156; P41182: BCL6; NbExp=3; IntAct=EBI-740434, EBI-765407;
CC       O15156; P62993: GRB2; NbExp=3; IntAct=EBI-740434, EBI-401755;
CC       O15156; Q96G21: IMP4; NbExp=4; IntAct=EBI-740434, EBI-8641721;
CC       O15156; Q15014: MORF4L2; NbExp=3; IntAct=EBI-740434, EBI-399257;
CC       O15156; O43639: NCK2; NbExp=3; IntAct=EBI-740434, EBI-713635;
CC       O15156; Q13526: PIN1; NbExp=3; IntAct=EBI-740434, EBI-714158;
CC       O15156; P32969: RPL9P9; NbExp=3; IntAct=EBI-740434, EBI-358122;
CC       O15156; Q96HL8: SH3YL1; NbExp=3; IntAct=EBI-740434, EBI-722667;
CC       O15156; O60504: SORBS3; NbExp=3; IntAct=EBI-740434, EBI-741237;
CC       O15156; Q96C24: SYTL4; NbExp=3; IntAct=EBI-740434, EBI-747142;
CC       O15156; O15062: ZBTB5; NbExp=3; IntAct=EBI-740434, EBI-722671;
CC       O15156; Q5JPT6; NbExp=3; IntAct=EBI-740434, EBI-10244213;
CC       O15156-2; A8KA13: BCL6B; NbExp=3; IntAct=EBI-11522250, EBI-10174813;
CC       O15156-2; Q96S94-5: CCNL2; NbExp=3; IntAct=EBI-11522250, EBI-12024864;
CC       O15156-2; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-11522250, EBI-6658203;
CC       O15156-2; Q96G21: IMP4; NbExp=3; IntAct=EBI-11522250, EBI-8641721;
CC       O15156-2; O43639: NCK2; NbExp=3; IntAct=EBI-11522250, EBI-713635;
CC       O15156-2; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-11522250, EBI-10181968;
CC       O15156-2; Q96B97: SH3KBP1; NbExp=3; IntAct=EBI-11522250, EBI-346595;
CC       O15156-2; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-11522250, EBI-6550597;
CC       O15156-2; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-11522250, EBI-17208936;
CC       O15156-2; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-11522250, EBI-12287587;
CC       O15156-2; O15062: ZBTB5; NbExp=3; IntAct=EBI-11522250, EBI-722671;
CC       O15156-2; A6NJL1: ZSCAN5B; NbExp=3; IntAct=EBI-11522250, EBI-17968892;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q64321}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O15156-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O15156-2; Sequence=VSP_044721;
CC   -!- PTM: Acetylated directly and specifically by EP300 (PubMed:20810990).
CC       EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes
CC       the protein by antagonizing ubiquitin conjugation (By similarity).
CC       {ECO:0000250|UniProtKB:Q64321, ECO:0000269|PubMed:20810990}.
CC   -!- PTM: Ubiquitinated, leading to proteasomal degradation
CC       (PubMed:20810990). Competes with acetylation on Lys-206, Lys-212 and
CC       Lys-335 (By similarity). {ECO:0000250|UniProtKB:Q64321,
CC       ECO:0000269|PubMed:20810990}.
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DR   EMBL; AF007833; AAC51847.1; -; mRNA.
DR   EMBL; AK304762; BAG65517.1; -; mRNA.
DR   EMBL; CR749303; CAH18158.1; -; mRNA.
DR   EMBL; AL451085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53149.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53150.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53151.1; -; Genomic_DNA.
DR   EMBL; BC012070; AAH12070.1; -; mRNA.
DR   CCDS; CCDS1081.1; -. [O15156-1]
DR   CCDS; CCDS58030.1; -. [O15156-2]
DR   RefSeq; NP_001239335.1; NM_001252406.2. [O15156-2]
DR   RefSeq; NP_001243384.1; NM_001256455.1. [O15156-1]
DR   RefSeq; XP_006711412.2; XM_006711349.2.
DR   RefSeq; XP_006711416.1; XM_006711353.1.
DR   RefSeq; XP_006711417.1; XM_006711354.1.
DR   RefSeq; XP_006711419.1; XM_006711356.3. [O15156-1]
DR   RefSeq; XP_006711420.1; XM_006711357.1.
DR   RefSeq; XP_006711421.1; XM_006711358.1.
DR   RefSeq; XP_006711422.1; XM_006711359.2. [O15156-1]
DR   RefSeq; XP_011507900.1; XM_011509598.2.
DR   RefSeq; XP_011507901.1; XM_011509599.2. [O15156-1]
DR   AlphaFoldDB; O15156; -.
DR   SMR; O15156; -.
DR   BioGRID; 119242; 66.
DR   IntAct; O15156; 28.
DR   MINT; O15156; -.
DR   STRING; 9606.ENSP00000406286; -.
DR   iPTMnet; O15156; -.
DR   PhosphoSitePlus; O15156; -.
DR   SwissPalm; O15156; -.
DR   BioMuta; ZBTB7B; -.
DR   EPD; O15156; -.
DR   jPOST; O15156; -.
DR   MassIVE; O15156; -.
DR   MaxQB; O15156; -.
DR   PaxDb; 9606-ENSP00000406286; -.
DR   PeptideAtlas; O15156; -.
DR   ProteomicsDB; 48480; -. [O15156-1]
DR   Pumba; O15156; -.
DR   ABCD; O15156; 4 sequenced antibodies.
DR   Antibodypedia; 20407; 319 antibodies from 38 providers.
DR   DNASU; 51043; -.
DR   Ensembl; ENST00000292176.2; ENSP00000292176.2; ENSG00000160685.14. [O15156-1]
DR   Ensembl; ENST00000368426.3; ENSP00000357411.3; ENSG00000160685.14. [O15156-1]
DR   Ensembl; ENST00000417934.6; ENSP00000406286.2; ENSG00000160685.14. [O15156-2]
DR   Ensembl; ENST00000535420.6; ENSP00000438647.1; ENSG00000160685.14. [O15156-1]
DR   GeneID; 51043; -.
DR   KEGG; hsa:51043; -.
DR   MANE-Select; ENST00000535420.6; ENSP00000438647.1; NM_001256455.2; NP_001243384.1.
DR   UCSC; uc001fgk.5; human. [O15156-1]
DR   AGR; HGNC:18668; -.
DR   CTD; 51043; -.
DR   DisGeNET; 51043; -.
DR   GeneCards; ZBTB7B; -.
DR   HGNC; HGNC:18668; ZBTB7B.
DR   HPA; ENSG00000160685; Low tissue specificity.
DR   MIM; 607646; gene.
DR   neXtProt; NX_O15156; -.
DR   OpenTargets; ENSG00000160685; -.
DR   PharmGKB; PA38630; -.
DR   VEuPathDB; HostDB:ENSG00000160685; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160219; -.
DR   HOGENOM; CLU_025627_0_0_1; -.
DR   InParanoid; O15156; -.
DR   OrthoDB; 783166at2759; -.
DR   PhylomeDB; O15156; -.
DR   TreeFam; TF331824; -.
DR   PathwayCommons; O15156; -.
DR   SignaLink; O15156; -.
DR   BioGRID-ORCS; 51043; 50 hits in 1229 CRISPR screens.
DR   ChiTaRS; ZBTB7B; human.
DR   GeneWiki; ZBTB7B; -.
DR   GenomeRNAi; 51043; -.
DR   Pharos; O15156; Tbio.
DR   PRO; PR:O15156; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O15156; Protein.
DR   Bgee; ENSG00000160685; Expressed in lower esophagus mucosa and 156 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001217; F:DNA-binding transcription repressor activity; ISS:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
DR   GO; GO:0007398; P:ectoderm development; TAS:ProtInc.
DR   GO; GO:0007595; P:lactation; ISS:UniProtKB.
DR   GO; GO:0043377; P:negative regulation of CD8-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0051141; P:negative regulation of NK T cell proliferation; ISS:UniProtKB.
DR   GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0001865; P:NK T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
DR   GO; GO:2000640; P:positive regulation of SREBP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0032868; P:response to insulin; ISS:UniProtKB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR   CDD; cd18327; BTB_POZ_ZBTB7B_ZBTB15; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
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; PTHR46105; AGAP004733-PA; 1.
DR   PANTHER; PTHR46105:SF4; ZINC FINGER AND BTB DOMAIN-CONTAINING PROTEIN 7B; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
DR   Genevisible; O15156; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Developmental protein; Differentiation;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..539
FT                   /note="Zinc finger and BTB domain-containing protein 7B"
FT                   /id="PRO_0000047719"
FT   DOMAIN          34..115
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         346..368
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         374..396
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         402..424
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         430..454
FT                   /note="C2H2-type 4; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          171..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..400
FT                   /note="Required for interaction with and acetylation by
FT                   EP300"
FT                   /evidence="ECO:0000250|UniProtKB:Q64321"
FT   REGION          458..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..197
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         206
FT                   /note="N6-acetyllysine; by EP300; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64321"
FT   MOD_RES         212
FT                   /note="N6-acetyllysine; by EP300; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64321"
FT   MOD_RES         335
FT                   /note="N6-acetyllysine; by EP300; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64321"
FT   MOD_RES         369
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CROSSLNK        206
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64321"
FT   CROSSLNK        212
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64321"
FT   CROSSLNK        335
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q64321"
FT   VAR_SEQ         1
FT                   /note="M -> MLQPGPHPPSPQAAAPGEAWPGPSQAPWQSLEEKM (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044721"
FT   CONFLICT        90
FT                   /note="E -> K (in Ref. 2; BAG65517)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="E -> G (in Ref. 2; BAG65517)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="K -> R (in Ref. 1; AAC51847)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        480
FT                   /note="S -> F (in Ref. 1; AAC51847)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509..510
FT                   /note="GP -> WA (in Ref. 1; AAC51847)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   539 AA;  58027 MW;  86B3616504B05B7E CRC64;
     MGSPEDDLIG IPFPDHSSEL LSCLNEQRQL GHLCDLTIRT QGLEYRTHRA VLAACSHYFK
     KLFTEGGGGA VMGAGGSGTA TGGAGAGVCE LDFVGPEALG ALLEFAYTAT LTTSSANMPA
     VLQAARLLEI PCVIAACMEI LQGSGLEAPS PDEDDCERAR QYLEAFATAT ASGVPNGEDS
     PPQVPLPPPP PPPPRPVARR SRKPRKAFLQ TKGARANHLV PEVPTVPAHP LTYEEEEVAG
     RVGSSGGSGP GDSYSPPTGT ASPPEGPQSY EPYEGEEEEE ELVYPPAYGL AQGGGPPLSP
     EELGSDEDAI DPDLMAYLSS LHQDNLAPGL DSQDKLVRKR RSQMPQECPV CHKIIHGAGK
     LPRHMRTHTG EKPFACEVCG VRFTRNDKLK IHMRKHTGER PYSCPHCPAR FLHSYDLKNH
     MHLHTGDRPY ECHLCHKAFA KEDHLQRHLK GQNCLEVRTR RRRKDDAPPH YPPPSTAAAS
     PAGLDLSNGH LDTFRLSLAR FWEQSAPTGP PVSTPGPPDD DEEEGAPTTP QAEGAMESS
//