ZBT7B_HUMAN
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 03-AUG-2022, entry version 188.
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}; 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. [O15156-1]
DR RefSeq; XP_006711419.1; XM_006711356.3. [O15156-1]
DR RefSeq; XP_006711420.1; XM_006711357.1. [O15156-1]
DR RefSeq; XP_006711421.1; XM_006711358.1. [O15156-1]
DR RefSeq; XP_006711422.1; XM_006711359.2. [O15156-1]
DR RefSeq; XP_011507900.1; XM_011509598.2. [O15156-2]
DR RefSeq; XP_011507901.1; XM_011509599.2. [O15156-1]
DR AlphaFoldDB; O15156; -.
DR SMR; O15156; -.
DR BioGRID; 119242; 62.
DR IntAct; O15156; 30.
DR MINT; O15156; -.
DR STRING; 9606.ENSP00000406286; -.
DR iPTMnet; O15156; -.
DR PhosphoSitePlus; O15156; -.
DR BioMuta; ZBTB7B; -.
DR EPD; O15156; -.
DR jPOST; O15156; -.
DR MassIVE; O15156; -.
DR MaxQB; O15156; -.
DR PaxDb; O15156; -.
DR PeptideAtlas; O15156; -.
DR PRIDE; O15156; -.
DR ProteomicsDB; 48480; -. [O15156-1]
DR ABCD; O15156; 4 sequenced antibodies.
DR Antibodypedia; 20407; 293 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 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; 1318335at2759; -.
DR PhylomeDB; O15156; -.
DR TreeFam; TF331824; -.
DR PathwayCommons; O15156; -.
DR SignaLink; O15156; -.
DR BioGRID-ORCS; 51043; 48 hits in 1151 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 tissues.
DR Genevisible; O15156; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
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: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; ISS:UniProtKB.
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:0031065; P:positive regulation of histone deacetylation; 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 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; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
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
