ZBT7A_MOUSE
ID ZBT7A_MOUSE Reviewed; 569 AA.
AC O88939; B2RRP7; B7ZNL6; Q3U372; Q9CRJ0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Zinc finger and BTB domain-containing protein 7A {ECO:0000305};
DE AltName: Full=Leukemia/lymphoma-related factor {ECO:0000303|PubMed:9927193};
DE AltName: Full=POZ and Krueppel erythroid myeloid ontogenic factor {ECO:0000303|PubMed:15662416};
DE Short=POK erythroid myeloid ontogenic factor {ECO:0000303|PubMed:15662416};
DE Short=Pokemon {ECO:0000303|PubMed:15662416};
GN Name=Zbtb7a {ECO:0000312|MGI:MGI:1335091};
GN Synonyms=Lrf {ECO:0000303|PubMed:9927193}, Zbtb7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH BCL6, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=9927193; DOI=10.1038/sj.onc.1202332;
RA Davies J.M., Hawe N., Kabarowski J., Huang Q.-H., Zhu J., Brand N.J.,
RA Leprince D., Dhordain P., Cook M., Moriss-Kay G., Zelent A.;
RT "Novel BTB/POZ domain zinc-finger protein, LRF, is a potential target of
RT the LAZ-3/BCL-6 oncogene.";
RL Oncogene 18:365-375(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NMRI; TISSUE=Brain, and Mammary tumor;
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 [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=14701838; DOI=10.1074/jbc.m310240200;
RA Laudes M., Christodoulides C., Sewter C., Rochford J.J., Considine R.V.,
RA Sethi J.K., Vidal-Puig A., O'Rahilly S.;
RT "Role of the POZ zinc finger transcription factor FBI-1 in human and murine
RT adipogenesis.";
RL J. Biol. Chem. 279:11711-11718(2004).
RN [6]
RP FUNCTION.
RX PubMed=15337766; DOI=10.1074/jbc.m405288200;
RA Liu C.J., Prazak L., Fajardo M., Yu S., Tyagi N., Di Cesare P.E.;
RT "Leukemia/lymphoma-related factor, a POZ domain-containing transcriptional
RT repressor, interacts with histone deacetylase-1 and inhibits cartilage
RT oligomeric matrix protein gene expression and chondrogenesis.";
RL J. Biol. Chem. 279:47081-47091(2004).
RN [7]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15662416; DOI=10.1038/nature03203;
RA Maeda T., Hobbs R.M., Merghoub T., Guernah I., Zelent A., Cordon-Cardo C.,
RA Teruya-Feldstein J., Pandolfi P.P.;
RT "Role of the proto-oncogene Pokemon in cellular transformation and ARF
RT repression.";
RL Nature 433:278-285(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17495164; DOI=10.1126/science.1140881;
RA Maeda T., Merghoub T., Hobbs R.M., Dong L., Maeda M., Zakrzewski J.,
RA van den Brink M.R.M., Zelent A., Shigematsu H., Akashi K.,
RA Teruya-Feldstein J., Cattoretti G., Pandolfi P.P.;
RT "Regulation of B versus T lymphoid lineage fate decision by the proto-
RT oncogene LRF.";
RL Science 316:860-866(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-537, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, INTERACTION WITH THE DNA-DEPENDENT PROTEIN KINASE COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26446488; DOI=10.1038/ncomms9325;
RA Liu X.S., Chandramouly G., Rass E., Guan Y., Wang G., Hobbs R.M.,
RA Rajendran A., Xie A., Shah J.V., Davis A.J., Scully R., Lunardi A.,
RA Pandolfi P.P.;
RT "LRF maintains genome integrity by regulating the non-homologous end
RT joining pathway of DNA repair.";
RL Nat. Commun. 6:8325-8325(2015).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26816381; DOI=10.1126/science.aad3312;
RA Masuda T., Wang X., Maeda M., Canver M.C., Sher F., Funnell A.P.,
RA Fisher C., Suciu M., Martyn G.E., Norton L.J., Zhu C., Kurita R.,
RA Nakamura Y., Xu J., Higgs D.R., Crossley M., Bauer D.E., Orkin S.H.,
RA Kharchenko P.V., Maeda T.;
RT "Transcription factors LRF and BCL11A independently repress expression of
RT fetal hemoglobin.";
RL Science 351:285-289(2016).
RN [13]
RP FUNCTION, INTERACTION WITH RELA, REGION, AND DNA-BINDING.
RX PubMed=29813070; DOI=10.1371/journal.pbio.2004526;
RA Ramos Pittol J.M., Oruba A., Mittler G., Saccani S., van Essen D.;
RT "Zbtb7a is a transducer for the control of promoter accessibility by NF-
RT kappa B and multiple other transcription factors.";
RL PLoS Biol. 16:E2004526-E2004526(2018).
CC -!- FUNCTION: Transcription factor that represses the transcription of a
CC wide range of genes involved in cell proliferation and differentiation
CC (PubMed:15337766, PubMed:15662416, PubMed:17495164, PubMed:26816381,
CC PubMed:29813070). Directly and specifically binds to the consensus
CC sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses transcription both by
CC regulating the organization of chromatin and through the direct
CC recruitment of transcription factors to gene regulatory regions
CC (PubMed:15337766, PubMed:15662416, PubMed:26816381, PubMed:29813070).
CC Negatively regulates SMAD4 transcriptional activity in the TGF-beta
CC signaling pathway through these two mechanisms (By similarity). That
CC is, recruits the chromatin regulator HDAC1 to the SMAD4-DNA complex and
CC in parallel prevents the recruitment of the transcriptional activators
CC CREBBP and EP300 (By similarity). Collaborates with transcription
CC factors like RELA to modify the accessibility of gene transcription
CC regulatory regions to secondary transcription factors
CC (PubMed:29813070). Also directly interacts with transcription factors
CC like SP1 to prevent their binding to DNA (By similarity). Functions as
CC an androgen receptor/AR transcriptional corepressor by recruiting NCOR1
CC and NCOR2 to the androgen response elements/ARE on target genes (By
CC similarity). Thereby, negatively regulates androgen receptor signaling
CC and androgen-induced cell proliferation (By similarity). Involved in
CC the switch between fetal and adult globin expression during erythroid
CC cells maturation (PubMed:26816381). Through its interaction with the
CC NuRD complex regulates chromatin at the fetal globin genes to repress
CC their transcription (PubMed:26816381). Specifically represses the
CC transcription of the tumor suppressor ARF isoform from the CDKN2A gene
CC (PubMed:15662416). Efficiently abrogates E2F1-dependent CDKN2A
CC transactivation (PubMed:15662416). Regulates chondrogenesis through the
CC transcriptional repression of specific genes via a mechanism that also
CC requires histone deacetylation (PubMed:15337766). Regulates cell
CC proliferation through the transcriptional regulation of genes involved
CC in glycolysis (By similarity). Involved in adipogenesis through the
CC regulation of genes involved in adipocyte differentiation (By
CC similarity). Plays a key role in the differentiation of lymphoid
CC progenitors into B and T lineages (PubMed:17495164). Promotes
CC differentiation towards the B lineage by inhibiting the T-cell
CC instructive Notch signaling pathway through the specific
CC transcriptional repression of Notch downstream target genes
CC (PubMed:17495164). Also regulates osteoclast differentiation (By
CC similarity). May also play a role, independently of its transcriptional
CC activity, in double-strand break repair via classical non-homologous
CC end joining/cNHEJ (PubMed:26446488). Recruited to double-strand break
CC sites on damage DNA, interacts with the DNA-dependent protein kinase
CC complex and directly regulates its stability and activity in DNA repair
CC (PubMed:26446488). May also modulate the splicing activity of KHDRBS1
CC toward BCL2L1 in a mechanism which is histone deacetylase-dependent and
CC thereby negatively regulates the pro-apoptotic effect of KHDRBS1 (By
CC similarity). {ECO:0000250|UniProtKB:O95365,
CC ECO:0000250|UniProtKB:Q9QZ48, ECO:0000269|PubMed:15337766,
CC ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:17495164,
CC ECO:0000269|PubMed:26446488, ECO:0000269|PubMed:26816381,
CC ECO:0000269|PubMed:29813070}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with BCL6
CC (PubMed:9927193). Interacts with RELA; involved in the control by RELA
CC of the accessibility of target gene promoters (PubMed:29813070).
CC Interacts with AR (via NR LBD domain); the interaction is direct and
CC androgen-dependent (By similarity). Interacts with NCOR1 (By
CC similarity). Interacts with NCOR2 (By similarity). Interacts with
CC SMAD4; the interaction is direct and stimulated by TGFB1 (By
CC similarity). Interacts with HDAC1 (By similarity). Interacts with SP1;
CC ZBTB7A prevents the binding to GC-rich motifs in promoters and
CC represses the transcriptional activity of SP1 (By similarity).
CC Interacts with the DNA-dependent protein kinase complex/DNA-PKc
CC (PubMed:26446488). Interacts with KHDRBS1; negatively regulates KHDRBS1
CC splicing activity (By similarity). {ECO:0000250|UniProtKB:O95365,
CC ECO:0000269|PubMed:26446488, ECO:0000269|PubMed:29813070,
CC ECO:0000269|PubMed:9927193}.
CC -!- INTERACTION:
CC O88939; O09106: Hdac1; NbExp=3; IntAct=EBI-595063, EBI-301912;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15662416,
CC ECO:0000269|PubMed:9927193}. Note=Recruited to double-strand break
CC sites of damaged DNA. {ECO:0000269|PubMed:26446488}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88939-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88939-2; Sequence=VSP_035026;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9927193). In normal
CC thymus, expressed in medullary epithelial cells and Hassle's corpuscles
CC (at protein level) (PubMed:15662416). In the spleen, mainly expressed
CC in the white pulp germinal centers (at protein level)
CC (PubMed:15662416). Up-regulated in thymic lymphomas (PubMed:15662416).
CC {ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:9927193}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 9.5-10.0 dpc in limb buds, pharyngeal
CC arches, tail bud, placenta and neural tube (PubMed:9927193). Up-
CC regulated during adipocyte differentiation (PubMed:14701838).
CC {ECO:0000269|PubMed:14701838, ECO:0000269|PubMed:9927193}.
CC -!- DOMAIN: The BTB domain mediates the interaction with the androgen
CC receptor/AR and HDAC1. Also mediates the interaction with SP1.
CC {ECO:0000250|UniProtKB:O95365}.
CC -!- PTM: Sumoylated. Undergoes sumoylation with SUMO1 that may regulate its
CC transcriptional activity. {ECO:0000250|UniProtKB:O95365}.
CC -!- DISRUPTION PHENOTYPE: Death around 16.5 dpc because of severe anemia
CC with a profound block in early B-cell development (PubMed:17495164).
CC Conditional knockout in erythroid cells, leads to the expression of
CC fetal globin in peripheral blood of adult mice and inefficient
CC erythroid terminal differentiation (PubMed:26816381).
CC {ECO:0000269|PubMed:17495164, ECO:0000269|PubMed:26816381}.
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DR EMBL; AF086830; AAC35367.1; -; mRNA.
DR EMBL; AK010379; BAB26897.1; -; mRNA.
DR EMBL; AK154907; BAE32917.1; -; mRNA.
DR EMBL; CH466553; EDL31455.1; -; Genomic_DNA.
DR EMBL; BC057204; AAH57204.1; -; mRNA.
DR EMBL; BC138524; AAI38525.1; -; mRNA.
DR EMBL; BC145311; AAI45312.1; -; mRNA.
DR CCDS; CCDS35991.1; -. [O88939-1]
DR RefSeq; NP_034861.3; NM_010731.3. [O88939-1]
DR RefSeq; XP_006513342.2; XM_006513279.2. [O88939-1]
DR RefSeq; XP_006513343.2; XM_006513280.3. [O88939-1]
DR RefSeq; XP_006513345.1; XM_006513282.2. [O88939-1]
DR AlphaFoldDB; O88939; -.
DR SMR; O88939; -.
DR BioGRID; 201199; 10.
DR DIP; DIP-33318N; -.
DR IntAct; O88939; 9.
DR STRING; 10090.ENSMUSP00000047333; -.
DR iPTMnet; O88939; -.
DR PhosphoSitePlus; O88939; -.
DR EPD; O88939; -.
DR jPOST; O88939; -.
DR MaxQB; O88939; -.
DR PaxDb; O88939; -.
DR PeptideAtlas; O88939; -.
DR PRIDE; O88939; -.
DR ProteomicsDB; 302106; -. [O88939-1]
DR ProteomicsDB; 302107; -. [O88939-2]
DR Antibodypedia; 11338; 359 antibodies from 39 providers.
DR DNASU; 16969; -.
DR Ensembl; ENSMUST00000048128; ENSMUSP00000047333; ENSMUSG00000035011. [O88939-1]
DR Ensembl; ENSMUST00000117956; ENSMUSP00000113428; ENSMUSG00000035011. [O88939-1]
DR Ensembl; ENSMUST00000119606; ENSMUSP00000113612; ENSMUSG00000035011. [O88939-1]
DR GeneID; 16969; -.
DR KEGG; mmu:16969; -.
DR UCSC; uc007gfz.1; mouse. [O88939-1]
DR CTD; 51341; -.
DR MGI; MGI:1335091; Zbtb7a.
DR VEuPathDB; HostDB:ENSMUSG00000035011; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162053; -.
DR HOGENOM; CLU_025627_1_0_1; -.
DR InParanoid; O88939; -.
DR OMA; CKVRFTQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O88939; -.
DR TreeFam; TF331824; -.
DR BioGRID-ORCS; 16969; 18 hits in 74 CRISPR screens.
DR ChiTaRS; Zbtb7a; mouse.
DR PRO; PR:O88939; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O88939; protein.
DR Bgee; ENSMUSG00000035011; Expressed in ascending aorta and 247 other tissues.
DR ExpressionAtlas; O88939; baseline and differential.
DR Genevisible; O88939; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0070418; C:DNA-dependent protein kinase complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISS:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
DR GO; GO:0051216; P:cartilage development; NAS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0043249; P:erythrocyte maturation; IMP:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:UniProtKB.
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 Alternative splicing; Developmental protein; Differentiation; DNA damage;
KW DNA repair; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..569
FT /note="Zinc finger and BTB domain-containing protein 7A"
FT /id="PRO_0000047716"
FT DOMAIN 34..101
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 376..398
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 404..426
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 432..454
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 460..484
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 214..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..569
FT /note="Mediates interaction with KHDRBS1"
FT /evidence="ECO:0000250|UniProtKB:O95365"
FT REGION 343..569
FT /note="Mediates interaction with RELA"
FT /evidence="ECO:0000269|PubMed:29813070"
FT REGION 371..569
FT /note="Mediates interaction with SMAD4"
FT /evidence="ECO:0000250|UniProtKB:O95365"
FT REGION 480..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95365"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95365"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95365"
FT VAR_SEQ 532..535
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9927193"
FT /id="VSP_035026"
FT CONFLICT 433
FT /note="L -> M (in Ref. 2; BAB26897)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="G -> D (in Ref. 2; BAE32917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 60281 MW; B4F79FF89A88CBD5 CRC64;
MAGGVDGPIG IPFPDHSSDI LSGLNEQRTQ GLLCDVVILV EGREFPTHRS VLAACSQYFK
KLFTSGAVVD QQNVYEIDFV SAEALTALMD FAYTATLTVS TANVGDILSA ARLLEIPAVS
HVCADLLERQ ILAADDVGDA SQPDGAGPTD QRNLLRAKEY LEFFRSNPMN SLPPTAFPWS
GFGAPDDDLD ATKEAVAAAV AAVAAGDCNG LDFYGPGPPA DRPPAGDGDE GDSTPGLWPE
RDEDAPPGGL FPPPTAPPAT TQNGHYGRAG AGTGEEEAAA LSEAAPEPGD SPGFLSGAAE
GEDGDAADVD GLAASTLLQQ MMSSVGRAGD SDEESRTDDK GVMDYYLKYF SGAHEGDVYP
AWSQKGEKKI RAKAFQKCPI CEKVIQGAGK LPRHIRTHTG EKPYECNICK VRFTRQDKLK
VHMRKHTGEK PYLCQQCGAA FAHNYDLKNH MRVHTGLRPY QCDSCCKTFV RSDHLHRHLK
KDGCNGVPSR RGRKPRVRGV PPDVPAGAGA PPGLPDAPRN GQEKHFKDEE EDEEEASPDG
SGRLNVAGSG GDDGAGGPAV ATAEGNFAT
