ZBT8A_HUMAN
ID ZBT8A_HUMAN Reviewed; 441 AA.
AC Q96BR9; Q8IUL5; Q8IWR9; Q8N2Y5; Q96BX0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Zinc finger and BTB domain-containing protein 8A;
DE AltName: Full=BTB/POZ and zinc-finger domain-containing factor;
DE AltName: Full=BTB/POZ and zinc-finger domains factor on chromosome 1;
DE Short=BOZ-F1;
GN Name=ZBTB8A; Synonyms=BOZF1;
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] (ISOFORMS 1 AND 2), AND VARIANT GLY-418.
RC TISSUE=Brain;
RA Goudou D., Bitoun M., Perin J.P., Alliel P.M.;
RT "Structure, genomic organization and expression of BOZ-F1.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate, Skin, and 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-437, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-199, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-199, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178; LYS-182; LYS-191 AND
RP LYS-199, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q96BR9; Q8WYK0: ACOT12; NbExp=4; IntAct=EBI-742740, EBI-11954993;
CC Q96BR9; Q8WTP8: AEN; NbExp=3; IntAct=EBI-742740, EBI-8637627;
CC Q96BR9; Q9BXS5: AP1M1; NbExp=7; IntAct=EBI-742740, EBI-541426;
CC Q96BR9; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-742740, EBI-742909;
CC Q96BR9; Q9P291: ARMCX1; NbExp=6; IntAct=EBI-742740, EBI-2843626;
CC Q96BR9; Q9UIF8-2: BAZ2B; NbExp=3; IntAct=EBI-742740, EBI-10321972;
CC Q96BR9; P51451: BLK; NbExp=3; IntAct=EBI-742740, EBI-2105445;
CC Q96BR9; Q13895: BYSL; NbExp=8; IntAct=EBI-742740, EBI-358049;
CC Q96BR9; Q9HC52: CBX8; NbExp=3; IntAct=EBI-742740, EBI-712912;
CC Q96BR9; Q16543: CDC37; NbExp=3; IntAct=EBI-742740, EBI-295634;
CC Q96BR9; Q8IVW4: CDKL3; NbExp=6; IntAct=EBI-742740, EBI-3919850;
CC Q96BR9; P48730: CSNK1D; NbExp=3; IntAct=EBI-742740, EBI-751621;
CC Q96BR9; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-742740, EBI-5453285;
CC Q96BR9; P26196: DDX6; NbExp=6; IntAct=EBI-742740, EBI-351257;
CC Q96BR9; Q92997: DVL3; NbExp=3; IntAct=EBI-742740, EBI-739789;
CC Q96BR9; Q08426: EHHADH; NbExp=3; IntAct=EBI-742740, EBI-2339219;
CC Q96BR9; Q8N9N8: EIF1AD; NbExp=6; IntAct=EBI-742740, EBI-750700;
CC Q96BR9; Q3B820: FAM161A; NbExp=6; IntAct=EBI-742740, EBI-719941;
CC Q96BR9; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-742740, EBI-6658203;
CC Q96BR9; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-742740, EBI-5666657;
CC Q96BR9; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-742740, EBI-14103818;
CC Q96BR9; V9HW29: HEL-S-61; NbExp=3; IntAct=EBI-742740, EBI-10330057;
CC Q96BR9; Q96JB3: HIC2; NbExp=5; IntAct=EBI-742740, EBI-726282;
CC Q96BR9; O75564-2: JRK; NbExp=3; IntAct=EBI-742740, EBI-17181882;
CC Q96BR9; Q92993: KAT5; NbExp=4; IntAct=EBI-742740, EBI-399080;
CC Q96BR9; P33176: KIF5B; NbExp=3; IntAct=EBI-742740, EBI-355878;
CC Q96BR9; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-742740, EBI-8472129;
CC Q96BR9; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-742740, EBI-2125614;
CC Q96BR9; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-742740, EBI-14069005;
CC Q96BR9; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-742740, EBI-10274069;
CC Q96BR9; P55081: MFAP1; NbExp=3; IntAct=EBI-742740, EBI-1048159;
CC Q96BR9; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-742740, EBI-5453723;
CC Q96BR9; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-742740, EBI-741158;
CC Q96BR9; O75928: PIAS2; NbExp=3; IntAct=EBI-742740, EBI-348555;
CC Q96BR9; P54646: PRKAA2; NbExp=3; IntAct=EBI-742740, EBI-1383852;
CC Q96BR9; Q9NV39: PRR34; NbExp=3; IntAct=EBI-742740, EBI-11959565;
CC Q96BR9; P62191: PSMC1; NbExp=3; IntAct=EBI-742740, EBI-357598;
CC Q96BR9; P54725: RAD23A; NbExp=6; IntAct=EBI-742740, EBI-746453;
CC Q96BR9; P32969: RPL9P9; NbExp=6; IntAct=EBI-742740, EBI-358122;
CC Q96BR9; O00560: SDCBP; NbExp=6; IntAct=EBI-742740, EBI-727004;
CC Q96BR9; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-742740, EBI-10246152;
CC Q96BR9; Q15560: TCEA2; NbExp=3; IntAct=EBI-742740, EBI-710310;
CC Q96BR9; Q96KP6: TNIP3; NbExp=3; IntAct=EBI-742740, EBI-2509913;
CC Q96BR9; Q8WV44: TRIM41; NbExp=4; IntAct=EBI-742740, EBI-725997;
CC Q96BR9; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-742740, EBI-10180829;
CC Q96BR9; P07947: YES1; NbExp=6; IntAct=EBI-742740, EBI-515331;
CC Q96BR9; Q13105: ZBTB17; NbExp=3; IntAct=EBI-742740, EBI-372156;
CC Q96BR9; O43167: ZBTB24; NbExp=6; IntAct=EBI-742740, EBI-744471;
CC Q96BR9; P10074: ZBTB48; NbExp=7; IntAct=EBI-742740, EBI-744864;
CC Q96BR9; Q6ZSB9: ZBTB49; NbExp=6; IntAct=EBI-742740, EBI-2859943;
CC Q96BR9; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-742740, EBI-597063;
CC Q96BR9; A0A0S2Z6H0: ZGPAT; NbExp=3; IntAct=EBI-742740, EBI-16428984;
CC Q96BR9; Q8N5A5: ZGPAT; NbExp=3; IntAct=EBI-742740, EBI-3439227;
CC Q96BR9; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-742740, EBI-2682299;
CC Q96BR9; P52744: ZNF138; NbExp=3; IntAct=EBI-742740, EBI-10746567;
CC Q96BR9; P52744-2: ZNF138; NbExp=3; IntAct=EBI-742740, EBI-10213071;
CC Q96BR9; P15622-3: ZNF250; NbExp=3; IntAct=EBI-742740, EBI-10177272;
CC Q96BR9; Q8N554: ZNF276; NbExp=7; IntAct=EBI-742740, EBI-750821;
CC Q96BR9; Q8N554-2: ZNF276; NbExp=3; IntAct=EBI-742740, EBI-10265849;
CC Q96BR9; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-742740, EBI-7233259;
CC Q96BR9; P13682: ZNF35; NbExp=3; IntAct=EBI-742740, EBI-11041653;
CC Q96BR9; Q9H9D4: ZNF408; NbExp=4; IntAct=EBI-742740, EBI-347633;
CC Q96BR9; Q8TAU3: ZNF417; NbExp=6; IntAct=EBI-742740, EBI-740727;
CC Q96BR9; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-742740, EBI-11962468;
CC Q96BR9; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-742740, EBI-10486136;
CC Q96BR9; Q32MK9: ZNF509; NbExp=3; IntAct=EBI-742740, EBI-10239929;
CC Q96BR9; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-742740, EBI-10172590;
CC Q96BR9; Q96SQ5: ZNF587; NbExp=6; IntAct=EBI-742740, EBI-6427977;
CC Q96BR9; Q5T619: ZNF648; NbExp=3; IntAct=EBI-742740, EBI-11985915;
CC Q96BR9; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-742740, EBI-11962574;
CC Q96BR9; A8K932; NbExp=3; IntAct=EBI-742740, EBI-10174671;
CC Q96BR9; Q9NWJ2; NbExp=3; IntAct=EBI-742740, EBI-10315029;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96BR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96BR9-2; Sequence=VSP_037597;
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DR EMBL; AF548353; AAN40800.1; -; mRNA.
DR EMBL; AY157873; AAN77376.1; -; mRNA.
DR EMBL; AK074546; BAC11050.1; -; mRNA.
DR EMBL; AL033529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07521.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07522.1; -; Genomic_DNA.
DR EMBL; BC015067; AAH15067.1; -; mRNA.
DR EMBL; BC015239; AAH15239.1; -; mRNA.
DR EMBL; BC029654; AAH29654.1; -; mRNA.
DR CCDS; CCDS30664.1; -. [Q96BR9-1]
DR RefSeq; NP_001035531.2; NM_001040441.2.
DR RefSeq; NP_001278425.1; NM_001291496.1.
DR AlphaFoldDB; Q96BR9; -.
DR BioGRID; 575543; 94.
DR IntAct; Q96BR9; 80.
DR STRING; 9606.ENSP00000362609; -.
DR iPTMnet; Q96BR9; -.
DR PhosphoSitePlus; Q96BR9; -.
DR BioMuta; ZBTB8A; -.
DR DMDM; 251765171; -.
DR EPD; Q96BR9; -.
DR jPOST; Q96BR9; -.
DR MassIVE; Q96BR9; -.
DR MaxQB; Q96BR9; -.
DR PaxDb; Q96BR9; -.
DR PeptideAtlas; Q96BR9; -.
DR PRIDE; Q96BR9; -.
DR ProteomicsDB; 76104; -. [Q96BR9-1]
DR ProteomicsDB; 76105; -. [Q96BR9-2]
DR Antibodypedia; 31329; 89 antibodies from 22 providers.
DR DNASU; 653121; -.
DR Ensembl; ENST00000373510.9; ENSP00000362609.3; ENSG00000160062.15. [Q96BR9-1]
DR GeneID; 653121; -.
DR KEGG; hsa:653121; -.
DR MANE-Select; ENST00000373510.9; ENSP00000362609.3; NM_001040441.3; NP_001035531.2.
DR UCSC; uc001bvn.4; human. [Q96BR9-1]
DR CTD; 653121; -.
DR GeneCards; ZBTB8A; -.
DR HGNC; HGNC:24172; ZBTB8A.
DR HPA; ENSG00000160062; Low tissue specificity.
DR MIM; 618742; gene.
DR neXtProt; NX_Q96BR9; -.
DR OpenTargets; ENSG00000160062; -.
DR PharmGKB; PA164727627; -.
DR VEuPathDB; HostDB:ENSG00000160062; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157491; -.
DR HOGENOM; CLU_022356_1_1_1; -.
DR InParanoid; Q96BR9; -.
DR OrthoDB; 755439at2759; -.
DR PhylomeDB; Q96BR9; -.
DR TreeFam; TF330979; -.
DR PathwayCommons; Q96BR9; -.
DR SignaLink; Q96BR9; -.
DR BioGRID-ORCS; 653121; 7 hits in 1131 CRISPR screens.
DR ChiTaRS; ZBTB8A; human.
DR GenomeRNAi; 653121; -.
DR Pharos; Q96BR9; Tdark.
DR PRO; PR:Q96BR9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96BR9; protein.
DR Bgee; ENSG00000160062; Expressed in cortical plate and 100 other tissues.
DR ExpressionAtlas; Q96BR9; baseline and differential.
DR Genevisible; Q96BR9; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ARUK-UCL.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..441
FT /note="Zinc finger and BTB domain-containing protein 8A"
FT /id="PRO_0000378508"
FT DOMAIN 24..92
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 282..304
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..333
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 143..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 332..441
FT /note="IHQACKLICRKCKRHVTDLTGQVVQEGTRRYRLCNECLAEFGIDSLPIDLEA
FT EQHLMSPSDGDKDSRWHLSEDENRSYVEIVEDGSADLVIQQVDDSEEEEEKEIKPNIR
FT -> MEIRIPD (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037597"
FT VARIANT 418
FT /note="A -> G (in dbSNP:rs704886)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_058085"
FT CONFLICT 206
FT /note="S -> G (in Ref. 5; AAH15067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 50155 MW; 2A2C7B30C1E8C01C CRC64;
MEISSHQSHL LQQLNEQRRQ DVFCDCSILV EGKVFKAHRN VLFASSGYFK MLLSQNSKET
SQPTTATFQA FSPDTFTVIL DFVYSGKLSL TGQNVIEVMS AASFLQMTDV ISVCKTFIKS
SLDISEKEKD RYFSLSDKDA NSNGVERSSF YSGGWQEGSS SPRSHLSPEQ GTGIISGKSW
NKYNYHPASQ KNTQQPLAKH EPRKESIKKT KHLRLSQPSE VTHYKSSKRE VRTSDSSSHV
SQSEEQAQID AEMDSTPVGY QYGQGSDVTS KSFPDDLPRM RFKCPYCTHV VKRKADLKRH
LRCHTGERPY PCQACGKRFS RLDHLSSHFR TIHQACKLIC RKCKRHVTDL TGQVVQEGTR
RYRLCNECLA EFGIDSLPID LEAEQHLMSP SDGDKDSRWH LSEDENRSYV EIVEDGSADL
VIQQVDDSEE EEEKEIKPNI R
