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ZBT12_HUMAN
ID   ZBT12_HUMAN             Reviewed;         459 AA.
AC   Q9Y330; B0UY00; Q5JQ98;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 12;
DE   AltName: Full=Protein G10;
GN   Name=ZBTB12; Synonyms=C6orf46, G10, NG35;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA   Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shiina S., Tamiya G., Oka A., Inoko H.;
RT   "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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 THR-19, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA   Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA   Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT   "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT   network: indicating the involvement of ribonucleoside-diphosphate reductase
RT   M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT   transduction.";
RL   Mol. Cell. Proteomics 6:1952-1967(2007).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       Q9Y330; P62993: GRB2; NbExp=5; IntAct=EBI-12377219, EBI-401755;
CC       Q9Y330; O43639: NCK2; NbExp=3; IntAct=EBI-12377219, EBI-713635;
CC       Q9Y330; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-12377219, EBI-3918996;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; AF134726; AAD21810.1; -; Genomic_DNA.
DR   EMBL; BA000025; BAB63293.1; -; Genomic_DNA.
DR   EMBL; AL671762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR388219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03546.1; -; Genomic_DNA.
DR   EMBL; BC043609; AAH43609.1; -; mRNA.
DR   CCDS; CCDS4727.1; -.
DR   RefSeq; NP_862825.1; NM_181842.2.
DR   RefSeq; XP_011512685.2; XM_011514383.2.
DR   AlphaFoldDB; Q9Y330; -.
DR   SMR; Q9Y330; -.
DR   BioGRID; 128737; 27.
DR   IntAct; Q9Y330; 4.
DR   STRING; 9606.ENSP00000364677; -.
DR   iPTMnet; Q9Y330; -.
DR   PhosphoSitePlus; Q9Y330; -.
DR   BioMuta; ZBTB12; -.
DR   DMDM; 38257796; -.
DR   EPD; Q9Y330; -.
DR   jPOST; Q9Y330; -.
DR   MassIVE; Q9Y330; -.
DR   PaxDb; Q9Y330; -.
DR   PeptideAtlas; Q9Y330; -.
DR   PRIDE; Q9Y330; -.
DR   ProteomicsDB; 85966; -.
DR   Antibodypedia; 28048; 90 antibodies from 16 providers.
DR   DNASU; 221527; -.
DR   Ensembl; ENST00000375525.4; ENSP00000364675.4; ENSG00000206366.6.
DR   Ensembl; ENST00000375527.3; ENSP00000364677.2; ENSG00000204366.4.
DR   Ensembl; ENST00000432044.2; ENSP00000392328.2; ENSG00000234196.2.
DR   Ensembl; ENST00000441555.2; ENSP00000414777.2; ENSG00000237900.2.
DR   Ensembl; ENST00000458242.2; ENSP00000391563.2; ENSG00000234852.2.
DR   GeneID; 221527; -.
DR   KEGG; hsa:221527; -.
DR   MANE-Select; ENST00000375527.3; ENSP00000364677.2; NM_181842.3; NP_862825.1.
DR   UCSC; uc003nyd.2; human.
DR   CTD; 221527; -.
DR   DisGeNET; 221527; -.
DR   GeneCards; ZBTB12; -.
DR   HGNC; HGNC:19066; ZBTB12.
DR   HPA; ENSG00000204366; Low tissue specificity.
DR   neXtProt; NX_Q9Y330; -.
DR   OpenTargets; ENSG00000204366; -.
DR   PharmGKB; PA38784; -.
DR   VEuPathDB; HostDB:ENSG00000204366; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162418; -.
DR   HOGENOM; CLU_037856_0_0_1; -.
DR   InParanoid; Q9Y330; -.
DR   OMA; HFHHSTN; -.
DR   PhylomeDB; Q9Y330; -.
DR   TreeFam; TF333162; -.
DR   PathwayCommons; Q9Y330; -.
DR   SignaLink; Q9Y330; -.
DR   BioGRID-ORCS; 221527; 29 hits in 1138 CRISPR screens.
DR   GenomeRNAi; 221527; -.
DR   Pharos; Q9Y330; Tbio.
DR   PRO; PR:Q9Y330; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9Y330; protein.
DR   Bgee; ENSG00000204366; Expressed in cortical plate and 101 other tissues.
DR   Genevisible; Q9Y330; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; 4.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..459
FT                   /note="Zinc finger and BTB domain-containing protein 12"
FT                   /id="PRO_0000047728"
FT   DOMAIN          33..97
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         333..356
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         359..381
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         387..409
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         415..438
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          153..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..179
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17693683"
SQ   SEQUENCE   459 AA;  49148 MW;  EF6DD3FCC888E86F CRC64;
     MASGVEVLRF QLPGHEAATL RNMNQLRAEE RFCDVTIVAD SLKFRGHKVI LAACSPFLRD
     QFLLNPSSEL QVSLMHSARI VADLLLSCYT GALEFAVRDI VNYLTAASYL QMEHVVEKCR
     NALSQFIEPK IGLKEDGVSE ASLVSSISAT KSLLPPARTP KPAPKPPPPP PLPPPLLRPV
     KLEFPLDEDL ELKAEEEDED EDEDVSDICI VKVESALEVA HRLKPPGGLG GGLGIGGSVG
     GHLGELAQSS VPPSTVAPPQ GVVKACYSLS EDAEGEGLLL IPGGRASVGA TSGLVEAAAV
     AMAARGAGGS LGAGGSRGPL PGGFSGGNPL KNIKCTKCPE VFQGVEKLVF HMRAQHFIFM
     CPRCGKQFNH SSNLNRHMNV HRGVKSHSCG ICGKCFTQKS TLHDHLNLHS GARPYRCSYC
     DVRFAHKPAI RRHLKEQHGK TTAENVLEAS VAEINVLIR
 
 
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