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Z512B_HUMAN
ID   Z512B_HUMAN             Reviewed;         892 AA.
AC   Q96KM6; Q08AK9; Q9ULM4;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Zinc finger protein 512B;
GN   Name=ZNF512B; Synonyms=KIAA1196;
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=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-892.
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-892.
RC   TISSUE=Testis;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, 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   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   [8]
RP   STRUCTURE BY NMR OF 493-577.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the two ZF-C2H2-like domains (493-575) of human zinc
RT   finger protein KIAA1196.";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       Q96KM6; Q96IF1: AJUBA; NbExp=3; IntAct=EBI-1049952, EBI-949782;
CC       Q96KM6; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-1049952, EBI-11524452;
CC       Q96KM6; Q9H3H3-3: C11orf68; NbExp=3; IntAct=EBI-1049952, EBI-12002214;
CC       Q96KM6; Q13643: FHL3; NbExp=8; IntAct=EBI-1049952, EBI-741101;
CC       Q96KM6; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1049952, EBI-618309;
CC       Q96KM6; Q99750: MDFI; NbExp=3; IntAct=EBI-1049952, EBI-724076;
CC       Q96KM6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1049952, EBI-16439278;
CC       Q96KM6; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-1049952, EBI-11522433;
CC       Q96KM6; Q96RE7: NACC1; NbExp=3; IntAct=EBI-1049952, EBI-7950997;
CC       Q96KM6; Q15276: RABEP1; NbExp=3; IntAct=EBI-1049952, EBI-447043;
CC       Q96KM6; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-1049952, EBI-747107;
CC       Q96KM6; Q13077: TRAF1; NbExp=7; IntAct=EBI-1049952, EBI-359224;
CC       Q96KM6; P52747: ZNF143; NbExp=3; IntAct=EBI-1049952, EBI-2849334;
CC       Q96KM6; Q15942: ZYX; NbExp=3; IntAct=EBI-1049952, EBI-444225;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AL118506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC125128; AAI25129.1; -; mRNA.
DR   EMBL; BC125129; AAI25130.1; -; mRNA.
DR   EMBL; AB033022; BAA86510.1; -; mRNA.
DR   EMBL; AL834525; CAD39181.1; -; mRNA.
DR   CCDS; CCDS13548.1; -.
DR   RefSeq; NP_065764.1; NM_020713.2.
DR   RefSeq; XP_011527231.1; XM_011528929.2.
DR   PDB; 2GQJ; NMR; -; A=493-577.
DR   PDBsum; 2GQJ; -.
DR   AlphaFoldDB; Q96KM6; -.
DR   SMR; Q96KM6; -.
DR   BioGRID; 121543; 179.
DR   IntAct; Q96KM6; 101.
DR   MINT; Q96KM6; -.
DR   STRING; 9606.ENSP00000393795; -.
DR   GlyGen; Q96KM6; 6 sites, 2 O-linked glycans (6 sites).
DR   iPTMnet; Q96KM6; -.
DR   PhosphoSitePlus; Q96KM6; -.
DR   BioMuta; ZNF512B; -.
DR   DMDM; 23822331; -.
DR   EPD; Q96KM6; -.
DR   jPOST; Q96KM6; -.
DR   MassIVE; Q96KM6; -.
DR   MaxQB; Q96KM6; -.
DR   PaxDb; Q96KM6; -.
DR   PeptideAtlas; Q96KM6; -.
DR   PRIDE; Q96KM6; -.
DR   ProteomicsDB; 77083; -.
DR   Antibodypedia; 29948; 108 antibodies from 17 providers.
DR   DNASU; 57473; -.
DR   Ensembl; ENST00000369888.6; ENSP00000358904.1; ENSG00000196700.9.
DR   GeneID; 57473; -.
DR   KEGG; hsa:57473; -.
DR   MANE-Select; ENST00000369888.6; ENSP00000358904.1; NM_020713.3; NP_065764.1.
DR   UCSC; uc002yhl.3; human.
DR   CTD; 57473; -.
DR   DisGeNET; 57473; -.
DR   GeneCards; ZNF512B; -.
DR   HGNC; HGNC:29212; ZNF512B.
DR   HPA; ENSG00000196700; Low tissue specificity.
DR   MIM; 617886; gene.
DR   neXtProt; NX_Q96KM6; -.
DR   OpenTargets; ENSG00000196700; -.
DR   PharmGKB; PA162410181; -.
DR   VEuPathDB; HostDB:ENSG00000196700; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000159165; -.
DR   HOGENOM; CLU_020005_1_0_1; -.
DR   InParanoid; Q96KM6; -.
DR   OMA; LAGKYHC; -.
DR   OrthoDB; 222563at2759; -.
DR   PhylomeDB; Q96KM6; -.
DR   TreeFam; TF331185; -.
DR   PathwayCommons; Q96KM6; -.
DR   Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR   SignaLink; Q96KM6; -.
DR   BioGRID-ORCS; 57473; 23 hits in 1098 CRISPR screens.
DR   ChiTaRS; ZNF512B; human.
DR   EvolutionaryTrace; Q96KM6; -.
DR   GenomeRNAi; 57473; -.
DR   Pharos; Q96KM6; Tbio.
DR   PRO; PR:Q96KM6; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q96KM6; protein.
DR   Bgee; ENSG00000196700; Expressed in parotid gland and 188 other tissues.
DR   Genevisible; Q96KM6; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IDA:ARUK-UCL.
DR   GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:ARUK-UCL.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; SSF57667; 7.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..892
FT                   /note="Zinc finger protein 512B"
FT                   /id="PRO_0000047779"
FT   ZN_FING         105..129
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         140..163
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         540..563
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         594..618
FT                   /note="C2H2-type 4; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         630..653
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         750..774
FT                   /note="C2H2-type 6; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         784..807
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..677
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   MOD_RES         686
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VARIANT         288
FT                   /note="V -> M (in dbSNP:rs45486695)"
FT                   /id="VAR_061954"
FT   VARIANT         372
FT                   /note="M -> V (in dbSNP:rs817326)"
FT                   /id="VAR_024226"
FT   VARIANT         453
FT                   /note="A -> T (in dbSNP:rs6062599)"
FT                   /id="VAR_024227"
FT   HELIX           499..502
FT                   /evidence="ECO:0007829|PDB:2GQJ"
FT   TURN            503..507
FT                   /evidence="ECO:0007829|PDB:2GQJ"
FT   TURN            513..515
FT                   /evidence="ECO:0007829|PDB:2GQJ"
FT   HELIX           524..540
FT                   /evidence="ECO:0007829|PDB:2GQJ"
FT   STRAND          543..545
FT                   /evidence="ECO:0007829|PDB:2GQJ"
FT   HELIX           552..562
FT                   /evidence="ECO:0007829|PDB:2GQJ"
SQ   SEQUENCE   892 AA;  97264 MW;  50449C476DFCE4DF CRC64;
     MTDPFCVGGR RLPGSSKSGP GKDGSRKEVR LPMLHDPPKM GMPVVRGGQT VPGQAPLCFD
     PGSPASDKTE GKKKGRPKAE NQALRDIPLS LMNDWKDEFK AHSRVKCPNS GCWLEFPSIY
     GLKYHYQRCQ GGAISDRLAF PCPFCEAAFT SKTQLEKHRI WNHMDRPLPA SKPGPISRPV
     TISRPVGVSK PIGVSKPVTI GKPVGVSKPI GISKPVSVGR PMPVTKAIPV TRPVPVTKPV
     TVSRPMPVTK AMPVTKPITV TKSVPVTKPV PVTKPITVTK LVTVTKPVPV TKPVTVSRPI
     VVSKPVTVSR PIAISRHTPP CKMVLLTRSE NKAPRATGRN SGKKRAADSL DTCPIPPKQA
     RPENGEYGPS SMGQSSAFQL SADTSSGSLS PGSRPSGGME ALKAAGPASP PEEDPERTKH
     RRKQKTPKKF TGEQPSISGT FGLKGLVKAE DKARVHRSKK QEGPGPEDAR KKVPAAPITV
     SKEAPAPVAH PAPGGPEEQW QRAIHERGEA VCPTCNVVTR KTLVGLKKHM EVCQKLQDAL
     KCQHCRKQFK SKAGLNYHTM AEHSAKPSDA EASEGGEQEE RERLRKVLKQ MGRLRCPQEG
     CGAAFSSLMG YQYHQRRCGK PPCEVDSPSF PCTHCGKTYR SKAGHDYHVR SEHTAPPPEE
     PTDKSPEAED PLGVERTPSG RVRRTSAQVA VFHLQEIAED ELARDWTKRR MKDDLVPETA
     RLNYTRPGLP TLNPQLLEAW KNEVKEKGHV NCPNDCCEAI YSSVSGLKAH LASCSKGAHL
     AGKYRCLLCP KEFSSESGVK YHILKTHAEN WFRTSADPPP KHRSQDSLVP KKEKKKNLAG
     GKKRGRKPKE RTPEEPVAKL PPRRDDWPPG CRDKGARGST GRKVGVSKAP EK
 
 
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