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ZBT44_HUMAN
ID   ZBT44_HUMAN             Reviewed;         570 AA.
AC   Q8NCP5; Q6IPT8; Q86VJ7; Q86XX5;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 44;
DE   AltName: Full=BTB/POZ domain-containing protein 15;
DE   AltName: Full=Zinc finger protein 851;
GN   Name=ZBTB44; Synonyms=BTBD15, ZNF851;
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 MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP   VARIANT GLU-185.
RC   TISSUE=Brain, Liver, and Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-194, AND
RP   IDENTIFICATION BY 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP   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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-194, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-290, 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   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP   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. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8NCP5; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-5658292, EBI-541426;
CC       Q8NCP5; Q86V42: FAM124A; NbExp=3; IntAct=EBI-5658292, EBI-744506;
CC       Q8NCP5; O76003: GLRX3; NbExp=3; IntAct=EBI-5658292, EBI-374781;
CC       Q8NCP5; Q9UNA4: POLI; NbExp=3; IntAct=EBI-5658292, EBI-741774;
CC       Q8NCP5; P60900: PSMA6; NbExp=3; IntAct=EBI-5658292, EBI-357793;
CC       Q8NCP5; P54725: RAD23A; NbExp=3; IntAct=EBI-5658292, EBI-746453;
CC       Q8NCP5; Q8NB12: SMYD1; NbExp=5; IntAct=EBI-5658292, EBI-8463848;
CC       Q8NCP5; Q8IZQ1-2: WDFY3; NbExp=3; IntAct=EBI-5658292, EBI-10264625;
CC       Q8NCP5-3; P40337-2: VHL; NbExp=3; IntAct=EBI-25895743, EBI-12157263;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8NCP5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NCP5-2; Sequence=VSP_022834;
CC       Name=3;
CC         IsoId=Q8NCP5-3; Sequence=VSP_022836, VSP_022837;
CC       Name=4;
CC         IsoId=Q8NCP5-4; Sequence=VSP_022835;
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DR   EMBL; BC030580; AAH30580.1; -; mRNA.
DR   EMBL; BC049375; AAH49375.1; -; mRNA.
DR   EMBL; BC050723; AAH50723.1; -; mRNA.
DR   EMBL; BC071729; AAH71729.1; -; mRNA.
DR   CCDS; CCDS44776.1; -. [Q8NCP5-3]
DR   CCDS; CCDS73414.1; -. [Q8NCP5-1]
DR   CCDS; CCDS73415.1; -. [Q8NCP5-2]
DR   RefSeq; NP_001288027.1; NM_001301098.1.
DR   RefSeq; NP_001288028.1; NM_001301099.1. [Q8NCP5-2]
DR   RefSeq; NP_054874.3; NM_014155.4. [Q8NCP5-3]
DR   RefSeq; XP_016873112.1; XM_017017623.1.
DR   AlphaFoldDB; Q8NCP5; -.
DR   SMR; Q8NCP5; -.
DR   BioGRID; 118842; 63.
DR   IntAct; Q8NCP5; 26.
DR   MINT; Q8NCP5; -.
DR   STRING; 9606.ENSP00000380861; -.
DR   iPTMnet; Q8NCP5; -.
DR   PhosphoSitePlus; Q8NCP5; -.
DR   BioMuta; ZBTB44; -.
DR   DMDM; 74760158; -.
DR   EPD; Q8NCP5; -.
DR   jPOST; Q8NCP5; -.
DR   MassIVE; Q8NCP5; -.
DR   MaxQB; Q8NCP5; -.
DR   PaxDb; Q8NCP5; -.
DR   PeptideAtlas; Q8NCP5; -.
DR   PRIDE; Q8NCP5; -.
DR   ProteomicsDB; 72915; -. [Q8NCP5-1]
DR   ProteomicsDB; 72916; -. [Q8NCP5-2]
DR   ProteomicsDB; 72917; -. [Q8NCP5-3]
DR   ProteomicsDB; 72918; -. [Q8NCP5-4]
DR   Antibodypedia; 33097; 169 antibodies from 24 providers.
DR   DNASU; 29068; -.
DR   Ensembl; ENST00000445008.6; ENSP00000408079.1; ENSG00000196323.14. [Q8NCP5-4]
DR   Ensembl; ENST00000525842.5; ENSP00000433457.1; ENSG00000196323.14. [Q8NCP5-3]
DR   Ensembl; ENST00000530205.5; ENSP00000434177.1; ENSG00000196323.14. [Q8NCP5-2]
DR   GeneID; 29068; -.
DR   KEGG; hsa:29068; -.
DR   UCSC; uc001qfz.4; human. [Q8NCP5-1]
DR   CTD; 29068; -.
DR   DisGeNET; 29068; -.
DR   GeneCards; ZBTB44; -.
DR   HGNC; HGNC:25001; ZBTB44.
DR   HPA; ENSG00000196323; Low tissue specificity.
DR   neXtProt; NX_Q8NCP5; -.
DR   OpenTargets; ENSG00000196323; -.
DR   PharmGKB; PA162409447; -.
DR   VEuPathDB; HostDB:ENSG00000196323; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000153306; -.
DR   HOGENOM; CLU_034849_1_0_1; -.
DR   InParanoid; Q8NCP5; -.
DR   PhylomeDB; Q8NCP5; -.
DR   TreeFam; TF332673; -.
DR   PathwayCommons; Q8NCP5; -.
DR   SignaLink; Q8NCP5; -.
DR   BioGRID-ORCS; 29068; 12 hits in 1136 CRISPR screens.
DR   ChiTaRS; ZBTB44; human.
DR   GenomeRNAi; 29068; -.
DR   Pharos; Q8NCP5; Tdark.
DR   PRO; PR:Q8NCP5; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q8NCP5; protein.
DR   Bgee; ENSG00000196323; Expressed in sperm and 191 other tissues.
DR   ExpressionAtlas; Q8NCP5; baseline and differential.
DR   Genevisible; Q8NCP5; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.
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; 4.
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..570
FT                   /note="Zinc finger and BTB domain-containing protein 44"
FT                   /id="PRO_0000274608"
FT   DOMAIN          31..98
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         399..421
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         427..449
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         455..479
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         487..511
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          194..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT   MOD_RES         191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         200
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R0A2"
FT   CROSSLNK        4
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        290
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364"
FT   VAR_SEQ         451..570
FT                   /note="GKRCFRCQICSATFTSFGEYKHHMRVSRHIIRKPRIYECKTCGAMLTNSGNL
FT                   IVHLRSLNHEASELANYFQSSDFLVPDYLNQEQEETLVQYDLGEHGFESNSSVQMPVIS
FT                   QYHSKGKEP -> VPLQRQGTMIDNSQAVDEMTRNGE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022834"
FT   VAR_SEQ         451..570
FT                   /note="GKRCFRCQICSATFTSFGEYKHHMRVSRHIIRKPRIYECKTCGAMLTNSGNL
FT                   IVHLRSLNHEASELANYFQSSDFLVPDYLNQEQEETLVQYDLGEHGFESNSSVQMPVIS
FT                   QYHSKGKEP -> GHPRKSASRSSSATNCC (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022835"
FT   VAR_SEQ         451..558
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022836"
FT   VAR_SEQ         562..570
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022837"
FT   VARIANT         185
FT                   /note="K -> E (in dbSNP:rs17857365)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_030336"
SQ   SEQUENCE   570 AA;  63848 MW;  9C0E64DB7D0343DF CRC64;
     MGVKTFTHSS SSHSQEMLGK LNMLRNDGHF CDITIRVQDK IFRAHKVVLA ACSDFFRTKL
     VGQAEDENKN VLDLHHVTVT GFIPLLEYAY TATLSINTEN IIDVLAAASY MQMFSVASTC
     SEFMKSSILW NTPNSQPEKG LDAGQENNSN CNFTSRDGSI SPVSSECSVV ERTIPVCRES
     RRKRKSYIVM SPESPVKCGT QTSSPQVLNS SASYSENRNQ PVDSSLAFPW TFPFGIDRRI
     QPEKVKQAEN TRTLELPGPS ETGRRMADYV TCESTKTTLP LGTEEDVRVK VERLSDEEVH
     EEVSQPVSAS QSSLSDQQTV PGSEQVQEDL LISPQSSSIG SVDEGVSEGL PTLQSTSSTN
     APPDDDDRLE NVQYPYQLYI APSTSSTERP SPNGPDRPFQ CPTCGVRFTR IQNLKQHMLI
     HSGIKPFQCD RCGKKFTRAY SLKMHRLKHE GKRCFRCQIC SATFTSFGEY KHHMRVSRHI
     IRKPRIYECK TCGAMLTNSG NLIVHLRSLN HEASELANYF QSSDFLVPDY LNQEQEETLV
     QYDLGEHGFE SNSSVQMPVI SQYHSKGKEP
 
 
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