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ZN445_HUMAN
ID   ZN445_HUMAN             Reviewed;        1031 AA.
AC   P59923; Q3MJD1;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Zinc finger protein 445 {ECO:0000305};
DE            Short=ZFP445 {ECO:0000303|PubMed:30602440};
DE   AltName: Full=Zinc finger protein 168;
DE   AltName: Full=Zinc finger protein with KRAB and SCAN domains 15;
GN   Name=ZNF445 {ECO:0000312|HGNC:HGNC:21018};
GN   Synonyms=ZFP445 {ECO:0000303|PubMed:30602440}, ZKSCAN15, ZNF168;
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].
RA   Shan Y.X., Luo K.T., Guo Z.K., Tang W.W., Ye G.M., Yu L., Huang C.Q.;
RT   "Cloning and characterization of a novel zinc finger protein.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-938, 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   [4]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-28, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [5]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-938, 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   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-317; LYS-374; LYS-375; LYS-399;
RP   LYS-567; LYS-654; LYS-736; LYS-758; LYS-938; LYS-956 AND LYS-975, AND
RP   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).
RN   [7]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=30602440; DOI=10.1101/gad.320069.118;
RA   Takahashi N., Coluccio A., Thorball C.W., Planet E., Shi H., Offner S.,
RA   Turelli P., Imbeault M., Ferguson-Smith A.C., Trono D.;
RT   "ZNF445 is a primary regulator of genomic imprinting.";
RL   Genes Dev. 33:49-54(2019).
CC   -!- FUNCTION: Transcription regulator required to maintain maternal and
CC       paternal gene imprinting, a process by which gene expression is
CC       restricted in a parent of origin-specific manner by epigenetic
CC       modification of genomic DNA and chromatin, including DNA methylation.
CC       Acts by controlling DNA methylation during the earliest multicellular
CC       stages of development at multiple imprinting control regions (ICRs)
CC       (PubMed:30602440). Acts together with ZFP57, but seems to be the major
CC       factor in human early embryonic imprinting maintenance. In contrast, in
CC       mice, ZFP57 plays the predominant role in imprinting maintenance
CC       (PubMed:30602440). {ECO:0000269|PubMed:30602440}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30602440}. Note=Binds
CC       various differentially methylated regions (DMR).
CC       {ECO:0000269|PubMed:30602440}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the oocyte, expression is maintained
CC       at least until blastocyst stage. {ECO:0000269|PubMed:30602440}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AY262260; AAP36990.1; -; mRNA.
DR   EMBL; AY295873; AAP50258.1; -; mRNA.
DR   EMBL; BC101486; AAI01487.1; -; mRNA.
DR   CCDS; CCDS2713.1; -.
DR   RefSeq; NP_852466.1; NM_181489.5.
DR   RefSeq; XP_005265159.1; XM_005265102.2.
DR   RefSeq; XP_011531976.1; XM_011533674.2.
DR   AlphaFoldDB; P59923; -.
DR   SMR; P59923; -.
DR   BioGRID; 131672; 57.
DR   IntAct; P59923; 21.
DR   MINT; P59923; -.
DR   STRING; 9606.ENSP00000413073; -.
DR   iPTMnet; P59923; -.
DR   PhosphoSitePlus; P59923; -.
DR   BioMuta; ZNF445; -.
DR   DMDM; 45593854; -.
DR   EPD; P59923; -.
DR   jPOST; P59923; -.
DR   MassIVE; P59923; -.
DR   MaxQB; P59923; -.
DR   PaxDb; P59923; -.
DR   PeptideAtlas; P59923; -.
DR   PRIDE; P59923; -.
DR   ProteomicsDB; 57172; -.
DR   Antibodypedia; 29430; 48 antibodies from 13 providers.
DR   DNASU; 353274; -.
DR   Ensembl; ENST00000396077.8; ENSP00000379387.2; ENSG00000185219.18.
DR   Ensembl; ENST00000425708.6; ENSP00000413073.2; ENSG00000185219.18.
DR   Ensembl; ENST00000634579.1; ENSP00000489139.1; ENSG00000283034.2.
DR   Ensembl; ENST00000635479.2; ENSP00000489368.1; ENSG00000283034.2.
DR   GeneID; 353274; -.
DR   KEGG; hsa:353274; -.
DR   MANE-Select; ENST00000396077.8; ENSP00000379387.2; NM_181489.6; NP_852466.1.
DR   UCSC; uc003cnf.3; human.
DR   CTD; 353274; -.
DR   GeneCards; ZNF445; -.
DR   HGNC; HGNC:21018; ZNF445.
DR   HPA; ENSG00000185219; Low tissue specificity.
DR   MIM; 619508; gene.
DR   neXtProt; NX_P59923; -.
DR   OpenTargets; ENSG00000185219; -.
DR   PharmGKB; PA134904986; -.
DR   VEuPathDB; HostDB:ENSG00000185219; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00900000141186; -.
DR   HOGENOM; CLU_002678_23_0_1; -.
DR   InParanoid; P59923; -.
DR   OMA; CHKCNIC; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P59923; -.
DR   TreeFam; TF350827; -.
DR   PathwayCommons; P59923; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; P59923; -.
DR   BioGRID-ORCS; 353274; 23 hits in 1111 CRISPR screens.
DR   ChiTaRS; ZNF445; human.
DR   GenomeRNAi; 353274; -.
DR   Pharos; P59923; Tdark.
DR   PRO; PR:P59923; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P59923; protein.
DR   Bgee; ENSG00000185219; Expressed in cortical plate and 110 other tissues.
DR   ExpressionAtlas; P59923; baseline and differential.
DR   Genevisible; P59923; HS.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB.
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:0010216; P:maintenance of DNA methylation; IMP:UniProtKB.
DR   GO; GO:2000653; P:regulation of genetic imprinting; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 11.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 14.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 9.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1031
FT                   /note="Zinc finger protein 445"
FT                   /id="PRO_0000047594"
FT   DOMAIN          55..137
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   DOMAIN          234..304
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         485..507
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         513..535
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         541..563
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         597..619
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         625..647
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         681..703
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         709..731
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         762..784
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         790..812
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         840..862
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         868..890
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         896..918
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         978..1000
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1006..1028
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        28
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        317
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        374
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        375
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        399
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        567
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        654
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        736
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        758
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        938
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT   CROSSLNK        956
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        975
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         428
FT                   /note="Y -> C (in dbSNP:rs11710965)"
FT                   /id="VAR_052832"
SQ   SEQUENCE   1031 AA;  118963 MW;  39C288802894006E CRC64;
     MPPGRWHAAY PAQAQSSRER GRLQTVKKEE EDESYTPVQA ARPQTLNRPG QELFRQLFRQ
     LRYHESSGPL ETLSRLRELC RWWLRPDVLS KAQILELLVL EQFLSILPGE LRVWVQLHNP
     ESGEEAVALL EELQRDLDGT SWRDPGPAQS PDVHWMGTGA LRSAQIWSLA SPLRSSSALG
     DHLEPPYEIE ARDFLAGQSD TPAAQMPALF PREGCPGDQV TPTRSLTAQL QETMTFKDVE
     VTFSQDEWGW LDSAQRNLYR DVMLENYRNM ASLVGPFTKP ALISWLEARE PWGLNMQAAQ
     PKGNPVAAPT GDDLQSKTNK FILNQEPLEE AETLAVSSGC PATSVSEGIG LRESFQQKSR
     QKDQCENPIQ VRVKKEETNF SHRTGKDSEV SGSNSLDLKH VTYLRVSGRK ESLKHGCGKH
     FRMSSHHYDY KKYGKGLRHM IGGFSLHQRI HSGLKGNKKD VCGKDFSLSS HHQRGQSLHT
     VGVSFKCSDC GRTFSHSSHL AYHQRLHTQE KAFKCRVCGK AFRWSSNCAR HEKIHTGVKP
     YKCDLCEKAF RRLSAYRLHR ETHAKKKFLE LNQYRAALTY SSGFDHHLGD QSGEKLFDCS
     QCRKSFHCKS YVLEHQRIHT QEKPYKCTKC RKTFRWRSNF TRHMRLHEEE KFYKQDECRE
     GFRQSPDCSQ PQGAPAVEKT FLCQQCGKTF TRKKTLVDHQ RIHTGEKPYQ CSDCGKDFAY
     RSAFIVHKKK HAMKRKPEGG PSFSQDTVFQ VPQSSHSKEE PYKCSQCGKA FRNHSFLLIH
     QRVHTGEKPY KCRECGKAFR WSSNLYRHQR IHSLQKQYDC HESEKTPNVE PKILTGEKRF
     WCQECGKTFT RKRTLLDHKG IHSGEKRYKC NLCGKSYDRN YRLVNHQRIH STERPFKCQW
     CGKEFIGRHT LSSHQRKHTR AAQAERSPPA RSSSQDTKLR LQKLKPSEEM PLEDCKEACS
     QSSRLTGLQD ISIGKKCHKC SICGKTFNKS SQLISHKRFH TRERPFKCSK CGKTFRWSSN
     LARHMKNHIR D
 
 
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