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ZFP54_MOUSE
ID   ZFP54_MOUSE             Reviewed;         585 AA.
AC   E9PW05; O88631; Q66JT2; Q6R5P4;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Zinc finger protein 54 {ECO:0000303|PubMed:10384051};
DE   AltName: Full=Krueppel-associated box protein 10 {ECO:0000303|PubMed:10384051};
DE            Short=KRAB10 {ECO:0000303|PubMed:10384051};
GN   Name=Zfp54 {ECO:0000303|PubMed:10384051, ECO:0000312|MGI:MGI:99201};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN   [1] {ECO:0000312|EMBL:AAC29445.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10384051; DOI=10.1007/s003359901082;
RA   Shannon M., Stubbs L.;
RT   "Molecular characterization of Zfp54, a zinc-finger-containing gene that is
RT   deleted in the embryonic lethal mutation tw18.";
RL   Mamm. Genome 10:739-743(1999).
RN   [2] {ECO:0000312|EMBL:AAR91691.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129S6/SvEvTac {ECO:0000312|EMBL:AAR91691.1};
RA   Brathwaite M., Waeltz P., Dudekula D., Qian Y., Nagaraja R.;
RT   "Genomic sequence analysis in the mouse t-complex region.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0000312|EMBL:AAH80782.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH80782.1};
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH80782.1};
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   [5] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=20624068; DOI=10.1089/dna.2010.1040;
RA   Albertsen M., Teperek M., Elholm G., Fuechtbauer E.M., Lykke-Hartmann K.;
RT   "Localization and differential expression of the Krueppel-associated box
RT   zinc finger proteins 1 and 54 in early mouse development.";
RL   DNA Cell Biol. 29:589-601(2010).
CC   -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20624068}. Note=Shows
CC       widespread expression throughout the nucleus, but appears to be
CC       excluded from nucleoli. {ECO:0000269|PubMed:20624068}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in testis, may also be
CC       expressed at low levels in heart, brain, and skeletal muscle.
CC       {ECO:0000269|PubMed:10384051}.
CC   -!- DEVELOPMENTAL STAGE: Expression is initially maternally contributed,
CC       with increased expression at the two-cell stage followed by significant
CC       decrease at the 4-cell stage, remaining consistently low through to the
CC       morula stage (PubMed:20624068). Elevated expression in early embryonic
CC       stage (7 days post coitum (dpc)) with decreased but consistent
CC       expression thereafter in whole embryos (PubMed:10384051). Increased
CC       expression at 20 dpc in testis, with lower but consistent expression
CC       thereafter (PubMed:10384051). {ECO:0000269|PubMed:10384051,
CC       ECO:0000269|PubMed:20624068}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC29445.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAR91691.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF080070; AAC29445.1; ALT_INIT; mRNA.
DR   EMBL; AY510701; AAR91691.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CT009594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC080782; AAH80782.1; -; mRNA.
DR   CCDS; CCDS37462.1; -.
DR   PIR; C40984; C40984.
DR   RefSeq; NP_035890.2; NM_011760.2.
DR   AlphaFoldDB; E9PW05; -.
DR   SMR; E9PW05; -.
DR   IntAct; E9PW05; 1.
DR   iPTMnet; E9PW05; -.
DR   PhosphoSitePlus; E9PW05; -.
DR   PaxDb; E9PW05; -.
DR   PRIDE; E9PW05; -.
DR   ProteomicsDB; 341017; -.
DR   DNASU; 22712; -.
DR   Ensembl; ENSMUST00000007884; ENSMUSP00000007884; ENSMUSG00000023882.
DR   Ensembl; ENSMUST00000165230; ENSMUSP00000132983; ENSMUSG00000023882.
DR   GeneID; 22712; -.
DR   KEGG; mmu:22712; -.
DR   UCSC; uc008aqu.1; mouse.
DR   CTD; 22712; -.
DR   MGI; MGI:99201; Zfp54.
DR   VEuPathDB; HostDB:ENSMUSG00000023882; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000153165; -.
DR   HOGENOM; CLU_002678_44_11_1; -.
DR   InParanoid; E9PW05; -.
DR   OMA; CTSEDCE; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; E9PW05; -.
DR   TreeFam; TF350864; -.
DR   Reactome; R-MMU-212436; Generic Transcription Pathway.
DR   BioGRID-ORCS; 22712; 0 hits in 71 CRISPR screens.
DR   ChiTaRS; Zfp54; mouse.
DR   PRO; PR:E9PW05; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; E9PW05; protein.
DR   Bgee; ENSMUSG00000023882; Expressed in spermatocyte and 206 other tissues.
DR   ExpressionAtlas; E9PW05; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 13.
DR   SUPFAM; SSF109640; SSF109640; 1.
DR   SUPFAM; SSF57667; SSF57667; 8.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..585
FT                   /note="Zinc finger protein 54"
FT                   /id="PRO_0000446016"
FT   DOMAIN          13..95
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         183..205
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         211..233
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         243..265
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         271..293
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         299..321
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         327..349
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         355..377
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         383..405
FT                   /note="C2H2-type 8; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         411..433
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         439..461
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         467..489
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         495..517
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         523..545
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         551..573
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..167
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000269|PubMed:20624068"
FT   CONFLICT        165
FT                   /note="F -> Y (in Ref. 1; AAC29445)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="E -> G (in Ref. 1; AAC29445)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        438
FT                   /note="T -> I (in Ref. 4; AAH80782)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   585 AA;  68369 MW;  9D9CC8C249AB375B CRC64;
     MADSSVNLSQ GLLTFRDVTV DFSQEEWECL DSAQRALYIE VMLENYSNLV YVENYCICDT
     VCQHVKTEKE SCNELGEMLH EPSNCALYNR SDTTEASNNY RCCKDQDASL DSSNPDRLKS
     THTGKERCES KDCAKSSSLC SSIAQDQRTN STNKEQRQEK YDDHFISTHS LMQQAIYIGE
     NPHQCMKYGK CFSSASSLGV QQRTDTGNKP YKCNICDKSF TECSSLKEHR KTHQRLRAGT
     NPYKCNDCGK SFSYLSALQS HHKRHTGEKR YKCKECGKSY AYRTGLKRHQ KIHTAEECYS
     CQYCGKVFHQ LSHFKSHFTL HTGEKPYKCN ECHRSFPHYV FFRRHKKNHS LQKSHKCKEC
     GKSFFILSHL KTHYRIHTGE KPYKCTKCDK LFTQYSHLRR HQRIYTGKKL YRCEVCDKWF
     TLSSSLSRHQ KIHTEAKTYK CKDCDIFFNH YSSLRRHQKV HTGERHYTCK QCGKSFTRGS
     TLRVHQRIHT GEKPYKCSEC DKSFTQASQL RTHQRVHTGE KPYVCKECGK SLTTCAILRA
     HQKIHTGEKP YKCMECDRSY IQYSHLKRHQ KVHTGEKHKI VNNVT
 
 
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