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FAF1_MOUSE
ID   FAF1_MOUSE              Reviewed;         649 AA.
AC   P54731; Q6P1F8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=FAS-associated factor 1;
GN   Name=Faf1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=8524870; DOI=10.1073/pnas.92.25.11894;
RA   Chu K., Niu X., Williams L.T.;
RT   "A Fas-associated protein factor, FAF1, potentiates Fas-mediated
RT   apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:11894-11898(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319 AND SER-581, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Ubiquitin-binding protein (By similarity). Required for the
CC       progression of DNA replication forks by targeting DNA replication
CC       licensing factor CDT1 for degradation (By similarity). Potentiates but
CC       cannot initiate FAS-induced apoptosis (PubMed:8524870).
CC       {ECO:0000250|UniProtKB:Q9UNN5, ECO:0000269|PubMed:8524870}.
CC   -!- SUBUNIT: Interacts with CDT1 and ATPase VCP/p97. Interacts (via UBA
CC       domain) with FAS (via death domain). Interacts (via UBA domain) with
CC       NLRP12 (via DAPIN/PYRIN domain). {ECO:0000250|UniProtKB:Q9UNN5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNN5}.
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DR   EMBL; U39643; AAA92091.1; -; mRNA.
DR   EMBL; AL627188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL627392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466527; EDL30696.1; -; Genomic_DNA.
DR   EMBL; BC065098; AAH65098.1; -; mRNA.
DR   CCDS; CCDS18468.1; -.
DR   RefSeq; NP_032009.2; NM_007983.2.
DR   AlphaFoldDB; P54731; -.
DR   BMRB; P54731; -.
DR   SMR; P54731; -.
DR   BioGRID; 199588; 34.
DR   IntAct; P54731; 2.
DR   MINT; P54731; -.
DR   STRING; 10090.ENSMUSP00000099785; -.
DR   iPTMnet; P54731; -.
DR   PhosphoSitePlus; P54731; -.
DR   EPD; P54731; -.
DR   jPOST; P54731; -.
DR   MaxQB; P54731; -.
DR   PaxDb; P54731; -.
DR   PeptideAtlas; P54731; -.
DR   PRIDE; P54731; -.
DR   ProteomicsDB; 275850; -.
DR   Antibodypedia; 18936; 418 antibodies from 41 providers.
DR   DNASU; 14084; -.
DR   Ensembl; ENSMUST00000102724; ENSMUSP00000099785; ENSMUSG00000010517.
DR   GeneID; 14084; -.
DR   KEGG; mmu:14084; -.
DR   UCSC; uc008uct.1; mouse.
DR   CTD; 11124; -.
DR   MGI; MGI:109419; Faf1.
DR   VEuPathDB; HostDB:ENSMUSG00000010517; -.
DR   eggNOG; KOG1363; Eukaryota.
DR   GeneTree; ENSGT00940000154831; -.
DR   HOGENOM; CLU_028119_0_0_1; -.
DR   InParanoid; P54731; -.
DR   OMA; RNQQWKG; -.
DR   OrthoDB; 845154at2759; -.
DR   PhylomeDB; P54731; -.
DR   TreeFam; TF314172; -.
DR   BioGRID-ORCS; 14084; 6 hits in 74 CRISPR screens.
DR   ChiTaRS; Faf1; mouse.
DR   PRO; PR:P54731; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P54731; protein.
DR   Bgee; ENSMUSG00000010517; Expressed in floor plate of midbrain and 250 other tissues.
DR   Genevisible; P54731; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990917; C:ooplasm; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISO:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR   GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR   GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISS:UniProtKB.
DR   GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR   GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR   GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   CDD; cd14413; UBA_FAF1; 1.
DR   CDD; cd01771; UBX_UBXN3A; 1.
DR   InterPro; IPR033043; FAF1-like_UBX.
DR   InterPro; IPR044541; FAF1_UBA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR006577; UAS.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR001012; UBX_dom.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00594; UAS; 1.
DR   SMART; SM00166; UBX; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54236; SSF54236; 3.
DR   PROSITE; PS50033; UBX; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..649
FT                   /note="FAS-associated factor 1"
FT                   /id="PRO_0000211039"
FT   DOMAIN          1..57
FT                   /note="UBA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNN5"
FT   DOMAIN          568..645
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          56..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         579
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UNN5"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        7..8
FT                   /note="RE -> LP (in Ref. 1; AAA92091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="G -> S (in Ref. 1; AAA92091)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352
FT                   /note="F -> Y (in Ref. 1; AAA92091)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   649 AA;  73863 MW;  0DA48081312EFE8D CRC64;
     MASNMDREMI LADFQACTGI ENIDEAITLL EQNNWDLVAA INGVIPQENG ILQSDFGGET
     MPGPTFDPAS HPAPASTPSS SAFRPVMPSR QIVERQPRML DFRVEYRDRN VDVVLEDSCT
     VGEIKQILEN ELQIPVPKML LKGWKTGDVE DSTVLKSLHL PKNNSLYVLT PDLPPPSSSS
     HAGALQESLN QNFMLIITHR EVQREYNLNF SGSSTVQEVK RNVYDLTSIP VRHQLWEGWP
     ASATDDSMCL AESGLSYPCH RLTVGRRTSP VQTREQSEEQ STDVHMVSDS DGDDFEDASE
     FGVDDGEVFG MASSTLRKSP MMPENAENEG DALLQFTAEF SSRYGDCHPV FFIGSLEAAF
     QEAFYVKARD RKLLAIYLHH DESVLTNVFC SQMLCAESIV SYLSQNFITW AWDLTKDTNR
     ARFLTMCNRH FGSVIAQTIR TQKTDQFPLF LIIMGKRSSN EVLNVIQGNT TVDELMMRLM
     AAMEIFSAQQ QEDIKDEDER EARENVKREQ DEAYRLSLEA DRAKREAHER EMAEQFRLEQ
     IRKEQEEERE AIRLSLEQAL PPEPKEENAE PVSKLRIRTP SGEFLERRFL ASNKLQIVFD
     FVASKGFPWD EFKLLSTFPR RDVTQLDPNK SLLEVNLFPQ ETLFLQAKE
 
 
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