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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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