Full text data of FAF1
FAF1
(UBXD12, UBXN3A)
[Confidence: low (only semi-automatic identification from reviews)]
FAS-associated factor 1; hFAF1 (UBX domain-containing protein 12; UBX domain-containing protein 3A)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
FAS-associated factor 1; hFAF1 (UBX domain-containing protein 12; UBX domain-containing protein 3A)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UNN5
ID FAF1_HUMAN Reviewed; 650 AA.
AC Q9UNN5; Q549F0; Q9UF34; Q9UNT3; Q9Y2Z3;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=FAS-associated factor 1;
DE Short=hFAF1;
DE AltName: Full=UBX domain-containing protein 12;
DE AltName: Full=UBX domain-containing protein 3A;
GN Name=FAF1; Synonyms=UBXD12, UBXN3A; ORFNames=CGI-03;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND
RP CHARACTERIZATION.
RC TISSUE=Brain, and Liver;
RX PubMed=10462485; DOI=10.1006/bbrc.1999.1217;
RA Ryu S.-W., Chae S.-K., Lee K.-J., Kim E.;
RT "Identification and characterization of human Fas associated factor 1,
RT hFAF1.";
RL Biochem. Biophys. Res. Commun. 262:388-394(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA Ding J.B., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Mus musculus FAF1.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA Boldyreff B.;
RT "Full length cDNA sequence and chromosomal localization of the human
RT Fas-associated factor 1 gene, hFaf1.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Brain, and Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-650 (ISOFORM LONG).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH NLRP12.
RX PubMed=21978668; DOI=10.1016/j.jmb.2011.09.024;
RA Pinheiro A.S., Eibl C., Ekman-Vural Z., Schwarzenbacher R., Peti W.;
RT "The NLRP12 pyrin domain: structure, dynamics, and functional
RT insights.";
RL J. Mol. Biol. 413:790-803(2011).
RN [14]
RP STRUCTURE BY NMR OF 569-650.
RX PubMed=11243799; DOI=10.1006/jmbi.2000.4462;
RA Buchberger A., Howard M.J., Proctor M., Bycroft M.M.;
RT "The UBX domain: a widespread ubiquitin-like module.";
RL J. Mol. Biol. 307:17-24(2001).
RN [15]
RP STRUCTURE BY NMR OF 99-191.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ubiquitin-like domain in human FAS-
RT associated factor 1 (hFAF1).";
RL Submitted (OCT-2007) to the PDB data bank.
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 5-47, AND DOMAIN UBA.
RX PubMed=19722279; DOI=10.1002/pro.237;
RA Song J., Park J.K., Lee J.J., Choi Y.S., Ryu K.S., Kim J.H., Kim E.,
RA Lee K.J., Jeon Y.H., Kim E.E.;
RT "Structure and interaction of ubiquitin-associated domain of human
RT Fas-associated factor 1.";
RL Protein Sci. 18:2265-2276(2009).
CC -!- FUNCTION: Potentiates but cannot initiate FAS-induced apoptosis.
CC -!- SUBUNIT: Specifically interacts with the cytoplasmic domain of
CC FAS. Interacts with NLRP12 DAPIN/PYRIN domain via its UBA domain.
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9UNN5-1; Sequence=Displayed;
CC Name=Short; Synonyms=hFAF1(s);
CC IsoId=Q9UNN5-2; Sequence=VSP_006704;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Most abundant in testis, slightly less
CC abundant in skeletal muscle and heart, followed by prostate,
CC thymus, ovary, small intestine, and colon. Not detected in the
CC peripheral blood leukocytes.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51876.1; Type=Erroneous initiation;
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DR EMBL; AF106798; AAD51886.1; -; mRNA.
DR EMBL; AF094700; AAD51876.1; ALT_INIT; mRNA.
DR EMBL; AF136173; AAP97263.1; -; mRNA.
DR EMBL; AJ271408; CAB67705.1; -; mRNA.
DR EMBL; AF132938; AAD27713.1; -; mRNA.
DR EMBL; AL359977; CAH70189.1; -; Genomic_DNA.
DR EMBL; AC091610; CAH70189.1; JOINED; Genomic_DNA.
DR EMBL; AC118557; CAH70189.1; JOINED; Genomic_DNA.
DR EMBL; AL049637; CAH70189.1; JOINED; Genomic_DNA.
DR EMBL; AL603746; CAH70189.1; JOINED; Genomic_DNA.
DR EMBL; AL603746; CAH72113.1; -; Genomic_DNA.
DR EMBL; AC091610; CAH72113.1; JOINED; Genomic_DNA.
DR EMBL; AC118557; CAH72113.1; JOINED; Genomic_DNA.
DR EMBL; AL049637; CAH72113.1; JOINED; Genomic_DNA.
DR EMBL; AL359977; CAH72113.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX06837.1; -; Genomic_DNA.
DR EMBL; BC004970; AAH04970.1; -; mRNA.
DR EMBL; BC067100; AAH67100.1; -; mRNA.
DR EMBL; AL133631; CAB63755.1; -; mRNA.
DR PIR; JC7093; JC7093.
DR PIR; T43466; T43466.
DR RefSeq; NP_008982.1; NM_007051.2.
DR UniGene; Hs.530402; -.
DR PDB; 1H8C; NMR; -; A=569-650.
DR PDB; 2DZM; NMR; -; A=99-191.
DR PDB; 2EC4; NMR; -; A=325-495.
DR PDB; 3E21; X-ray; 1.73 A; A=5-47.
DR PDB; 3QC8; X-ray; 2.20 A; B=571-650.
DR PDB; 3QCA; X-ray; 2.90 A; A/B/C/D=571-650.
DR PDB; 3QQ8; X-ray; 2.00 A; B=568-650.
DR PDB; 3QWZ; X-ray; 2.00 A; B=571-650.
DR PDB; 3QX1; X-ray; 1.60 A; A/B=571-650.
DR PDB; 3R3M; X-ray; 3.00 A; A/B/C/D=568-650.
DR PDBsum; 1H8C; -.
DR PDBsum; 2DZM; -.
DR PDBsum; 2EC4; -.
DR PDBsum; 3E21; -.
DR PDBsum; 3QC8; -.
DR PDBsum; 3QCA; -.
DR PDBsum; 3QQ8; -.
DR PDBsum; 3QWZ; -.
DR PDBsum; 3QX1; -.
DR PDBsum; 3R3M; -.
DR ProteinModelPortal; Q9UNN5; -.
DR SMR; Q9UNN5; 5-44, 99-191, 325-495, 570-649.
DR DIP; DIP-38245N; -.
DR IntAct; Q9UNN5; 49.
DR MINT; MINT-88745; -.
DR STRING; 9606.ENSP00000379457; -.
DR PhosphoSite; Q9UNN5; -.
DR DMDM; 20454906; -.
DR PaxDb; Q9UNN5; -.
DR PRIDE; Q9UNN5; -.
DR DNASU; 11124; -.
DR Ensembl; ENST00000371778; ENSP00000360843; ENSG00000185104.
DR Ensembl; ENST00000396153; ENSP00000379457; ENSG00000185104.
DR GeneID; 11124; -.
DR KEGG; hsa:11124; -.
DR UCSC; uc001cse.1; human.
DR CTD; 11124; -.
DR GeneCards; GC01M050905; -.
DR HGNC; HGNC:3578; FAF1.
DR HPA; HPA018253; -.
DR HPA; HPA019008; -.
DR MIM; 604460; gene.
DR neXtProt; NX_Q9UNN5; -.
DR PharmGKB; PA27976; -.
DR eggNOG; NOG288188; -.
DR HOGENOM; HOG000043073; -.
DR HOVERGEN; HBG002876; -.
DR InParanoid; Q9UNN5; -.
DR OMA; WEGWPAS; -.
DR OrthoDB; EOG72NRPV; -.
DR PhylomeDB; Q9UNN5; -.
DR SignaLink; Q9UNN5; -.
DR ChiTaRS; FAF1; human.
DR EvolutionaryTrace; Q9UNN5; -.
DR GeneWiki; FAF1; -.
DR GenomeRNAi; 11124; -.
DR NextBio; 42280; -.
DR PRO; PR:Q9UNN5; -.
DR ArrayExpress; Q9UNN5; -.
DR Bgee; Q9UNN5; -.
DR CleanEx; HS_FAF1; -.
DR Genevestigator; Q9UNN5; -.
DR GO; GO:0031265; C:CD95 death-inducing signaling complex; NAS:UniProtKB.
DR GO; GO:0034098; C:Cdc48p-Npl4p-Ufd1p AAA ATPase complex; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0019887; F:protein kinase regulator activity; NAS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008219; P:cell death; IMP:UniProtKB.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein complex assembly; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0042176; P:regulation of protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR001012; UBX.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50030; UBA; FALSE_NEG.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Complete proteome;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1 650 FAS-associated factor 1.
FT /FTId=PRO_0000211038.
FT DOMAIN 1 57 UBA.
FT DOMAIN 569 646 UBX.
FT MOD_RES 320 320 Phosphoserine.
FT VAR_SEQ 188 339 Missing (in isoform Short).
FT /FTId=VSP_006704.
FT CONFLICT 448 448 F -> K (in Ref. 1; AAD51886/AAD51876).
FT CONFLICT 498 498 E -> G (in Ref. 1; AAD51886/AAD51876).
FT CONFLICT 529 529 H -> R (in Ref. 1; AAD51886/AAD51876).
FT HELIX 7 18
FT HELIX 23 32
FT TURN 33 35
FT HELIX 37 41
FT STRAND 100 106
FT STRAND 111 117
FT HELIX 122 133
FT TURN 137 139
FT STRAND 146 148
FT HELIX 156 159
FT STRAND 163 169
FT STRAND 172 174
FT HELIX 330 345
FT HELIX 357 362
FT STRAND 365 367
FT TURN 369 371
FT STRAND 374 380
FT HELIX 386 393
FT TURN 394 396
FT HELIX 398 406
FT STRAND 408 414
FT HELIX 418 431
FT HELIX 434 442
FT STRAND 449 454
FT STRAND 463 467
FT HELIX 473 490
FT STRAND 573 579
FT STRAND 585 591
FT HELIX 596 605
FT TURN 610 612
FT STRAND 613 616
FT STRAND 618 620
FT HELIX 624 626
FT TURN 633 637
FT STRAND 640 648
SQ SEQUENCE 650 AA; 73954 MW; 7FB9018B9A230488 CRC64;
MASNMDREMI LADFQACTGI ENIDEAITLL EQNNWDLVAA INGVIPQENG ILQSEYGGET
IPGPAFNPAS HPASAPTSSS SSAFRPVMPS RQIVERQPRM LDFRVEYRDR NVDVVLEDTC
TVGEIKQILE NELQIPVSKM LLKGWKTGDV EDSTVLKSLH LPKNNSLYVL TPDLPPPSSS
SHAGALQESL NQNFMLIITH REVQREYNLN FSGSSTIQEV KRNVYDLTSI PVRHQLWEGW
PTSATDDSMC LAESGLSYPC HRLTVGRRSS PAQTREQSEE QITDVHMVSD SDGDDFEDAT
EFGVDDGEVF GMASSALRKS PMMPENAENE GDALLQFTAE FSSRYGDCHP VFFIGSLEAA
FQEAFYVKAR DRKLLAIYLH HDESVLTNVF CSQMLCAESI VSYLSQNFIT WAWDLTKDSN
RARFLTMCNR HFGSVVAQTI RTQKTDQFPL FLIIMGKRSS NEVLNVIQGN TTVDELMMRL
MAAMEIFTAQ QQEDIKDEDE REARENVKRE QDEAYRLSLE ADRAKREAHE REMAEQFRLE
QIRKEQEEER EAIRLSLEQA LPPEPKEENA EPVSKLRIRT PSGEFLERRF LASNKLQIVF
DFVASKGFPW DEYKLLSTFP RRDVTQLDPN KSLLEVKLFP QETLFLEAKE
//
ID FAF1_HUMAN Reviewed; 650 AA.
AC Q9UNN5; Q549F0; Q9UF34; Q9UNT3; Q9Y2Z3;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=FAS-associated factor 1;
DE Short=hFAF1;
DE AltName: Full=UBX domain-containing protein 12;
DE AltName: Full=UBX domain-containing protein 3A;
GN Name=FAF1; Synonyms=UBXD12, UBXN3A; ORFNames=CGI-03;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND
RP CHARACTERIZATION.
RC TISSUE=Brain, and Liver;
RX PubMed=10462485; DOI=10.1006/bbrc.1999.1217;
RA Ryu S.-W., Chae S.-K., Lee K.-J., Kim E.;
RT "Identification and characterization of human Fas associated factor 1,
RT hFAF1.";
RL Biochem. Biophys. Res. Commun. 262:388-394(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA Ding J.B., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Mus musculus FAF1.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RA Boldyreff B.;
RT "Full length cDNA sequence and chromosomal localization of the human
RT Fas-associated factor 1 gene, hFaf1.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Brain, and Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-650 (ISOFORM LONG).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH NLRP12.
RX PubMed=21978668; DOI=10.1016/j.jmb.2011.09.024;
RA Pinheiro A.S., Eibl C., Ekman-Vural Z., Schwarzenbacher R., Peti W.;
RT "The NLRP12 pyrin domain: structure, dynamics, and functional
RT insights.";
RL J. Mol. Biol. 413:790-803(2011).
RN [14]
RP STRUCTURE BY NMR OF 569-650.
RX PubMed=11243799; DOI=10.1006/jmbi.2000.4462;
RA Buchberger A., Howard M.J., Proctor M., Bycroft M.M.;
RT "The UBX domain: a widespread ubiquitin-like module.";
RL J. Mol. Biol. 307:17-24(2001).
RN [15]
RP STRUCTURE BY NMR OF 99-191.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ubiquitin-like domain in human FAS-
RT associated factor 1 (hFAF1).";
RL Submitted (OCT-2007) to the PDB data bank.
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 5-47, AND DOMAIN UBA.
RX PubMed=19722279; DOI=10.1002/pro.237;
RA Song J., Park J.K., Lee J.J., Choi Y.S., Ryu K.S., Kim J.H., Kim E.,
RA Lee K.J., Jeon Y.H., Kim E.E.;
RT "Structure and interaction of ubiquitin-associated domain of human
RT Fas-associated factor 1.";
RL Protein Sci. 18:2265-2276(2009).
CC -!- FUNCTION: Potentiates but cannot initiate FAS-induced apoptosis.
CC -!- SUBUNIT: Specifically interacts with the cytoplasmic domain of
CC FAS. Interacts with NLRP12 DAPIN/PYRIN domain via its UBA domain.
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9UNN5-1; Sequence=Displayed;
CC Name=Short; Synonyms=hFAF1(s);
CC IsoId=Q9UNN5-2; Sequence=VSP_006704;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Most abundant in testis, slightly less
CC abundant in skeletal muscle and heart, followed by prostate,
CC thymus, ovary, small intestine, and colon. Not detected in the
CC peripheral blood leukocytes.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51876.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AF106798; AAD51886.1; -; mRNA.
DR EMBL; AF094700; AAD51876.1; ALT_INIT; mRNA.
DR EMBL; AF136173; AAP97263.1; -; mRNA.
DR EMBL; AJ271408; CAB67705.1; -; mRNA.
DR EMBL; AF132938; AAD27713.1; -; mRNA.
DR EMBL; AL359977; CAH70189.1; -; Genomic_DNA.
DR EMBL; AC091610; CAH70189.1; JOINED; Genomic_DNA.
DR EMBL; AC118557; CAH70189.1; JOINED; Genomic_DNA.
DR EMBL; AL049637; CAH70189.1; JOINED; Genomic_DNA.
DR EMBL; AL603746; CAH70189.1; JOINED; Genomic_DNA.
DR EMBL; AL603746; CAH72113.1; -; Genomic_DNA.
DR EMBL; AC091610; CAH72113.1; JOINED; Genomic_DNA.
DR EMBL; AC118557; CAH72113.1; JOINED; Genomic_DNA.
DR EMBL; AL049637; CAH72113.1; JOINED; Genomic_DNA.
DR EMBL; AL359977; CAH72113.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX06837.1; -; Genomic_DNA.
DR EMBL; BC004970; AAH04970.1; -; mRNA.
DR EMBL; BC067100; AAH67100.1; -; mRNA.
DR EMBL; AL133631; CAB63755.1; -; mRNA.
DR PIR; JC7093; JC7093.
DR PIR; T43466; T43466.
DR RefSeq; NP_008982.1; NM_007051.2.
DR UniGene; Hs.530402; -.
DR PDB; 1H8C; NMR; -; A=569-650.
DR PDB; 2DZM; NMR; -; A=99-191.
DR PDB; 2EC4; NMR; -; A=325-495.
DR PDB; 3E21; X-ray; 1.73 A; A=5-47.
DR PDB; 3QC8; X-ray; 2.20 A; B=571-650.
DR PDB; 3QCA; X-ray; 2.90 A; A/B/C/D=571-650.
DR PDB; 3QQ8; X-ray; 2.00 A; B=568-650.
DR PDB; 3QWZ; X-ray; 2.00 A; B=571-650.
DR PDB; 3QX1; X-ray; 1.60 A; A/B=571-650.
DR PDB; 3R3M; X-ray; 3.00 A; A/B/C/D=568-650.
DR PDBsum; 1H8C; -.
DR PDBsum; 2DZM; -.
DR PDBsum; 2EC4; -.
DR PDBsum; 3E21; -.
DR PDBsum; 3QC8; -.
DR PDBsum; 3QCA; -.
DR PDBsum; 3QQ8; -.
DR PDBsum; 3QWZ; -.
DR PDBsum; 3QX1; -.
DR PDBsum; 3R3M; -.
DR ProteinModelPortal; Q9UNN5; -.
DR SMR; Q9UNN5; 5-44, 99-191, 325-495, 570-649.
DR DIP; DIP-38245N; -.
DR IntAct; Q9UNN5; 49.
DR MINT; MINT-88745; -.
DR STRING; 9606.ENSP00000379457; -.
DR PhosphoSite; Q9UNN5; -.
DR DMDM; 20454906; -.
DR PaxDb; Q9UNN5; -.
DR PRIDE; Q9UNN5; -.
DR DNASU; 11124; -.
DR Ensembl; ENST00000371778; ENSP00000360843; ENSG00000185104.
DR Ensembl; ENST00000396153; ENSP00000379457; ENSG00000185104.
DR GeneID; 11124; -.
DR KEGG; hsa:11124; -.
DR UCSC; uc001cse.1; human.
DR CTD; 11124; -.
DR GeneCards; GC01M050905; -.
DR HGNC; HGNC:3578; FAF1.
DR HPA; HPA018253; -.
DR HPA; HPA019008; -.
DR MIM; 604460; gene.
DR neXtProt; NX_Q9UNN5; -.
DR PharmGKB; PA27976; -.
DR eggNOG; NOG288188; -.
DR HOGENOM; HOG000043073; -.
DR HOVERGEN; HBG002876; -.
DR InParanoid; Q9UNN5; -.
DR OMA; WEGWPAS; -.
DR OrthoDB; EOG72NRPV; -.
DR PhylomeDB; Q9UNN5; -.
DR SignaLink; Q9UNN5; -.
DR ChiTaRS; FAF1; human.
DR EvolutionaryTrace; Q9UNN5; -.
DR GeneWiki; FAF1; -.
DR GenomeRNAi; 11124; -.
DR NextBio; 42280; -.
DR PRO; PR:Q9UNN5; -.
DR ArrayExpress; Q9UNN5; -.
DR Bgee; Q9UNN5; -.
DR CleanEx; HS_FAF1; -.
DR Genevestigator; Q9UNN5; -.
DR GO; GO:0031265; C:CD95 death-inducing signaling complex; NAS:UniProtKB.
DR GO; GO:0034098; C:Cdc48p-Npl4p-Ufd1p AAA ATPase complex; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0019887; F:protein kinase regulator activity; NAS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008219; P:cell death; IMP:UniProtKB.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein complex assembly; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0042176; P:regulation of protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR001012; UBX.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50030; UBA; FALSE_NEG.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Complete proteome;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1 650 FAS-associated factor 1.
FT /FTId=PRO_0000211038.
FT DOMAIN 1 57 UBA.
FT DOMAIN 569 646 UBX.
FT MOD_RES 320 320 Phosphoserine.
FT VAR_SEQ 188 339 Missing (in isoform Short).
FT /FTId=VSP_006704.
FT CONFLICT 448 448 F -> K (in Ref. 1; AAD51886/AAD51876).
FT CONFLICT 498 498 E -> G (in Ref. 1; AAD51886/AAD51876).
FT CONFLICT 529 529 H -> R (in Ref. 1; AAD51886/AAD51876).
FT HELIX 7 18
FT HELIX 23 32
FT TURN 33 35
FT HELIX 37 41
FT STRAND 100 106
FT STRAND 111 117
FT HELIX 122 133
FT TURN 137 139
FT STRAND 146 148
FT HELIX 156 159
FT STRAND 163 169
FT STRAND 172 174
FT HELIX 330 345
FT HELIX 357 362
FT STRAND 365 367
FT TURN 369 371
FT STRAND 374 380
FT HELIX 386 393
FT TURN 394 396
FT HELIX 398 406
FT STRAND 408 414
FT HELIX 418 431
FT HELIX 434 442
FT STRAND 449 454
FT STRAND 463 467
FT HELIX 473 490
FT STRAND 573 579
FT STRAND 585 591
FT HELIX 596 605
FT TURN 610 612
FT STRAND 613 616
FT STRAND 618 620
FT HELIX 624 626
FT TURN 633 637
FT STRAND 640 648
SQ SEQUENCE 650 AA; 73954 MW; 7FB9018B9A230488 CRC64;
MASNMDREMI LADFQACTGI ENIDEAITLL EQNNWDLVAA INGVIPQENG ILQSEYGGET
IPGPAFNPAS HPASAPTSSS SSAFRPVMPS RQIVERQPRM LDFRVEYRDR NVDVVLEDTC
TVGEIKQILE NELQIPVSKM LLKGWKTGDV EDSTVLKSLH LPKNNSLYVL TPDLPPPSSS
SHAGALQESL NQNFMLIITH REVQREYNLN FSGSSTIQEV KRNVYDLTSI PVRHQLWEGW
PTSATDDSMC LAESGLSYPC HRLTVGRRSS PAQTREQSEE QITDVHMVSD SDGDDFEDAT
EFGVDDGEVF GMASSALRKS PMMPENAENE GDALLQFTAE FSSRYGDCHP VFFIGSLEAA
FQEAFYVKAR DRKLLAIYLH HDESVLTNVF CSQMLCAESI VSYLSQNFIT WAWDLTKDSN
RARFLTMCNR HFGSVVAQTI RTQKTDQFPL FLIIMGKRSS NEVLNVIQGN TTVDELMMRL
MAAMEIFTAQ QQEDIKDEDE REARENVKRE QDEAYRLSLE ADRAKREAHE REMAEQFRLE
QIRKEQEEER EAIRLSLEQA LPPEPKEENA EPVSKLRIRT PSGEFLERRF LASNKLQIVF
DFVASKGFPW DEYKLLSTFP RRDVTQLDPN KSLLEVKLFP QETLFLEAKE
//
MIM
604460
*RECORD*
*FIELD* NO
604460
*FIELD* TI
*604460 FAS-ASSOCIATED FACTOR 1; FAF1
;;HFAF1
*FIELD* TX
CLONING
Interaction of Fas ligand (TNFSF6; 134638) with the FAS antigen
read more(TNFRSF6; 134637) mediates programmed cell death, also called apoptosis,
in a number of organ systems, notably the immune and nervous systems.
Although these molecules are in the same family as TNF-alpha (191160)
and TNFR (191190), the latter function to activate not only apoptosis
but also NFKB1 (164011), a key transcription factor in chronic
inflammatory diseases. By screening tumor-related proteins derived from
a HeLa cDNA library in a yeast 2-hybrid assay, Ryu et al. (1999)
isolated a truncated version of FAS-associated factor-1 (FAF1), which
can enhance but not initiate apoptosis. Using PCR as well as sequence
information from an EST database to screen HeLa as well as brain and
kidney cDNA libraries, they derived a product corresponding to the
expected size of the complete coding region of 1,970 bp. The deduced
amino acid sequence was 96% and 85% homologous to mouse and quail Faf1,
respectively. Northern blot analysis revealed a single FAF1 mRNA
transcript of 2.8 kb to be most abundant in testis, slightly less
abundant in skeletal muscle and heart, followed by prostate, thymus,
ovary, small intestine, and colon. Expression was detected in all other
tissues tested with the exception of peripheral blood leukocytes. By
immunoblotting with a mouse polyclonal antibody to FAF1, a 74-kD protein
was detected in 6 of 8 tumor cell lines. A 40-kD protein was detected in
1 of the 2 remaining cell lines. Interaction of FAF1 and FAS was shown
in both the yeast 2-hybrid and the GST pull-down assay systems. The
N-terminal 201 amino acids of FAF1, containing a ubiquitin homology
domain, bound to the FAS death domain but not to a death domain mutant
in the yeast 2-hybrid system.
Using whole-mount in-situ hybridization in zebrafish embryos,
Ghassibe-Sabbagh et al. (2011) detected faf1 transcripts at 24 and 30
hours postfertilization (hpf) in the pharyngeal arch primordia. At 56
hpf, when the pharyngeal cartilages were forming, faf1 was strongly
expressed in all arches, with the most prominent expression in the first
(mandibular) and second (hyoid) arch. Knockdown of zebrafish faf1 led to
pharyngeal cartilage defects and jaw abnormalities as a result of a
failure of the cranial neural crest to differentiate and to express
cartilage-specific markers, such as sox9a (see 608160) and col2a1 (see
120140). Administration of faf1 mRNA rescued the phenotype.
MAPPING
Gross (2011) mapped the FAF1 gene to chromosome 1p32.3 based on an
alignment of the FAF1 sequence (GenBank GENBANK AF136173) with the
genomic sequence (GRCh37).
MOLECULAR GENETICS
For discussion of a possible association between variation in the FAF1
gene and orofacial clefting, see OFC13 (613857).
*FIELD* RF
1. Ghassibe-Sabbagh, M.; Desmyter, L.; Langenberg, T.; Claes, F.;
Boute, O.; Bayet, B.; Pellerin, P.; Hermans, K.; Backx, L.; Mansilla,
M. A.; Imoehl, S.; Nowak, S.; and 17 others: FAF1, a gene that
is disrupted in cleft palate and has conserved function in zebrafish. Am.
J. Hum. Genet. 88: 150-161, 2011.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 4/1/2011.
3. Ryu, S. W.; Chae, S. K.; Lee, K. J.; Kim, E.: Identification and
characterization of human Fas associated factor 1, hFAF1. Biochem.
Biophys. Res. Commun. 262: 388-394, 1999.
*FIELD* CN
Matthew B. Gross - updated: 4/1/2011
Marla J. F. O'Neill - updated: 4/1/2011
*FIELD* CD
Paul J. Converse: 1/24/2000
*FIELD* ED
carol: 04/01/2011
carol: 4/1/2011
carol: 1/24/2000
*RECORD*
*FIELD* NO
604460
*FIELD* TI
*604460 FAS-ASSOCIATED FACTOR 1; FAF1
;;HFAF1
*FIELD* TX
CLONING
Interaction of Fas ligand (TNFSF6; 134638) with the FAS antigen
read more(TNFRSF6; 134637) mediates programmed cell death, also called apoptosis,
in a number of organ systems, notably the immune and nervous systems.
Although these molecules are in the same family as TNF-alpha (191160)
and TNFR (191190), the latter function to activate not only apoptosis
but also NFKB1 (164011), a key transcription factor in chronic
inflammatory diseases. By screening tumor-related proteins derived from
a HeLa cDNA library in a yeast 2-hybrid assay, Ryu et al. (1999)
isolated a truncated version of FAS-associated factor-1 (FAF1), which
can enhance but not initiate apoptosis. Using PCR as well as sequence
information from an EST database to screen HeLa as well as brain and
kidney cDNA libraries, they derived a product corresponding to the
expected size of the complete coding region of 1,970 bp. The deduced
amino acid sequence was 96% and 85% homologous to mouse and quail Faf1,
respectively. Northern blot analysis revealed a single FAF1 mRNA
transcript of 2.8 kb to be most abundant in testis, slightly less
abundant in skeletal muscle and heart, followed by prostate, thymus,
ovary, small intestine, and colon. Expression was detected in all other
tissues tested with the exception of peripheral blood leukocytes. By
immunoblotting with a mouse polyclonal antibody to FAF1, a 74-kD protein
was detected in 6 of 8 tumor cell lines. A 40-kD protein was detected in
1 of the 2 remaining cell lines. Interaction of FAF1 and FAS was shown
in both the yeast 2-hybrid and the GST pull-down assay systems. The
N-terminal 201 amino acids of FAF1, containing a ubiquitin homology
domain, bound to the FAS death domain but not to a death domain mutant
in the yeast 2-hybrid system.
Using whole-mount in-situ hybridization in zebrafish embryos,
Ghassibe-Sabbagh et al. (2011) detected faf1 transcripts at 24 and 30
hours postfertilization (hpf) in the pharyngeal arch primordia. At 56
hpf, when the pharyngeal cartilages were forming, faf1 was strongly
expressed in all arches, with the most prominent expression in the first
(mandibular) and second (hyoid) arch. Knockdown of zebrafish faf1 led to
pharyngeal cartilage defects and jaw abnormalities as a result of a
failure of the cranial neural crest to differentiate and to express
cartilage-specific markers, such as sox9a (see 608160) and col2a1 (see
120140). Administration of faf1 mRNA rescued the phenotype.
MAPPING
Gross (2011) mapped the FAF1 gene to chromosome 1p32.3 based on an
alignment of the FAF1 sequence (GenBank GENBANK AF136173) with the
genomic sequence (GRCh37).
MOLECULAR GENETICS
For discussion of a possible association between variation in the FAF1
gene and orofacial clefting, see OFC13 (613857).
*FIELD* RF
1. Ghassibe-Sabbagh, M.; Desmyter, L.; Langenberg, T.; Claes, F.;
Boute, O.; Bayet, B.; Pellerin, P.; Hermans, K.; Backx, L.; Mansilla,
M. A.; Imoehl, S.; Nowak, S.; and 17 others: FAF1, a gene that
is disrupted in cleft palate and has conserved function in zebrafish. Am.
J. Hum. Genet. 88: 150-161, 2011.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 4/1/2011.
3. Ryu, S. W.; Chae, S. K.; Lee, K. J.; Kim, E.: Identification and
characterization of human Fas associated factor 1, hFAF1. Biochem.
Biophys. Res. Commun. 262: 388-394, 1999.
*FIELD* CN
Matthew B. Gross - updated: 4/1/2011
Marla J. F. O'Neill - updated: 4/1/2011
*FIELD* CD
Paul J. Converse: 1/24/2000
*FIELD* ED
carol: 04/01/2011
carol: 4/1/2011
carol: 1/24/2000