FAF1_HUMAN
ID FAF1_HUMAN Reviewed; 650 AA.
AC Q9UNN5; Q549F0; Q9UF34; Q9UNT3; Q9Y2Z3;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 194.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), INTERACTION WITH FAS,
RP AND TISSUE SPECIFICITY.
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 Fas-
RT 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 insights.";
RL J. Mol. Biol. 413:790-803(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-580 AND SER-582, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION, INTERACTION WITH CDT1 AND VCP, AND SUBCELLULAR LOCATION.
RX PubMed=26842564; DOI=10.1038/ncomms10612;
RA Franz A., Pirson P.A., Pilger D., Halder S., Achuthankutty D., Kashkar H.,
RA Ramadan K., Hoppe T.;
RT "Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard
RT DNA replication fork progression.";
RL Nat. Commun. 7:10612-10612(2016).
RN [16]
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 [17]
RP STRUCTURE BY NMR OF 99-191.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ubiquitin-like domain in human FAS-associated
RT factor 1 (hFAF1).";
RL Submitted (OCT-2007) to the PDB data bank.
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 5-47, FUNCTION, 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 Fas-
RT associated factor 1.";
RL Protein Sci. 18:2265-2276(2009).
CC -!- FUNCTION: Ubiquitin-binding protein (PubMed:19722279). Required for the
CC progression of DNA replication forks by targeting DNA replication
CC licensing factor CDT1 for degradation (PubMed:26842564). Potentiates
CC but cannot initiate FAS-induced apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:P54731, ECO:0000269|PubMed:19722279,
CC ECO:0000269|PubMed:26842564}.
CC -!- SUBUNIT: Interacts with CDT1 and ATPase VCP/p97 (PubMed:26842564).
CC Interacts (via UBA domain) with FAS (via death domain)
CC (PubMed:10462485). Interacts (via UBA domain) with NLRP12 (via
CC DAPIN/PYRIN domain) (PubMed:21978668). {ECO:0000269|PubMed:10462485,
CC ECO:0000269|PubMed:21978668, ECO:0000269|PubMed:26842564}.
CC -!- INTERACTION:
CC Q9UNN5; P28799: GRN; NbExp=3; IntAct=EBI-718246, EBI-747754;
CC Q9UNN5; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-718246, EBI-5235340;
CC Q9UNN5; Q7Z739: YTHDF3; NbExp=3; IntAct=EBI-718246, EBI-2849837;
CC Q9UNN5-1; P55072: VCP; NbExp=4; IntAct=EBI-15930546, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26842564}.
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 -!- TISSUE SPECIFICITY: Most abundant in testis, slightly less abundant in
CC skeletal muscle and heart, followed by prostate, thymus, ovary, small
CC intestine, and colon. Not detected in the peripheral blood leukocytes.
CC {ECO:0000269|PubMed:10462485}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51876.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; AC091610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603746; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS554.1; -. [Q9UNN5-1]
DR PIR; JC7093; JC7093.
DR PIR; T43466; T43466.
DR RefSeq; NP_008982.1; NM_007051.2. [Q9UNN5-1]
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 AlphaFoldDB; Q9UNN5; -.
DR BMRB; Q9UNN5; -.
DR SMR; Q9UNN5; -.
DR BioGRID; 116298; 314.
DR DIP; DIP-38245N; -.
DR IntAct; Q9UNN5; 63.
DR MINT; Q9UNN5; -.
DR STRING; 9606.ENSP00000379457; -.
DR ChEMBL; CHEMBL3758063; -.
DR GlyGen; Q9UNN5; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9UNN5; -.
DR PhosphoSitePlus; Q9UNN5; -.
DR BioMuta; FAF1; -.
DR DMDM; 20454906; -.
DR EPD; Q9UNN5; -.
DR jPOST; Q9UNN5; -.
DR MassIVE; Q9UNN5; -.
DR MaxQB; Q9UNN5; -.
DR PaxDb; Q9UNN5; -.
DR PeptideAtlas; Q9UNN5; -.
DR PRIDE; Q9UNN5; -.
DR ProteomicsDB; 85315; -. [Q9UNN5-1]
DR ProteomicsDB; 85316; -. [Q9UNN5-2]
DR Antibodypedia; 18936; 418 antibodies from 41 providers.
DR CPTC; Q9UNN5; 3 antibodies.
DR DNASU; 11124; -.
DR Ensembl; ENST00000396153.7; ENSP00000379457.2; ENSG00000185104.21. [Q9UNN5-1]
DR GeneID; 11124; -.
DR KEGG; hsa:11124; -.
DR MANE-Select; ENST00000396153.7; ENSP00000379457.2; NM_007051.3; NP_008982.1.
DR UCSC; uc001cse.2; human. [Q9UNN5-1]
DR CTD; 11124; -.
DR DisGeNET; 11124; -.
DR GeneCards; FAF1; -.
DR HGNC; HGNC:3578; FAF1.
DR HPA; ENSG00000185104; Low tissue specificity.
DR MIM; 604460; gene.
DR neXtProt; NX_Q9UNN5; -.
DR OpenTargets; ENSG00000185104; -.
DR PharmGKB; PA27976; -.
DR VEuPathDB; HostDB:ENSG00000185104; -.
DR eggNOG; KOG1363; Eukaryota.
DR GeneTree; ENSGT00940000154831; -.
DR HOGENOM; CLU_028119_0_0_1; -.
DR InParanoid; Q9UNN5; -.
DR OMA; RNQQWKG; -.
DR OrthoDB; 845154at2759; -.
DR PhylomeDB; Q9UNN5; -.
DR TreeFam; TF314172; -.
DR PathwayCommons; Q9UNN5; -.
DR SignaLink; Q9UNN5; -.
DR SIGNOR; Q9UNN5; -.
DR BioGRID-ORCS; 11124; 19 hits in 1085 CRISPR screens.
DR ChiTaRS; FAF1; human.
DR EvolutionaryTrace; Q9UNN5; -.
DR GeneWiki; FAF1; -.
DR GenomeRNAi; 11124; -.
DR Pharos; Q9UNN5; Tbio.
DR PRO; PR:Q9UNN5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UNN5; protein.
DR Bgee; ENSG00000185104; Expressed in gastrocnemius and 195 other tissues.
DR ExpressionAtlas; Q9UNN5; baseline and differential.
DR Genevisible; Q9UNN5; HS.
DR GO; GO:0031265; C:CD95 death-inducing signaling complex; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990917; C:ooplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:BHF-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
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:0010942; P:positive regulation of cell death; IDA:CACAO.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing 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 GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd14413; UBA_FAF1; 1.
DR CDD; cd01771; UBX_UBXN3A; 1.
DR IDEAL; IID00401; -.
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 3D-structure; Alternative splicing; Apoptosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..650
FT /note="FAS-associated factor 1"
FT /id="PRO_0000211038"
FT DOMAIN 1..57
FT /note="UBA"
FT /evidence="ECO:0000269|PubMed:19722279"
FT DOMAIN 569..646
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 62..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 580
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 188..339
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10462485"
FT /id="VSP_006704"
FT CONFLICT 448
FT /note="F -> K (in Ref. 1; AAD51886/AAD51876)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="E -> G (in Ref. 1; AAD51886/AAD51876)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="H -> R (in Ref. 1; AAD51886/AAD51876)"
FT /evidence="ECO:0000305"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:3E21"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3E21"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3E21"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:3E21"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2DZM"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2DZM"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:2DZM"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2DZM"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2DZM"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:2DZM"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2DZM"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2DZM"
FT HELIX 330..345
FT /evidence="ECO:0007829|PDB:2EC4"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:2EC4"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:2EC4"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:2EC4"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:2EC4"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:2EC4"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2EC4"
FT HELIX 398..406
FT /evidence="ECO:0007829|PDB:2EC4"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:2EC4"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:2EC4"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:2EC4"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:2EC4"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:2EC4"
FT HELIX 473..490
FT /evidence="ECO:0007829|PDB:2EC4"
FT STRAND 573..579
FT /evidence="ECO:0007829|PDB:3QX1"
FT STRAND 585..591
FT /evidence="ECO:0007829|PDB:3QX1"
FT HELIX 596..605
FT /evidence="ECO:0007829|PDB:3QX1"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:3QX1"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:3QX1"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:3QX1"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:3QX1"
FT TURN 633..637
FT /evidence="ECO:0007829|PDB:3QX1"
FT STRAND 640..648
FT /evidence="ECO:0007829|PDB:3QX1"
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
