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Q9UNN5 (FAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FAS-associated factor 1

Short name=hFAF1
Alternative name(s):
UBX domain-containing protein 12
UBX domain-containing protein 3A
Gene names
Name:FAF1
Synonyms:UBXD12, UBXN3A
ORF Names:CGI-03
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length650 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potentiates but cannot initiate FAS-induced apoptosis.

Subunit structure

Specifically interacts with the cytoplasmic domain of FAS. Interacts with NLRP12 DAPIN/PYRIN domain via its UBA domain. Ref.13

Subcellular location

Nucleus Potential.

Tissue specificity

Most abundant in testis, slightly less abundant in skeletal muscle and heart, followed by prostate, thymus, ovary, small intestine, and colon. Not detected in the peripheral blood leukocytes.

Sequence similarities

Contains 1 UBA domain.

Contains 1 UBX domain.

Sequence caution

The sequence AAD51876.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell death

Inferred from mutant phenotype PubMed 15743842. Source: UniProtKB

cytoplasmic sequestering of NF-kappaB

Inferred from mutant phenotype PubMed 14600157. Source: UniProtKB

positive regulation of apoptotic process

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein complex assembly

Inferred from mutant phenotype PubMed 15688372. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Non-traceable author statement PubMed 15743842. Source: UniProtKB

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of protein catabolic process

Inferred from mutant phenotype PubMed 15743842. Source: UniProtKB

regulation of protein kinase activity

Non-traceable author statement PubMed 11713579. Source: GOC

   Cellular_componentCD95 death-inducing signaling complex

Non-traceable author statement PubMed 12702723. Source: UniProtKB

Cdc48p-Npl4p-Ufd1p AAA ATPase complex

Inferred from direct assay PubMed 18775313. Source: BHF-UCL

cytosol

Inferred from direct assay PubMed 15596450. Source: UniProtKB

nuclear envelope

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 15596450. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 11713579. Source: UniProtKB

   Molecular_functionNF-kappaB binding

Inferred from physical interaction PubMed 14600157. Source: UniProtKB

heat shock protein binding

Inferred from direct assay PubMed 15596450. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15688372PubMed 15743842. Source: UniProtKB

protein kinase binding

Inferred from direct assay PubMed 11713579. Source: UniProtKB

protein kinase regulator activity

Non-traceable author statement PubMed 11713579. Source: UniProtKB

ubiquitin binding

Inferred from direct assay PubMed 18775313. Source: BHF-UCL

ubiquitin protein ligase binding

Inferred from direct assay PubMed 18775313. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q9UNN5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q9UNN5-2)

Also known as: hFAF1(s);

The sequence of this isoform differs from the canonical sequence as follows:
     188-339: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 650650FAS-associated factor 1
PRO_0000211038

Regions

Domain1 – 5757UBA
Domain569 – 64678UBX

Amino acid modifications

Modified residue3201Phosphoserine Ref.9 Ref.10 Ref.11

Natural variations

Alternative sequence188 – 339152Missing in isoform Short.
VSP_006704

Experimental info

Sequence conflict4481F → K in AAD51886. Ref.1
Sequence conflict4481F → K in AAD51876. Ref.1
Sequence conflict4981E → G in AAD51886. Ref.1
Sequence conflict4981E → G in AAD51876. Ref.1
Sequence conflict5291H → R in AAD51886. Ref.1
Sequence conflict5291H → R in AAD51876. Ref.1

Secondary structure

.................................................................... 650
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 7FB9018B9A230488

FASTA65073,954
        10         20         30         40         50         60 
MASNMDREMI LADFQACTGI ENIDEAITLL EQNNWDLVAA INGVIPQENG ILQSEYGGET 

        70         80         90        100        110        120 
IPGPAFNPAS HPASAPTSSS SSAFRPVMPS RQIVERQPRM LDFRVEYRDR NVDVVLEDTC 

       130        140        150        160        170        180 
TVGEIKQILE NELQIPVSKM LLKGWKTGDV EDSTVLKSLH LPKNNSLYVL TPDLPPPSSS 

       190        200        210        220        230        240 
SHAGALQESL NQNFMLIITH REVQREYNLN FSGSSTIQEV KRNVYDLTSI PVRHQLWEGW 

       250        260        270        280        290        300 
PTSATDDSMC LAESGLSYPC HRLTVGRRSS PAQTREQSEE QITDVHMVSD SDGDDFEDAT 

       310        320        330        340        350        360 
EFGVDDGEVF GMASSALRKS PMMPENAENE GDALLQFTAE FSSRYGDCHP VFFIGSLEAA 

       370        380        390        400        410        420 
FQEAFYVKAR DRKLLAIYLH HDESVLTNVF CSQMLCAESI VSYLSQNFIT WAWDLTKDSN 

       430        440        450        460        470        480 
RARFLTMCNR HFGSVVAQTI RTQKTDQFPL FLIIMGKRSS NEVLNVIQGN TTVDELMMRL 

       490        500        510        520        530        540 
MAAMEIFTAQ QQEDIKDEDE REARENVKRE QDEAYRLSLE ADRAKREAHE REMAEQFRLE 

       550        560        570        580        590        600 
QIRKEQEEER EAIRLSLEQA LPPEPKEENA EPVSKLRIRT PSGEFLERRF LASNKLQIVF 

       610        620        630        640        650 
DFVASKGFPW DEYKLLSTFP RRDVTQLDPN KSLLEVKLFP QETLFLEAKE 

« Hide

Isoform Short (hFAF1(s)) [UniParc].

Checksum: A9B444F8E8257017
Show »

FASTA49856,934

References

« Hide 'large scale' references
[1]"Identification and characterization of human Fas associated factor 1, hFAF1."
Ryu S.-W., Chae S.-K., Lee K.-J., Kim E.
Biochem. Biophys. Res. Commun. 262:388-394(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), CHARACTERIZATION.
Tissue: Brain and Liver.
[2]"Cloning of a new human cDNA homologous to Mus musculus FAF1."
Ding J.B., Yu L., Zhao S.Y.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[3]"Full length cDNA sequence and chromosomal localization of the human Fas-associated factor 1 gene, hFaf1."
Boldyreff B.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[4]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Tissue: Brain and Kidney.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-650 (ISOFORM LONG).
Tissue: Testis.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The NLRP12 pyrin domain: structure, dynamics, and functional insights."
Pinheiro A.S., Eibl C., Ekman-Vural Z., Schwarzenbacher R., Peti W.
J. Mol. Biol. 413:790-803(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NLRP12.
[14]"The UBX domain: a widespread ubiquitin-like module."
Buchberger A., Howard M.J., Proctor M., Bycroft M.M.
J. Mol. Biol. 307:17-24(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 569-650.
[15]"Solution structure of the ubiquitin-like domain in human FAS-associated factor 1 (hFAF1)."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 99-191.
[16]"Structure and interaction of ubiquitin-associated domain of human Fas-associated factor 1."
Song J., Park J.K., Lee J.J., Choi Y.S., Ryu K.S., Kim J.H., Kim E., Lee K.J., Jeon Y.H., Kim E.E.
Protein Sci. 18:2265-2276(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 5-47, DOMAIN UBA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF106798 mRNA. Translation: AAD51886.1.
AF094700 mRNA. Translation: AAD51876.1. Different initiation.
AF136173 mRNA. Translation: AAP97263.1.
AJ271408 mRNA. Translation: CAB67705.1.
AF132938 mRNA. Translation: AAD27713.1.
AL359977 expand/collapse EMBL AC list , AC091610, AC118557, AL049637, AL603746 Genomic DNA. Translation: CAH70189.1.
AL603746 expand/collapse EMBL AC list , AC091610, AC118557, AL049637, AL359977 Genomic DNA. Translation: CAH72113.1.
CH471059 Genomic DNA. Translation: EAX06837.1.
BC004970 mRNA. Translation: AAH04970.1.
BC067100 mRNA. Translation: AAH67100.1.
AL133631 mRNA. Translation: CAB63755.1.
CCDSCCDS554.1. [Q9UNN5-1]
PIRJC7093.
T43466.
RefSeqNP_008982.1. NM_007051.2. [Q9UNN5-1]
UniGeneHs.530402.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8CNMR-A569-650[»]
2DZMNMR-A99-191[»]
2EC4NMR-A325-495[»]
3E21X-ray1.73A5-47[»]
3QC8X-ray2.20B571-650[»]
3QCAX-ray2.90A/B/C/D571-650[»]
3QQ8X-ray2.00B568-650[»]
3QWZX-ray2.00B571-650[»]
3QX1X-ray1.60A/B571-650[»]
3R3MX-ray3.00A/B/C/D568-650[»]
ProteinModelPortalQ9UNN5.
SMRQ9UNN5. Positions 5-44, 99-191, 325-495, 570-649.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116298. 86 interactions.
DIPDIP-38245N.
IntActQ9UNN5. 49 interactions.
MINTMINT-88745.
STRING9606.ENSP00000379457.

PTM databases

PhosphoSiteQ9UNN5.

Polymorphism databases

DMDM20454906.

Proteomic databases

MaxQBQ9UNN5.
PaxDbQ9UNN5.
PRIDEQ9UNN5.

Protocols and materials databases

DNASU11124.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371778; ENSP00000360843; ENSG00000185104. [Q9UNN5-1]
ENST00000396153; ENSP00000379457; ENSG00000185104. [Q9UNN5-1]
GeneID11124.
KEGGhsa:11124.
UCSCuc001cse.1. human. [Q9UNN5-1]

Organism-specific databases

CTD11124.
GeneCardsGC01M050905.
HGNCHGNC:3578. FAF1.
HPAHPA018253.
HPA019008.
MIM604460. gene.
neXtProtNX_Q9UNN5.
PharmGKBPA27976.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288188.
HOGENOMHOG000043073.
HOVERGENHBG002876.
InParanoidQ9UNN5.
OMAWEGWPAS.
OrthoDBEOG72NRPV.
PhylomeDBQ9UNN5.
TreeFamTF314172.

Enzyme and pathway databases

SignaLinkQ9UNN5.

Gene expression databases

ArrayExpressQ9UNN5.
BgeeQ9UNN5.
CleanExHS_FAF1.
GenevestigatorQ9UNN5.

Family and domain databases

InterProIPR012336. Thioredoxin-like_fold.
IPR006577. UAS.
IPR029071. Ubiquitin-rel_dom.
IPR001012. UBX_dom.
[Graphical view]
PfamPF00789. UBX. 1 hit.
[Graphical view]
SMARTSM00594. UAS. 1 hit.
SM00166. UBX. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
SSF54236. SSF54236. 3 hits.
PROSITEPS50033. UBX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFAF1. human.
EvolutionaryTraceQ9UNN5.
GeneWikiFAF1.
GenomeRNAi11124.
NextBio42280.
PROQ9UNN5.
SOURCESearch...

Entry information

Entry nameFAF1_HUMAN
AccessionPrimary (citable) accession number: Q9UNN5
Secondary accession number(s): Q549F0 expand/collapse secondary AC list , Q9UF34, Q9UNT3, Q9Y2Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: July 9, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM