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Q9UNN5

- FAF1_HUMAN

UniProt

Q9UNN5 - FAF1_HUMAN

Protein

FAS-associated factor 1

Gene

FAF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    Functioni

    Potentiates but cannot initiate FAS-induced apoptosis.

    GO - Molecular functioni

    1. heat shock protein binding Source: UniProtKB
    2. NF-kappaB binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein kinase binding Source: UniProtKB
    5. protein kinase regulator activity Source: UniProtKB
    6. ubiquitin binding Source: BHF-UCL
    7. ubiquitin protein ligase binding Source: BHF-UCL

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell death Source: UniProtKB
    3. cytoplasmic sequestering of NF-kappaB Source: UniProtKB
    4. positive regulation of apoptotic process Source: UniProtKB
    5. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    6. positive regulation of protein complex assembly Source: UniProtKB
    7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    8. regulation of cell adhesion Source: Ensembl
    9. regulation of protein catabolic process Source: UniProtKB
    10. regulation of protein kinase activity Source: GOC

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    SignaLinkiQ9UNN5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FAS-associated factor 1
    Short name:
    hFAF1
    Alternative name(s):
    UBX domain-containing protein 12
    UBX domain-containing protein 3A
    Gene namesi
    Name:FAF1
    Synonyms:UBXD12, UBXN3A
    ORF Names:CGI-03
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3578. FAF1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. CD95 death-inducing signaling complex Source: UniProtKB
    2. Cdc48p-Npl4p-Ufd1p AAA ATPase complex Source: BHF-UCL
    3. cytosol Source: UniProtKB
    4. nuclear envelope Source: Ensembl
    5. nucleus Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27976.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 650650FAS-associated factor 1PRO_0000211038Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei320 – 3201Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UNN5.
    PaxDbiQ9UNN5.
    PRIDEiQ9UNN5.

    PTM databases

    PhosphoSiteiQ9UNN5.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiQ9UNN5.
    BgeeiQ9UNN5.
    CleanExiHS_FAF1.
    GenevestigatoriQ9UNN5.

    Organism-specific databases

    HPAiHPA018253.
    HPA019008.

    Interactioni

    Subunit structurei

    Specifically interacts with the cytoplasmic domain of FAS. Interacts with NLRP12 DAPIN/PYRIN domain via its UBA domain.1 Publication

    Protein-protein interaction databases

    BioGridi116298. 86 interactions.
    DIPiDIP-38245N.
    IntActiQ9UNN5. 49 interactions.
    MINTiMINT-88745.
    STRINGi9606.ENSP00000379457.

    Structurei

    Secondary structure

    1
    650
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 1812
    Helixi23 – 3210
    Turni33 – 353
    Helixi37 – 415
    Beta strandi100 – 1067
    Beta strandi111 – 1177
    Helixi122 – 13312
    Turni137 – 1393
    Beta strandi146 – 1483
    Helixi156 – 1594
    Beta strandi163 – 1697
    Beta strandi172 – 1743
    Helixi330 – 34516
    Helixi357 – 3626
    Beta strandi365 – 3673
    Turni369 – 3713
    Beta strandi374 – 3807
    Helixi386 – 3938
    Turni394 – 3963
    Helixi398 – 4069
    Beta strandi408 – 4147
    Helixi418 – 43114
    Helixi434 – 4429
    Beta strandi449 – 4546
    Beta strandi463 – 4675
    Helixi473 – 49018
    Beta strandi573 – 5797
    Beta strandi585 – 5917
    Helixi596 – 60510
    Turni610 – 6123
    Beta strandi613 – 6164
    Beta strandi618 – 6203
    Helixi624 – 6263
    Turni633 – 6375
    Beta strandi640 – 6489

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ9UNN5.
    SMRiQ9UNN5. Positions 5-44, 99-191, 325-495, 570-649.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UNN5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 5757UBAAdd
    BLAST
    Domaini569 – 64678UBXPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 UBA domain.Curated
    Contains 1 UBX domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG288188.
    HOGENOMiHOG000043073.
    HOVERGENiHBG002876.
    InParanoidiQ9UNN5.
    OMAiWEGWPAS.
    OrthoDBiEOG72NRPV.
    PhylomeDBiQ9UNN5.
    TreeFamiTF314172.

    Family and domain databases

    InterProiIPR012336. Thioredoxin-like_fold.
    IPR006577. UAS.
    IPR029071. Ubiquitin-rel_dom.
    IPR001012. UBX_dom.
    [Graphical view]
    PfamiPF00789. UBX. 1 hit.
    [Graphical view]
    SMARTiSM00594. UAS. 1 hit.
    SM00166. UBX. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    SSF54236. SSF54236. 3 hits.
    PROSITEiPS50033. UBX. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q9UNN5-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MASNMDREMI LADFQACTGI ENIDEAITLL EQNNWDLVAA INGVIPQENG    50
    ILQSEYGGET IPGPAFNPAS HPASAPTSSS SSAFRPVMPS RQIVERQPRM 100
    LDFRVEYRDR NVDVVLEDTC TVGEIKQILE NELQIPVSKM LLKGWKTGDV 150
    EDSTVLKSLH LPKNNSLYVL TPDLPPPSSS SHAGALQESL NQNFMLIITH 200
    REVQREYNLN FSGSSTIQEV KRNVYDLTSI PVRHQLWEGW PTSATDDSMC 250
    LAESGLSYPC HRLTVGRRSS PAQTREQSEE QITDVHMVSD SDGDDFEDAT 300
    EFGVDDGEVF GMASSALRKS PMMPENAENE GDALLQFTAE FSSRYGDCHP 350
    VFFIGSLEAA FQEAFYVKAR DRKLLAIYLH HDESVLTNVF CSQMLCAESI 400
    VSYLSQNFIT WAWDLTKDSN RARFLTMCNR HFGSVVAQTI RTQKTDQFPL 450
    FLIIMGKRSS NEVLNVIQGN TTVDELMMRL MAAMEIFTAQ QQEDIKDEDE 500
    REARENVKRE QDEAYRLSLE ADRAKREAHE REMAEQFRLE QIRKEQEEER 550
    EAIRLSLEQA LPPEPKEENA EPVSKLRIRT PSGEFLERRF LASNKLQIVF 600
    DFVASKGFPW DEYKLLSTFP RRDVTQLDPN KSLLEVKLFP QETLFLEAKE 650
    Length:650
    Mass (Da):73,954
    Last modified:May 2, 2002 - v2
    Checksum:i7FB9018B9A230488
    GO
    Isoform Short (identifier: Q9UNN5-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:498
    Mass (Da):56,934
    Checksum:iA9B444F8E8257017
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti448 – 4481F → K in AAD51886. (PubMed:10462485)Curated
    Sequence conflicti448 – 4481F → K in AAD51876. (PubMed:10462485)Curated
    Sequence conflicti498 – 4981E → G in AAD51886. (PubMed:10462485)Curated
    Sequence conflicti498 – 4981E → G in AAD51876. (PubMed:10462485)Curated
    Sequence conflicti529 – 5291H → R in AAD51886. (PubMed:10462485)Curated
    Sequence conflicti529 – 5291H → R in AAD51876. (PubMed:10462485)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei188 – 339152Missing in isoform Short. 1 PublicationVSP_006704Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , AC091610, AC118557, AL049637, AL603746 Genomic DNA. Translation: CAH70189.1.
    AL603746
    , 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.
    CCDSiCCDS554.1. [Q9UNN5-1]
    PIRiJC7093.
    T43466.
    RefSeqiNP_008982.1. NM_007051.2. [Q9UNN5-1]
    UniGeneiHs.530402.

    Genome annotation databases

    EnsembliENST00000371778; ENSP00000360843; ENSG00000185104. [Q9UNN5-1]
    ENST00000396153; ENSP00000379457; ENSG00000185104. [Q9UNN5-1]
    GeneIDi11124.
    KEGGihsa:11124.
    UCSCiuc001cse.1. human. [Q9UNN5-1]

    Polymorphism databases

    DMDMi20454906.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , AC091610 , AC118557 , AL049637 , AL603746 Genomic DNA. Translation: CAH70189.1 .
    AL603746
    , 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 .
    CCDSi CCDS554.1. [Q9UNN5-1 ]
    PIRi JC7093.
    T43466.
    RefSeqi NP_008982.1. NM_007051.2. [Q9UNN5-1 ]
    UniGenei Hs.530402.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H8C NMR - A 569-650 [» ]
    2DZM NMR - A 99-191 [» ]
    2EC4 NMR - A 325-495 [» ]
    3E21 X-ray 1.73 A 5-47 [» ]
    3QC8 X-ray 2.20 B 571-650 [» ]
    3QCA X-ray 2.90 A/B/C/D 571-650 [» ]
    3QQ8 X-ray 2.00 B 568-650 [» ]
    3QWZ X-ray 2.00 B 571-650 [» ]
    3QX1 X-ray 1.60 A/B 571-650 [» ]
    3R3M X-ray 3.00 A/B/C/D 568-650 [» ]
    ProteinModelPortali Q9UNN5.
    SMRi Q9UNN5. Positions 5-44, 99-191, 325-495, 570-649.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116298. 86 interactions.
    DIPi DIP-38245N.
    IntActi Q9UNN5. 49 interactions.
    MINTi MINT-88745.
    STRINGi 9606.ENSP00000379457.

    PTM databases

    PhosphoSitei Q9UNN5.

    Polymorphism databases

    DMDMi 20454906.

    Proteomic databases

    MaxQBi Q9UNN5.
    PaxDbi Q9UNN5.
    PRIDEi Q9UNN5.

    Protocols and materials databases

    DNASUi 11124.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371778 ; ENSP00000360843 ; ENSG00000185104 . [Q9UNN5-1 ]
    ENST00000396153 ; ENSP00000379457 ; ENSG00000185104 . [Q9UNN5-1 ]
    GeneIDi 11124.
    KEGGi hsa:11124.
    UCSCi uc001cse.1. human. [Q9UNN5-1 ]

    Organism-specific databases

    CTDi 11124.
    GeneCardsi GC01M050905.
    HGNCi HGNC:3578. FAF1.
    HPAi HPA018253.
    HPA019008.
    MIMi 604460. gene.
    neXtProti NX_Q9UNN5.
    PharmGKBi PA27976.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG288188.
    HOGENOMi HOG000043073.
    HOVERGENi HBG002876.
    InParanoidi Q9UNN5.
    OMAi WEGWPAS.
    OrthoDBi EOG72NRPV.
    PhylomeDBi Q9UNN5.
    TreeFami TF314172.

    Enzyme and pathway databases

    SignaLinki Q9UNN5.

    Miscellaneous databases

    ChiTaRSi FAF1. human.
    EvolutionaryTracei Q9UNN5.
    GeneWikii FAF1.
    GenomeRNAii 11124.
    NextBioi 42280.
    PROi Q9UNN5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNN5.
    Bgeei Q9UNN5.
    CleanExi HS_FAF1.
    Genevestigatori Q9UNN5.

    Family and domain databases

    InterProi IPR012336. Thioredoxin-like_fold.
    IPR006577. UAS.
    IPR029071. Ubiquitin-rel_dom.
    IPR001012. UBX_dom.
    [Graphical view ]
    Pfami PF00789. UBX. 1 hit.
    [Graphical view ]
    SMARTi SM00594. UAS. 1 hit.
    SM00166. UBX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    SSF54236. SSF54236. 3 hits.
    PROSITEi PS50033. UBX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-650 (ISOFORM LONG).
      Tissue: Testis.
    9. 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. 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.

    Entry informationi

    Entry nameiFAF1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNN5
    Secondary accession number(s): Q549F0
    , Q9UF34, Q9UNT3, Q9Y2Z3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: May 2, 2002
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3