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P39428

- TRAF1_MOUSE

UniProt

P39428 - TRAF1_MOUSE

Protein

TNF receptor-associated factor 1

Gene

Traf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei156 – 1572Cleavage; by CASP8By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    3. regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    4. signal transduction Source: InterPro

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TNF receptor-associated factor 1
    Gene namesi
    Name:Traf1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:101836. Traf1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Mice have normal B-cell proliferation and antibody response, but increased T-cell proliferation in response to CD3 signaling. Their T-cells show enhanced activation of JNK and NF-kappa-B. Mice are highly susceptible to TNF-induced skin necrosis.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi139 – 1391S → A: Loss of phosphorylation site. Reduces global phosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 409409TNF receptor-associated factor 1PRO_0000056398Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei139 – 1391Phosphoserine1 Publication
    Cross-linki178 – 178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki186 – 186Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Polyubiquitinated by BIRC2 and/or BIRC3, leading to its subsequent proteasomal degradation.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP39428.

    PTM databases

    PhosphoSiteiP39428.

    Expressioni

    Gene expression databases

    BgeeiP39428.
    CleanExiMM_TRAF1.
    GenevestigatoriP39428.

    Interactioni

    Subunit structurei

    Homotrimer. Heterotrimer with TRAF2. Interacts with TNFRSF1A/TNFR1, TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13C, TNFRSF18/AITR, TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1, TANK/ITRAF, TRAIP and RIPK2. Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2. Interacts with MAP3K14 By similarity. Interacts with NFATC2IP, TRAFD1 and with HIVEP3.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AhcyP502473EBI-520123,EBI-646982
    Hmg20bQ9Z1043EBI-520123,EBI-646920
    Plekhn1Q8C8866EBI-520123,EBI-646708
    TankP70347-112EBI-520123,EBI-646125
    Tcf7l2Q924A06EBI-520123,EBI-646713

    Protein-protein interaction databases

    BioGridi204302. 6 interactions.
    DIPiDIP-260N.
    IntActiP39428. 35 interactions.
    MINTiMINT-1518514.
    STRINGi10090.ENSMUSP00000108687.

    Structurei

    3D structure databases

    ProteinModelPortaliP39428.
    SMRiP39428. Positions 174-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini259 – 405147MATHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili167 – 25690By similarityAdd
    BLAST

    Domaini

    The coiled coil domain mediates homo- and hetero-oligomerization.By similarity
    The MATH/TRAF domain binds to receptor cytoplasmic domains.
    Cleavage by CASP8 liberates a C-terminal fragment that promotes apoptosis and inhibits the activation of NF-kappa-B in response to TNF signaling.By similarity

    Sequence similaritiesi

    Contains 1 MATH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG264247.
    GeneTreeiENSGT00550000074359.
    HOGENOMiHOG000231558.
    HOVERGENiHBG058222.
    InParanoidiQ8CE28.
    KOiK03172.
    OMAiHFMKEKL.
    OrthoDBiEOG7966G5.
    TreeFamiTF321154.

    Family and domain databases

    InterProiIPR002083. MATH.
    IPR012227. TNF_rcpt--assoc_TRAF.
    IPR008974. TRAF-like.
    IPR027136. TRAF1.
    [Graphical view]
    PANTHERiPTHR10131:SF29. PTHR10131:SF29. 1 hit.
    PfamiPF00917. MATH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015614. TRAF. 1 hit.
    SMARTiSM00061. MATH. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 1 hit.
    PROSITEiPS50144. MATH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39428-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSSAPDEN EFQFGCPPAP CQDPSEPRVL CCTACLSENL RDDEDRICPK    50
    CRADNLHPVS PGSPLTQEKV HSDVAEAEIM CPFAGVGCSF KGSPQSMQEH 100
    EATSQSSHLY LLLAVLKEWK SSPGSNLGSA PMALERNLSE LQLQAAVEAT 150
    GDLEVDCYRA PCCESQEELA LQHLVKEKLL AQLEEKLRVF ANIVAVLNKE 200
    VEASHLALAA SIHQSQLDRE HILSLEQRVV ELQQTLAQKD QVLGKLEHSL 250
    RLMEEASFDG TFLWKITNVT KRCHESVCGR TVSLFSPAFY TAKYGYKLCL 300
    RLYLNGDGSG KKTHLSLFIV IMRGEYDALL PWPFRNKVTF MLLDQNNREH 350
    AIDAFRPDLS SASFQRPQSE TNVASGCPLF FPLSKLQSPK HAYVKDDTMF 400
    LKCIVDTSA 409
    Length:409
    Mass (Da):45,465
    Last modified:July 27, 2011 - v2
    Checksum:iADD7F997169D9AAD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti222 – 2221I → L in AAC37663. (PubMed:8069916)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35302 mRNA. Translation: AAC37663.1.
    AK029135 mRNA. Translation: BAC26315.1.
    AK169515 mRNA. Translation: BAE41205.1.
    AK172598 mRNA. Translation: BAE43086.1.
    AL929068 Genomic DNA. Translation: CAM27599.1.
    CH466542 Genomic DNA. Translation: EDL08637.1.
    CCDSiCCDS15956.1.
    PIRiA54750.
    RefSeqiNP_033447.2. NM_009421.3.
    XP_006497906.1. XM_006497843.1.
    XP_006497907.1. XM_006497844.1.
    XP_006497908.1. XM_006497845.1.
    UniGeneiMm.239514.

    Genome annotation databases

    EnsembliENSMUST00000028234; ENSMUSP00000028234; ENSMUSG00000026875.
    ENSMUST00000113064; ENSMUSP00000108687; ENSMUSG00000026875.
    ENSMUST00000172159; ENSMUSP00000130759; ENSMUSG00000026875.
    GeneIDi22029.
    KEGGimmu:22029.
    UCSCiuc008jjj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35302 mRNA. Translation: AAC37663.1 .
    AK029135 mRNA. Translation: BAC26315.1 .
    AK169515 mRNA. Translation: BAE41205.1 .
    AK172598 mRNA. Translation: BAE43086.1 .
    AL929068 Genomic DNA. Translation: CAM27599.1 .
    CH466542 Genomic DNA. Translation: EDL08637.1 .
    CCDSi CCDS15956.1.
    PIRi A54750.
    RefSeqi NP_033447.2. NM_009421.3.
    XP_006497906.1. XM_006497843.1.
    XP_006497907.1. XM_006497844.1.
    XP_006497908.1. XM_006497845.1.
    UniGenei Mm.239514.

    3D structure databases

    ProteinModelPortali P39428.
    SMRi P39428. Positions 174-409.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204302. 6 interactions.
    DIPi DIP-260N.
    IntActi P39428. 35 interactions.
    MINTi MINT-1518514.
    STRINGi 10090.ENSMUSP00000108687.

    PTM databases

    PhosphoSitei P39428.

    Proteomic databases

    PRIDEi P39428.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028234 ; ENSMUSP00000028234 ; ENSMUSG00000026875 .
    ENSMUST00000113064 ; ENSMUSP00000108687 ; ENSMUSG00000026875 .
    ENSMUST00000172159 ; ENSMUSP00000130759 ; ENSMUSG00000026875 .
    GeneIDi 22029.
    KEGGi mmu:22029.
    UCSCi uc008jjj.1. mouse.

    Organism-specific databases

    CTDi 7185.
    MGIi MGI:101836. Traf1.

    Phylogenomic databases

    eggNOGi NOG264247.
    GeneTreei ENSGT00550000074359.
    HOGENOMi HOG000231558.
    HOVERGENi HBG058222.
    InParanoidi Q8CE28.
    KOi K03172.
    OMAi HFMKEKL.
    OrthoDBi EOG7966G5.
    TreeFami TF321154.

    Miscellaneous databases

    NextBioi 301776.
    PROi P39428.
    SOURCEi Search...

    Gene expression databases

    Bgeei P39428.
    CleanExi MM_TRAF1.
    Genevestigatori P39428.

    Family and domain databases

    InterProi IPR002083. MATH.
    IPR012227. TNF_rcpt--assoc_TRAF.
    IPR008974. TRAF-like.
    IPR027136. TRAF1.
    [Graphical view ]
    PANTHERi PTHR10131:SF29. PTHR10131:SF29. 1 hit.
    Pfami PF00917. MATH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015614. TRAF. 1 hit.
    SMARTi SM00061. MATH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 1 hit.
    PROSITEi PS50144. MATH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor."
      Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.
      Cell 78:681-692(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 123-135 AND 390-402, INTERACTION WITH TRAF2 AND TNFRSF1B.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Skin, Spleen and Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-kappaB activation."
      Lee S.Y., Lee S.Y., Choi Y.
      J. Exp. Med. 185:1275-1285(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAIP.
    6. "TRAF1 is a negative regulator of TNF signaling. enhanced TNF signaling in TRAF1-deficient mice."
      Tsitsikov E.N., Laouini D., Dunn I.F., Sannikova T.Y., Davidson L., Alt F.W., Geha R.S.
      Immunity 15:647-657(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    7. "A mammalian homolog of Drosophila schnurri, KRC, regulates TNF receptor-driven responses and interacts with TRAF2."
      Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.
      Mol. Cell 9:121-131(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIVEP3.
    8. "TRAF1 regulates Th2 differentiation, allergic inflammation and nuclear localization of the Th2 transcription factor, NIP45."
      Bryce P.J., Oyoshi M.K., Kawamoto S., Oettgen H.C., Tsitsikov E.N.
      Int. Immunol. 18:101-111(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFATC2IP.
    9. "Negative regulation of constitutive NF-kappaB and JNK signaling by PKN1-mediated phosphorylation of TRAF1."
      Kato T. Jr., Gotoh Y., Hoffmann A., Ono Y.
      Genes Cells 13:509-520(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-139, INTERACTION WITH TNFRSF1B, MUTAGENESIS OF SER-139.
    10. "FLN29 deficiency reveals its negative regulatory role in the Toll-like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like helicase signaling pathway."
      Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T., Yoshimura A.
      J. Biol. Chem. 283:33858-33864(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAFD1.
    11. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTRAF1_MOUSE
    AccessioniPrimary (citable) accession number: P39428
    Secondary accession number(s): Q8CE28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Lacks a RING domain and has therefore no E3 ubiquitin-protein ligase activity by itself.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3