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P39429

- TRAF2_MOUSE

UniProt

P39429 - TRAF2_MOUSE

Protein

TNF receptor-associated factor 2

Gene

Traf2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Isoform 2 does not seem to mediate activation of NF-kappa-B but inhibits isoform 1 activity. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.8 Publications

    Enzyme regulationi

    Has very low E3 ubiquitin ligase activity in the absence of sphingosine-1-phosphate. E3 ubiquitin ligase activity is strongly activated by cytoplasmic sphingosine-1-phosphate By similarity.By similarity

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri34 – 7340RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri124 – 18057TRAF-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri177 – 23357TRAF-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. CD40 receptor binding Source: BHF-UCL
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. sphingolipid binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of NF-kappaB-inducing kinase activity Source: InterPro
    2. apoptotic process Source: UniProtKB-KW
    3. cellular protein complex assembly Source: BHF-UCL
    4. cellular response to nitric oxide Source: MGI
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of glial cell apoptotic process Source: Ensembl
    7. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    8. positive regulation of interleukin-2 production Source: Ensembl
    9. positive regulation of JUN kinase activity Source: UniProtKB
    10. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    11. positive regulation of protein homodimerization activity Source: Ensembl
    12. positive regulation of T cell cytokine production Source: Ensembl
    13. programmed necrotic cell death Source: MGI
    14. protein autoubiquitination Source: UniProtKB
    15. protein catabolic process Source: MGI
    16. protein heterooligomerization Source: Ensembl
    17. protein homotrimerization Source: Ensembl
    18. protein K63-linked ubiquitination Source: UniProtKB
    19. regulation of apoptotic process Source: UniProtKB
    20. regulation of immunoglobulin secretion Source: MGI
    21. regulation of JNK cascade Source: MGI
    22. signal transduction Source: MGI
    23. tumor necrosis factor-mediated signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Apoptosis, Ubl conjugation pathway

    Keywords - Ligandi

    Lipid-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198521. TRAF6 mediated IRF7 activation.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_215122. Regulation by c-FLIP.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TNF receptor-associated factor 2 (EC:6.3.2.-)
    Alternative name(s):
    E3 ubiquitin-protein ligase TRAF2
    Gene namesi
    Name:Traf2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:101835. Traf2.

    Subcellular locationi

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cell cortex Source: Ensembl
    3. cytoplasmic side of plasma membrane Source: BHF-UCL
    4. cytosol Source: MGI
    5. membrane raft Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Important embryonic and perinatal mortality. Life-born mutants appear normal at birth, but are smaller than their littermates after three days, fail to thrive, and few survive more than three weeks. Thymus and spleen are severely atrophic, and mice display lymphopenia of both T and B lymphocytes, with normal erythrocyte counts. Their thymocytes are abnormally sensitive to TNF-induced cell death and exhibit high levels of spontaneous apoptosis. Macrophages are highly sensitive to TNF and produce high levels of nitric oxide (NO) in response to TNF. Likewise, endogenous TNF production is abnormally increased upon exposure to TNF. Symptoms are much attenuated in mice that are deficient for both Traf2 and Tnfrsf1a/Tnfr1, or Traf2 and Tnf. Likewise, deletion of one Map3k14 allele alleviates symptoms and rescues splenic atrophy and reduction of splenocyte numbers. Mice show normal IgM production in response to viral infection, but lack CD40-mediated proliferation of B-cells. They are deficient in antibody isotype switching and fail to produce IgG.4 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi34 – 341C → S: Loss of autoubiquitination. 1 Publication
    Mutagenesisi283 – 2831E → A: Reduces interaction with BIRC2. 1 Publication
    Mutagenesisi292 – 2921E → A: Almost abolishes interaction with BIRC2; when associated with A-294. 1 Publication
    Mutagenesisi294 – 2941E → A: Almost abolishes interaction with BIRC2; when associated with A-292. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 501500TNF receptor-associated factor 2PRO_0000056400Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei7 – 71PhosphothreonineBy similarity
    Modified residuei11 – 111PhosphoserineBy similarity
    Modified residuei22 – 221PhosphothreonineBy similarity
    Cross-linki31 – 31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei117 – 1171Phosphothreonine; by PKCBy similarity

    Post-translational modificationi

    Phosphorylated at several serine residues within the first 128 amino acid residues. Phosphorylated at Thr-117 in response to signaling via TNF and TNFRSF1A. Phosphorylation at Thr-117 is required for 'Lys-63'-linked polyubiquitination, but not for 'Lys-48'-linked polyubiquitination. Phosphorylation at Thr-117 is important for interaction with IKKA and IKKB, activation of IKK and subsequent activation of NF-kappa-B By similarity.By similarity
    Undergoes both 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination. Polyubiquitinated via 'Lys-63'-linked ubiquitin in response to TNF signaling; this requires prior phosphorylation at Thr-117. 'Lys-63'-linked polyubiquitination promotes TRAF2-mediated activation of NF-kappa-B. Can be polyubiquitinated at several Lys residues via 'Lys-48'-linked ubiquitin chains in response to TNF signaling, leading to proteasomal degradation. Autoubiquitinated, leading to its subsequent proteasomal degradation. Polyubiquitinated by BIRC2 and SIAH2, leading to its subsequent proteasomal degradation. Not ubiquitinated by BIRC3 or SIAH1. Deubiquitinated by CYLD, a protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP39429.
    PaxDbiP39429.
    PRIDEiP39429.

    PTM databases

    PhosphoSiteiP39429.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed in spleen, adipose tissues, skeletal muscles, thymus, testis, heart, lung, brain. Isoform 2 is very weakly expressed in heart, lung and brain.

    Gene expression databases

    BgeeiP39429.
    CleanExiMM_TRAF2.
    GenevestigatoriP39429.

    Interactioni

    Subunit structurei

    Homotrimer, and heterotrimer with TRAF1 and TRAF3 (via TRAF domain). The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro). Interacts with TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40, CD27/TNFRSF7, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR, TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1 and IL15RA. Interacts with CDK9, CSK, MAP3K1, MAP3K5, MAP3K11, MAP4K2, RIPK2, TNIK, TBK1, SPHK1, TRAIP, TANK/ITRAF, TDP2, MAVS/IPS1, TICAM1 and TRPC4AP. Interacts with CASP8AP2, NFATC2IP, PEG3 and HIVEP3. Interacts with CYLD, USP48, IKKA and IKKB. Interacts (via 'Lys-63'-linked polyubiquitin chains) with TAB2 and TAB3. Interaction with TAOK3 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation. Interacts with CASP12 under resting conditions; this interaction is reduced in ER stress conditions. Interacts (via zinc fingers) with DAB2IP (via C-terminus PER domain); the interaction occurs in a TNF-alpha-dependent manner. Interacts with ERN1; the interaction requires DAB2IP. Interacts with DAB2IP. Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain). Interacts with CARD14 By similarity. Interacts with TRAFD1, TRADD and TNFAIP3. Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2, or a TRAF2 homotrimer. Identified in a complex composed of TRAF2, TRAF3, BIRC2 and/or BIRC3. Interaction with BIRC2 and/or BIRC3 is essential for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts with MAP3K14 and RIPK1. Interacts with PTPN2; probably involved in tumor necrosis factor-mediated signaling.By similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279585EBI-520016,EBI-8753518From a different organism.
    Birc3O088637EBI-520016,EBI-642236
    FcrlaQ920A95EBI-520016,EBI-646587
    Map3k7Q620732EBI-520016,EBI-1775345
    Mknk2Q8CDB03EBI-520016,EBI-646209
    TankP70347-17EBI-520016,EBI-646125
    Tnfaip3Q607693EBI-520016,EBI-646595
    Tnfrsf11aO353052EBI-520016,EBI-647362
    Tnfrsf4P477413EBI-520016,EBI-520001
    Traf3Q608032EBI-520016,EBI-520135

    Protein-protein interaction databases

    BioGridi204303. 30 interactions.
    DIPiDIP-468N.
    IntActiP39429. 47 interactions.
    MINTiMINT-197749.

    Structurei

    3D structure databases

    ProteinModelPortaliP39429.
    SMRiP39429. Positions 15-183, 267-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini351 – 496146MATHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni283 – 29311Important for interaction with BIRC2 and BIRC3Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili298 – 34851By similarityAdd
    BLAST

    Domaini

    The coiled coil domain mediates homo- and hetero-oligomerization.1 Publication
    The MATH/TRAF domain binds to receptor cytoplasmic domains.1 Publication
    The RING-type zinc finger domain is essential for E3 ubiquitin-protein ligase activity. It is not essential for the stabilization of BIRC2, or for the ubiquitination of RIPK1 in response to TNFR1 signaling By similarity.By similarity

    Sequence similaritiesi

    Contains 1 MATH domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 2 TRAF-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri34 – 7340RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri124 – 18057TRAF-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri177 – 23357TRAF-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG264247.
    GeneTreeiENSGT00550000074359.
    HOGENOMiHOG000231558.
    HOVERGENiHBG058222.
    InParanoidiA2AJA3.
    KOiK03173.
    OMAiSDGCTWK.
    OrthoDBiEOG7966G5.
    PhylomeDBiP39429.
    TreeFamiTF321154.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR002083. MATH.
    IPR012227. TNF_rcpt--assoc_TRAF.
    IPR008974. TRAF-like.
    IPR027133. TRAF2.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    IPR001293. Znf_TRAF.
    [Graphical view]
    PANTHERiPTHR10131:SF21. PTHR10131:SF21. 1 hit.
    PfamiPF00917. MATH. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015614. TRAF. 1 hit.
    SMARTiSM00061. MATH. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 2 hits.
    PROSITEiPS50144. MATH. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    PS50145. ZF_TRAF. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P39429-1) [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

    MAAASVTSPG SLELLQPGFS KTLLGTRLEA KYLCSACKNI LRRPFQAQCG    50
    HRYCSFCLTS ILSSGPQNCA ACVYEGLYEE GISILESSSA FPDNAARREV 100
    ESLPAVCPND GCTWKGTLKE YESCHEGLCP FLLTECPACK GLVRLSEKEH 150
    HTEQECPKRS LSCQHCRAPC SHVDLEVHYE VCPKFPLTCD GCGKKKIPRE 200
    TFQDHVRACS KCRVLCRFHT VGCSEMVETE NLQDHELQRL REHLALLLSS 250
    FLEAQASPGT LNQVGPELLQ RCQILEQKIA TFENIVCVLN REVERVAVTA 300
    EACSRQHRLD QDKIEALSNK VQQLERSIGL KDLAMADLEQ KVSELEVSTY 350
    DGVFIWKISD FTRKRQEAVA GRTPAIFSPA FYTSRYGYKM CLRVYLNGDG 400
    TGRGTHLSLF FVVMKGPNDA LLQWPFNQKV TLMLLDHNNR EHVIDAFRPD 450
    VTSSSFQRPV SDMNIASGCP LFCPVSKMEA KNSYVRDDAI FIKAIVDLTG 500
    L 501
    Length:501
    Mass (Da):56,026
    Last modified:February 1, 1995 - v1
    Checksum:i043B391180365F10
    GO
    Isoform 2 (identifier: P39429-2) [UniParc]FASTAAdd to Basket

    Also known as: TRAF2A

    The sequence of this isoform differs from the canonical sequence as follows:
         62-62: L → LRCASILS

    Note: No experimental confirmation available. On mRNA level, has a significantly shorter half-life than isoform 1.

    Show »
    Length:508
    Mass (Da):56,757
    Checksum:i74B8B26BFCF9B1C4
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei62 – 621L → LRCASILS in isoform 2. 1 PublicationVSP_007402

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35303 mRNA. Translation: AAC37662.1.
    AF027570 mRNA. Translation: AAC53545.1.
    AF233332
    , AF233326, AF233327, AF233328, AF233329, AF233330, AF233331 Genomic DNA. Translation: AAF59928.1.
    AL732590 Genomic DNA. Translation: CAM25164.1.
    BC003801 mRNA. Translation: AAH03801.1.
    CCDSiCCDS15779.1. [P39429-1]
    CCDS71002.1. [P39429-2]
    PIRiI61512.
    RefSeqiNP_001277342.1. NM_001290413.1. [P39429-2]
    NP_033448.2. NM_009422.3. [P39429-1]
    XP_006497911.1. XM_006497848.1. [P39429-2]
    UniGeneiMm.3399.

    Genome annotation databases

    EnsembliENSMUST00000028311; ENSMUSP00000028311; ENSMUSG00000026942. [P39429-1]
    ENSMUST00000114234; ENSMUSP00000109872; ENSMUSG00000026942. [P39429-2]
    GeneIDi22030.
    KEGGimmu:22030.
    UCSCiuc008isl.1. mouse. [P39429-2]
    uc008ism.1. mouse. [P39429-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35303 mRNA. Translation: AAC37662.1 .
    AF027570 mRNA. Translation: AAC53545.1 .
    AF233332
    , AF233326 , AF233327 , AF233328 , AF233329 , AF233330 , AF233331 Genomic DNA. Translation: AAF59928.1 .
    AL732590 Genomic DNA. Translation: CAM25164.1 .
    BC003801 mRNA. Translation: AAH03801.1 .
    CCDSi CCDS15779.1. [P39429-1 ]
    CCDS71002.1. [P39429-2 ]
    PIRi I61512.
    RefSeqi NP_001277342.1. NM_001290413.1. [P39429-2 ]
    NP_033448.2. NM_009422.3. [P39429-1 ]
    XP_006497911.1. XM_006497848.1. [P39429-2 ]
    UniGenei Mm.3399.

    3D structure databases

    ProteinModelPortali P39429.
    SMRi P39429. Positions 15-183, 267-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204303. 30 interactions.
    DIPi DIP-468N.
    IntActi P39429. 47 interactions.
    MINTi MINT-197749.

    PTM databases

    PhosphoSitei P39429.

    Proteomic databases

    MaxQBi P39429.
    PaxDbi P39429.
    PRIDEi P39429.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028311 ; ENSMUSP00000028311 ; ENSMUSG00000026942 . [P39429-1 ]
    ENSMUST00000114234 ; ENSMUSP00000109872 ; ENSMUSG00000026942 . [P39429-2 ]
    GeneIDi 22030.
    KEGGi mmu:22030.
    UCSCi uc008isl.1. mouse. [P39429-2 ]
    uc008ism.1. mouse. [P39429-1 ]

    Organism-specific databases

    CTDi 7186.
    MGIi MGI:101835. Traf2.

    Phylogenomic databases

    eggNOGi NOG264247.
    GeneTreei ENSGT00550000074359.
    HOGENOMi HOG000231558.
    HOVERGENi HBG058222.
    InParanoidi A2AJA3.
    KOi K03173.
    OMAi SDGCTWK.
    OrthoDBi EOG7966G5.
    PhylomeDBi P39429.
    TreeFami TF321154.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_198521. TRAF6 mediated IRF7 activation.
    REACT_202898. TRAF6 mediated NF-kB activation.
    REACT_215122. Regulation by c-FLIP.

    Miscellaneous databases

    NextBioi 301780.
    PROi P39429.
    SOURCEi Search...

    Gene expression databases

    Bgeei P39429.
    CleanExi MM_TRAF2.
    Genevestigatori P39429.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR002083. MATH.
    IPR012227. TNF_rcpt--assoc_TRAF.
    IPR008974. TRAF-like.
    IPR027133. TRAF2.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    IPR001293. Znf_TRAF.
    [Graphical view ]
    PANTHERi PTHR10131:SF21. PTHR10131:SF21. 1 hit.
    Pfami PF00917. MATH. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015614. TRAF. 1 hit.
    SMARTi SM00061. MATH. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 2 hits.
    PROSITEi PS50144. MATH. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    PS50145. ZF_TRAF. 2 hits.
    [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] (ISOFORM 1), INTERACTION WITH TRAF1 AND TNFRSF1B.
    2. "Tumor necrosis factor receptor (TNFR)-associated factor 2A (TRAF2A), a TRAF2 splice variant with an extended RING finger domain that inhibits TNFR2-mediated NF-kappaB activation."
      Brink R., Lodish H.F.
      J. Biol. Chem. 273:4129-4134(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Kidney.
    3. "Complete structural characterisation of the mammalian and Drosophila TRAF genes: implications for TRAF evolution and the role of RING finger splice variants."
      Grech A., Quinn R., Srinivasan D., Badoux X., Brink R.
      Mol. Immunol. 37:721-734(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
      Strain: C57BL/6.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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 1).
      Strain: Czech II.
      Tissue: Mammary tumor.
    6. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 430-440, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    7. "TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways."
      Hsu H., Shu H.-B., Pan M.G., Goeddel D.V.
      Cell 84:299-308(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRADD.
    8. "The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation."
      Song H.Y., Rothe M., Goeddel D.V.
      Proc. Natl. Acad. Sci. U.S.A. 93:6721-6725(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFAIP3.
    9. "Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice."
      Yeh W.C., Shahinian A., Speiser D., Kraunus J., Billia F., Wakeham A., de la Pompa J.L., Ferrick D., Hum B., Iscove N., Ohashi P., Rothe M., Goeddel D.V., Mak T.W.
      Immunity 7:715-725(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    10. "Peg3/Pw1 is an imprinted gene involved in the TNF-NFkappaB signal transduction pathway."
      Relaix F., Wei X.-J., Wu X., Sassoon D.A.
      Nat. Genet. 18:287-291(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PEG3.
    11. "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.
    12. "TRAF2 deficiency results in hyperactivity of certain TNFR1 signals and impairment of CD40-mediated responses."
      Nguyen L.T., Duncan G.S., Mirtsos C., Ng M., Speiser D.E., Shahinian A., Marino M.W., Mak T.W., Ohashi P.S., Yeh W.C.
      Immunity 11:379-389(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    13. Cited for: INTERACTION WITH CASP8AP2.
    14. "Tumor necrosis factor receptor-associated factor (TRAF)2 represses the T helper cell type 2 response through interaction with NFAT-interacting protein (NIP45)."
      Lieberson R., Mowen K.A., McBride K.D., Leautaud V., Zhang X., Suh W.-K., Wu L., Glimcher L.H.
      J. Exp. Med. 194:89-98(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFATC2IP.
    15. "Regulation of TRAF2 signaling by self-induced degradation."
      Brown K.D., Hostager B.S., Bishop G.A.
      J. Biol. Chem. 277:19433-19438(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOUBIQUITINATION, DEGRADATION, INTERACTION WITH CD40, MUTAGENESIS OF CYS-34.
    16. "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.
    17. "The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2."
      Lee T.H., Shank J., Cusson N., Kelliher M.A.
      J. Biol. Chem. 279:33185-33191(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. Cited for: FUNCTION.
    19. "TRUSS, a tumor necrosis factor receptor-1-interacting protein, activates c-Jun NH(2)-terminal kinase and transcription factor AP-1."
      Soond S.M., Terry J.L., Riches D.W.H.
      FEBS Lett. 580:4591-4596(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRPC4AP.
    20. "AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response."
      Luo D., He Y., Zhang H., Yu L., Chen H., Xu Z., Tang S., Urano F., Min W.
      J. Biol. Chem. 283:11905-11912(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP AND ERN1.
    21. "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.
    22. "Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling."
      Vallabhapurapu S., Matsuzawa A., Zhang W., Tseng P.H., Keats J.J., Wang H., Vignali D.A., Bergsagel P.L., Karin M.
      Nat. Immunol. 9:1364-1370(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN A COMPLEX WITH MAP3K14; BIRC3 AND TRAF3.
    23. "Noncanonical NF-kappaB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK."
      Zarnegar B.J., Wang Y., Mahoney D.J., Dempsey P.W., Cheung H.H., He J., Shiba T., Yang X., Yeh W.C., Mak T.W., Korneluk R.G., Cheng G.
      Nat. Immunol. 9:1371-1378(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH TRAF3; BIRC2 AND BIRC3.
    24. "Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2."
      Csomos R.A., Brady G.F., Duckett C.S.
      J. Biol. Chem. 284:20531-20539(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC2.
    25. "TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (TNF) to efficiently activate NF-{kappa}B and to prevent TNF-induced apoptosis."
      Vince J.E., Pantaki D., Feltham R., Mace P.D., Cordier S.M., Schmukle A.C., Davidson A.J., Callus B.A., Wong W.W., Gentle I.E., Carter H., Lee E.F., Walczak H., Day C.L., Vaux D.L., Silke J.
      J. Biol. Chem. 284:35906-35915(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BIRC2; TRADD AND RIPK1, DOMAIN, MUTAGENESIS OF GLU-283; GLU-292 AND GLU-294.
    26. "TRAF2 suppresses basal IKK activity in resting cells and TNFalpha can activate IKK in TRAF2 and TRAF5 double knockout cells."
      Zhang L., Blackwell K., Thomas G.S., Sun S., Yeh W.C., Habelhah H.
      J. Mol. Biol. 389:495-510(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.

    Entry informationi

    Entry nameiTRAF2_MOUSE
    AccessioniPrimary (citable) accession number: P39429
    Secondary accession number(s): A2AJA3, O54896
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3