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Q12933

- TRAF2_HUMAN

UniProt

Q12933 - TRAF2_HUMAN

Protein

TNF receptor-associated factor 2

Gene

TRAF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      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. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.16 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.1 Publication

    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. enzyme binding Source: BHF-UCL
    3. identical protein binding Source: IntAct
    4. ligase activity Source: UniProtKB-KW
    5. protein binding Source: IntAct
    6. protein phosphatase binding Source: UniProtKB
    7. signal transducer activity Source: ProtInc
    8. sphingolipid binding Source: UniProtKB
    9. thioesterase binding Source: UniProtKB
    10. tumor necrosis factor receptor binding Source: UniProtKB
    11. ubiquitin protein ligase binding Source: UniProtKB
    12. ubiquitin-protein transferase activity Source: UniProtKB
    13. zinc ion binding Source: InterPro

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
    2. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
    3. apoptotic process Source: Reactome
    4. apoptotic signaling pathway Source: Reactome
    5. cellular protein complex assembly Source: BHF-UCL
    6. innate immune response Source: Reactome
    7. negative regulation of glial cell apoptotic process Source: Ensembl
    8. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    9. positive regulation of interleukin-2 production Source: UniProtKB
    10. positive regulation of JUN kinase activity Source: UniProtKB
    11. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    12. positive regulation of protein homodimerization activity Source: UniProtKB
    13. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    14. positive regulation of T cell activation Source: UniProtKB
    15. positive regulation of T cell cytokine production Source: UniProtKB
    16. protein autoubiquitination Source: UniProtKB
    17. protein catabolic process Source: Ensembl
    18. protein complex assembly Source: ProtInc
    19. protein heterooligomerization Source: Ensembl
    20. protein homotrimerization Source: UniProtKB
    21. protein K63-linked ubiquitination Source: UniProtKB
    22. regulation of apoptotic process Source: UniProtKB
    23. regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
    24. regulation of immunoglobulin secretion Source: Ensembl
    25. signal transduction Source: ProtInc
    26. 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_1432. TNF signaling.
    REACT_1503. Caspase-8 activation.
    REACT_164011. Regulation by c-FLIP.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_832. Dimerization of procaspase-8.
    SignaLinkiQ12933.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TNF receptor-associated factor 2 (EC:6.3.2.-)
    Alternative name(s):
    E3 ubiquitin-protein ligase TRAF2
    Tumor necrosis factor type 2 receptor-associated protein 3
    Gene namesi
    Name:TRAF2
    Synonyms:TRAP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12032. TRAF2.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111S → A: Reduces global phosphorylation. Partial reduction of TNF-dependent activation of NF-kappa-B and activation of JNK. 1 Publication
    Mutagenesisi11 – 111S → D: Slight increase of TNF-dependent activation of NF-kappa-B and activation of JNK. 1 Publication
    Mutagenesisi31 – 311K → R: Abolishes 'Lys-63'-linked polyubiquitination.
    Mutagenesisi117 – 1171T → A: Loss of phosphorylation site. Abolishes activation of NF-kappa-B. 1 Publication
    Mutagenesisi285 – 2851I → A: Strongly reduced interaction with BIRC3. 1 Publication
    Mutagenesisi288 – 2881V → A: Strongly reduced interaction with BIRC3. 1 Publication
    Mutagenesisi292 – 2921E → A: Strongly reduced interaction with BIRC3. 1 Publication

    Organism-specific databases

    PharmGKBiPA164742666.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 501500TNF receptor-associated factor 2PRO_0000056399Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei7 – 71Phosphothreonine1 Publication
    Modified residuei11 – 111Phosphoserine2 Publications
    Modified residuei22 – 221Phosphothreonine1 Publication
    Cross-linki31 – 31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei117 – 1171Phosphothreonine; by PKC1 Publication

    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.1 Publication
    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. Deubiquitinated by CYLD, a protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ12933.
    PaxDbiQ12933.
    PRIDEiQ12933.

    PTM databases

    PhosphoSiteiQ12933.

    Expressioni

    Gene expression databases

    ArrayExpressiQ12933.
    BgeeiQ12933.
    CleanExiHS_TRAF2.
    GenevestigatoriQ12933.

    Organism-specific databases

    HPAiCAB004603.
    HPA009972.
    HPA010634.

    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, MAP3K14, MAP4K2, RIPK1, RIPK2, TNIK, TBK1, SPHK1, TRADD, TRAFD1, TRAIP, TANK/ITRAF, TNFAIP3, TDP2, MAVS/IPS1, TICAM1 and TRPC4AP. Interacts with CASP8AP2, NFATC2IP, PEG3 and HIVEP3. Interacts with ERN1; the interaction requires DAB2IP. 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 BIRC3. Interaction with BIRC2 and/or BIRC3 is essential for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts with CYLD, USP48, IKKA and IKKB. Identified in a complex with TNFRSF1A, RIPK1 and IKKB. Interacts (via 'Lys-63'-linked polyubiquitin chains) with TAB2 and TAB3. Interacts with ERN1 and TAOK3. Interaction with TAOK3 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation. Interacts (via zinc fingers) with DAB2IP (via C-terminus PER domain); the interaction occurs in a TNF-alpha-dependent manner. Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain). Interacts with CARD14. Interacts with PTPN2; probably involved in tumor necrosis factor-mediated signaling.50 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-355744,EBI-355744
    P889613EBI-355744,EBI-7907665From a different organism.
    APPL1Q9UKG12EBI-355744,EBI-741243
    ATXN1P542532EBI-355744,EBI-930964
    BIRC2Q1349010EBI-355744,EBI-514538
    BIRC3Q134897EBI-355744,EBI-517709
    Casp12O087366EBI-355744,EBI-6140033From a different organism.
    CDKN1BP465272EBI-355744,EBI-519280
    ERN1O754603EBI-355744,EBI-371750
    GSTP1P092115EBI-355744,EBI-353467
    Hoxa1P090223EBI-355744,EBI-3957603From a different organism.
    MAP3K1Q132332EBI-355744,EBI-49776
    NgfrP071743EBI-355744,EBI-1038810From a different organism.
    TANKQ928444EBI-355744,EBI-356349
    TAOK3Q9H2K82EBI-355744,EBI-1384100
    TBK1Q9UHD23EBI-355744,EBI-356402
    TNFRSF12AQ9NP843EBI-355744,EBI-2851995
    TNFRSF14Q929564EBI-355760,EBI-1056653
    TNFRSF1AP194384EBI-355744,EBI-299451
    TNFRSF1BP203333EBI-355744,EBI-358983
    TRADDQ156283EBI-355744,EBI-359215
    TRAF1Q130774EBI-355744,EBI-359224
    Traf5P701912EBI-355744,EBI-523899From a different organism.
    TRAF6Q9Y4K33EBI-355744,EBI-359276
    ZBTB16Q055162EBI-355744,EBI-711925
    ZFAND6Q6FIF06EBI-355744,EBI-724630

    Protein-protein interaction databases

    BioGridi113038. 223 interactions.
    DIPiDIP-6223N.
    IntActiQ12933. 145 interactions.
    MINTiMINT-107429.
    STRINGi9606.ENSP00000247668.

    Structurei

    Secondary structure

    1
    501
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 233
    Helixi25 – 273
    Helixi30 – 323
    Turni35 – 373
    Beta strandi42 – 465
    Beta strandi52 – 543
    Helixi55 – 617
    Helixi62 – 643
    Helixi70 – 745
    Turni80 – 834
    Helixi87 – 893
    Helixi94 – 1018
    Beta strandi103 – 1064
    Beta strandi115 – 1173
    Helixi118 – 1247
    Turni125 – 1273
    Helixi130 – 1334
    Helixi315 – 3184
    Helixi335 – 34713
    Beta strandi350 – 3589
    Helixi361 – 3699
    Beta strandi375 – 3773
    Beta strandi381 – 3844
    Beta strandi389 – 3957
    Helixi400 – 4023
    Turni403 – 4053
    Beta strandi406 – 4149
    Helixi419 – 4213
    Beta strandi430 – 4345
    Beta strandi443 – 4475
    Helixi454 – 4563
    Beta strandi460 – 4634
    Beta strandi467 – 4748
    Helixi476 – 4805
    Turni482 – 4843
    Beta strandi490 – 4967

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CA4X-ray2.20A/B/C/D/E/F334-501[»]
    1CA9X-ray2.30A/B/C/D/E/F310-501[»]
    1CZYX-ray2.00A/B/C334-501[»]
    1CZZX-ray2.70A/B/C315-501[»]
    1D00X-ray2.00A/B/C/D/E/F/G/H334-501[»]
    1D01X-ray2.00A/B/C/D/E/F334-501[»]
    1D0AX-ray2.00A/B/C/D/E/F334-501[»]
    1D0JX-ray2.50A/B/C/D/E/F334-501[»]
    1F3VX-ray2.00B331-501[»]
    1QSCX-ray2.40A/B/C311-501[»]
    3KNVX-ray1.90A1-133[»]
    3M06X-ray2.67A/B/C/D/E/F266-329[»]
    3M0AX-ray2.61A/B/C266-329[»]
    3M0DX-ray2.80A/B266-329[»]
    ProteinModelPortaliQ12933.
    SMRiQ12933. Positions 15-183, 267-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12933.

    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 BIRC3By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili299 – 348501 PublicationAdd
    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.1 Publication

    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.
    HOGENOMiHOG000231558.
    HOVERGENiHBG058222.
    InParanoidiQ12933.
    KOiK03173.
    OMAiSDGCTWK.
    OrthoDBiEOG7966G5.
    PhylomeDBiQ12933.
    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. 1 hit.
    PROSITEiPS50144. MATH. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    PS50145. ZF_TRAF. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12933-1) [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

    MAAASVTPPG SLELLQPGFS KTLLGTKLEA KYLCSACRNV LRRPFQAQCG    50
    HRYCSFCLAS ILSSGPQNCA ACVHEGIYEE GISILESSSA FPDNAARREV 100
    ESLPAVCPSD GCTWKGTLKE YESCHEGRCP LMLTECPACK GLVRLGEKER 150
    HLEHECPERS LSCRHCRAPC CGADVKAHHE VCPKFPLTCD GCGKKKIPRE 200
    KFQDHVKTCG KCRVPCRFHA IGCLETVEGE KQQEHEVQWL REHLAMLLSS 250
    VLEAKPLLGD QSHAGSELLQ RCESLEKKTA TFENIVCVLN REVERVAMTA 300
    EACSRQHRLD QDKIEALSSK VQQLERSIGL KDLAMADLEQ KVLEMEASTY 350
    DGVFIWKISD FARKRQEAVA GRIPAIFSPA FYTSRYGYKM CLRIYLNGDG 400
    TGRGTHLSLF FVVMKGPNDA LLRWPFNQKV TLMLLDQNNR EHVIDAFRPD 450
    VTSSSFQRPV NDMNIASGCP LFCPVSKMEA KNSYVRDDAI FIKAIVDLTG 500
    L 501
    Length:501
    Mass (Da):55,859
    Last modified:September 19, 2002 - v2
    Checksum:iC508BE185B783B20
    GO
    Isoform 2 (identifier: Q12933-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         122-122: E → EVKMPACGMVTEAPAVGSRPRSPSSYDLVLHVPLTGAEACLMSVEEETELLLR

    Note: No experimental confirmation available.

    Show »
    Length:553
    Mass (Da):61,384
    Checksum:iE5000CF242B2F404
    GO
    Isoform 3 (identifier: Q12933-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         53-63: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:490
    Mass (Da):54,671
    Checksum:i9CAF6DDAB0DE64DD
    GO
    Isoform 4 (identifier: Q12933-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         176-200: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:476
    Mass (Da):53,055
    Checksum:iBB290C92E8D33D79
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti205 – 310106Missing in BAB70792. (PubMed:14702039)CuratedAdd
    BLAST
    Sequence conflicti343 – 36523LEMEA…FARKR → RPFQAQCGHRYCSFCLASIL RKL in AAA87706. (PubMed:7639698)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei53 – 6311Missing in isoform 3. 1 PublicationVSP_039687Add
    BLAST
    Alternative sequencei122 – 1221E → EVKMPACGMVTEAPAVGSRP RSPSSYDLVLHVPLTGAEAC LMSVEEETELLLR in isoform 2. 1 PublicationVSP_007401
    Alternative sequencei176 – 20025Missing in isoform 4. 1 PublicationVSP_039688Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12597 mRNA. Translation: AAA87706.1.
    AK054686 mRNA. Translation: BAB70792.1.
    AK289722 mRNA. Translation: BAF82411.1.
    AK298370 mRNA. Translation: BAG60609.1.
    BX538160 mRNA. Translation: CAD98040.1.
    AY623660 Genomic DNA. Translation: AAT27320.1.
    AL355987, AL449425 Genomic DNA. Translation: CAI12703.1.
    AL449425, AL355987 Genomic DNA. Translation: CAI15106.1.
    CH471090 Genomic DNA. Translation: EAW88299.1.
    BC032410 mRNA. Translation: AAH32410.1.
    BC033810 mRNA. Translation: AAH33810.1.
    BC043492 mRNA. Translation: AAH43492.1.
    BC064662 mRNA. Translation: AAH64662.1.
    CCDSiCCDS7013.1. [Q12933-1]
    PIRiS56163.
    RefSeqiNP_066961.2. NM_021138.3. [Q12933-1]
    UniGeneiHs.522506.

    Genome annotation databases

    EnsembliENST00000247668; ENSP00000247668; ENSG00000127191. [Q12933-1]
    GeneIDi7186.
    KEGGihsa:7186.
    UCSCiuc004cjv.3. human. [Q12933-1]
    uc010nbw.3. human. [Q12933-4]
    uc011mek.2. human. [Q12933-3]

    Polymorphism databases

    DMDMi23503103.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12597 mRNA. Translation: AAA87706.1 .
    AK054686 mRNA. Translation: BAB70792.1 .
    AK289722 mRNA. Translation: BAF82411.1 .
    AK298370 mRNA. Translation: BAG60609.1 .
    BX538160 mRNA. Translation: CAD98040.1 .
    AY623660 Genomic DNA. Translation: AAT27320.1 .
    AL355987 , AL449425 Genomic DNA. Translation: CAI12703.1 .
    AL449425 , AL355987 Genomic DNA. Translation: CAI15106.1 .
    CH471090 Genomic DNA. Translation: EAW88299.1 .
    BC032410 mRNA. Translation: AAH32410.1 .
    BC033810 mRNA. Translation: AAH33810.1 .
    BC043492 mRNA. Translation: AAH43492.1 .
    BC064662 mRNA. Translation: AAH64662.1 .
    CCDSi CCDS7013.1. [Q12933-1 ]
    PIRi S56163.
    RefSeqi NP_066961.2. NM_021138.3. [Q12933-1 ]
    UniGenei Hs.522506.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CA4 X-ray 2.20 A/B/C/D/E/F 334-501 [» ]
    1CA9 X-ray 2.30 A/B/C/D/E/F 310-501 [» ]
    1CZY X-ray 2.00 A/B/C 334-501 [» ]
    1CZZ X-ray 2.70 A/B/C 315-501 [» ]
    1D00 X-ray 2.00 A/B/C/D/E/F/G/H 334-501 [» ]
    1D01 X-ray 2.00 A/B/C/D/E/F 334-501 [» ]
    1D0A X-ray 2.00 A/B/C/D/E/F 334-501 [» ]
    1D0J X-ray 2.50 A/B/C/D/E/F 334-501 [» ]
    1F3V X-ray 2.00 B 331-501 [» ]
    1QSC X-ray 2.40 A/B/C 311-501 [» ]
    3KNV X-ray 1.90 A 1-133 [» ]
    3M06 X-ray 2.67 A/B/C/D/E/F 266-329 [» ]
    3M0A X-ray 2.61 A/B/C 266-329 [» ]
    3M0D X-ray 2.80 A/B 266-329 [» ]
    ProteinModelPortali Q12933.
    SMRi Q12933. Positions 15-183, 267-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113038. 223 interactions.
    DIPi DIP-6223N.
    IntActi Q12933. 145 interactions.
    MINTi MINT-107429.
    STRINGi 9606.ENSP00000247668.

    PTM databases

    PhosphoSitei Q12933.

    Polymorphism databases

    DMDMi 23503103.

    Proteomic databases

    MaxQBi Q12933.
    PaxDbi Q12933.
    PRIDEi Q12933.

    Protocols and materials databases

    DNASUi 7186.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000247668 ; ENSP00000247668 ; ENSG00000127191 . [Q12933-1 ]
    GeneIDi 7186.
    KEGGi hsa:7186.
    UCSCi uc004cjv.3. human. [Q12933-1 ]
    uc010nbw.3. human. [Q12933-4 ]
    uc011mek.2. human. [Q12933-3 ]

    Organism-specific databases

    CTDi 7186.
    GeneCardsi GC09P139776.
    H-InvDB HIX0169360.
    HGNCi HGNC:12032. TRAF2.
    HPAi CAB004603.
    HPA009972.
    HPA010634.
    MIMi 601895. gene.
    neXtProti NX_Q12933.
    PharmGKBi PA164742666.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264247.
    HOGENOMi HOG000231558.
    HOVERGENi HBG058222.
    InParanoidi Q12933.
    KOi K03173.
    OMAi SDGCTWK.
    OrthoDBi EOG7966G5.
    PhylomeDBi Q12933.
    TreeFami TF321154.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_1432. TNF signaling.
    REACT_1503. Caspase-8 activation.
    REACT_164011. Regulation by c-FLIP.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24969. TRAF6 mediated NF-kB activation.
    REACT_832. Dimerization of procaspase-8.
    SignaLinki Q12933.

    Miscellaneous databases

    EvolutionaryTracei Q12933.
    GeneWikii TRAF2.
    GenomeRNAii 7186.
    NextBioi 28172.
    PROi Q12933.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12933.
    Bgeei Q12933.
    CleanExi HS_TRAF2.
    Genevestigatori Q12933.

    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. 1 hit.
    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. "Association of a RING finger protein with the cytoplasmic domain of the human type-2 tumour necrosis factor receptor."
      Song H.Y., Donner D.B.
      Biochem. J. 309:825-829(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Brain, Cerebellum and Kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Endometrium.
    4. SeattleSNPs variation discovery resource
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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 1).
      Tissue: Colon, Fetal brain, Kidney, Leukocyte, Stomach and Uterus.
    8. "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] OF 201-501, INTERACTION WITH TRAF1 AND TNFRSF1B.
    9. "T cell receptor-dependent cell death of T cell hybridomas mediated by the CD30 cytoplasmic domain in association with tumor necrosis factor receptor-associated factors."
      Lee S.Y., Park C.G., Choi Y.
      J. Exp. Med. 183:669-674(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF8.
    10. "I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction."
      Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A., Goeddel D.V.
      Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TANK.
    11. "ATAR, a novel tumor necrosis factor receptor family member, signals through TRAF2 and TRAF5."
      Hsu H., Solovyev I., Colombero A., Elliott R., Kelley M., Boyle W.J.
      J. Biol. Chem. 272:13471-13474(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF14.
    12. "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.
    13. "MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1."
      Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D.
      Nature 385:540-544(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K14.
    14. "CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions: regulation of CD40 signaling through multiple TRAF binding sites and TRAF hetero-oligomerization."
      Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J., Kehry M.R.
      Biochemistry 37:11836-11845(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF5.
    15. "Identification of CARDIAK, a RIP-like kinase that associates with caspase-1."
      Thome M., Hofmann K., Burns K., Martinon F., Bodmer J.-L., Mattmann C., Tschopp J.
      Curr. Biol. 8:885-888(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIPK2.
    16. "The TNF receptor family member CD27 signals to Jun N-terminal kinase via Traf-2."
      Gravestein L.A., Amsen D., Boes M., Calvo C.R., Kruisbeek A.M., Borst J.
      Eur. J. Immunol. 28:2208-2216(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD27.
    17. "Activation of OX40 signal transduction pathways leads to tumor necrosis factor receptor-associated factor (TRAF) 2- and TRAF5-mediated NF-kappaB activation."
      Kawamata S., Hori T., Imura A., Takaori-Kondo A., Uchiyama T.
      J. Biol. Chem. 273:5808-5814(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF4.
    18. "The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor."
      Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.
      J. Biol. Chem. 273:28355-28359(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF11A.
    19. Cited for: INTERACTION WITH CDK9.
    20. "CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-1BB ligand."
      Saoulli K., Lee S.Y., Cannons J.L., Yeh W.C., Santana A., Goldstein M.D., Bangia N., DeBenedette M.A., Mak T.W., Choi Y., Watts T.H.
      J. Exp. Med. 187:1849-1862(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF9.
    21. Cited for: INTERACTION WITH MAP3K5.
    22. "4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth factor receptor subfamily that bind TNF receptor-associated factors and activate nuclear factor kappaB."
      Arch R.H., Thompson C.B.
      Mol. Cell. Biol. 18:558-565(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF4 AND TNFRSF9.
    23. "NF-kB activation by a signaling complex containing TRAF2, TANK, and TBK1, a novel IKK-related kinase."
      Pomerantz J.L., Baltimore D.
      EMBO J. 18:6694-6704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TBK1.
      Tissue: Spleen.
    24. "Death deflected: IL-15 inhibits TNF-alpha-mediated apoptosis in fibroblasts by TRAF2 recruitment to the IL-15Ralpha chain."
      Bulfone-Paus S., Bulanova E., Pohl T., Budagian V., Duerkop H., Rueckert R., Kunzendorf U., Paus R., Krause H.
      FASEB J. 13:1575-1585(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IL15RA.
    25. "Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain."
      Baud V., Liu Z.-G., Bennett B., Suzuki N., Xia Y., Karin M.
      Genes Dev. 13:1297-1308(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K1, FUNCTION.
    26. "Identification of a novel activation-inducible protein of the tumor necrosis factor receptor superfamily and its ligand."
      Kwon B., Yu K.-Y., Ni J., Yu G.-L., Jang I.-K., Kim Y.-J., Xing L., Liu D., Wang S.-X., Kwon B.S.
      J. Biol. Chem. 274:6056-6061(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF18.
      Tissue: T-cell.
    27. "TRAF family proteins interact with the common neurotrophin receptor and modulate apoptosis induction."
      Ye X., Mehlen P., Rabizadeh S., VanArsdale T., Zhang H., Shin H., Wang J.J.L., Leo E., Zapata J.M., Hauser C.A., Reed J.C., Bredesen D.E.
      J. Biol. Chem. 274:30202-30208(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF16.
    28. "TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton."
      Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.
      J. Biol. Chem. 274:30729-30737(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNIK.
    29. "TAJ, a novel member of the tumor necrosis factor receptor family, activates the c-Jun N-terminal kinase pathway and mediates caspase-independent cell death."
      Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.
      J. Biol. Chem. 275:15336-15342(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF19.
    30. "TTRAP, a novel protein that associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that inhibits nuclear factor-kappa B activation."
      Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I., Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.
      J. Biol. Chem. 275:18586-18593(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TDP2.
    31. "TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation."
      Xia X.-Z., Treanor J., Senaldi G., Khare S.D., Boone T., Kelley M., Theill L.E., Colombero A., Solovyev I., Lee F., McCabe S., Elliott R., Miner K., Hawkins N., Guo J., Stolina M., Yu G., Wang J.
      , Delaney J., Meng S.-Y., Boyle W.J., Hsu H.
      J. Exp. Med. 192:137-143(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF13B.
    32. "Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress."
      Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.
      J. Biol. Chem. 276:13935-13940(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERN1 AND TAOK3.
    33. "Stress-induced decrease in TRAF2 stability is mediated by Siah2."
      Habelhah H., Frew I.J., Laine A., Janes P.W., Relaix F., Sassoon D., Bowtell D.D.L., Ronai Z.
      EMBO J. 21:5756-5765(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH2, DEGRADATION.
    34. "Direct activation of mitogen-activated protein kinase kinase kinase MEKK1 by the Ste20p homologue GCK and the adapter protein TRAF2."
      Chadee D.N., Yuasa T., Kyriakis J.M.
      Mol. Cell. Biol. 22:737-749(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP4K2.
    35. "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2."
      Li X., Yang Y., Ashwell J.D.
      Nature 416:345-347(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BIRC2 AND BIRC3, UBIQUITINATION BY BIRC2, DEGRADATION.
    36. "CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members."
      Trompouki E., Hatzivassiliou E., Tsichritzis T., Farmer H., Ashworth A., Mosialos G.
      Nature 424:793-796(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, DEUBIQUITINATION BY CYLD.
    37. "The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination."
      Kovalenko A., Chable-Bessia C., Cantarella G., Israeel A., Wallach D., Courtois G.
      Nature 424:801-805(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYLD, UBIQUITINATION, DEUBIQUITINATION BY CYLD.
    38. "AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation."
      Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.
      J. Biol. Chem. 279:44955-44965(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP.
    39. "TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation."
      He L., Grammer A.C., Wu X., Lipsky P.E.
      J. Biol. Chem. 279:55855-55865(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    40. Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
    41. "VISA is an adapter protein required for virus-triggered IFN-beta Signaling."
      Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.
      Mol. Cell 19:727-740(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAVS.
    42. "Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation."
      Reiley W., Zhang M., Wu X., Granger E., Sun S.C.
      Mol. Cell. Biol. 25:3886-3895(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, DEUBIQUITINATION BY CYLD.
    43. "Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase."
      van Vliet C., Bukczynska P.E., Puryer M.A., Sadek C.M., Shields B.J., Tremblay M.L., Tiganis T.
      Nat. Immunol. 6:253-260(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN2.
    44. "Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB."
      Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G., Hatzivassiliou E.G.
      Cell. Signal. 18:83-92(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP48.
    45. "RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation."
      Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.
      J. Biol. Chem. 282:14788-14796(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP.
    46. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    47. "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: FUNCTION, INTERACTION WITH BIRC2.
    48. "PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and K63-linked polyubiquitination."
      Li S., Wang L., Dorf M.E.
      Mol. Cell 33:30-42(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IKKA; IKKB; TAB2 AND TAB3, UBIQUITINATION AT LYS-31, PHOSPHORYLATION AT THR-117, MUTAGENESIS OF THR-117, UBIQUITINATION, SUBCELLULAR LOCATION.
    49. "TRAF2 phosphorylation modulates tumor necrosis factor alpha-induced gene expression and cell resistance to apoptosis."
      Blackwell K., Zhang L., Thomas G.S., Sun S., Nakano H., Habelhah H.
      Mol. Cell. Biol. 29:303-314(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH TNFRSF1A; RIPK1 AND IKKB, MUTAGENESIS OF SER-11, PHOSPHORYLATION AT SER-11.
    50. "TRAF2-MLK3 interaction is essential for TNF-alpha-induced MLK3 activation."
      Sondarva G., Kundu C.N., Mehrotra S., Mishra R., Rangasamy V., Sathyanarayana P., Ray R.S., Rana B., Rana A.
      Cell Res. 20:89-98(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K11.
    51. Cited for: INTERACTION WITH BIRC2, SUBUNIT, HOMOTRIMERIZATION.
    52. "The RING domain of TRAF2 plays an essential role in the inhibition of TNFalpha-induced cell death but not in the activation of NF-kappaB."
      Zhang L., Blackwell K., Shi Z., Habelhah H.
      J. Mol. Biol. 396:528-539(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN.
    53. "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
      Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
      Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, FUNCTION.
    54. "Direct binding of TRAF2 and TRAF6 to TICAM-1/TRIF adaptor participates in activation of the Toll-like receptor 3/4 pathway."
      Sasai M., Tatematsu M., Oshiumi H., Funami K., Matsumoto M., Hatakeyama S., Seya T.
      Mol. Immunol. 47:1283-1291(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1, FUNCTION.
    55. "Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2."
      Alvarez S.E., Harikumar K.B., Hait N.C., Allegood J., Strub G.M., Kim E.Y., Maceyka M., Jiang H., Luo C., Kordula T., Milstien S., Spiegel S.
      Nature 465:1084-1088(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, UBIQUITINATION, INTERACTION WITH SPHK1, SPHINGOLIPID BINDING.
    56. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    57. "Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes."
      Shembade N., Ma A., Harhaj E.W.
      Science 327:1135-1139(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFAIP3.
    58. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    59. "Alternative splicing of CARMA2/CARD14 transcripts generates protein variants with differential effect on NF-kappaB activation and endoplasmic reticulum stress-induced cell death."
      Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P., Stilo R.
      J. Cell. Physiol. 226:3121-3131(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARD14.
    60. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; SER-11 AND THR-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    61. "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
      Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
      Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN IKBKE UBIQUITINATION.
    62. "Structural basis for self-association and receptor recognition of human TRAF2."
      Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.
      Nature 398:533-538(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 310-501 IN COMPLEX WITH TNFRSF1B.
    63. "Crystallographic analysis of CD40 recognition and signaling by human TRAF2."
      McWhirter S.M., Pullen S.S., Holton J.M., Crute J.J., Kehry M.R., Alber T.
      Proc. Natl. Acad. Sci. U.S.A. 96:8408-8413(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 334-501 IN COMPLEX WITH EBV BNFL1, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 315-501 IN COMPLEX WITH TNFRSF5, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 334-501 IN COMPLEX WITH TNFRSF4, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 334-501 IN COMPLEX WITH TNFRSF9.
    64. "A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction."
      Park Y.C., Ye H., Hsia C., Segal D., Rich R.L., Liou H.C., Myszka D.G., Wu H.
      Cell 101:777-787(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 331-501 IN COMPLEX WITH TRADD.
    65. "Structural basis for the lack of E2 interaction in the RING domain of TRAF2."
      Yin Q., Lamothe B., Darnay B.G., Wu H.
      Biochemistry 48:10558-10567(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-133, FUNCTION, SUBUNIT.
    66. "Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation."
      Zheng C., Kabaleeswaran V., Wang Y., Cheng G., Wu H.
      Mol. Cell 38:101-113(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 266-330 IN COMPLEXES WITH TRAF1 AND BIRC3, FUNCTION, SUBUNIT, COILED-COIL DOMAIN, MUTAGENESIS OF ILE-285; VAL-288 AND GLU-292.

    Entry informationi

    Entry nameiTRAF2_HUMAN
    AccessioniPrimary (citable) accession number: Q12933
    Secondary accession number(s): A8K107
    , B4DPJ7, Q7Z337, Q96NT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 179 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 9
      Human chromosome 9: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3