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P39429 (TRAF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TNF receptor-associated factor 2

EC=6.3.2.-
Alternative name(s):
E3 ubiquitin-protein ligase TRAF2
Gene names
Name:Traf2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.12 Ref.17 Ref.18 Ref.22 Ref.23 Ref.25 Ref.26

Enzyme regulation

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.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.1 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

Subcellular location

Cytoplasm.

Tissue specificity

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.

Domain

The coiled coil domain mediates homo- and hetero-oligomerization. Ref.25

The MATH/TRAF domain binds to receptor cytoplasmic domains. Ref.25

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. Ref.25

Post-translational modification

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.

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.

Disruption phenotype

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. Ref.9 Ref.12 Ref.22 Ref.26

Sequence similarities

Belongs to the TNF receptor-associated factor family. A subfamily.

Contains 1 MATH domain.

Contains 1 RING-type zinc finger.

Contains 2 TRAF-type zinc fingers.

Ontologies

Keywords
   Biological processApoptosis
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
Zinc-finger
   LigandLipid-binding
Metal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of NF-kappaB-inducing kinase activity

Inferred from electronic annotation. Source: InterPro

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein complex assembly

Inferred from direct assay PubMed 20614026. Source: BHF-UCL

cellular response to nitric oxide

Inferred from mutant phenotype PubMed 18007661. Source: MGI

negative regulation of apoptotic process

Non-traceable author statement PubMed 9692890. Source: UniProtKB

negative regulation of glial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of JUN kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of T cell cytokine production

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-2 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein homodimerization activity

Inferred from electronic annotation. Source: Ensembl

programmed necrotic cell death

Inferred from mutant phenotype PubMed 18007661. Source: MGI

protein K63-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein autoubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein catabolic process

Inferred from mutant phenotype PubMed 12958312. Source: MGI

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from electronic annotation. Source: Ensembl

regulation of JNK cascade

Inferred from direct assay PubMed 12958312. Source: MGI

regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of immunoglobulin secretion

Inferred from mutant phenotype PubMed 12958312. Source: MGI

signal transduction

Inferred from direct assay PubMed 12958312. Source: MGI

tumor necrosis factor-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentCD40 receptor complex

Inferred from direct assay PubMed 20614026. Source: BHF-UCL

cell cortex

Inferred from electronic annotation. Source: Ensembl

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 20614026. Source: BHF-UCL

cytosol

Inferred from direct assay PubMed 18007661. Source: MGI

membrane raft

Inferred from direct assay PubMed 18007661. Source: MGI

   Molecular_functionCD40 receptor binding

Inferred from physical interaction PubMed 20614026. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 12884866Ref.21PubMed 9692890. Source: UniProtKB

sphingolipid binding

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P39429-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P39429-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 501500TNF receptor-associated factor 2
PRO_0000056400

Regions

Domain351 – 496146MATH
Zinc finger34 – 7340RING-type
Zinc finger124 – 18057TRAF-type 1
Zinc finger177 – 23357TRAF-type 2
Region283 – 29311Important for interaction with BIRC2 and BIRC3
Coiled coil298 – 34851 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue71Phosphothreonine By similarity
Modified residue111Phosphoserine By similarity
Modified residue221Phosphothreonine By similarity
Modified residue1171Phosphothreonine; by PKC By similarity
Cross-link31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence621L → LRCASILS in isoform 2.
VSP_007402

Experimental info

Mutagenesis341C → S: Loss of autoubiquitination. Ref.15
Mutagenesis2831E → A: Reduces interaction with BIRC2. Ref.25
Mutagenesis2921E → A: Almost abolishes interaction with BIRC2; when associated with A-294. Ref.25
Mutagenesis2941E → A: Almost abolishes interaction with BIRC2; when associated with A-292. Ref.25

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 043B391180365F10

FASTA50156,026
        10         20         30         40         50         60 
MAAASVTSPG SLELLQPGFS KTLLGTRLEA KYLCSACKNI LRRPFQAQCG HRYCSFCLTS 

        70         80         90        100        110        120 
ILSSGPQNCA ACVYEGLYEE GISILESSSA FPDNAARREV ESLPAVCPND GCTWKGTLKE 

       130        140        150        160        170        180 
YESCHEGLCP FLLTECPACK GLVRLSEKEH HTEQECPKRS LSCQHCRAPC SHVDLEVHYE 

       190        200        210        220        230        240 
VCPKFPLTCD GCGKKKIPRE TFQDHVRACS KCRVLCRFHT VGCSEMVETE NLQDHELQRL 

       250        260        270        280        290        300 
REHLALLLSS FLEAQASPGT LNQVGPELLQ RCQILEQKIA TFENIVCVLN REVERVAVTA 

       310        320        330        340        350        360 
EACSRQHRLD QDKIEALSNK VQQLERSIGL KDLAMADLEQ KVSELEVSTY DGVFIWKISD 

       370        380        390        400        410        420 
FTRKRQEAVA GRTPAIFSPA FYTSRYGYKM CLRVYLNGDG TGRGTHLSLF FVVMKGPNDA 

       430        440        450        460        470        480 
LLQWPFNQKV TLMLLDHNNR EHVIDAFRPD VTSSSFQRPV SDMNIASGCP LFCPVSKMEA 

       490        500 
KNSYVRDDAI FIKAIVDLTG L 

« Hide

Isoform 2 (TRAF2A) [UniParc].

Checksum: 74B8B26BFCF9B1C4
Show »

FASTA50856,757

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"FLASH coordinates NF-kappa B activity via TRAF2."
Choi Y.-H., Kim K.-B., Kim H.-H., Hong G.-S., Kwon Y.-K., Chung C.-W., Park Y.-M., Shen Z.-J., Kim B.J., Lee S.-Y., Jung Y.-K.
J. Biol. Chem. 276:25073-25077(2001) [PubMed] [Europe PMC] [Abstract]
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]"TRAF family proteins link PKR with NF-kappa B activation."
Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J., Nakano H., Alcami J., Esteban M.
Mol. Cell. Biol. 24:4502-4512(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L35303 mRNA. Translation: AAC37662.1.
AF027570 mRNA. Translation: AAC53545.1.
AF233332 expand/collapse EMBL AC list , AF233326, AF233327, AF233328, AF233329, AF233330, AF233331 Genomic DNA. Translation: AAF59928.1.
AL732590 Genomic DNA. Translation: CAM25164.1.
BC003801 mRNA. Translation: AAH03801.1.
CCDSCCDS15779.1. [P39429-1]
PIRI61512.
RefSeqNP_001277342.1. NM_001290413.1. [P39429-2]
NP_033448.2. NM_009422.3. [P39429-1]
XP_006497911.1. XM_006497848.1. [P39429-2]
UniGeneMm.3399.

3D structure databases

ProteinModelPortalP39429.
SMRP39429. Positions 15-183, 267-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204303. 29 interactions.
DIPDIP-468N.
IntActP39429. 47 interactions.
MINTMINT-197749.

PTM databases

PhosphoSiteP39429.

Proteomic databases

MaxQBP39429.
PaxDbP39429.
PRIDEP39429.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028311; ENSMUSP00000028311; ENSMUSG00000026942. [P39429-1]
ENSMUST00000114234; ENSMUSP00000109872; ENSMUSG00000026942. [P39429-2]
GeneID22030.
KEGGmmu:22030.
UCSCuc008isl.1. mouse. [P39429-2]
uc008ism.1. mouse. [P39429-1]

Organism-specific databases

CTD7186.
MGIMGI:101835. Traf2.

Phylogenomic databases

eggNOGNOG264247.
GeneTreeENSGT00550000074359.
HOGENOMHOG000231558.
HOVERGENHBG058222.
InParanoidA2AJA3.
KOK03173.
OMASDGCTWK.
OrthoDBEOG7966G5.
PhylomeDBP39429.
TreeFamTF321154.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeP39429.
CleanExMM_TRAF2.
GenevestigatorP39429.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR002083. 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]
PANTHERPTHR10131:SF21. PTHR10131:SF21. 1 hit.
PfamPF00917. MATH. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PIRSFPIRSF015614. TRAF. 1 hit.
SMARTSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49599. SSF49599. 2 hits.
PROSITEPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio301780.
PROP39429.
SOURCESearch...

Entry information

Entry nameTRAF2_MOUSE
AccessionPrimary (citable) accession number: P39429
Secondary accession number(s): A2AJA3, O54896
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot