Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P39429

- TRAF2_MOUSE

UniProt

P39429 - TRAF2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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. sphingolipid binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. 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
Complete GO annotation...

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.
REACT_241657. Caspase-8 activation by cleavage.
REACT_243608. Dimerization of procaspase-8.
REACT_256171. TNF signaling.
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
Complete GO annotation...

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.
ExpressionAtlasiP39429. baseline and differential.
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. 31 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.
InParanoidiP39429.
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

        10         20         30         40         50
MAAASVTSPG SLELLQPGFS KTLLGTRLEA KYLCSACKNI LRRPFQAQCG
60 70 80 90 100
HRYCSFCLTS ILSSGPQNCA ACVYEGLYEE GISILESSSA FPDNAARREV
110 120 130 140 150
ESLPAVCPND GCTWKGTLKE YESCHEGLCP FLLTECPACK GLVRLSEKEH
160 170 180 190 200
HTEQECPKRS LSCQHCRAPC SHVDLEVHYE VCPKFPLTCD GCGKKKIPRE
210 220 230 240 250
TFQDHVRACS KCRVLCRFHT VGCSEMVETE NLQDHELQRL REHLALLLSS
260 270 280 290 300
FLEAQASPGT LNQVGPELLQ RCQILEQKIA TFENIVCVLN REVERVAVTA
310 320 330 340 350
EACSRQHRLD QDKIEALSNK VQQLERSIGL KDLAMADLEQ KVSELEVSTY
360 370 380 390 400
DGVFIWKISD FTRKRQEAVA GRTPAIFSPA FYTSRYGYKM CLRVYLNGDG
410 420 430 440 450
TGRGTHLSLF FVVMKGPNDA LLQWPFNQKV TLMLLDHNNR EHVIDAFRPD
460 470 480 490 500
VTSSSFQRPV SDMNIASGCP LFCPVSKMEA KNSYVRDDAI FIKAIVDLTG

L
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 31 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 P39429.
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.
REACT_241657. Caspase-8 activation by cleavage.
REACT_243608. Dimerization of procaspase-8.
REACT_256171. TNF signaling.

Miscellaneous databases

NextBioi 301780.
PROi P39429.
SOURCEi Search...

Gene expression databases

Bgeei P39429.
CleanExi MM_TRAF2.
ExpressionAtlasi P39429. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 155 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