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Q12933 (TRAF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Tumor necrosis factor type 2 receptor-associated protein 3
Gene names
Name:TRAF2
Synonyms:TRAP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE. Ref.25 Ref.35 Ref.36 Ref.39 Ref.40 Ref.47 Ref.48 Ref.49 Ref.50 Ref.52 Ref.53 Ref.54 Ref.55 Ref.61 Ref.65 Ref.66

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. Ref.55

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, 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44 Ref.45 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.54 Ref.55 Ref.57 Ref.59 Ref.65 Ref.66

Subcellular location

Cytoplasm Ref.39 Ref.48.

Domain

The coiled coil domain mediates homo- and hetero-oligomerization. Ref.52 Ref.66

The MATH/TRAF domain binds to receptor cytoplasmic domains. Ref.52 Ref.66

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. Ref.52 Ref.66

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. Ref.48 Ref.49

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.

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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of NF-kappaB-inducing kinase activity

Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

cellular protein complex assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

innate immune response

Traceable author statement. Source: Reactome

negative regulation of glial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of JUN kinase activity

Inferred from direct assay Ref.35. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 11279055. Source: UniProtKB

positive regulation of T cell activation

Inferred by curator PubMed 15125833. Source: UniProtKB

positive regulation of T cell cytokine production

Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21525013. Source: UniProtKB

positive regulation of interleukin-2 production

Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB

positive regulation of protein homodimerization activity

Inferred from mutant phenotype Ref.32. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 12296995. Source: BHF-UCL

protein K63-linked ubiquitination

Inferred from direct assay PubMed 15258597Ref.55. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.55. Source: UniProtKB

protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein complex assembly

Traceable author statement PubMed 8702708. Source: ProtInc

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from physical interaction Ref.51. Source: UniProtKB

regulation of apoptotic process

Inferred from direct assay Ref.35. Source: UniProtKB

regulation of extrinsic apoptotic signaling pathway in absence of ligand

Traceable author statement. Source: Reactome

regulation of immunoglobulin secretion

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 8702708. Source: ProtInc

tumor necrosis factor-mediated signaling pathway

Inferred from direct assay Ref.35. Source: UniProtKB

   Cellular_componentCD40 receptor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

cell cortex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

membrane raft

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionCD40 receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 16636664. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 16189514PubMed 20562859Ref.8. Source: IntAct

protein phosphatase binding

Inferred from physical interaction Ref.43. Source: UniProtKB

signal transducer activity

Non-traceable author statement PubMed 8702708. Source: ProtInc

sphingolipid binding

Inferred from direct assay Ref.55. Source: UniProtKB

thioesterase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

tumor necrosis factor receptor binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 15258597Ref.55. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12933-1)

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: Q12933-2)

The sequence of this isoform differs from the canonical sequence as follows:
     122-122: E → EVKMPACGMVTEAPAVGSRPRSPSSYDLVLHVPLTGAEACLMSVEEETELLLR
Note: No experimental confirmation available.
Isoform 3 (identifier: Q12933-3)

The sequence of this isoform differs from the canonical sequence as follows:
     53-63: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q12933-4)

The sequence of this isoform differs from the canonical sequence as follows:
     176-200: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.46
Chain2 – 501500TNF receptor-associated factor 2
PRO_0000056399

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 By similarity
Coiled coil299 – 34850 Ref.66

Amino acid modifications

Modified residue21N-acetylalanine Ref.46 Ref.56 Ref.60
Modified residue71Phosphothreonine Ref.60
Modified residue111Phosphoserine Ref.49 Ref.60
Modified residue221Phosphothreonine Ref.60
Modified residue1171Phosphothreonine; by PKC Ref.48
Cross-link31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.48

Natural variations

Alternative sequence53 – 6311Missing in isoform 3.
VSP_039687
Alternative sequence1221E → EVKMPACGMVTEAPAVGSRP RSPSSYDLVLHVPLTGAEAC LMSVEEETELLLR in isoform 2.
VSP_007401
Alternative sequence176 – 20025Missing in isoform 4.
VSP_039688

Experimental info

Mutagenesis111S → A: Reduces global phosphorylation. Partial reduction of TNF-dependent activation of NF-kappa-B and activation of JNK. Ref.49
Mutagenesis111S → D: Slight increase of TNF-dependent activation of NF-kappa-B and activation of JNK. Ref.49
Mutagenesis311K → R: Abolishes 'Lys-63'-linked polyubiquitination.
Mutagenesis1171T → A: Loss of phosphorylation site. Abolishes activation of NF-kappa-B. Ref.48
Mutagenesis2851I → A: Strongly reduced interaction with BIRC3. Ref.66
Mutagenesis2881V → A: Strongly reduced interaction with BIRC3. Ref.66
Mutagenesis2921E → A: Strongly reduced interaction with BIRC3. Ref.66
Sequence conflict205 – 310106Missing in BAB70792. Ref.2
Sequence conflict343 – 36523LEMEA…FARKR → RPFQAQCGHRYCSFCLASIL RKL in AAA87706. Ref.1

Secondary structure

................................................................... 501
Helix Strand Turn

Details...

Sequences

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

Last modified September 19, 2002. Version 2.
Checksum: C508BE185B783B20

FASTA50155,859
        10         20         30         40         50         60 
MAAASVTPPG SLELLQPGFS KTLLGTKLEA KYLCSACRNV LRRPFQAQCG HRYCSFCLAS 

        70         80         90        100        110        120 
ILSSGPQNCA ACVHEGIYEE GISILESSSA FPDNAARREV ESLPAVCPSD GCTWKGTLKE 

       130        140        150        160        170        180 
YESCHEGRCP LMLTECPACK GLVRLGEKER HLEHECPERS LSCRHCRAPC CGADVKAHHE 

       190        200        210        220        230        240 
VCPKFPLTCD GCGKKKIPRE KFQDHVKTCG KCRVPCRFHA IGCLETVEGE KQQEHEVQWL 

       250        260        270        280        290        300 
REHLAMLLSS VLEAKPLLGD QSHAGSELLQ RCESLEKKTA TFENIVCVLN REVERVAMTA 

       310        320        330        340        350        360 
EACSRQHRLD QDKIEALSSK VQQLERSIGL KDLAMADLEQ KVLEMEASTY DGVFIWKISD 

       370        380        390        400        410        420 
FARKRQEAVA GRIPAIFSPA FYTSRYGYKM CLRIYLNGDG TGRGTHLSLF FVVMKGPNDA 

       430        440        450        460        470        480 
LLRWPFNQKV TLMLLDQNNR EHVIDAFRPD VTSSSFQRPV NDMNIASGCP LFCPVSKMEA 

       490        500 
KNSYVRDDAI FIKAIVDLTG L 

« Hide

Isoform 2 [UniParc].

Checksum: E5000CF242B2F404
Show »

FASTA55361,384
Isoform 3 [UniParc].

Checksum: 9CAF6DDAB0DE64DD
Show »

FASTA49054,671
Isoform 4 [UniParc].

Checksum: BB290C92E8D33D79
Show »

FASTA47653,055

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Binding of CDK9 to TRAF2."
MacLachlan T.K., Sang N., De Luca A., Puri P.L., Levrero M., Giordano A.
J. Cell. Biochem. 71:467-478(1998) [PubMed] [Europe PMC] [Abstract]
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]"ASK1 is essential for JNK/SAPK activation by TRAF2."
Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M., Miyazono K., Ichijo H.
Mol. Cell 2:389-395(1998) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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, 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]"Asymmetric recruitment of cIAPs by TRAF2."
Mace P.D., Smits C., Vaux D.L., Silke J., Day C.L.
J. Mol. Biol. 400:8-15(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS56163.
RefSeqNP_066961.2. NM_021138.3.
UniGeneHs.522506.

3D structure databases

PDBe
RCSB PDB
PDBj
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/F266-330[»]
3M0AX-ray2.61A/B/C266-330[»]
3M0DX-ray2.80A/B266-330[»]
ProteinModelPortalQ12933.
SMRQ12933. Positions 15-241, 267-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113038. 219 interactions.
DIPDIP-6223N.
IntActQ12933. 137 interactions.
MINTMINT-107429.
STRING9606.ENSP00000247668.

PTM databases

PhosphoSiteQ12933.

Polymorphism databases

DMDM23503103.

Proteomic databases

PaxDbQ12933.
PRIDEQ12933.

Protocols and materials databases

DNASU7186.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247668; ENSP00000247668; ENSG00000127191. [Q12933-1]
ENST00000359662; ENSP00000352685; ENSG00000127191. [Q12933-2]
ENST00000536468; ENSP00000446414; ENSG00000127191. [Q12933-1]
GeneID7186.
KEGGhsa:7186.
UCSCuc004cjv.3. human. [Q12933-1]
uc010nbw.3. human. [Q12933-4]
uc011mek.2. human. [Q12933-3]

Organism-specific databases

CTD7186.
GeneCardsGC09P139776.
H-InvDBHIX0169360.
HGNCHGNC:12032. TRAF2.
HPACAB004603.
HPA009972.
HPA010634.
MIM601895. gene.
neXtProtNX_Q12933.
PharmGKBPA164742666.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264247.
HOGENOMHOG000231558.
HOVERGENHBG058222.
InParanoidQ12933.
KOK03173.
OMASDGCTWK.
OrthoDBEOG7966G5.
PhylomeDBQ12933.
TreeFamTF321154.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
REACT_6900. Immune System.
SignaLinkQ12933.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ12933.
BgeeQ12933.
CleanExHS_TRAF2.
GenevestigatorQ12933.

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. 1 hit.
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

EvolutionaryTraceQ12933.
GeneWikiTRAF2.
GenomeRNAi7186.
NextBio28172.
PROQ12933.
SOURCESearch...

Entry information

Entry nameTRAF2_HUMAN
AccessionPrimary (citable) accession number: Q12933
Secondary accession number(s): A8K107 expand/collapse secondary AC list , B4DPJ7, Q7Z337, Q96NT2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 19, 2002
Last modified: April 16, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM