P39429 (TRAF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TNF receptor-associated factor 2
EC=6.3.2.-

Alternative name(s):
E3 ubiquitin-protein ligase TRAF2

Gene names

Name:

Traf2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.9 Ref.12 Ref.17 Ref.20 Ref.21 Ref.23 Ref.24
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, 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 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 degradation of NFKBIA and activation of NF-kappa-B. Interacts with CYLD, USP48, DAB2IP, IKKA and IKKB. Interacts (via 'Lys-63'-linked polyubiquitin chains) with TAB2 and TAB3 By similarity. Interaction with TAOK3 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation By similarity. Interacts with CASP12 under resting conditions; this interaction is reduced in ER stress conditions By similarity. Ref.1 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23
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.23 The MATH/TRAF domain binds to receptor cytoplasmic domains. Ref.23 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.23
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.20 Ref.24
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 process	Apoptosis Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Zinc-finger
Ligand	Lipid-binding Metal-binding Zinc
Molecular function	Ligase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of NF-kappaB-inducing kinase activity Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular protein complex assembly Inferred from direct assay PubMed 20614026. Source: BHF-UCL negative regulation of apoptotic process Non-traceable author statement PubMed 9692890. Source: UniProtKB positive regulation of JUN kinase activity Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of T cell cytokine production Inferred from electronic annotation. Source: Compara positive regulation of extrinsic apoptotic signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of interleukin-2 production Inferred from electronic annotation. Source: Compara positive regulation of protein homodimerization activity Inferred from electronic annotation. Source: Compara positive regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara 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 homotrimerization Inferred from electronic annotation. Source: Compara regulation of immunoglobulin secretion Inferred from mutant phenotype PubMed 12958312. Source: MGI tumor necrosis factor-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	CD40 receptor complex Inferred from direct assay PubMed 20614026. Source: BHF-UCL cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell internal side of plasma membrane Inferred from direct assay PubMed 20614026. Source: BHF-UCL
Molecular_function	sphingolipid binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Birc3	O08863	7	EBI-520016,EBI-642236
Fcrla	Q920A9	5	EBI-520016,EBI-646587
Mknk2	Q8CDB0	3	EBI-520016,EBI-646209
Tank	P70347-1	7	EBI-520016,EBI-646125
Tnfaip3	Q60769	3	EBI-520016,EBI-646595
Tnfrsf4	P47741	3	EBI-520016,EBI-520001
Traf3	Q60803	2	EBI-520016,EBI-520135

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 501	500	TNF receptor-associated factor 2		PRO_0000056400
Regions
	Domain	351 – 496	146	MATH
	Zinc finger	34 – 73	40	RING-type
	Zinc finger	124 – 180	57	TRAF-type 1
	Zinc finger	177 – 233	57	TRAF-type 2
	Region	283 – 293	11	Important for interaction with BIRC2 and BIRC3
	Coiled coil	298 – 348	51	By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	7	1	Phosphothreonine By similarity
	Modified residue	11	1	Phosphoserine By similarity
	Modified residue	22	1	Phosphothreonine By similarity
	Modified residue	117	1	Phosphothreonine; by PKC By similarity
	Cross-link	31		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Natural variations
	Alternative sequence	62	1	L → LRCASILS in isoform 2.		VSP_007402
Experimental info
	Mutagenesis	34	1	C → S: Loss of autoubiquitination. Ref.15
	Mutagenesis	283	1	E → A: Reduces interaction with BIRC2. Ref.23
	Mutagenesis	292	1	E → A: Almost abolishes interaction with BIRC2; when associated with A-294. Ref.23
	Mutagenesis	294	1	E → A: Almost abolishes interaction with BIRC2; when associated with A-292. Ref.23

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 043B391180365F10	FASTA	501	56,026
	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
	Isoform 2 (TRAF2A) [UniParc]. Checksum: 74B8B26BFCF9B1C4	FASTA	508	56,757
	10 20 30 40 50 60 MAAASVTSPG SLELLQPGFS KTLLGTRLEA KYLCSACKNI LRRPFQAQCG HRYCSFCLTS 70 80 90 100 110 120 ILRCASILSS SGPQNCAACV YEGLYEEGIS ILESSSAFPD NAARREVESL PAVCPNDGCT 130 140 150 160 170 180 WKGTLKEYES CHEGLCPFLL TECPACKGLV RLSEKEHHTE QECPKRSLSC QHCRAPCSHV 190 200 210 220 230 240 DLEVHYEVCP KFPLTCDGCG KKKIPRETFQ DHVRACSKCR VLCRFHTVGC SEMVETENLQ 250 260 270 280 290 300 DHELQRLREH LALLLSSFLE AQASPGTLNQ VGPELLQRCQ ILEQKIATFE NIVCVLNREV 310 320 330 340 350 360 ERVAVTAEAC SRQHRLDQDK IEALSNKVQQ LERSIGLKDL AMADLEQKVS ELEVSTYDGV 370 380 390 400 410 420 FIWKISDFTR KRQEAVAGRT PAIFSPAFYT SRYGYKMCLR VYLNGDGTGR GTHLSLFFVV 430 440 450 460 470 480 MKGPNDALLQ WPFNQKVTLM LLDHNNREHV IDAFRPDVTS SSFQRPVSDM NIASGCPLFC 490 500 PVSKMEAKNS YVRDDAIFIK AIVDLTGL

References

	« Hide 'large scale' referencesShow '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. , 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, 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]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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 , AF233326, AF233327, AF233328, AF233329, AF233330, AF233331 Genomic DNA. Translation: AAF59928.1. AL732590 Genomic DNA. Translation: CAM25164.1. BC003801 mRNA. Translation: AAH03801.1.
IPI	IPI00135901. IPI00271450.
PIR	I61512.
RefSeq	NP_033448.2. NM_009422.2.
UniGene	Mm.3399.
3D structure databases
ProteinModelPortal	P39429.
SMR	P39429. Positions 15-183, 267-501.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-468N.
IntAct	P39429. 42 interactions.
MINT	MINT-197749.
PTM databases
PhosphoSite	P39429.
Proteomic databases
PaxDb	P39429.
PRIDE	P39429.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028311; ENSMUSP00000028311; ENSMUSG00000026942. ENSMUST00000114234; ENSMUSP00000109872; ENSMUSG00000026942.
GeneID	22030.
KEGG	mmu:22030.
UCSC	uc008isl.1. mouse.
Organism-specific databases
CTD	7186.
MGI	MGI:101835. Traf2.
Phylogenomic databases
eggNOG	NOG264247.
GeneTree	ENSGT00550000074359.
HOGENOM	HOG000231558.
HOVERGEN	HBG058222.
InParanoid	A2AJA3.
KO	K03173.
OMA	PSDGCTW.
OrthoDB	EOG4R502J.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	P39429.
Bgee	P39429.
CleanEx	MM_TRAF2.
Genevestigator	P39429.
GermOnline	ENSMUSG00000026942. Mus musculus.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	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]
PANTHER	PTHR10131:SF21. PTHR10131:SF21. 1 hit.
Pfam	PF00917. MATH. 1 hit. PF00097. zf-C3HC4. 1 hit. [Graphical view]
PIRSF	PIRSF015614. TRAF. 1 hit.
SMART	SM00061. MATH. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF49599. Traf_like. 2 hits.
PROSITE	PS50144. MATH. 1 hit. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. PS50145. ZF_TRAF. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	301780.
SOURCE	Search...

Entry information

Entry name

TRAF2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program