Reviewed, UniProtKB/Swiss-Prot Q12933 (TRAF2_HUMAN)

Names and origin

Protein names

Recommended name:
    TNF receptor-associated factor 2
Alternative name(s):
    Tumor necrosis factor type 2 receptor-associated protein 3

Gene names

Name:	TRAF2
Synonyms:	TRAP3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Association to the receptor is also mediated by the interaction with TRADD. Mediates activation of NF-kappa-B and JNK and is involved in apoptosis. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. Seems to be involved in IL-15 signaling.
Subunit structure	Homotrimer Probable. Heteromer with TRAF1. Binds to TNFRSF1B/TNFR2, TNFRSF4 and TNFRSF5/CD40. Associates with CD27, 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, IL15RA, TANK/ITRAF, RIPK2, TNIK, MAP3K14, MAP3K5, MAP3K1, MAP4K2, CDK9, CSK, and TRAF-interacting protein TRAIP and TRAF and TNF receptor associated protein TTRAP. Interacts with TNFAIP3 and TRPC4AP. Interacts with PEG3 By similarity. Binds to TRADD. Interacts with BIRC2 and BIRC3 N-terminus. Interacts with CYLD and TBK1. Interacts with MAVS/IPS1. Interacts with CASP8AP2 and USP48. Interacts with DAB2IP. Interacts wtih NFATC2IP and with HIVEP3 By similarity.
Subcellular location	Cytoplasm.
Domain	The coiled coil domain mediates homo- and hetero-oligomerization. The MATH/TRAF domain binds to receptor cytoplasmic domains.
Post-translational modification	Ubiquitinated; mediated by SIAH2 and leading to its subsequent proteasomal degradation. Not ubiquitinated by SIAH1. Ref.32
Sequence similarities	Contains 1 MATH domain. Contains 1 RING-type zinc finger. Contains 2 TRAF-type zinc fingers.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	activation of NF-kappaB-inducing kinase activity Inferred from mutant phenotype. Source: UniProtKB activation of pro-apoptotic gene products Inferred from Experiment. Source: Reactome positive regulation of T cell activation Inferred by curator. Source: UniProtKB positive regulation of T cell cytokine production Inferred from mutant phenotype. Source: UniProtKB positive regulation of interleukin-2 production Inferred from mutant phenotype. Source: UniProtKB protein complex assembly Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	protein binding Ref.5 Ref.11 Ref.16 Ref.17 Ref.27 Ref.40 Inferred from physical interaction. Source: UniProtKB signal transducer activity Non-traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	1	EBI-355744,EBI-930964
BIRC2	Q13490	3	EBI-355744,EBI-514538
BIRC3	Q13489	2	EBI-355744,EBI-517709
CD27	P26842	2	EBI-355744,EBI-520729
GSTP1	P09211	3	EBI-355744,EBI-353467
MAP3K1	Q13233	1	EBI-355744,EBI-49776
MAP3K5	Q99683	1	EBI-355744,EBI-476263
TNFRSF11A	Q9Y6Q6	1	EBI-355744,EBI-525675
TNFRSF14	Q92956	4	EBI-355760,EBI-1056653
TNFRSF19	Q9NS68	1	EBI-355744,EBI-530381
TNFRSF1B	P20333	2	EBI-355744,EBI-358983
Tnfrsf4	P47741	1	EBI-355744,EBI-520001	From a different organism.
Tnfrsf9	P20334	1	EBI-355744,EBI-520693	From a different organism.
TRADD	Q15628	1	EBI-355744,EBI-359215

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 501

501

TNF receptor-associated factor 2

PRO_0000056399

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

Coiled coil

299 – 348

50

Potential

Natural variations

Alternative sequence

122

1

E → EVKMPACGMVTEAPAVGSRP RSPSSYDLVLHVPLTGAEAC LMSVEEETELLLR in isoform 2.

VSP_007401

Experimental info

Sequence conflict

205 – 310

106

Missing Ref.2

Sequence conflict

343 – 365

23

LEMEA…FARKR → RPFQAQCGHRYCSFCLASIL RKL in AAA87706. Ref.1

Secondary structure

1

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501

Helix Strand Turn

Details...

Helix

315 – 318

4

Helix

335 – 347

13

Beta strand

350 – 360

11

Helix

361 – 369

9

Beta strand

381 – 384

4

Beta strand

389 – 395

7

Helix

400 – 402

3

Turn

403 – 405

3

Beta strand

406 – 414

9

Helix

419 – 421

3

Beta strand

430 – 434

5

Beta strand

443 – 447

5

Helix

454 – 456

3

Beta strand

460 – 463

4

Beta strand

467 – 474

8

Turn

475 – 480

6

Turn

482 – 484

3

Beta strand

489 – 496

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 19, 2002. Version 2. Checksum: C508BE185B783B20	FASTA	501	55,859
	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
	Isoform 2. Checksum: E5000CF242B2F404	FASTA	553	61,384
	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 YEVKMPACGM VTEAPAVGSR PRSPSSYDLV LHVPLTGAEA CLMSVEEETE LLLRSCHEGR 190 200 210 220 230 240 CPLMLTECPA CKGLVRLGEK ERHLEHECPE RSLSCRHCRA PCCGADVKAH HEVCPKFPLT 250 260 270 280 290 300 CDGCGKKKIP REKFQDHVKT CGKCRVPCRF HAIGCLETVE GEKQQEHEVQ WLREHLAMLL 310 320 330 340 350 360 SSVLEAKPLL GDQSHAGSEL LQRCESLEKK TATFENIVCV LNREVERVAM TAEACSRQHR 370 380 390 400 410 420 LDQDKIEALS SKVQQLERSI GLKDLAMADL EQKVLEMEAS TYDGVFIWKI SDFARKRQEA 430 440 450 460 470 480 VAGRIPAIFS PAFYTSRYGY KMCLRIYLNG DGTGRGTHLS LFFVVMKGPN DALLRWPFNQ 490 500 510 520 530 540 KVTLMLLDQN NREHVIDAFR PDVTSSSFQR PVNDMNIASG CPLFCPVSKM EAKNSYVRDD 550 AIFIKAIVDL TGL

References

	« Hide 'large scale' referencesShow '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: 7639698] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[3]	SeattleSNPs variation discovery resource Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon, Fetal brain, Kidney, Leukocyte, Stomach and Uterus.
[5]	"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: 8069916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 201-501, INTERACTION WITH TRAF1 AND TNFRSF1B.
[6]	"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: 10581243] [Abstract] Cited for: INTERACTION WITH TBK1. Tissue: Spleen.
[7]	"The TNF-receptor-associated factor family: scaffold molecules for cytokine receptors, kinases and their regulators." Wajant H., Henkler F., Scheurich P. Cell. Signal. 13:389-400(2001) [PubMed: 11384837] [Abstract] Cited for: REVIEW.
[8]	"Tumor necrosis factor receptor-associated factors (TRAFs)." Bradley J.R., Pober J.S. Oncogene 20:6482-6491(2001) [PubMed: 11607847] [Abstract] Cited for: REVIEW.
[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: 8627180] [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: 8710854] [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: 9153189] [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: 9104814] [Abstract] Cited for: INTERACTION WITH TRIP.
[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: 9020361] [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: 9718306] [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: 9705938] [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: 9692890] [Abstract] Cited for: INTERACTION WITH CD27.
[17]	"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: 9418902] [Abstract] Cited for: INTERACTION WITH TNFRSF4 AND TNFRSF9.
[18]	"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: 9488716] [Abstract] Cited for: INTERACTION WITH TNFRSF4.
[19]	"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: 9774460] [Abstract] Cited for: INTERACTION WITH TNFRSF11A.
[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: 9607925] [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: 9774977] [Abstract] Cited for: INTERACTION WITH MAP3K5.
[22]	"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: 10463949] [Abstract] Cited for: INTERACTION WITH IL15RA.
[23]	"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: 10037686] [Abstract] Cited for: INTERACTION WITH TNFRSF18. Tissue: T-cell.
[24]	"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: 10514511] [Abstract] Cited for: INTERACTION WITH TNFRSF16.
[25]	"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: 10521462] [Abstract] Cited for: INTERACTION WITH TNIK.
[26]	"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: 9827693] [Abstract] Cited for: INTERACTION WITH CDK9.
[27]	"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: 10809768] [Abstract] Cited for: INTERACTION WITH TNFRSF19.
[28]	"TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation." Xia X.-Z., Treanor J., Senaldi G., Khare S.D., Boone T., Kelley M., Theill L.E., Colombero A., Solovyev I., Lee F., McCabe S., Elliott R., Miner K., Hawkins N., Guo J., Stolina M., Yu G., Wang J. , Delaney J., Meng S.-Y., Boyle W.J., Hsu H. J. Exp. Med. 192:137-143(2000) [PubMed: 10880535] [Abstract] Cited for: INTERACTION WITH TNFRSF13B.
[29]	"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: 11784851] [Abstract] Cited for: INTERACTION WITH MAP4K2.
[30]	"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: 10346818] [Abstract] Cited for: INTERACTION WITH MAP3K1.
[31]	"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: 10764746] [Abstract] Cited for: INTERACTION WITH TTRAP.
[32]	"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: 12411493] [Abstract] Cited for: INTERACTION WITH SIAH2, DEGRADATION.
[33]	"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: 12917691] [Abstract] Cited for: INTERACTION WITH CYLD.
[34]	"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: 15310755] [Abstract] Cited for: INTERACTION WITH DAB2IP.
[35]	"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: 16153868] [Abstract] Cited for: INTERACTION WITH MAVS.
[36]	"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: 16214042] [Abstract] Cited for: INTERACTION WITH USP48.
[37]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[38]	"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: 10206649] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 310-501 IN COMPLEX WITH TNFRSF1B.
[39]	"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: 10411888] [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.
[40]	"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: 10892748] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 331-501 IN COMPLEX WITH TRADD.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

U12597 mRNA. Translation: AAA87706.1.
AK054686 mRNA. Translation: BAB70792.1.
AY623660 Genomic DNA. Translation: AAT27320.1.
BC032410 mRNA. Translation: AAH32410.1.
BC033810 mRNA. Translation: AAH33810.1.
BC043492 mRNA. Translation: AAH43492.1.
BC064662 mRNA. Translation: AAH64662.1.

IPI

IPI00030278.
IPI00292635.

PIR

S56163.

RefSeq

NP_066961.2.

UniGene

Hs.522506

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CA4	X-ray	2.20	A/B/C/D/E/F	334-501	[»]
1CA9	X-ray	2.30	A/B/C/D/E/F	310-501	[»]
1CZY	X-ray	2.00	A/B/C	334-501	[»]
1CZZ	X-ray	2.70	A/B/C	315-501	[»]
1D00	X-ray	2.00	A/B/C/D/E/F/G/H	334-501	[»]
1D01	X-ray	2.00	A/B/C/D/E/F	334-501	[»]
1D0A	X-ray	2.00	A/B/C/D/E/F	334-501	[»]
1D0J	X-ray	2.50	A/B/C/D/E/F	334-501	[»]
1F3V	X-ray	2.00	B	331-501	[»]
1QSC	X-ray	2.40	A/B/C	311-501	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6223N.

IntAct

Q12933. 125 interactions.

PTM databases

PhosphoSite

Q12933.

Proteomic databases

PRIDE

Q12933.

Genome annotation databases

Ensembl

ENSG00000127191. Homo sapiens. [Contig view]

GeneID

7186.

KEGG

hsa:7186.

UCSC

uc004cjv.1. human.

Organism-specific databases

GeneCards

GC09P138900.

H-InvDB

HIX0008562.

HGNC

HGNC:12032. TRAF2.

HPA

CAB004603.
HPA009972.
HPA010634.

MIM

601895. gene.

PharmGKB

PA36709.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q12933.

OMA

Q12933. METRVAT.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
ceramidepathway. Ceramide signaling pathway.
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
tnfpathway. TNF receptor signaling pathway.
trail_pathway. TRAIL signaling pathway.

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q12933.

Bgee

Q12933.

CleanEx

HS_TRAF2.

GermOnline

ENSG00000127191. Homo sapiens.

Family and domain databases

InterPro

IPR002083. MATH.
IPR012227. TNF_recpt_TRAF.
IPR013322. TRAF-type.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]

Gene3D

G3DSA:2.60.210.10. TRAF-type. 1 hit.

Pfam

PF00917. MATH. 1 hit.
PF00097. zf-C3HC4. 1 hit.
PF02176. zf-TRAF. 1 hit.
[Graphical view]

PIRSF

PIRSF015614. TRAF. 1 hit.

SMART

SM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

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 Resources

NextBio

28172.

SOURCE

Search...

Entry information

Entry name

TRAF2_HUMAN

Accession

Primary (citable) accession number: Q12933
Secondary accession number(s): Q96NT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	September 19, 2002
Last modified:	July 7, 2009
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)