Q12933 (TRAF2_HUMAN) 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
Tumor necrosis factor type 2 receptor-associated protein 3

Gene names

Name:	TRAF2
Synonyms:	TRAP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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. Ref.25 Ref.35 Ref.36 Ref.39 Ref.43 Ref.44 Ref.45 Ref.46 Ref.48 Ref.49 Ref.50 Ref.51 Ref.59 Ref.60
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.51
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 By similarity. 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 degradation of NFKBIA and activation of NF-kappa-B. Interacts with CYLD, USP48, DAB2IP, 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. 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.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.50 Ref.51 Ref.53 Ref.59 Ref.60
Subcellular location	Cytoplasm Ref.39 Ref.44.
Domain	The coiled coil domain mediates homo- and hetero-oligomerization. Ref.48 Ref.60 The MATH/TRAF domain binds to receptor cytoplasmic domains. Ref.48 Ref.60 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.48 Ref.60
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.44 Ref.45 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 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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation 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 cellular protein complex assembly Inferred from sequence or structural similarity. Source: BHF-UCL innate immune response Traceable author statement. Source: Reactome 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 protein K63-linked ubiquitination Inferred from direct assay PubMed 15258597Ref.51. Source: UniProtKB protein autoubiquitination Inferred from direct assay Ref.51. Source: UniProtKB protein catabolic process Inferred from electronic annotation. Source: Compara protein homotrimerization Inferred from physical interaction Ref.47. Source: UniProtKB regulation of immunoglobulin secretion Inferred from electronic annotation. Source: Compara tumor necrosis factor-mediated signaling pathway Inferred from direct assay Ref.35. Source: UniProtKB
Cellular_component	CD40 receptor complex Inferred from sequence or structural similarity. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome internal side of plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	CD40 receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL signal transducer activity Non-traceable author statement PubMed 8702708. Source: ProtInc sphingolipid binding Inferred from direct assay Ref.51. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay PubMed 15258597Ref.51. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-355744,EBI-355744
ATXN1	P54253	2	EBI-355744,EBI-930964
BIRC2	Q13490	8	EBI-355744,EBI-514538
BIRC3	Q13489	5	EBI-355744,EBI-517709
Casp12	O08736	6	EBI-355744,EBI-6140033	From a different organism.
ERN1	O75460	2	EBI-355744,EBI-371750
GSTP1	P09211	4	EBI-355744,EBI-353467
Hoxa1	P09022	3	EBI-355744,EBI-3957603	From a different organism.
Ngfr	P07174	3	EBI-355744,EBI-1038810	From a different organism.
TANK	Q92844	3	EBI-355744,EBI-356349
TAOK3	Q9H2K8	2	EBI-355744,EBI-1384100
TNFRSF12A	Q9NP84	3	EBI-355744,EBI-2851995
TNFRSF14	Q92956	4	EBI-355760,EBI-1056653
Traf5	P70191	2	EBI-355744,EBI-523899	From a different organism.
ZFAND6	Q6FIF0	6	EBI-355744,EBI-724630

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.52

Chain

2 – 501

500

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

Region

283 – 293

11

Important for interaction with BIRC2 and BIRC3 By similarity

Coiled coil

299 – 348

50

Ref.60

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.52 Ref.55

Modified residue

7

1

Phosphothreonine Ref.55

Modified residue

11

1

Phosphoserine Ref.45 Ref.55

Modified residue

22

1

Phosphothreonine Ref.55

Modified residue

117

1

Phosphothreonine; by PKC Ref.44

Cross-link

31

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.44

Natural variations

Alternative sequence

53 – 63

11

Missing in isoform 3.

VSP_039687

Alternative sequence

122

1

E → EVKMPACGMVTEAPAVGSRP RSPSSYDLVLHVPLTGAEAC LMSVEEETELLLR in isoform 2.

VSP_007401

Alternative sequence

176 – 200

25

Missing in isoform 4.

VSP_039688

Experimental info

Mutagenesis

11

1

S → A: Reduces global phosphorylation. Partial reduction of TNF-dependent activation of NF-kappa-B and activation of JNK. Ref.45

Mutagenesis

11

1

S → D: Slight increase of TNF-dependent activation of NF-kappa-B and activation of JNK. Ref.45

Mutagenesis

31

1

K → R: Abolishes 'Lys-63'-linked polyubiquitination.

Mutagenesis

117

1

T → A: Loss of phosphorylation site. Abolishes activation of NF-kappa-B. Ref.44

Mutagenesis

285

1

I → A: Strongly reduced interaction with BIRC3. Ref.60

Mutagenesis

288

1

V → A: Strongly reduced interaction with BIRC3. Ref.60

Mutagenesis

292

1

E → A: Strongly reduced interaction with BIRC3. Ref.60

Sequence conflict

205 – 310

106

Missing in BAB70792. Ref.2

Sequence conflict

343 – 365

23

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

Secondary structure

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501

Helix Strand Turn

Details...

Helix

21 – 23

3

Helix

25 – 27

3

Helix

30 – 32

3

Turn

35 – 37

3

Beta strand

42 – 46

5

Beta strand

52 – 54

3

Helix

55 – 61

7

Helix

62 – 64

3

Helix

70 – 74

5

Turn

80 – 83

4

Helix

87 – 89

3

Helix

94 – 101

8

Beta strand

103 – 106

4

Beta strand

115 – 117

3

Helix

118 – 124

7

Turn

125 – 127

3

Helix

130 – 133

4

Helix

315 – 318

4

Helix

335 – 347

13

Beta strand

350 – 358

9

Helix

361 – 369

9

Beta strand

375 – 377

3

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

Helix

476 – 480

5

Turn

482 – 484

3

Beta strand

490 – 496

7

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 [UniParc]. 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
	Isoform 3 [UniParc]. Checksum: 9CAF6DDAB0DE64DD	FASTA	490	54,671
	10 20 30 40 50 60 MAAASVTPPG SLELLQPGFS KTLLGTKLEA KYLCSACRNV LRRPFQAQCG HRSGPQNCAA 70 80 90 100 110 120 CVHEGIYEEG ISILESSSAF PDNAARREVE SLPAVCPSDG CTWKGTLKEY ESCHEGRCPL 130 140 150 160 170 180 MLTECPACKG LVRLGEKERH LEHECPERSL SCRHCRAPCC GADVKAHHEV CPKFPLTCDG 190 200 210 220 230 240 CGKKKIPREK FQDHVKTCGK CRVPCRFHAI GCLETVEGEK QQEHEVQWLR EHLAMLLSSV 250 260 270 280 290 300 LEAKPLLGDQ SHAGSELLQR CESLEKKTAT FENIVCVLNR EVERVAMTAE ACSRQHRLDQ 310 320 330 340 350 360 DKIEALSSKV QQLERSIGLK DLAMADLEQK VLEMEASTYD GVFIWKISDF ARKRQEAVAG 370 380 390 400 410 420 RIPAIFSPAF YTSRYGYKMC LRIYLNGDGT GRGTHLSLFF VVMKGPNDAL LRWPFNQKVT 430 440 450 460 470 480 LMLLDQNNRE HVIDAFRPDV TSSSFQRPVN DMNIASGCPL FCPVSKMEAK NSYVRDDAIF 490 IKAIVDLTGL
	Isoform 4 [UniParc]. Checksum: BB290C92E8D33D79	FASTA	476	53,055
	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 CGADVKFQDH 190 200 210 220 230 240 VKTCGKCRVP CRFHAIGCLE TVEGEKQQEH EVQWLREHLA MLLSSVLEAK PLLGDQSHAG 250 260 270 280 290 300 SELLQRCESL EKKTATFENI VCVLNREVER VAMTAEACSR QHRLDQDKIE ALSSKVQQLE 310 320 330 340 350 360 RSIGLKDLAM ADLEQKVLEM EASTYDGVFI WKISDFARKR QEAVAGRIPA IFSPAFYTSR 370 380 390 400 410 420 YGYKMCLRIY LNGDGTGRGT HLSLFFVVMK GPNDALLRWP FNQKVTLMLL DQNNREHVID 430 440 450 460 470 AFRPDVTSSS FQRPVNDMNI ASGCPLFCPV SKMEAKNSYV RDDAIFIKAI VDLTGL

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] [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. , 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. , 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. , 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. , 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]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[53]	"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.
[54]	"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].
[55]	"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, MASS SPECTROMETRY.
[56]	"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.
[57]	"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.
[58]	"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.
[59]	"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.
[60]	"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

SeattleSNPs

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.

IPI

IPI00030278.
IPI00292635.
IPI00970911.
IPI00970988.

PIR

S56163.

RefSeq

NP_066961.2. NM_021138.3.

UniGene

Hs.522506.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3KNV	X-ray	1.90	A	1-133	[»]
3M06	X-ray	2.67	A/B/C/D/E/F	266-330	[»]
3M0A	X-ray	2.61	A/B/C	266-330	[»]
3M0D	X-ray	2.80	A/B	266-330	[»]

ProteinModelPortal

Q12933.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6223N.

IntAct

Q12933. 122 interactions.

MINT

MINT-107429.

STRING

9606.ENSP00000247668.

PTM databases

PhosphoSite

Q12933.

Polymorphism databases

DMDM

23503103.

Proteomic databases

PaxDb

Q12933.

PRIDE

Q12933.

Protocols and materials databases

DNASU

7186.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000247668; ENSP00000247668; ENSG00000127191.
ENST00000359662; ENSP00000352685; ENSG00000127191.
ENST00000536468; ENSP00000446414; ENSG00000127191.

GeneID

7186.

KEGG

hsa:7186.

UCSC

uc004cjv.3. human.
uc010nbw.3. human.
uc011mek.2. human.

Organism-specific databases

CTD

7186.

GeneCards

GC09P139776.

H-InvDB

HIX0169360.

HGNC

HGNC:12032. TRAF2.

HPA

CAB004603.
HPA009972.
HPA010634.

MIM

601895. gene.

neXtProt

NX_Q12933.

PharmGKB

PA164742666.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG264247.

HOGENOM

HOG000231558.

HOVERGEN

HBG058222.

InParanoid

Q12933.

KO

K03173.

OMA

PSDGCTW.

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.
REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q12933.

Bgee

Q12933.

CleanEx

HS_TRAF2.

Genevestigator

Q12933.

GermOnline

ENSG00000127191. Homo sapiens.

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. 1 hit.

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

EvolutionaryTrace

Q12933.

GenomeRNAi

7186.

NextBio

28172.

SOURCE

Search...

Entry information

Entry name

TRAF2_HUMAN

Accession

Primary (citable) accession number: Q12933
Secondary accession number(s): A8K107 , B4DPJ7, Q7Z337, Q96NT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	September 19, 2002
Last modified:	May 1, 2013
This is version 163 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.