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Protein

TNF receptor-associated factor 2

Gene

TRAF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.16 Publications

Enzyme regulationi

Has very low E3 ubiquitin ligase activity in the absence of sphingosine-1-phosphate. E3 ubiquitin ligase activity is strongly activated by cytoplasmic sphingosine-1-phosphate.1 Publication

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri34 – 7340RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri124 – 18057TRAF-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri177 – 23357TRAF-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • CD40 receptor binding Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • ligase activity Source: UniProtKB-KW
  • protein kinase binding Source: ParkinsonsUK-UCL
  • protein phosphatase binding Source: UniProtKB
  • signal transducer activity Source: ProtInc
  • sphingolipid binding Source: UniProtKB
  • thioesterase binding Source: UniProtKB
  • tumor necrosis factor receptor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  • activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: Reactome
  • activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  • apoptotic process Source: Reactome
  • cell surface receptor signaling pathway Source: Reactome
  • cellular protein complex assembly Source: BHF-UCL
  • cellular response to nitric oxide Source: Ensembl
  • death-inducing signaling complex assembly Source: Reactome
  • extrinsic apoptotic signaling pathway Source: Reactome
  • innate immune response Source: Reactome
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • necroptotic process Source: Reactome
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  • negative regulation of glial cell apoptotic process Source: Ensembl
  • negative regulation of neuron death Source: ParkinsonsUK-UCL
  • positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of interleukin-2 production Source: UniProtKB
  • positive regulation of JUN kinase activity Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of protein homodimerization activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of T cell activation Source: UniProtKB
  • positive regulation of T cell cytokine production Source: UniProtKB
  • programmed cell death Source: Reactome
  • programmed necrotic cell death Source: Reactome
  • protein autoubiquitination Source: UniProtKB
  • protein catabolic process Source: Ensembl
  • protein complex assembly Source: ProtInc
  • protein heterooligomerization Source: Ensembl
  • protein homotrimerization Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Reactome
  • regulation of immunoglobulin secretion Source: Ensembl
  • regulation of necrotic cell death Source: Reactome
  • response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • signal transduction Source: ProtInc
  • tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1432. TNF signaling.
REACT_1503. Ligand-dependent caspase activation.
REACT_164011. Regulation by c-FLIP.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_355072. TNFR1-mediated proapoptotic signaling.
REACT_355311. CASP8 activity is inhibited.
REACT_355409. RIPK1-mediated regulated necrosis.
REACT_832. Dimerization of procaspase-8.
SignaLinkiQ12933.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TRAF2
Synonyms:TRAP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12032. TRAF2.

Subcellular locationi

GO - Cellular componenti

  • CD40 receptor complex Source: BHF-UCL
  • cell cortex Source: Ensembl
  • cytoplasm Source: HPA
  • cytoplasmic side of plasma membrane Source: BHF-UCL
  • cytosol Source: Reactome
  • IRE1-TRAF2-ASK1 complex Source: ParkinsonsUK-UCL
  • membrane raft Source: Ensembl
  • TRAF2-GSTP1 complex Source: UniProtKB
  • ubiquitin ligase complex Source: ParkinsonsUK-UCL
  • vesicle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111S → A: Reduces global phosphorylation. Partial reduction of TNF-dependent activation of NF-kappa-B and activation of JNK. 1 Publication
Mutagenesisi11 – 111S → D: Slight increase of TNF-dependent activation of NF-kappa-B and activation of JNK. 1 Publication
Mutagenesisi31 – 311K → R: Abolishes 'Lys-63'-linked polyubiquitination.
Mutagenesisi117 – 1171T → A: Loss of phosphorylation site. Abolishes activation of NF-kappa-B. 1 Publication
Mutagenesisi285 – 2851I → A: Strongly reduced interaction with BIRC3. 1 Publication
Mutagenesisi288 – 2881V → A: Strongly reduced interaction with BIRC3. 1 Publication
Mutagenesisi292 – 2921E → A: Strongly reduced interaction with BIRC3. 1 Publication

Organism-specific databases

PharmGKBiPA164742666.

Polymorphism and mutation databases

BioMutaiTRAF2.
DMDMi23503103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 501500TNF receptor-associated factor 2PRO_0000056399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei7 – 71Phosphothreonine1 Publication
Modified residuei11 – 111Phosphoserine2 Publications
Modified residuei22 – 221Phosphothreonine1 Publication
Cross-linki31 – 31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei117 – 1171Phosphothreonine; by PKC1 Publication

Post-translational modificationi

Phosphorylated at several serine residues within the first 128 amino acid residues. Phosphorylated at Thr-117 in response to signaling via TNF and TNFRSF1A. Phosphorylation at Thr-117 is required for 'Lys-63'-linked polyubiquitination, but not for 'Lys-48'-linked polyubiquitination. Phosphorylation at Thr-117 is important for interaction with IKKA and IKKB, activation of IKK and subsequent activation of NF-kappa-B.1 Publication
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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ12933.
PaxDbiQ12933.
PRIDEiQ12933.

PTM databases

PhosphoSiteiQ12933.

Expressioni

Gene expression databases

BgeeiQ12933.
CleanExiHS_TRAF2.
ExpressionAtlasiQ12933. baseline and differential.
GenevisibleiQ12933. HS.

Organism-specific databases

HPAiCAB004603.
HPA009972.
HPA010634.

Interactioni

Subunit structurei

Homotrimer, and heterotrimer with TRAF1 and TRAF3 (via TRAF domain). The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro). Interacts with TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40, CD27/TNFRSF7, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR, TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1 and IL15RA. Interacts with CDK9, CSK, MAP3K1, MAP3K5, MAP3K11, MAP3K14, MAP4K2, RIPK1, RIPK2, TNIK, TBK1, SPHK1, TRADD, TRAFD1, TRAIP, TANK/ITRAF, TNFAIP3, TDP2, MAVS/IPS1, TICAM1 and TRPC4AP. Interacts with CASP8AP2, NFATC2IP, PEG3 and HIVEP3. Interacts with ERN1; the interaction requires DAB2IP. Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2, or a TRAF2 homotrimer. Identified in a complex composed of TRAF2, TRAF3, BIRC2 and BIRC3. Interaction with BIRC2 and/or BIRC3 is essential for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts with CYLD, USP48, IKKA and IKKB. Identified in a complex with TNFRSF1A, RIPK1 and IKKB. Interacts (via 'Lys-63'-linked polyubiquitin chains) with TAB2 and TAB3. Interacts with ERN1 and TAOK3. Interaction with TAOK3 is facilitated under ER stress conditions, such as treatment with tunicamycin, and may promote TRAF2 phosphorylation. Interacts (via zinc fingers) with DAB2IP (via C-terminus PER domain); the interaction occurs in a TNF-alpha-dependent manner. Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain). Interacts with CARD14. Interacts with PTPN2; probably involved in tumor necrosis factor-mediated signaling.50 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-355744,EBI-355744
B2R8Y43EBI-355744,EBI-10175581
G2XKQ03EBI-355744,EBI-10175576
P889613EBI-355744,EBI-7907665From a different organism.
AASDHPPTQ9NRN74EBI-355744,EBI-740884
AESQ081173EBI-355744,EBI-717810
AFF4Q9UHB73EBI-355744,EBI-395282
AFF4Q9UHB7-23EBI-355744,EBI-10261324
AMOTL2Q9Y2J4-43EBI-355744,EBI-10187270
ANKRD36BP1Q96IX94EBI-355744,EBI-744859
APPL1Q9UKG12EBI-355744,EBI-741243
AQP1P299723EBI-355744,EBI-745213
ARSJQ8N5N63EBI-355744,EBI-10266832
ASCC1Q8N9N23EBI-355744,EBI-10268317
ATXN1P542535EBI-355744,EBI-930964
BANPQ8N9N54EBI-355744,EBI-744695
BCL10O959993EBI-355744,EBI-958922
BEX2Q9BXY83EBI-355744,EBI-745073
BIRC2Q1349010EBI-355744,EBI-514538
BIRC3Q134897EBI-355744,EBI-517709
C14orf105Q17R993EBI-355744,EBI-10238351
C17orf82Q86X593EBI-355744,EBI-8465536
Casp12O087366EBI-355744,EBI-6140033From a different organism.
CATSPER1Q8NEC53EBI-355744,EBI-744545
CBX8Q9HC523EBI-355744,EBI-712912
CCHCR1Q8TD31-33EBI-355744,EBI-10175300
CCNJLF6RF563EBI-355744,EBI-10177725
CD40P259424EBI-355744,EBI-525714
CDC20BQ86Y333EBI-355744,EBI-10260504
CDCA3Q996184EBI-355744,EBI-739534
CDKN1BP465272EBI-355744,EBI-519280
CEP57L1Q8IYX8-23EBI-355744,EBI-10181988
CREB5Q02930-33EBI-355744,EBI-10192698
CYB5R2Q6BCY43EBI-355744,EBI-744761
DTNBO609414EBI-355744,EBI-740402
EDARADDQ8WWZ35EBI-355744,EBI-2949647
EFEMP1Q128053EBI-355744,EBI-536772
EGFRP005333EBI-355744,EBI-297353
ENKD1Q9H0I24EBI-355744,EBI-744099
ERN1O754603EBI-355744,EBI-371750
EWSR1Q018443EBI-355744,EBI-739737
EXOC3-AS1Q8N2X64EBI-355744,EBI-749333
FAM192AQ9GZU83EBI-355744,EBI-2371956
FAM90A1Q86YD73EBI-355744,EBI-6658203
FDXACB1Q9BRP73EBI-355744,EBI-10297077
FNDC3BQ53EP0-33EBI-355744,EBI-10242151
GABPB1Q065474EBI-355744,EBI-618165
GORASP2Q9H8Y84EBI-355744,EBI-739467
GPKOWQ929173EBI-355744,EBI-746309
GSG1Q2KHT43EBI-355744,EBI-10239244
GSTP1P092115EBI-355744,EBI-353467
HENMT1Q5T8I93EBI-355744,EBI-9675710
Hoxa1P090223EBI-355744,EBI-3957603From a different organism.
IQUBQ8NA543EBI-355744,EBI-10220600
KIFC3Q9BVG83EBI-355744,EBI-2125614
KLF3P576823EBI-355744,EBI-8472267
MAP3K1Q132332EBI-355744,EBI-49776
Map3k1Q629252EBI-355744,EBI-636664From a different organism.
MAP3K14Q995583EBI-355744,EBI-358011
MORN3Q6PF183EBI-355744,EBI-9675802
NATD1Q8N6N63EBI-355744,EBI-8656665
NEBLO760413EBI-355744,EBI-2880203
NFIL3Q166493EBI-355744,EBI-3951858
NgfrP071743EBI-355744,EBI-1038810From a different organism.
NMUR2Q9GZQ43EBI-355744,EBI-10303844
NRF1Q166563EBI-355744,EBI-2547810
NUDT16L1Q9BRJ73EBI-355744,EBI-2949792
PCGF5Q86SE93EBI-355744,EBI-2827999
PGBD1Q96JS33EBI-355744,EBI-10290053
PIN1Q135264EBI-355744,EBI-714158
PPLO604373EBI-355744,EBI-368321
PPP1R18Q6NYC83EBI-355744,EBI-2557469
PRKAB2O437414EBI-355744,EBI-1053424
PRKRIP1Q9H8753EBI-355744,EBI-744488
RAD23AP547254EBI-355744,EBI-746453
RASSF5Q8WWW03EBI-355744,EBI-367390
RBM41Q96IZ53EBI-355744,EBI-740773
RCOR3Q9P2K34EBI-355744,EBI-743428
RIPK1Q135464EBI-355744,EBI-358507
RIPPLY1Q0D2K33EBI-355744,EBI-10226430
RNF146Q9NTX73EBI-355744,EBI-722397
SH2D4AQ9H7883EBI-355744,EBI-747035
SMG9Q9H0W83EBI-355744,EBI-2872322
SNRNP25Q9BV903EBI-355744,EBI-9675976
SPG21Q9NZD84EBI-355744,EBI-742688
SYT17Q9BSW73EBI-355744,EBI-745392
TANKQ928444EBI-355744,EBI-356349
TAOK3Q9H2K82EBI-355744,EBI-1384100
TBK1Q9UHD23EBI-355744,EBI-356402
TCEA2Q155604EBI-355744,EBI-710310
TEKT3Q9BXF93EBI-355744,EBI-8644516
THAP7Q9BT494EBI-355744,EBI-741350
THOP1Q96CV83EBI-355744,EBI-6137619
TIFAQ96CG35EBI-355744,EBI-740711
TNFAIP3P215803EBI-355744,EBI-527670
TNFRSF12AQ9NP843EBI-355744,EBI-2851995
TNFRSF14Q929564EBI-355760,EBI-1056653
TNFRSF1AP194384EBI-355744,EBI-299451
TNFRSF1BP203333EBI-355744,EBI-358983
TRADDQ156283EBI-355744,EBI-359215
TRAF1Q130774EBI-355744,EBI-359224
Traf5P701912EBI-355744,EBI-523899From a different organism.
TRAF6Q9Y4K36EBI-355744,EBI-359276
TRIM42A1L4B63EBI-355744,EBI-10172216
TROAPQ128153EBI-355744,EBI-2349743
TSHZ3A1L0U73EBI-355744,EBI-10171826
TSSC4Q9Y5U23EBI-355744,EBI-717229
UBXN11Q5T1245EBI-355744,EBI-746004
USF1P224153EBI-355744,EBI-1054489
USP2O756044EBI-355744,EBI-743272
VWA2Q5GFL63EBI-355744,EBI-10243723
YES1P079473EBI-355744,EBI-515331
ZBTB16Q055162EBI-355744,EBI-711925
ZBTB25P242784EBI-355744,EBI-739899
ZC2HC1CQ53FD03EBI-355744,EBI-740767
ZFAND6Q6FIF06EBI-355744,EBI-724630
ZMAT2Q96NC03EBI-355744,EBI-2682299
ZNF410Q86VK43EBI-355744,EBI-720304
ZNF488Q96MN93EBI-355744,EBI-948288
ZNF509Q32MK93EBI-355744,EBI-10239929
ZNF544Q6NX493EBI-355744,EBI-2841978
ZNF655Q8N7203EBI-355744,EBI-625509
ZNF662Q6ZS27-33EBI-355744,EBI-10255155
ZSCAN32I3L3J23EBI-355744,EBI-10178206

Protein-protein interaction databases

BioGridi113038. 323 interactions.
DIPiDIP-6223N.
IntActiQ12933. 222 interactions.
MINTiMINT-107429.
STRINGi9606.ENSP00000247668.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 233Combined sources
Helixi25 – 273Combined sources
Helixi30 – 323Combined sources
Turni35 – 373Combined sources
Beta strandi42 – 465Combined sources
Beta strandi52 – 543Combined sources
Helixi55 – 617Combined sources
Helixi62 – 643Combined sources
Helixi70 – 745Combined sources
Turni80 – 834Combined sources
Helixi87 – 893Combined sources
Helixi94 – 1018Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi115 – 1173Combined sources
Helixi118 – 1247Combined sources
Turni125 – 1273Combined sources
Helixi130 – 1334Combined sources
Helixi315 – 3184Combined sources
Helixi335 – 34713Combined sources
Beta strandi350 – 3589Combined sources
Helixi361 – 3699Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi381 – 3844Combined sources
Beta strandi389 – 3957Combined sources
Helixi400 – 4023Combined sources
Turni403 – 4053Combined sources
Beta strandi406 – 4149Combined sources
Helixi419 – 4213Combined sources
Beta strandi430 – 4345Combined sources
Beta strandi443 – 4475Combined sources
Helixi454 – 4563Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi467 – 4748Combined sources
Helixi476 – 4805Combined sources
Turni482 – 4843Combined sources
Beta strandi490 – 4967Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CA4X-ray2.20A/B/C/D/E/F334-501[»]
1CA9X-ray2.30A/B/C/D/E/F310-501[»]
1CZYX-ray2.00A/B/C334-501[»]
1CZZX-ray2.70A/B/C315-501[»]
1D00X-ray2.00A/B/C/D/E/F/G/H334-501[»]
1D01X-ray2.00A/B/C/D/E/F334-501[»]
1D0AX-ray2.00A/B/C/D/E/F334-501[»]
1D0JX-ray2.50A/B/C/D/E/F334-501[»]
1F3VX-ray2.00B331-501[»]
1QSCX-ray2.40A/B/C311-501[»]
3KNVX-ray1.90A1-133[»]
3M06X-ray2.67A/B/C/D/E/F266-329[»]
3M0AX-ray2.61A/B/C266-329[»]
3M0DX-ray2.80A/B266-329[»]
ProteinModelPortaliQ12933.
SMRiQ12933. Positions 15-183, 267-501.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12933.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini351 – 496146MATHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29311Important for interaction with BIRC2 and BIRC3By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili299 – 348501 PublicationAdd
BLAST

Domaini

The coiled coil domain mediates homo- and hetero-oligomerization.1 Publication
The MATH/TRAF domain binds to receptor cytoplasmic domains.1 Publication
The RING-type zinc finger domain is essential for E3 ubiquitin-protein ligase activity. It is not essential for the stabilization of BIRC2, or for the ubiquitination of RIPK1 in response to TNFR1 signaling.1 Publication

Sequence similaritiesi

Contains 1 MATH domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 2 TRAF-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri34 – 7340RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri124 – 18057TRAF-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri177 – 23357TRAF-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG264247.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiQ12933.
KOiK03173.
OMAiSDGCTWK.
OrthoDBiEOG7966G5.
PhylomeDBiQ12933.
TreeFamiTF321154.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027133. TRAF2.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]
PANTHERiPTHR10131:SF21. PTHR10131:SF21. 1 hit.
PfamiPF00917. MATH. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PIRSFiPIRSF015614. TRAF. 1 hit.
SMARTiSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12933-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAASVTPPG SLELLQPGFS KTLLGTKLEA KYLCSACRNV LRRPFQAQCG
60 70 80 90 100
HRYCSFCLAS ILSSGPQNCA ACVHEGIYEE GISILESSSA FPDNAARREV
110 120 130 140 150
ESLPAVCPSD GCTWKGTLKE YESCHEGRCP LMLTECPACK GLVRLGEKER
160 170 180 190 200
HLEHECPERS LSCRHCRAPC CGADVKAHHE VCPKFPLTCD GCGKKKIPRE
210 220 230 240 250
KFQDHVKTCG KCRVPCRFHA IGCLETVEGE KQQEHEVQWL REHLAMLLSS
260 270 280 290 300
VLEAKPLLGD QSHAGSELLQ RCESLEKKTA TFENIVCVLN REVERVAMTA
310 320 330 340 350
EACSRQHRLD QDKIEALSSK VQQLERSIGL KDLAMADLEQ KVLEMEASTY
360 370 380 390 400
DGVFIWKISD FARKRQEAVA GRIPAIFSPA FYTSRYGYKM CLRIYLNGDG
410 420 430 440 450
TGRGTHLSLF FVVMKGPNDA LLRWPFNQKV TLMLLDQNNR EHVIDAFRPD
460 470 480 490 500
VTSSSFQRPV NDMNIASGCP LFCPVSKMEA KNSYVRDDAI FIKAIVDLTG

L
Length:501
Mass (Da):55,859
Last modified:September 19, 2002 - v2
Checksum:iC508BE185B783B20
GO
Isoform 2 (identifier: Q12933-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-122: E → EVKMPACGMVTEAPAVGSRPRSPSSYDLVLHVPLTGAEACLMSVEEETELLLR

Note: No experimental confirmation available.
Show »
Length:553
Mass (Da):61,384
Checksum:iE5000CF242B2F404
GO
Isoform 3 (identifier: Q12933-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-63: Missing.

Note: No experimental confirmation available.
Show »
Length:490
Mass (Da):54,671
Checksum:i9CAF6DDAB0DE64DD
GO
Isoform 4 (identifier: Q12933-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     176-200: Missing.

Note: No experimental confirmation available.
Show »
Length:476
Mass (Da):53,055
Checksum:iBB290C92E8D33D79
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 310106Missing in BAB70792 (PubMed:14702039).CuratedAdd
BLAST
Sequence conflicti343 – 36523LEMEA…FARKR → RPFQAQCGHRYCSFCLASIL RKL in AAA87706 (PubMed:7639698).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei53 – 6311Missing in isoform 3. 1 PublicationVSP_039687Add
BLAST
Alternative sequencei122 – 1221E → EVKMPACGMVTEAPAVGSRP RSPSSYDLVLHVPLTGAEAC LMSVEEETELLLR in isoform 2. 1 PublicationVSP_007401
Alternative sequencei176 – 20025Missing in isoform 4. 1 PublicationVSP_039688Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7013.1. [Q12933-1]
PIRiS56163.
RefSeqiNP_066961.2. NM_021138.3. [Q12933-1]
UniGeneiHs.522506.

Genome annotation databases

EnsembliENST00000247668; ENSP00000247668; ENSG00000127191. [Q12933-1]
GeneIDi7186.
KEGGihsa:7186.
UCSCiuc004cjv.3. human. [Q12933-1]
uc010nbw.3. human. [Q12933-4]
uc011mek.2. human. [Q12933-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7013.1. [Q12933-1]
PIRiS56163.
RefSeqiNP_066961.2. NM_021138.3. [Q12933-1]
UniGeneiHs.522506.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CA4X-ray2.20A/B/C/D/E/F334-501[»]
1CA9X-ray2.30A/B/C/D/E/F310-501[»]
1CZYX-ray2.00A/B/C334-501[»]
1CZZX-ray2.70A/B/C315-501[»]
1D00X-ray2.00A/B/C/D/E/F/G/H334-501[»]
1D01X-ray2.00A/B/C/D/E/F334-501[»]
1D0AX-ray2.00A/B/C/D/E/F334-501[»]
1D0JX-ray2.50A/B/C/D/E/F334-501[»]
1F3VX-ray2.00B331-501[»]
1QSCX-ray2.40A/B/C311-501[»]
3KNVX-ray1.90A1-133[»]
3M06X-ray2.67A/B/C/D/E/F266-329[»]
3M0AX-ray2.61A/B/C266-329[»]
3M0DX-ray2.80A/B266-329[»]
ProteinModelPortaliQ12933.
SMRiQ12933. Positions 15-183, 267-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113038. 323 interactions.
DIPiDIP-6223N.
IntActiQ12933. 222 interactions.
MINTiMINT-107429.
STRINGi9606.ENSP00000247668.

PTM databases

PhosphoSiteiQ12933.

Polymorphism and mutation databases

BioMutaiTRAF2.
DMDMi23503103.

Proteomic databases

MaxQBiQ12933.
PaxDbiQ12933.
PRIDEiQ12933.

Protocols and materials databases

DNASUi7186.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247668; ENSP00000247668; ENSG00000127191. [Q12933-1]
GeneIDi7186.
KEGGihsa:7186.
UCSCiuc004cjv.3. human. [Q12933-1]
uc010nbw.3. human. [Q12933-4]
uc011mek.2. human. [Q12933-3]

Organism-specific databases

CTDi7186.
GeneCardsiGC09P139776.
H-InvDBHIX0169360.
HGNCiHGNC:12032. TRAF2.
HPAiCAB004603.
HPA009972.
HPA010634.
MIMi601895. gene.
neXtProtiNX_Q12933.
PharmGKBiPA164742666.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264247.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231558.
HOVERGENiHBG058222.
InParanoidiQ12933.
KOiK03173.
OMAiSDGCTWK.
OrthoDBiEOG7966G5.
PhylomeDBiQ12933.
TreeFamiTF321154.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_1432. TNF signaling.
REACT_1503. Ligand-dependent caspase activation.
REACT_164011. Regulation by c-FLIP.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_355072. TNFR1-mediated proapoptotic signaling.
REACT_355311. CASP8 activity is inhibited.
REACT_355409. RIPK1-mediated regulated necrosis.
REACT_832. Dimerization of procaspase-8.
SignaLinkiQ12933.

Miscellaneous databases

ChiTaRSiTRAF2. human.
EvolutionaryTraceiQ12933.
GeneWikiiTRAF2.
GenomeRNAii7186.
NextBioi28172.
PROiQ12933.
SOURCEiSearch...

Gene expression databases

BgeeiQ12933.
CleanExiHS_TRAF2.
ExpressionAtlasiQ12933. baseline and differential.
GenevisibleiQ12933. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR002083. MATH.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027133. TRAF2.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]
PANTHERiPTHR10131:SF21. PTHR10131:SF21. 1 hit.
PfamiPF00917. MATH. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PIRSFiPIRSF015614. TRAF. 1 hit.
SMARTiSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. Cited for: FUNCTION, INTERACTION WITH EIF2AK2.
  41. "VISA is an adapter protein required for virus-triggered IFN-beta Signaling."
    Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.
    Mol. Cell 19:727-740(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAVS.
  42. "Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation."
    Reiley W., Zhang M., Wu X., Granger E., Sun S.C.
    Mol. Cell. Biol. 25:3886-3895(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY CYLD.
  43. "Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase."
    van Vliet C., Bukczynska P.E., Puryer M.A., Sadek C.M., Shields B.J., Tremblay M.L., Tiganis T.
    Nat. Immunol. 6:253-260(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPN2.
  44. "Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB."
    Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G., Hatzivassiliou E.G.
    Cell. Signal. 18:83-92(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP48.
  45. "RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation."
    Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.
    J. Biol. Chem. 282:14788-14796(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2IP.
  46. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  47. "Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2."
    Csomos R.A., Brady G.F., Duckett C.S.
    J. Biol. Chem. 284:20531-20539(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIRC2.
  48. "PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and K63-linked polyubiquitination."
    Li S., Wang L., Dorf M.E.
    Mol. Cell 33:30-42(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKKA; IKKB; TAB2 AND TAB3, UBIQUITINATION AT LYS-31, PHOSPHORYLATION AT THR-117, MUTAGENESIS OF THR-117, UBIQUITINATION, SUBCELLULAR LOCATION.
  49. "TRAF2 phosphorylation modulates tumor necrosis factor alpha-induced gene expression and cell resistance to apoptosis."
    Blackwell K., Zhang L., Thomas G.S., Sun S., Nakano H., Habelhah H.
    Mol. Cell. Biol. 29:303-314(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH TNFRSF1A; RIPK1 AND IKKB, MUTAGENESIS OF SER-11, PHOSPHORYLATION AT SER-11.
  50. "TRAF2-MLK3 interaction is essential for TNF-alpha-induced MLK3 activation."
    Sondarva G., Kundu C.N., Mehrotra S., Mishra R., Rangasamy V., Sathyanarayana P., Ray R.S., Rana B., Rana A.
    Cell Res. 20:89-98(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAP3K11.
  51. Cited for: INTERACTION WITH BIRC2, SUBUNIT, HOMOTRIMERIZATION.
  52. "The RING domain of TRAF2 plays an essential role in the inhibition of TNFalpha-induced cell death but not in the activation of NF-kappaB."
    Zhang L., Blackwell K., Shi Z., Habelhah H.
    J. Mol. Biol. 396:528-539(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  53. "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
    Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
    Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, FUNCTION.
  54. "Direct binding of TRAF2 and TRAF6 to TICAM-1/TRIF adaptor participates in activation of the Toll-like receptor 3/4 pathway."
    Sasai M., Tatematsu M., Oshiumi H., Funami K., Matsumoto M., Hatakeyama S., Seya T.
    Mol. Immunol. 47:1283-1291(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TICAM1, FUNCTION.
  55. "Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2."
    Alvarez S.E., Harikumar K.B., Hait N.C., Allegood J., Strub G.M., Kim E.Y., Maceyka M., Jiang H., Luo C., Kordula T., Milstien S., Spiegel S.
    Nature 465:1084-1088(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, UBIQUITINATION, INTERACTION WITH SPHK1, SPHINGOLIPID BINDING.
  56. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  57. "Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes."
    Shembade N., Ma A., Harhaj E.W.
    Science 327:1135-1139(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFAIP3.
  58. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  59. "Alternative splicing of CARMA2/CARD14 transcripts generates protein variants with differential effect on NF-kappaB activation and endoplasmic reticulum stress-induced cell death."
    Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P., Stilo R.
    J. Cell. Physiol. 226:3121-3131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CARD14.
  60. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; SER-11 AND THR-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  61. "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
    Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
    Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IKBKE UBIQUITINATION.
  62. "Structural basis for self-association and receptor recognition of human TRAF2."
    Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.
    Nature 398:533-538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 310-501 IN COMPLEX WITH TNFRSF1B.
  63. "Crystallographic analysis of CD40 recognition and signaling by human TRAF2."
    McWhirter S.M., Pullen S.S., Holton J.M., Crute J.J., Kehry M.R., Alber T.
    Proc. Natl. Acad. Sci. U.S.A. 96:8408-8413(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 334-501 IN COMPLEX WITH EBV BNFL1, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 315-501 IN COMPLEX WITH TNFRSF5, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 334-501 IN COMPLEX WITH TNFRSF4, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 334-501 IN COMPLEX WITH TNFRSF9.
  64. "A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction."
    Park Y.C., Ye H., Hsia C., Segal D., Rich R.L., Liou H.C., Myszka D.G., Wu H.
    Cell 101:777-787(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 331-501 IN COMPLEX WITH TRADD.
  65. "Structural basis for the lack of E2 interaction in the RING domain of TRAF2."
    Yin Q., Lamothe B., Darnay B.G., Wu H.
    Biochemistry 48:10558-10567(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-133, FUNCTION, SUBUNIT.
  66. "Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation."
    Zheng C., Kabaleeswaran V., Wang Y., Cheng G., Wu H.
    Mol. Cell 38:101-113(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 266-330 IN COMPLEXES WITH TRAF1 AND BIRC3, FUNCTION, SUBUNIT, COILED-COIL DOMAIN, MUTAGENESIS OF ILE-285; VAL-288 AND GLU-292.

Entry informationi

Entry nameiTRAF2_HUMAN
AccessioniPrimary (citable) accession number: Q12933
Secondary accession number(s): A8K107
, B4DPJ7, Q7Z337, Q96NT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 19, 2002
Last modified: June 24, 2015
This is version 188 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.