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Q12933

- TRAF2_HUMAN

UniProt

Q12933 - TRAF2_HUMAN

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Protein
TNF receptor-associated factor 2
Gene
TRAF2, TRAP3
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Pathwayi

Regions

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

GO - Molecular functioni

  1. CD40 receptor binding Source: BHF-UCL
  2. enzyme binding Source: BHF-UCL
  3. identical protein binding Source: IntAct
  4. ligase activity Source: UniProtKB-KW
  5. protein binding Source: IntAct
  6. protein phosphatase binding Source: UniProtKB
  7. signal transducer activity Source: ProtInc
  8. sphingolipid binding Source: UniProtKB
  9. thioesterase binding Source: UniProtKB
  10. tumor necrosis factor receptor binding Source: UniProtKB
  11. ubiquitin protein ligase binding Source: UniProtKB
  12. ubiquitin-protein transferase activity Source: UniProtKB
  13. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. activation of NF-kappaB-inducing kinase activity Source: UniProtKB
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
  3. apoptotic process Source: Reactome
  4. apoptotic signaling pathway Source: Reactome
  5. cellular protein complex assembly Source: BHF-UCL
  6. innate immune response Source: Reactome
  7. negative regulation of glial cell apoptotic process Source: Ensembl
  8. positive regulation of JUN kinase activity Source: UniProtKB
  9. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  10. positive regulation of T cell activation Source: UniProtKB
  11. positive regulation of T cell cytokine production Source: UniProtKB
  12. positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  13. positive regulation of interleukin-2 production Source: UniProtKB
  14. positive regulation of protein homodimerization activity Source: UniProtKB
  15. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  16. protein K63-linked ubiquitination Source: UniProtKB
  17. protein autoubiquitination Source: UniProtKB
  18. protein catabolic process Source: Ensembl
  19. protein complex assembly Source: ProtInc
  20. protein heterooligomerization Source: Ensembl
  21. protein homotrimerization Source: UniProtKB
  22. regulation of apoptotic process Source: UniProtKB
  23. regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
  24. regulation of immunoglobulin secretion Source: Ensembl
  25. signal transduction Source: ProtInc
  26. 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. Caspase-8 activation.
REACT_164011. Regulation by c-FLIP.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24969. TRAF6 mediated NF-kB activation.
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: Chromosome 9

Organism-specific databases

HGNCiHGNC:12032. TRAF2.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. CD40 receptor complex Source: BHF-UCL
  2. cell cortex Source: Ensembl
  3. cytoplasm Source: HPA
  4. cytoplasmic side of plasma membrane Source: BHF-UCL
  5. cytosol Source: Reactome
  6. membrane raft 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 501500TNF receptor-associated factor 2
PRO_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.2 Publications
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.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ12933.
PaxDbiQ12933.
PRIDEiQ12933.

PTM databases

PhosphoSiteiQ12933.

Expressioni

Gene expression databases

ArrayExpressiQ12933.
BgeeiQ12933.
CleanExiHS_TRAF2.
GenevestigatoriQ12933.

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.47 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-355744,EBI-355744
P889613EBI-355744,EBI-7907665From a different organism.
ATXN1P542532EBI-355744,EBI-930964
BIRC2Q134909EBI-355744,EBI-514538
BIRC3Q134896EBI-355744,EBI-517709
Casp12O087366EBI-355744,EBI-6140033From a different organism.
ERN1O754602EBI-355744,EBI-371750
GSTP1P092114EBI-355744,EBI-353467
Hoxa1P090223EBI-355744,EBI-3957603From a different organism.
NgfrP071743EBI-355744,EBI-1038810From a different organism.
TANKQ928444EBI-355744,EBI-356349
TAOK3Q9H2K82EBI-355744,EBI-1384100
TBK1Q9UHD23EBI-355744,EBI-356402
TNFRSF12AQ9NP843EBI-355744,EBI-2851995
TNFRSF14Q929564EBI-355760,EBI-1056653
TNFRSF1BP203333EBI-355744,EBI-358983
TRADDQ156283EBI-355744,EBI-359215
TRAF1Q130773EBI-355744,EBI-359224
Traf5P701912EBI-355744,EBI-523899From a different organism.
TRAF6Q9Y4K33EBI-355744,EBI-359276
ZFAND6Q6FIF06EBI-355744,EBI-724630

Protein-protein interaction databases

BioGridi113038. 222 interactions.
DIPiDIP-6223N.
IntActiQ12933. 137 interactions.
MINTiMINT-107429.
STRINGi9606.ENSP00000247668.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ12933.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini351 – 496146MATH
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29311Important for interaction with BIRC2 and BIRC3 By similarity
Add
BLAST

Coiled coil

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

Domaini

The coiled coil domain mediates homo- and hetero-oligomerization.2 Publications
The MATH/TRAF domain binds to receptor cytoplasmic domains.2 Publications
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.2 Publications

Sequence similaritiesi

Contains 1 MATH domain.

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG264247.
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. Align

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

MAAASVTPPG SLELLQPGFS KTLLGTKLEA KYLCSACRNV LRRPFQAQCG    50
HRYCSFCLAS ILSSGPQNCA ACVHEGIYEE GISILESSSA FPDNAARREV 100
ESLPAVCPSD GCTWKGTLKE YESCHEGRCP LMLTECPACK GLVRLGEKER 150
HLEHECPERS LSCRHCRAPC CGADVKAHHE VCPKFPLTCD GCGKKKIPRE 200
KFQDHVKTCG KCRVPCRFHA IGCLETVEGE KQQEHEVQWL REHLAMLLSS 250
VLEAKPLLGD QSHAGSELLQ RCESLEKKTA TFENIVCVLN REVERVAMTA 300
EACSRQHRLD QDKIEALSSK VQQLERSIGL KDLAMADLEQ KVLEMEASTY 350
DGVFIWKISD FARKRQEAVA GRIPAIFSPA FYTSRYGYKM CLRIYLNGDG 400
TGRGTHLSLF FVVMKGPNDA LLRWPFNQKV TLMLLDQNNR EHVIDAFRPD 450
VTSSSFQRPV NDMNIASGCP LFCPVSKMEA KNSYVRDDAI FIKAIVDLTG 500
L 501
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei53 – 6311Missing in isoform 3.
VSP_039687Add
BLAST
Alternative sequencei122 – 1221E → EVKMPACGMVTEAPAVGSRP RSPSSYDLVLHVPLTGAEAC LMSVEEETELLLR in isoform 2.
VSP_007401
Alternative sequencei176 – 20025Missing in isoform 4.
VSP_039688Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 310106Missing in BAB70792. 1 Publication
Add
BLAST
Sequence conflicti343 – 36523LEMEA…FARKR → RPFQAQCGHRYCSFCLASIL RKL in AAA87706. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000359662; ENSP00000352685; ENSG00000127191. [Q12933-2]
ENST00000536468; ENSP00000446414; ENSG00000127191. [Q12933-1]
GeneIDi7186.
KEGGihsa:7186.
UCSCiuc004cjv.3. human. [Q12933-1]
uc010nbw.3. human. [Q12933-4]
uc011mek.2. human. [Q12933-3]

Polymorphism databases

DMDMi23503103.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7013.1. [Q12933-1 ]
PIRi S56163.
RefSeqi NP_066961.2. NM_021138.3. [Q12933-1 ]
UniGenei Hs.522506.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 266-329 [» ]
3M0A X-ray 2.61 A/B/C 266-329 [» ]
3M0D X-ray 2.80 A/B 266-329 [» ]
ProteinModelPortali Q12933.
SMRi Q12933. Positions 15-183, 267-501.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113038. 222 interactions.
DIPi DIP-6223N.
IntActi Q12933. 137 interactions.
MINTi MINT-107429.
STRINGi 9606.ENSP00000247668.

PTM databases

PhosphoSitei Q12933.

Polymorphism databases

DMDMi 23503103.

Proteomic databases

MaxQBi Q12933.
PaxDbi Q12933.
PRIDEi Q12933.

Protocols and materials databases

DNASUi 7186.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247668 ; ENSP00000247668 ; ENSG00000127191 . [Q12933-1 ]
ENST00000359662 ; ENSP00000352685 ; ENSG00000127191 . [Q12933-2 ]
ENST00000536468 ; ENSP00000446414 ; ENSG00000127191 . [Q12933-1 ]
GeneIDi 7186.
KEGGi hsa:7186.
UCSCi uc004cjv.3. human. [Q12933-1 ]
uc010nbw.3. human. [Q12933-4 ]
uc011mek.2. human. [Q12933-3 ]

Organism-specific databases

CTDi 7186.
GeneCardsi GC09P139776.
H-InvDB HIX0169360.
HGNCi HGNC:12032. TRAF2.
HPAi CAB004603.
HPA009972.
HPA010634.
MIMi 601895. gene.
neXtProti NX_Q12933.
PharmGKBi PA164742666.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264247.
HOGENOMi HOG000231558.
HOVERGENi HBG058222.
InParanoidi Q12933.
KOi K03173.
OMAi SDGCTWK.
OrthoDBi EOG7966G5.
PhylomeDBi Q12933.
TreeFami TF321154.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_1432. TNF signaling.
REACT_1503. Caspase-8 activation.
REACT_164011. Regulation by c-FLIP.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_832. Dimerization of procaspase-8.
SignaLinki Q12933.

Miscellaneous databases

EvolutionaryTracei Q12933.
GeneWikii TRAF2.
GenomeRNAii 7186.
NextBioi 28172.
PROi Q12933.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q12933.
Bgeei Q12933.
CleanExi HS_TRAF2.
Genevestigatori Q12933.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR10131:SF21. PTHR10131:SF21. 1 hit.
Pfami PF00917. MATH. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view ]
PIRSFi PIRSF015614. TRAF. 1 hit.
SMARTi SM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF49599. SSF49599. 1 hit.
PROSITEi PS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view ]
ProtoNeti Search...

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].
    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].
  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: September 3, 2014
This is version 178 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

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