Traf2
entrez
22030
canonical
uniprot
P39429
canonical
ensembl
ENSMUSG00000026942
resolver
ensp
ENSMUSP00000028311
resolver
ensp
ENSMUSP00000109872
resolver
genesymbol
Traf2
resolver
uniprot
A2AJA3
resolver
uniprot
O54896
resolver
uniprot
Q3U8L1
resolver
uniprot
Q8C6X9
resolver
uniprot_entry
Q3U8L1_MOUSE
resolver
uniprot_entry
Q8C6X9_MOUSE
resolver
uniprot_entry
TRAF2_MOUSE
resolver
uniprot_sec
A2AJA3
resolver
uniprot_sec
O54896
resolver
activity_regulation
ACTIVITY REGULATION: Has very low E3 ubiquitin ligase activity in the absence of sphingosine-1-phosphate. E3 ubiquitin ligase activity is strongly activated by cytoplasmic sphingosine-1-phosphate. {ECO:0000250|UniProtKB:Q12933}.
uniprot
proteins
amino_acid_sequence
MAAASVTSPGSLELLQPGFSKTLLGTRLEAKYLCSACKNILRRPFQAQCGHRYCSFCLTSILSSGPQNCAACVYEGLYEEGISILESSSAFPDNAARREVESLPAVCPNDGCTWKGTLKEYESCHEGLCPFLLTECPACKGLVRLSEKEHHTEQECPKRSLSCQHCRAPCSHVDLEVHYEVCPKFPLTCDGCGKKKIPRETFQDHVRACSKCRVLCRFHTVGCSEMVETENLQDHELQRLREHLALLLSSFLEAQASPGTLNQVGPELLQRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHRLDQDKIEALSNKVQQLERSIGLKDLAMADLEQKVSELEVSTYDGVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVTLMLLDHNNREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis (PubMed:15121867, PubMed:18997792, PubMed:19150425, PubMed:19409903, PubMed:19815541, PubMed:9390694). Catalyzes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, IKBKE, MLST8, RIPK1 and TICAM1 (PubMed:15175328, PubMed:28489822). 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 (By similarity). 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 (PubMed:18997794). Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR (By similarity). In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE (By similarity). Acts as a regulator of mTORC1 and mTORC2 assembly by mediating 'Lys-63'-linked ubiquitination of MLST8, thereby inhibiting formation of the mTORC2 complex, while facilitating assembly of the mTORC1 complex (PubMed:28489822). Required for normal antibody isotype switching from IgM to IgG (PubMed:10514016). {ECO:0000250|UniProtKB:Q12933, ECO:0000269|PubMed:10514016, ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15175328, ECO:0000269|PubMed:18997792, ECO:0000269|PubMed:18997794, ECO:0000269|PubMed:19150425, ECO:0000269|PubMed:19409903, ECO:0000269|PubMed:19815541, ECO:0000269|PubMed:28489822, ECO:0000269|PubMed:9390694}.
uniprot
proteins
mass_dalton
56026
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="C->S: Loss of autoubiquitination."; /evidence="ECO:0000269|PubMed:11909853"; MUTAGEN 283; /note="E->A: Reduces interaction with BIRC2."; /evidence="ECO:0000269|PubMed:19815541"; MUTAGEN 292; /note="E->A: Almost abolishes interaction with BIRC2; when associated with A-294."; /evidence="ECO:0000269|PubMed:19815541"; MUTAGEN 294; /note="E->A: Almost abolishes interaction with BIRC2; when associated with A-292."; /evidence="ECO:0000269|PubMed:19815541"; MUTAGEN 320; /note="K->R: Abolished ubiquitination by the SCF(FBXL2) complex."; /evidence="ECO:0000269|PubMed:23542741"; MUTAGEN 356; /note="W->A: Decreased interaction with FBXL2."; /evidence="ECO:0000269|PubMed:23542741
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:28489822}.
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:Q12933}.; PTM: Undergoes both 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination. Polyubiquitinated via 'Lys-63'-linked ubiquitin in response to TNF signaling; this requires prior phosphorylation at Thr-117. 'Lys-63'-linked polyubiquitination promotes TRAF2-mediated activation of NF-kappa-B. Can be polyubiquitinated at several Lys residues via 'Lys-48'-linked ubiquitin chains in response to TNF signaling, leading to proteasomal degradation. Autoubiquitinated, leading to its subsequent proteasomal degradation. Polyubiquitinated by BIRC2 and SIAH2, leading to its subsequent proteasomal degradation. Not ubiquitinated by BIRC3 or SIAH1. Deubiquitinated by CYLD, a protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Ubiquitination is inhibited by LRRC19; inhiits proteasomal degradation (PubMed:25026888). Ubiquitinated at Lys-320 by the SCF(FBXL2) complex, leading to its degradation by the proteasome (PubMed:23542741). Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO7; leading to repression of NF-kappa-B signaling (By similarity). {ECO:0000250|UniProtKB:Q12933, ECO:0000269|PubMed:23542741, ECO:0000269|PubMed:25026888}.
uniprot
proteins
protein_family
A subfamily
uniprot
proteins
protein_family
TNF receptor-associated factor family
uniprot
proteins
pubmed
10514016
uniprot
proteins
pubmed
11275257
uniprot
proteins
pubmed
11340079
uniprot
proteins
pubmed
11435475
uniprot
proteins
pubmed
11804591
uniprot
proteins
pubmed
11909853
uniprot
proteins
pubmed
15121867
uniprot
proteins
pubmed
15175328
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16876162
uniprot
proteins
pubmed
18281285
uniprot
proteins
pubmed
18849341
uniprot
proteins
pubmed
18997792
uniprot
proteins
pubmed
18997794
uniprot
proteins
pubmed
19150425
uniprot
proteins
pubmed
19409903
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19506082
uniprot
proteins
pubmed
19815541
uniprot
proteins
pubmed
20185725
uniprot
proteins
pubmed
21307340
uniprot
proteins
pubmed
22424771
uniprot
proteins
pubmed
23542741
uniprot
proteins
pubmed
25026888
uniprot
proteins
pubmed
28489822
uniprot
proteins
pubmed
8069916
uniprot
proteins
pubmed
8565075
uniprot
proteins
pubmed
8692885
uniprot
proteins
pubmed
9104814
uniprot
proteins
pubmed
9390694
uniprot
proteins
pubmed
9461607
uniprot
proteins
pubmed
9500555
uniprot
proteins
sequence_length
501
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm.
uniprot
proteins