P39429 · TRAF2_MOUSE
- ProteinTNF receptor-associated factor 2
- GeneTraf2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids501 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Isoform 2 does not seem to mediate activation of NF-kappa-B but inhibits isoform 1 activity. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.
Catalytic activity
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.
Pathway
Protein modification; protein ubiquitination.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTNF receptor-associated factor 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP39429
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Important embryonic and perinatal mortality. Life-born mutants appear normal at birth, but are smaller than their littermates after three days, fail to thrive, and few survive more than three weeks. Thymus and spleen are severely atrophic, and mice display lymphopenia of both T and B lymphocytes, with normal erythrocyte counts. Their thymocytes are abnormally sensitive to TNF-induced cell death and exhibit high levels of spontaneous apoptosis. Macrophages are highly sensitive to TNF and produce high levels of nitric oxide (NO) in response to TNF. Likewise, endogenous TNF production is abnormally increased upon exposure to TNF. Symptoms are much attenuated in mice that are deficient for both Traf2 and Tnfrsf1a/Tnfr1, or Traf2 and Tnf. Likewise, deletion of one Map3k14 allele alleviates symptoms and rescues splenic atrophy and reduction of splenocyte numbers. Mice show normal IgM production in response to viral infection, but lack CD40-mediated proliferation of B-cells. They are deficient in antibody isotype switching and fail to produce IgG.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 34 | Loss of autoubiquitination. | ||||
Sequence: C → S | ||||||
Mutagenesis | 283 | Reduces interaction with BIRC2. | ||||
Sequence: E → A | ||||||
Mutagenesis | 292 | Almost abolishes interaction with BIRC2; when associated with A-294. | ||||
Sequence: E → A | ||||||
Mutagenesis | 294 | Almost abolishes interaction with BIRC2; when associated with A-292. | ||||
Sequence: E → A | ||||||
Mutagenesis | 320 | Abolished ubiquitination by the SCF(FBXL2) complex. | ||||
Sequence: K → R | ||||||
Mutagenesis | 356 | Decreased interaction with FBXL2. | ||||
Sequence: W → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 36 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000056400 | 2-501 | TNF receptor-associated factor 2 | |||
Sequence: AAASVTSPGSLELLQPGFSKTLLGTRLEAKYLCSACKNILRRPFQAQCGHRYCSFCLTSILSSGPQNCAACVYEGLYEEGISILESSSAFPDNAARREVESLPAVCPNDGCTWKGTLKEYESCHEGLCPFLLTECPACKGLVRLSEKEHHTEQECPKRSLSCQHCRAPCSHVDLEVHYEVCPKFPLTCDGCGKKKIPRETFQDHVRACSKCRVLCRFHTVGCSEMVETENLQDHELQRLREHLALLLSSFLEAQASPGTLNQVGPELLQRCQILEQKIATFENIVCVLNREVERVAVTAEACSRQHRLDQDKIEALSNKVQQLERSIGLKDLAMADLEQKVSELEVSTYDGVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVTLMLLDHNNREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL | ||||||
Modified residue | 5 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 7 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 11 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 22 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 31 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 117 | Phosphothreonine; by PKC | ||||
Sequence: T | ||||||
Cross-link | 320 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Phosphorylated at several serine residues within the first 128 amino acid residues. Phosphorylated at Thr-117 in response to signaling via TNF and TNFRSF1A. Phosphorylation at Thr-117 is required for 'Lys-63'-linked polyubiquitination, but not for 'Lys-48'-linked polyubiquitination. Phosphorylation at Thr-117 is important for interaction with IKKA and IKKB, activation of IKK and subsequent activation of NF-kappa-B.
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. Ubiquination 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).
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).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homotrimer (By similarity).
Heterotrimer with TRAF1 (PubMed:8069916).
Heterotrimer with TRAF3 (via TRAF domain) (By similarity).
The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro) (By similarity).
Interacts with TNFRSF1B/TNFR2 (PubMed:8069916).
Interacts with TNFRSF5/CD40 (PubMed:11909853).
Interacts with TNFRSF4, TNFRSF7/CD27, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR, TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT and EDAR (By similarity).
Stimulation of TNF-alpha receptor TNFRSF1A leads to the formation of two distinct signaling complexes. Plasma membrane-bound complex I is composed of TNFRSF1A, TRADD, RIPK1, TRAF2 and BIRC2/c-IAP1 or BIRC3 which interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta and IKBKG/IKK-gamma promoting cell survival (PubMed:19150425, PubMed:19815541).
Subsequently, TRADD, RIPK1 and TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with FADD and caspase CASP8 promoting cell apoptosis (By similarity).
Interacts with TRADD (PubMed:8565075).
Identified in a complex with TNFRSF1A, RIPK1 and IKBKB/IKK-beta (By similarity).
Interacts with RIPK2 (By similarity).
Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2, or a TRAF2 homotrimer (By similarity).
Identified in a complex composed of TRAF2, TRAF3, BIRC2 and BIRC3 (PubMed:18997794).
Interacts with BIRC2; the interaction promotes BIRC2 stability (PubMed:19506082).
Interaction with BIRC2 and/or BIRC3 is essential for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B (PubMed:19815541).
Within complex I, phosphorylated TRAF2 interacts (via 'Lys-63'-linked polyubiquitin chains) with CHUCK/IKK-alpha, IKBKB/IKK-beta, IKBKG/IKK-gamma TAB2, TAB3 and TAK1 in response to TNF-alpha stimulation (PubMed:19150425).
Within complex I, interacts with UXT isoform 1 (via TPQE motif); the interaction prevents the recruitment of FADD and CASP8/caspase 8 to complex I (PubMed:21307340).
Forms a complex composed of TNFRSF8/CD30 or TNFRSF1B/TNFR2, and TRAF1, TRAF2 and E3 ligase TRAIP (PubMed:9104814).
Within the complex, interacts with TRAIP; the interaction inhibits TRAF2-mediated NF-kappa B activation (PubMed:9104814).
Component of a complex composed of TANK and TBK1 (By similarity).
Interacts with TRPC4AP (PubMed:16876162).
Interacts with MAP3K1/MEKK1, MAP3K5/ASK1 and MAP3K11/MLK3 in response to TNF-alpha stimulation; the interaction leads to JNK activation and interaction with MAP3K5 is inhibited by PRMT1 (By similarity).
Component of a complex composed of MAP3K14/NIK BIRC3 and TRAF3; the interaction leads to BIRC2/3-mediated ubiquitination of TRAF3 upon CD40 engagement in a TRAF2-dependent manner (PubMed:18997792).
Interacts with MAP3K14/NIK in response to TNF-alpha stimulation; the interaction leads to NF-kappa B activation (By similarity).
Interacts with PEG3; the interaction may promote TRAF2-mediated NF-kappa B activation (PubMed:9500555).
Interacts with HIVEP3; the interaction may inhibit TNF-alpha-TRAF2-mediated NF-kappa B and JNK activation (PubMed:11804591).
Interacts with TANK/ITRAF; the interaction prevents interaction between TNFRSF1B/TNFR2 and TRAF2 (By similarity).
Interacts with deubiquitinating enzyme CYLD; the interaction results in the deubiquitination and inactivation of TRAF2 (By similarity).
Interacts with SIAH2; the interaction leads to TRAF2 ubiquitination and degradation (By similarity).
Interacts with E2 conjugating enzyme UBE2N/Ubc13, E3 ligase ITCH and RNF11 in response to TNF-alpha stimulation (By similarity).
Interacts with ubiquitin-editing enzyme TNFAIP3/A20 in response to TNF-alpha stimulation; the interaction promotes TRAF2 dissociation from UBE2N/Ubc13, ITCH, RNF11 and TAX1BP1 and prevents prolonged TRAF-2 ubiquitination (PubMed:20185725, PubMed:8692885).
Interacts with TAX1BP1 in response to TNF-alpha stimulation; the interaction promotes TRAF2 dissociation from UBE2N/Ubc13 and TNFAIP3/A20, and prevents prolonged TRAF-2 ubiquitination (PubMed:20185725).
Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain) (By similarity).
Interacts with deubiquitinating enzyme USP48 (By similarity).
Interacts with PTPN2; probably involved in TNF-mediated signaling (By similarity).
Interacts with Toll-like receptor TLR4/3 adapter TICAM1/TRIF; the interaction may promote TICAM1 ubiquitination (By similarity).
Interacts with kinase/endoribonuclease ERN1/IRE1 and DAB2IP in response to ER stress; the interaction requires DAB2IP (PubMed:18281285).
Interacts with ERN1/IRE1 and TAOK3 in response to ER stress; the interaction may promote TRAF2 phosphorylation (By similarity).
Interacts (via zinc fingers) with DAB2IP (via C-terminus PER domain) in response to TNF-alpha stimulation (By similarity).
Interacts with CASP8AP2/FLASH (PubMed:11340079).
Interacts with NFATC2IP; the interaction may repress IL-4 production in T cells (PubMed:11435475).
Interacts with kinase CDK9. Interacts with sphingosine kinase 1 SPHK1 (By similarity).
Interacts with kinase TNIK (By similarity).
Interacts with TRAFD1 (PubMed:18849341).
Interacts with DNA phosphodiesterase TDP2 (By similarity).
Interacts with MAVS/IPS1. Interacts with CARD14 (By similarity).
Interacts with GPS2 (PubMed:22424771).
Interacts with XPNPEP3 (By similarity).
Interacts with RIPK3 (By similarity).
Interacts with RELL2 (By similarity).
Interacts with LRRC19 (By similarity).
Interacts with GAPDH; promoting TRAF2 ubiquitination (By similarity).
Heterotrimer with TRAF1 (PubMed:8069916).
Heterotrimer with TRAF3 (via TRAF domain) (By similarity).
The domain containing the RING-type and the first TRAF-type zinc finger can also form homodimers (in vitro) (By similarity).
Interacts with TNFRSF1B/TNFR2 (PubMed:8069916).
Interacts with TNFRSF5/CD40 (PubMed:11909853).
Interacts with TNFRSF4, TNFRSF7/CD27, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF16/NGFR, TNFRSF17/BCMA, TNFRSF18/AITR, TNFRSF19/TROY, TNFRSF19L/RELT and EDAR (By similarity).
Stimulation of TNF-alpha receptor TNFRSF1A leads to the formation of two distinct signaling complexes. Plasma membrane-bound complex I is composed of TNFRSF1A, TRADD, RIPK1, TRAF2 and BIRC2/c-IAP1 or BIRC3 which interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta and IKBKG/IKK-gamma promoting cell survival (PubMed:19150425, PubMed:19815541).
Subsequently, TRADD, RIPK1 and TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with FADD and caspase CASP8 promoting cell apoptosis (By similarity).
Interacts with TRADD (PubMed:8565075).
Identified in a complex with TNFRSF1A, RIPK1 and IKBKB/IKK-beta (By similarity).
Interacts with RIPK2 (By similarity).
Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2 or BIRC3 molecule interacts with a heterotrimer formed by TRAF1 and TRAF2, or a TRAF2 homotrimer (By similarity).
Identified in a complex composed of TRAF2, TRAF3, BIRC2 and BIRC3 (PubMed:18997794).
Interacts with BIRC2; the interaction promotes BIRC2 stability (PubMed:19506082).
Interaction with BIRC2 and/or BIRC3 is essential for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B (PubMed:19815541).
Within complex I, phosphorylated TRAF2 interacts (via 'Lys-63'-linked polyubiquitin chains) with CHUCK/IKK-alpha, IKBKB/IKK-beta, IKBKG/IKK-gamma TAB2, TAB3 and TAK1 in response to TNF-alpha stimulation (PubMed:19150425).
Within complex I, interacts with UXT isoform 1 (via TPQE motif); the interaction prevents the recruitment of FADD and CASP8/caspase 8 to complex I (PubMed:21307340).
Forms a complex composed of TNFRSF8/CD30 or TNFRSF1B/TNFR2, and TRAF1, TRAF2 and E3 ligase TRAIP (PubMed:9104814).
Within the complex, interacts with TRAIP; the interaction inhibits TRAF2-mediated NF-kappa B activation (PubMed:9104814).
Component of a complex composed of TANK and TBK1 (By similarity).
Interacts with TRPC4AP (PubMed:16876162).
Interacts with MAP3K1/MEKK1, MAP3K5/ASK1 and MAP3K11/MLK3 in response to TNF-alpha stimulation; the interaction leads to JNK activation and interaction with MAP3K5 is inhibited by PRMT1 (By similarity).
Component of a complex composed of MAP3K14/NIK BIRC3 and TRAF3; the interaction leads to BIRC2/3-mediated ubiquitination of TRAF3 upon CD40 engagement in a TRAF2-dependent manner (PubMed:18997792).
Interacts with MAP3K14/NIK in response to TNF-alpha stimulation; the interaction leads to NF-kappa B activation (By similarity).
Interacts with PEG3; the interaction may promote TRAF2-mediated NF-kappa B activation (PubMed:9500555).
Interacts with HIVEP3; the interaction may inhibit TNF-alpha-TRAF2-mediated NF-kappa B and JNK activation (PubMed:11804591).
Interacts with TANK/ITRAF; the interaction prevents interaction between TNFRSF1B/TNFR2 and TRAF2 (By similarity).
Interacts with deubiquitinating enzyme CYLD; the interaction results in the deubiquitination and inactivation of TRAF2 (By similarity).
Interacts with SIAH2; the interaction leads to TRAF2 ubiquitination and degradation (By similarity).
Interacts with E2 conjugating enzyme UBE2N/Ubc13, E3 ligase ITCH and RNF11 in response to TNF-alpha stimulation (By similarity).
Interacts with ubiquitin-editing enzyme TNFAIP3/A20 in response to TNF-alpha stimulation; the interaction promotes TRAF2 dissociation from UBE2N/Ubc13, ITCH, RNF11 and TAX1BP1 and prevents prolonged TRAF-2 ubiquitination (PubMed:20185725, PubMed:8692885).
Interacts with TAX1BP1 in response to TNF-alpha stimulation; the interaction promotes TRAF2 dissociation from UBE2N/Ubc13 and TNFAIP3/A20, and prevents prolonged TRAF-2 ubiquitination (PubMed:20185725).
Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain) (By similarity).
Interacts with deubiquitinating enzyme USP48 (By similarity).
Interacts with PTPN2; probably involved in TNF-mediated signaling (By similarity).
Interacts with Toll-like receptor TLR4/3 adapter TICAM1/TRIF; the interaction may promote TICAM1 ubiquitination (By similarity).
Interacts with kinase/endoribonuclease ERN1/IRE1 and DAB2IP in response to ER stress; the interaction requires DAB2IP (PubMed:18281285).
Interacts with ERN1/IRE1 and TAOK3 in response to ER stress; the interaction may promote TRAF2 phosphorylation (By similarity).
Interacts (via zinc fingers) with DAB2IP (via C-terminus PER domain) in response to TNF-alpha stimulation (By similarity).
Interacts with CASP8AP2/FLASH (PubMed:11340079).
Interacts with NFATC2IP; the interaction may repress IL-4 production in T cells (PubMed:11435475).
Interacts with kinase CDK9. Interacts with sphingosine kinase 1 SPHK1 (By similarity).
Interacts with kinase TNIK (By similarity).
Interacts with TRAFD1 (PubMed:18849341).
Interacts with DNA phosphodiesterase TDP2 (By similarity).
Interacts with MAVS/IPS1. Interacts with CARD14 (By similarity).
Interacts with GPS2 (PubMed:22424771).
Interacts with XPNPEP3 (By similarity).
Interacts with RIPK3 (By similarity).
Interacts with RELL2 (By similarity).
Interacts with LRRC19 (By similarity).
Interacts with GAPDH; promoting TRAF2 ubiquitination (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P39429 | Birc3 O08863 | 7 | EBI-520016, EBI-642236 | |
BINARY | P39429 | Cd40 P27512 | 3 | EBI-520016, EBI-525742 | |
BINARY | P39429 | Fcrla Q920A9 | 5 | EBI-520016, EBI-646587 | |
BINARY | P39429 | Irak1 Q62406 | 2 | EBI-520016, EBI-448533 | |
BINARY | P39429 | Ltbr P50284 | 3 | EBI-520016, EBI-647023 | |
BINARY | P39429 | Map3k7 Q62073 | 2 | EBI-520016, EBI-1775345 | |
BINARY | P39429 | Mknk2 Q8CDB0 | 3 | EBI-520016, EBI-646209 | |
XENO | P39429 | PRO_0000037576 P27958 | 5 | EBI-520016, EBI-8753518 | |
BINARY | P39429 | Tank P70347-1 | 7 | EBI-520016, EBI-646125 | |
BINARY | P39429 | Tnfaip3 Q60769 | 3 | EBI-520016, EBI-646595 | |
BINARY | P39429 | Tnfrsf11a O35305 | 2 | EBI-520016, EBI-647362 | |
BINARY | P39429 | Tnfrsf4 P47741 | 12 | EBI-520016, EBI-520001 | |
BINARY | P39429 | Traf3 Q60803 | 2 | EBI-520016, EBI-520135 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 34-73 | RING-type | ||||
Sequence: CSACKNILRRPFQAQCGHRYCSFCLTSILSSGPQNCAACV | ||||||
Zinc finger | 124-180 | TRAF-type 1 | ||||
Sequence: CHEGLCPFLLTECPACKGLVRLSEKEHHTEQECPKRSLSCQHCRAPCSHVDLEVHYE | ||||||
Zinc finger | 177-233 | TRAF-type 2 | ||||
Sequence: VHYEVCPKFPLTCDGCGKKKIPRETFQDHVRACSKCRVLCRFHTVGCSEMVETENLQ | ||||||
Region | 283-293 | Important for interaction with BIRC2 and BIRC3 | ||||
Sequence: ENIVCVLNREV | ||||||
Coiled coil | 298-348 | |||||
Sequence: VTAEACSRQHRLDQDKIEALSNKVQQLERSIGLKDLAMADLEQKVSELEVS | ||||||
Domain | 351-496 | MATH | ||||
Sequence: DGVFIWKISDFTRKRQEAVAGRTPAIFSPAFYTSRYGYKMCLRVYLNGDGTGRGTHLSLFFVVMKGPNDALLQWPFNQKVTLMLLDHNNREHVIDAFRPDVTSSSFQRPVSDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIV |
Domain
The coiled coil domain mediates homo- and hetero-oligomerization.
The MATH/TRAF domain binds to receptor cytoplasmic domains.
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.
Sequence similarities
Belongs to the TNF receptor-associated factor family. A subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P39429-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length501
- Mass (Da)56,026
- Last updated1995-02-01 v1
- Checksum043B391180365F10
P39429-2
- Name2
- SynonymsTRAF2A
- NoteOn mRNA level, has a significantly shorter half-life than isoform 1.
- Differences from canonical
- 62-62: L → LRCASILS
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007402 | 62 | in isoform 2 | |||
Sequence: L → LRCASILS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L35303 EMBL· GenBank· DDBJ | AAC37662.1 EMBL· GenBank· DDBJ | mRNA | ||
AF027570 EMBL· GenBank· DDBJ | AAC53545.1 EMBL· GenBank· DDBJ | mRNA | ||
AF233332 EMBL· GenBank· DDBJ | AAF59928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF233326 EMBL· GenBank· DDBJ | AAF59928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF233327 EMBL· GenBank· DDBJ | AAF59928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF233328 EMBL· GenBank· DDBJ | AAF59928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF233329 EMBL· GenBank· DDBJ | AAF59928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF233330 EMBL· GenBank· DDBJ | AAF59928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF233331 EMBL· GenBank· DDBJ | AAF59928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL732590 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC003801 EMBL· GenBank· DDBJ | AAH03801.1 EMBL· GenBank· DDBJ | mRNA |