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TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2)

 TRAF2_MOUSE             Reviewed;         501 AA.
P39429; A2AJA3; O54896;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 181.
RecName: Full=TNF receptor-associated factor 2;
EC=2.3.2.27;
AltName: Full=E3 ubiquitin-protein ligase TRAF2;
AltName: Full=RING-type E3 ubiquitin transferase TRAF2 {ECO:0000305};
Name=Traf2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TRAF1 AND
TNFRSF1B.
PubMed=8069916; DOI=10.1016/0092-8674(94)90532-0;
Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.;
"A novel family of putative signal transducers associated with the
cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.";
Cell 78:681-692(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=9461607; DOI=10.1074/jbc.273.7.4129;
Brink R., Lodish H.F.;
"Tumor necrosis factor receptor (TNFR)-associated factor 2A (TRAF2A),
a TRAF2 splice variant with an extended RING finger domain that
inhibits TNFR2-mediated NF-kappaB activation.";
J. Biol. Chem. 273:4129-4134(1998).
[3]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=11275257; DOI=10.1016/S0161-5890(00)00098-5;
Grech A., Quinn R., Srinivasan D., Badoux X., Brink R.;
"Complete structural characterisation of the mammalian and Drosophila
TRAF genes: implications for TRAF evolution and the role of RING
finger splice variants.";
Mol. Immunol. 37:721-734(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 430-440, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[7]
INTERACTION WITH TRADD.
PubMed=8565075; DOI=10.1016/S0092-8674(00)80984-8;
Hsu H., Shu H.-B., Pan M.G., Goeddel D.V.;
"TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF
receptor 1 signal transduction pathways.";
Cell 84:299-308(1996).
[8]
INTERACTION WITH TNFAIP3.
PubMed=8692885; DOI=10.1073/pnas.93.13.6721;
Song H.Y., Rothe M., Goeddel D.V.;
"The tumor necrosis factor-inducible zinc finger protein A20 interacts
with TRAF1/TRAF2 and inhibits NF-kappaB activation.";
Proc. Natl. Acad. Sci. U.S.A. 93:6721-6725(1996).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9390694; DOI=10.1016/S1074-7613(00)80391-X;
Yeh W.C., Shahinian A., Speiser D., Kraunus J., Billia F., Wakeham A.,
de la Pompa J.L., Ferrick D., Hum B., Iscove N., Ohashi P., Rothe M.,
Goeddel D.V., Mak T.W.;
"Early lethality, functional NF-kappaB activation, and increased
sensitivity to TNF-induced cell death in TRAF2-deficient mice.";
Immunity 7:715-725(1997).
[10]
INTERACTION WITH PEG3.
PubMed=9500555; DOI=10.1038/ng0398-287;
Relaix F., Wei X.-J., Wu X., Sassoon D.A.;
"Peg3/Pw1 is an imprinted gene involved in the TNF-NFkappaB signal
transduction pathway.";
Nat. Genet. 18:287-291(1998).
[11]
IDENTIFICATION IN A COMPLEX WITH TNFRSF8; TNFRSF1B, TRAF1 AND TRAIP,
AND INTERACTION WITH TRAIP.
PubMed=9104814; DOI=10.1084/jem.185.7.1275;
Lee S.Y., Lee S.Y., Choi Y.;
"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.";
J. Exp. Med. 185:1275-1285(1997).
[12]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10514016; DOI=10.1016/S1074-7613(00)80113-2;
Nguyen L.T., Duncan G.S., Mirtsos C., Ng M., Speiser D.E.,
Shahinian A., Marino M.W., Mak T.W., Ohashi P.S., Yeh W.C.;
"TRAF2 deficiency results in hyperactivity of certain TNFR1 signals
and impairment of CD40-mediated responses.";
Immunity 11:379-389(1999).
[13]
INTERACTION WITH CASP8AP2.
PubMed=11340079; DOI=10.1074/jbc.M102941200;
Choi Y.-H., Kim K.-B., Kim H.-H., Hong G.-S., Kwon Y.-K., Chung C.-W.,
Park Y.-M., Shen Z.-J., Kim B.J., Lee S.-Y., Jung Y.-K.;
"FLASH coordinates NF-kappa B activity via TRAF2.";
J. Biol. Chem. 276:25073-25077(2001).
[14]
INTERACTION WITH NFATC2IP.
PubMed=11435475; DOI=10.1084/jem.194.1.89;
Lieberson R., Mowen K.A., McBride K.D., Leautaud V., Zhang X.,
Suh W.-K., Wu L., Glimcher L.H.;
"Tumor necrosis factor receptor-associated factor (TRAF)2 represses
the T helper cell type 2 response through interaction with NFAT-
interacting protein (NIP45).";
J. Exp. Med. 194:89-98(2001).
[15]
AUTOUBIQUITINATION, DEGRADATION, INTERACTION WITH CD40, AND
MUTAGENESIS OF CYS-34.
PubMed=11909853; DOI=10.1074/jbc.M111522200;
Brown K.D., Hostager B.S., Bishop G.A.;
"Regulation of TRAF2 signaling by self-induced degradation.";
J. Biol. Chem. 277:19433-19438(2002).
[16]
INTERACTION WITH HIVEP3.
PubMed=11804591; DOI=10.1016/S1097-2765(01)00434-8;
Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.;
"A mammalian homolog of Drosophila schnurri, KRC, regulates TNF
receptor-driven responses and interacts with TRAF2.";
Mol. Cell 9:121-131(2002).
[17]
FUNCTION.
PubMed=15175328; DOI=10.1074/jbc.M404206200;
Lee T.H., Shank J., Cusson N., Kelliher M.A.;
"The kinase activity of Rip1 is not required for tumor necrosis
factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or
for the ubiquitination of Rip1 by Traf2.";
J. Biol. Chem. 279:33185-33191(2004).
[18]
FUNCTION.
PubMed=15121867; DOI=10.1128/MCB.24.10.4502-4512.2004;
Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J.,
Nakano H., Alcami J., Esteban M.;
"TRAF family proteins link PKR with NF-kappa B activation.";
Mol. Cell. Biol. 24:4502-4512(2004).
[19]
INTERACTION WITH TRPC4AP.
PubMed=16876162; DOI=10.1016/j.febslet.2006.06.098;
Soond S.M., Terry J.L., Riches D.W.H.;
"TRUSS, a tumor necrosis factor receptor-1-interacting protein,
activates c-Jun NH(2)-terminal kinase and transcription factor AP-1.";
FEBS Lett. 580:4591-4596(2006).
[20]
INTERACTION WITH DAB2IP AND ERN1.
PubMed=18281285; DOI=10.1074/jbc.M710557200;
Luo D., He Y., Zhang H., Yu L., Chen H., Xu Z., Tang S., Urano F.,
Min W.;
"AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum
stress response.";
J. Biol. Chem. 283:11905-11912(2008).
[21]
INTERACTION WITH TRAFD1.
PubMed=18849341; DOI=10.1074/jbc.M806923200;
Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T.,
Yoshimura A.;
"FLN29 deficiency reveals its negative regulatory role in the Toll-
like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like
helicase signaling pathway.";
J. Biol. Chem. 283:33858-33864(2008).
[22]
FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION IN A COMPLEX WITH
MAP3K14; BIRC3 AND TRAF3.
PubMed=18997792; DOI=10.1038/ni.1678;
Vallabhapurapu S., Matsuzawa A., Zhang W., Tseng P.H., Keats J.J.,
Wang H., Vignali D.A., Bergsagel P.L., Karin M.;
"Nonredundant and complementary functions of TRAF2 and TRAF3 in a
ubiquitination cascade that activates NIK-dependent alternative NF-
kappaB signaling.";
Nat. Immunol. 9:1364-1370(2008).
[23]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH TRAF3; BIRC2 AND BIRC3.
PubMed=18997794; DOI=10.1038/ni.1676;
Zarnegar B.J., Wang Y., Mahoney D.J., Dempsey P.W., Cheung H.H.,
He J., Shiba T., Yang X., Yeh W.C., Mak T.W., Korneluk R.G., Cheng G.;
"Noncanonical NF-kappaB activation requires coordinated assembly of a
regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and
the kinase NIK.";
Nat. Immunol. 9:1371-1378(2008).
[24]
FUNCTION, IDENTIFICATION IN COMPLEX I; INTERACTION WITH TAK1; IKKA;
IKKB; TAB2 AND TAB3, AND PHOSPHORYLATION AT THR-117.
PubMed=19150425; DOI=10.1016/j.molcel.2008.11.023;
Li S., Wang L., Dorf M.E.;
"PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and
K63-linked polyubiquitination.";
Mol. Cell 33:30-42(2009).
[25]
INTERACTION WITH BIRC2.
PubMed=19506082; DOI=10.1074/jbc.M109.029983;
Csomos R.A., Brady G.F., Duckett C.S.;
"Enhanced cytoprotective effects of the inhibitor of apoptosis protein
cellular IAP1 through stabilization with TRAF2.";
J. Biol. Chem. 284:20531-20539(2009).
[26]
FUNCTION, IDENTIFICATION IN COMPLEX I, DOMAIN, AND MUTAGENESIS OF
GLU-283; GLU-292 AND GLU-294.
PubMed=19815541; DOI=10.1074/jbc.M109.072256;
Vince J.E., Pantaki D., Feltham R., Mace P.D., Cordier S.M.,
Schmukle A.C., Davidson A.J., Callus B.A., Wong W.W., Gentle I.E.,
Carter H., Lee E.F., Walczak H., Day C.L., Vaux D.L., Silke J.;
"TRAF2 must bind to cellular inhibitors of apoptosis for tumor
necrosis factor (TNF) to efficiently activate NF-{kappa}B and to
prevent TNF-induced apoptosis.";
J. Biol. Chem. 284:35906-35915(2009).
[27]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19409903; DOI=10.1016/j.jmb.2009.04.054;
Zhang L., Blackwell K., Thomas G.S., Sun S., Yeh W.C., Habelhah H.;
"TRAF2 suppresses basal IKK activity in resting cells and TNFalpha can
activate IKK in TRAF2 and TRAF5 double knockout cells.";
J. Mol. Biol. 389:495-510(2009).
[28]
INTERACTION WITH TNFAIP3 AND TAX1BP1.
PubMed=20185725; DOI=10.1126/science.1182364;
Shembade N., Ma A., Harhaj E.W.;
"Inhibition of NF-kappaB signaling by A20 through disruption of
ubiquitin enzyme complexes.";
Science 327:1135-1139(2010).
[29]
INTERACTION WITH UXT.
PubMed=21307340; DOI=10.1091/mbc.E10-10-0827;
Huang Y., Chen L., Zhou Y., Liu H., Yang J., Liu Z., Wang C.;
"UXT-V1 protects cells against TNF-induced apoptosis through
modulating complex II formation.";
Mol. Biol. Cell 22:1389-1397(2011).
-!- 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. {ECO:0000269|PubMed:10514016,
ECO:0000269|PubMed:15121867, ECO:0000269|PubMed:15175328,
ECO:0000269|PubMed:18997792, ECO:0000269|PubMed:18997794,
ECO:0000269|PubMed:19409903, ECO:0000269|PubMed:19815541,
ECO:0000269|PubMed:9390694}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- ENZYME REGULATION: Has very low E3 ubiquitin ligase activity in
the absence of sphingosine-1-phosphate. E3 ubiquitin ligase
activity is strongly activated by cytoplasmic sphingosine-1-
phosphate. {ECO:0000250|UniProtKB:Q12933}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- 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, EDAR
and IL15RA (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 (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:8692885, PubMed:20185725). 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
promotes 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).
{ECO:0000250|UniProtKB:Q12933, ECO:0000269|PubMed:11340079,
ECO:0000269|PubMed:11435475, ECO:0000269|PubMed:11804591,
ECO:0000269|PubMed:11909853, ECO:0000269|PubMed:16876162,
ECO:0000269|PubMed:18281285, ECO:0000269|PubMed:18849341,
ECO:0000269|PubMed:18997792, ECO:0000269|PubMed:18997794,
ECO:0000269|PubMed:19150425, ECO:0000269|PubMed:19506082,
ECO:0000269|PubMed:19815541, ECO:0000269|PubMed:20185725,
ECO:0000269|PubMed:21307340, ECO:0000269|PubMed:8069916,
ECO:0000269|PubMed:8565075, ECO:0000269|PubMed:8692885,
ECO:0000269|PubMed:9104814, ECO:0000269|PubMed:9500555}.
-!- INTERACTION:
P27958:- (xeno); NbExp=5; IntAct=EBI-520016, EBI-8753518;
O08863:Birc3; NbExp=7; IntAct=EBI-520016, EBI-642236;
P27512:Cd40; NbExp=3; IntAct=EBI-520016, EBI-525742;
Q920A9:Fcrla; NbExp=5; IntAct=EBI-520016, EBI-646587;
Q62406:Irak1; NbExp=2; IntAct=EBI-520016, EBI-448533;
P50284:Ltbr; NbExp=3; IntAct=EBI-520016, EBI-647023;
Q62073:Map3k7; NbExp=2; IntAct=EBI-520016, EBI-1775345;
Q8CDB0:Mknk2; NbExp=3; IntAct=EBI-520016, EBI-646209;
P70347-1:Tank; NbExp=7; IntAct=EBI-520016, EBI-646125;
Q60769:Tnfaip3; NbExp=3; IntAct=EBI-520016, EBI-646595;
O35305:Tnfrsf11a; NbExp=2; IntAct=EBI-520016, EBI-647362;
P47741:Tnfrsf4; NbExp=13; IntAct=EBI-520016, EBI-520001;
Q60803:Traf3; NbExp=2; IntAct=EBI-520016, EBI-520135;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P39429-1; Sequence=Displayed;
Name=2; Synonyms=TRAF2A;
IsoId=P39429-2; Sequence=VSP_007402;
Note=No experimental confirmation available. On mRNA level, has
a significantly shorter half-life than isoform 1.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in
spleen, adipose tissues, skeletal muscles, thymus, testis, heart,
lung, brain. Isoform 2 is very weakly expressed in heart, lung and
brain.
-!- DOMAIN: The coiled coil domain mediates homo- and hetero-
oligomerization. {ECO:0000269|PubMed:19815541}.
-!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic
domains. {ECO:0000269|PubMed:19815541}.
-!- DOMAIN: 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. {ECO:0000250|UniProtKB:Q12933}.
-!- 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. {ECO:0000250|UniProtKB:Q12933}.
-!- 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.
{ECO:0000269|PubMed:10514016, ECO:0000269|PubMed:18997792,
ECO:0000269|PubMed:19409903, ECO:0000269|PubMed:9390694}.
-!- SIMILARITY: Belongs to the TNF receptor-associated factor family.
A subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L35303; AAC37662.1; -; mRNA.
EMBL; AF027570; AAC53545.1; -; mRNA.
EMBL; AF233332; AAF59928.1; -; Genomic_DNA.
EMBL; AF233326; AAF59928.1; JOINED; Genomic_DNA.
EMBL; AF233327; AAF59928.1; JOINED; Genomic_DNA.
EMBL; AF233328; AAF59928.1; JOINED; Genomic_DNA.
EMBL; AF233329; AAF59928.1; JOINED; Genomic_DNA.
EMBL; AF233330; AAF59928.1; JOINED; Genomic_DNA.
EMBL; AF233331; AAF59928.1; JOINED; Genomic_DNA.
EMBL; AL732590; CAM25164.1; -; Genomic_DNA.
EMBL; BC003801; AAH03801.1; -; mRNA.
CCDS; CCDS15779.1; -. [P39429-1]
CCDS; CCDS71002.1; -. [P39429-2]
PIR; I61512; I61512.
RefSeq; NP_001277342.1; NM_001290413.1. [P39429-2]
RefSeq; NP_033448.2; NM_009422.3. [P39429-1]
UniGene; Mm.3399; -.
ProteinModelPortal; P39429; -.
SMR; P39429; -.
BioGrid; 204303; 32.
CORUM; P39429; -.
DIP; DIP-468N; -.
IntAct; P39429; 50.
MINT; MINT-197749; -.
STRING; 10090.ENSMUSP00000028311; -.
iPTMnet; P39429; -.
PhosphoSitePlus; P39429; -.
EPD; P39429; -.
PaxDb; P39429; -.
PeptideAtlas; P39429; -.
PRIDE; P39429; -.
Ensembl; ENSMUST00000028311; ENSMUSP00000028311; ENSMUSG00000026942. [P39429-1]
Ensembl; ENSMUST00000114234; ENSMUSP00000109872; ENSMUSG00000026942. [P39429-2]
GeneID; 22030; -.
KEGG; mmu:22030; -.
UCSC; uc008isl.2; mouse. [P39429-2]
UCSC; uc008ism.2; mouse. [P39429-1]
CTD; 7186; -.
MGI; MGI:101835; Traf2.
eggNOG; ENOG410ISDM; Eukaryota.
eggNOG; ENOG4111M70; LUCA.
GeneTree; ENSGT00550000074359; -.
HOGENOM; HOG000231558; -.
HOVERGEN; HBG058222; -.
InParanoid; P39429; -.
KO; K03173; -.
OMA; SACRNVL; -.
OrthoDB; EOG091G0GHD; -.
PhylomeDB; P39429; -.
TreeFam; TF321154; -.
Reactome; R-MMU-3371378; Regulation by c-FLIP.
Reactome; R-MMU-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-MMU-5218900; CASP8 activity is inhibited.
Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-MMU-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-69416; Dimerization of procaspase-8.
Reactome; R-MMU-75893; TNF signaling.
UniPathway; UPA00143; -.
PRO; PR:P39429; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026942; -.
CleanEx; MM_TRAF2; -.
ExpressionAtlas; P39429; baseline and differential.
Genevisible; P39429; MM.
GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0097057; C:TRAF2-GSTP1 complex; ISO:MGI.
GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
GO; GO:0012506; C:vesicle membrane; IDA:MGI.
GO; GO:0005174; F:CD40 receptor binding; IPI:BHF-UCL.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0046625; F:sphingolipid binding; ISS:UniProtKB.
GO; GO:0031996; F:thioesterase binding; ISO:MGI.
GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0043623; P:cellular protein complex assembly; IDA:BHF-UCL.
GO; GO:0071732; P:cellular response to nitric oxide; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IEA:Ensembl.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:AgBase.
GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IDA:AgBase.
GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:MGI.
GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:AgBase.
GO; GO:0090073; P:positive regulation of protein homodimerization activity; ISO:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:MGI.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IDA:AgBase.
GO; GO:0097300; P:programmed necrotic cell death; IMP:MGI.
GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
GO; GO:0030163; P:protein catabolic process; IMP:MGI.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0051023; P:regulation of immunoglobulin secretion; IMP:MGI.
GO; GO:0046328; P:regulation of JNK cascade; IDA:MGI.
GO; GO:0007165; P:signal transduction; IDA:MGI.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
Gene3D; 2.60.210.10; -; 1.
Gene3D; 3.30.40.10; -; 4.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR012227; TNF_rcpt--assoc_TRAF.
InterPro; IPR008974; TRAF-like.
InterPro; IPR027133; TRAF2.
InterPro; IPR032070; TRAF_BIRC3-bd.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
InterPro; IPR001293; Znf_TRAF.
PANTHER; PTHR10131:SF21; PTHR10131:SF21; 1.
Pfam; PF16673; TRAF_BIRC3_bd; 1.
Pfam; PF00097; zf-C3HC4; 1.
Pfam; PF02176; zf-TRAF; 1.
PIRSF; PIRSF015614; TRAF; 1.
SMART; SM00061; MATH; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF49599; SSF49599; 2.
PROSITE; PS50144; MATH; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
PROSITE; PS50145; ZF_TRAF; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Coiled coil;
Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Lipid-binding; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q12933}.
CHAIN 2 501 TNF receptor-associated factor 2.
/FTId=PRO_0000056400.
DOMAIN 351 496 MATH. {ECO:0000255|PROSITE-
ProRule:PRU00129}.
ZN_FING 34 73 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 124 180 TRAF-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00207}.
ZN_FING 177 233 TRAF-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00207}.
REGION 283 293 Important for interaction with BIRC2 and
BIRC3.
COILED 298 348 {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q12933}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:Q12933}.
MOD_RES 7 7 Phosphothreonine.
{ECO:0000250|UniProtKB:Q12933}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:Q12933}.
MOD_RES 22 22 Phosphothreonine.
{ECO:0000250|UniProtKB:Q12933}.
MOD_RES 117 117 Phosphothreonine; by PKC.
{ECO:0000269|PubMed:19150425}.
CROSSLNK 31 31 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q12933}.
VAR_SEQ 62 62 L -> LRCASILS (in isoform 2).
{ECO:0000303|PubMed:9461607}.
/FTId=VSP_007402.
MUTAGEN 34 34 C->S: Loss of autoubiquitination.
{ECO:0000269|PubMed:11909853}.
MUTAGEN 283 283 E->A: Reduces interaction with BIRC2.
{ECO:0000269|PubMed:19815541}.
MUTAGEN 292 292 E->A: Almost abolishes interaction with
BIRC2; when associated with A-294.
{ECO:0000269|PubMed:19815541}.
MUTAGEN 294 294 E->A: Almost abolishes interaction with
BIRC2; when associated with A-292.
{ECO:0000269|PubMed:19815541}.
SEQUENCE 501 AA; 56026 MW; 043B391180365F10 CRC64;
MAAASVTSPG SLELLQPGFS KTLLGTRLEA KYLCSACKNI LRRPFQAQCG HRYCSFCLTS
ILSSGPQNCA ACVYEGLYEE GISILESSSA FPDNAARREV ESLPAVCPND GCTWKGTLKE
YESCHEGLCP FLLTECPACK GLVRLSEKEH HTEQECPKRS LSCQHCRAPC SHVDLEVHYE
VCPKFPLTCD GCGKKKIPRE TFQDHVRACS KCRVLCRFHT VGCSEMVETE NLQDHELQRL
REHLALLLSS FLEAQASPGT LNQVGPELLQ RCQILEQKIA TFENIVCVLN REVERVAVTA
EACSRQHRLD QDKIEALSNK VQQLERSIGL KDLAMADLEQ KVSELEVSTY DGVFIWKISD
FTRKRQEAVA GRTPAIFSPA FYTSRYGYKM CLRVYLNGDG TGRGTHLSLF FVVMKGPNDA
LLQWPFNQKV TLMLLDHNNR EHVIDAFRPD VTSSSFQRPV SDMNIASGCP LFCPVSKMEA
KNSYVRDDAI FIKAIVDLTG L


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