SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q60803

- TRAF3_MOUSE

UniProt

Q60803 - TRAF3_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
TNF receptor-associated factor 3
Gene
Traf3, Craf1, Trafamn
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regulates pathways leading to the activation of NF-kappa-B and MAP kinases, and plays a central role in the regulation of B-cell survival. Part of signaling pathways leading to the production of cytokines and interferon. Required for normal antibody isotype switching from IgM to IgG. Plays a role T-cell dependent immune responses. Plays a role in the regulation of antiviral responses. Is an essential constituent of several E3 ubiquitin-protein ligase complexes. May have E3 ubiquitin-protein ligase activity and promote 'Lys-63'-linked ubiquitination of target proteins. Inhibits activation of NF-kappa-B in response to LTBR stimulation. Inhibits TRAF2-mediated activation of NF-kappa-B. Down-regulates proteolytic processing of NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B. Promotes ubiquitination and proteasomal degradation of MAP3K14.10 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri67 – 7610RING-type
Zinc fingeri134 – 18956TRAF-type 1
Add
BLAST
Zinc fingeri190 – 24859TRAF-type 2
Add
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: InterPro
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. Toll signaling pathway Source: InterPro
  2. apoptotic process Source: UniProtKB-KW
  3. innate immune response Source: InterPro
  4. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  5. regulation of apoptotic process Source: InterPro
  6. regulation of cytokine production Source: UniProtKB
  7. regulation of defense response to virus Source: UniProtKB
  8. regulation of interferon-beta production Source: UniProtKB
  9. regulation of proteolysis Source: UniProtKB
  10. toll-like receptor signaling pathway Source: UniProtKB
  11. tumor necrosis factor-mediated signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Immunity, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.

Names & Taxonomyi

Protein namesi
Recommended name:
TNF receptor-associated factor 3 (EC:6.3.2.-)
Alternative name(s):
CD40 receptor-associated factor 1
Short name:
CRAF1
TRAFAMN
Gene namesi
Name:Traf3
Synonyms:Craf1, Trafamn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:108041. Traf3.

Subcellular locationi

Cytoplasm. Endosome
Note: Undergoes endocytosis together with TLR4 upon LPS signaling.1 Publication

GO - Cellular componenti

  1. CD40 receptor complex Source: BHF-UCL
  2. cytoplasmic side of plasma membrane Source: BHF-UCL
  3. endosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

Pathology & Biotechi

Disruption phenotypei

Newborns appear normal, but do not thrive. Their blood glucose levels and leukocyte levels decrease steadily, the spleen size is dramatically reduced, and they become progressively runted. They die about ten days after birth. Mice exhibit abnormally high MAP3K14 protein levels and constitutive proteolytic processing of NFKB2/p100, leading to constitutive activation of NF-kappa-B.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521C → A: Abolishes inhibition of NFKB2 processing; when associated with A-55. 1 Publication
Mutagenesisi55 – 551C → A: Abolishes inhibition of NFKB2 processing; when associated with A-52. 1 Publication
Mutagenesisi67 – 671C → A: Strongly reduces 'Lys-63'-linked ubiquitination; when associated with A-69. Abolishes inhibition of NFKB2 processing; when associated with A-69. 2 Publications
Mutagenesisi69 – 691H → A: Strongly reduces 'Lys-63'-linked ubiquitination; when associated with A-69. Abolishes inhibition of NFKB2 processing; when associated with A-67. 2 Publications
Mutagenesisi106 – 1061K → R: Reduces 'Lys-48'-linked polyubiquitination; when associated with R-155.
Mutagenesisi155 – 1551K → R: Reduces 'Lys-48'-linked polyubiquitination; when associated with R-106.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567TNF receptor-associated factor 3
PRO_0000056402Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki106 – 106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Inferred
Cross-linki155 – 155Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Inferred

Post-translational modificationi

Undergoes 'Lys-48'-linked polyubiquitination, leading to its proteasomal degradation in response to signaling by TNFSF13B, TLR4 or through CD40. 'Lys-48'-linked polyubiquitinated form is deubiquitinated by OTUD7B, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Undergoes 'Lys-63'-linked ubiquitination during early stages of virus infection, and 'Lys-48'-linked ubiquitination during later stages. Undergoes both 'Lys-48'-linked and 'Lys-63'-linked ubiquitination in response to TLR3 and TLR4 signaling. Deubiquitinated by OTUB1, OTUB2 and OTUD5.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ60803.
PaxDbiQ60803.
PRIDEiQ60803.

PTM databases

PhosphoSiteiQ60803.

Expressioni

Tissue specificityi

Detected in bone marrow macrophages and spleen B-cells (at protein level). In adult, highest in brain. Also found in kidney, heart, thymus, spleen, lung, muscle, testis and ovary. Not found in liver.3 Publications

Developmental stagei

In the embryo, expressed from E6.5 with highest levels found between E11.5 and E13.5. At late stages of gestation, from E14.5, only low levels are detected.

Gene expression databases

ArrayExpressiQ60803.
BgeeiQ60803.
CleanExiMM_TRAF3.
GenevestigatoriQ60803.

Interactioni

Subunit structurei

Homotrimer. Heterotrimer with TRAF2 and TRAF5. Interacts with LTBR/TNFRSF3, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF13C TNFRSF17/BCMA, TLR4 and EDAR. Interacts with MAP3K5, MAP3K14, TRAIP/TRIP, TDP2/TTRAP, TANK/ITRAF and TRAF3IP1. Interaction with TNFRSF5/CD40 is modulated by TANK/ITRAF, which competes for the same binding site. Interacts with TICAM1. Interacts with TRAFD1. Interacts with OTUB1, OTUB2 and OTUD5. Interacts with RNF216, MAVS, OPTN and TBK1 By similarity. Identified in a complex with TRAF2, MAP3K14 and BIRC3. Upon exposure to bacterial lipopolysaccharide (LPS), recruited to a transient complex containing TLR4, TRAF3, TRAF6, IKBKG, MAP3K7, MYD88, TICAM1, BIRC2, BIRC3 and UBE2N. Interacts (via RING-type zinc finger domain) with SRC. Interacts with CARD14 By similarity.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MavsQ8VCF04EBI-520135,EBI-3862816
Tnfrsf11aO353053EBI-520135,EBI-647362
Tnfrsf4P477413EBI-520135,EBI-520001
Traf2P394292EBI-520135,EBI-520016

Protein-protein interaction databases

BioGridi204304. 16 interactions.
DIPiDIP-34050N.
IntActiQ60803. 7 interactions.
MINTiMINT-1506326.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi377 – 40933
Beta strandi413 – 4219
Helixi424 – 4329
Beta strandi444 – 4474
Beta strandi452 – 4587
Helixi463 – 4653
Turni466 – 4683
Beta strandi469 – 4779
Helixi482 – 4843
Beta strandi493 – 4975
Beta strandi507 – 5115
Helixi518 – 5203
Beta strandi524 – 5274
Beta strandi531 – 5388
Helixi539 – 5446
Beta strandi552 – 5598

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GHUX-ray2.20A376-567[»]
ProteinModelPortaliQ60803.
SMRiQ60803. Positions 37-197, 376-567.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini414 – 559146MATH
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili266 – 33772 Reviewed prediction
Add
BLAST

Domaini

The MATH/TRAF domain binds to receptor cytoplasmic domains.1 Publication
The Ring-type zinc finger domain is required for its function in down-regulation of NFKB2 proteolytic processing.1 Publication

Sequence similaritiesi

Contains 1 MATH domain.

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG239194.
GeneTreeiENSGT00550000074359.
HOGENOMiHOG000231557.
HOVERGENiHBG058222.
InParanoidiB2RPW3.
KOiK03174.
OMAiYGCTFQG.
OrthoDBiEOG7966G5.
TreeFamiTF321154.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProiIPR002083. MATH.
IPR013323. SIAH-type.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027128. TRAF3.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]
PANTHERiPTHR10131:SF72. PTHR10131:SF72. 1 hit.
PfamiPF00917. MATH. 1 hit.
[Graphical view]
PIRSFiPIRSF015614. TRAF. 1 hit.
SMARTiSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 3 hits.
PROSITEiPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60803-1 [UniParc]FASTAAdd to Basket

« Hide

MESSKKMDAA GTLQPNPPLK LQPDRGAGSV LVPEQGGYKE KFVKTVEDKY    50
KCEKCRLVLC NPKQTECGHR FCESCMAALL SSSSPKCTAC QESIIKDKVF 100
KDNCCKREIL ALQVYCRNEG RGCAEQLTLG HLLVHLKNEC QFEELPCLRA 150
DCKEKVLRKD LRDHVEKACK YREATCSHCK SQVPMIKLQK HEDTDCPCVV 200
VSCPHKCSVQ TLLRSELSAH LSECVNAPST CSFKRYGCVF QGTNQQIKAH 250
EASSAVQHVN LLKEWSNSLE KKVSLLQNES VEKNKSIQSL HNQICSFEIE 300
IERQKEMLRN NESKILHLQR VIDSQAEKLK ELDKEIRPFR QNWEEADSMK 350
SSVESLQNRV TELESVDKSA GQAARNTGLL ESQLSRHDQM LSVHDIRLAD 400
MDLRFQVLET ASYNGVLIWK IRDYKRRKQE AVMGKTLSLY SQPFYTGYFG 450
YKMCARVYLN GDGMGKGTHL SLFFVIMRGE YDALLPWPFK QKVTLMLMDQ 500
GSSRRHLGDA FKPDPNSSSF KKPTGEMNIA SGCPVFVAQT VLENGTYIKD 550
DTIFIKVIVD TSDLPDP 567
Length:567
Mass (Da):64,294
Last modified:July 27, 2011 - v2
Checksum:iEC282EFFF84E5A3F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 732CE → WQ in AAC52710. 1 Publication
Sequence conflicti390 – 3901M → T in AAC52175. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21050 mRNA. Translation: AAC52175.1.
U33840 mRNA. Translation: AAC52710.1.
CH466549 Genomic DNA. Translation: EDL18642.1.
BC137634 mRNA. Translation: AAI37635.1.
BC137635 mRNA. Translation: AAI37636.1.
CCDSiCCDS26175.1.
PIRiI49272.
RefSeqiNP_035762.2. NM_011632.3.
XP_006515861.1. XM_006515798.1.
XP_006515862.1. XM_006515799.1.
XP_006515863.1. XM_006515800.1.
XP_006515864.1. XM_006515801.1.
UniGeneiMm.27431.

Genome annotation databases

EnsembliENSMUST00000021706; ENSMUSP00000021706; ENSMUSG00000021277.
GeneIDi22031.
KEGGimmu:22031.
UCSCiuc007pcl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21050 mRNA. Translation: AAC52175.1 .
U33840 mRNA. Translation: AAC52710.1 .
CH466549 Genomic DNA. Translation: EDL18642.1 .
BC137634 mRNA. Translation: AAI37635.1 .
BC137635 mRNA. Translation: AAI37636.1 .
CCDSi CCDS26175.1.
PIRi I49272.
RefSeqi NP_035762.2. NM_011632.3.
XP_006515861.1. XM_006515798.1.
XP_006515862.1. XM_006515799.1.
XP_006515863.1. XM_006515800.1.
XP_006515864.1. XM_006515801.1.
UniGenei Mm.27431.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GHU X-ray 2.20 A 376-567 [» ]
ProteinModelPortali Q60803.
SMRi Q60803. Positions 37-197, 376-567.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204304. 16 interactions.
DIPi DIP-34050N.
IntActi Q60803. 7 interactions.
MINTi MINT-1506326.

PTM databases

PhosphoSitei Q60803.

Proteomic databases

MaxQBi Q60803.
PaxDbi Q60803.
PRIDEi Q60803.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021706 ; ENSMUSP00000021706 ; ENSMUSG00000021277 .
GeneIDi 22031.
KEGGi mmu:22031.
UCSCi uc007pcl.1. mouse.

Organism-specific databases

CTDi 7187.
MGIi MGI:108041. Traf3.

Phylogenomic databases

eggNOGi NOG239194.
GeneTreei ENSGT00550000074359.
HOGENOMi HOG000231557.
HOVERGENi HBG058222.
InParanoidi B2RPW3.
KOi K03174.
OMAi YGCTFQG.
OrthoDBi EOG7966G5.
TreeFami TF321154.

Enzyme and pathway databases

Reactomei REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.

Miscellaneous databases

NextBioi 301784.
PROi Q60803.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q60803.
Bgeei Q60803.
CleanExi MM_TRAF3.
Genevestigatori Q60803.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProi IPR002083. MATH.
IPR013323. SIAH-type.
IPR012227. TNF_rcpt--assoc_TRAF.
IPR008974. TRAF-like.
IPR027128. TRAF3.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view ]
PANTHERi PTHR10131:SF72. PTHR10131:SF72. 1 hit.
Pfami PF00917. MATH. 1 hit.
[Graphical view ]
PIRSFi PIRSF015614. TRAF. 1 hit.
SMARTi SM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF49599. SSF49599. 3 hits.
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. "Involvement of CRAF1, a relative of TRAF, in CD40 signaling."
    Cheng G., Cleary A.M., Ye Z.S., Hong D.I., Lederman S., Baltimore D.
    Science 267:1494-1498(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TNFRSF5.
  2. "A candidate gene for the amnionless gastrulation stage mouse mutation encodes a TRAF-related protein."
    Wang X., Bornslaeger E.A., Haub O., Tomihara-Newberger C., Lonberg N., Dinulos M.B., Disteche C.M., Copeland N.G., Gilbert D.J., Jenkins N.A., Lacy E.
    Dev. Biol. 177:274-290(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain.
  5. "Targeted disruption of TRAF3 leads to postnatal lethality and defective T-dependent immune responses."
    Xu Y., Cheng G., Baltimore D.
    Immunity 5:407-415(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  6. Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. "Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6."
    Hacker H., Redecke V., Blagoev B., Kratchmarova I., Hsu L.C., Wang G.G., Kamps M.P., Raz E., Wagner H., Hacker G., Mann M., Karin M.
    Nature 439:204-207(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYD88, IDENTIFICATION IN A COMPLEX WITH TRAF6.
  8. "Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response."
    Oganesyan G., Saha S.K., Guo B., He J.Q., Shahangian A., Zarnegar B., Perry A., Cheng G.
    Nature 439:208-211(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TICAM1, FUNCTION.
  9. "Specificity of TRAF3 in its negative regulation of the noncanonical NF-kappa B pathway."
    He J.Q., Saha S.K., Kang J.R., Zarnegar B., Cheng G.
    J. Biol. Chem. 282:3688-3694(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH MAP3K14, MUTAGENESIS OF CYS-52; CYS-55; CYS-67 AND HIS-69.
  10. "TRAF2 and TRAF3 signal adapters act cooperatively to control the maturation and survival signals delivered to B cells by the BAFF receptor."
    Gardam S., Sierro F., Basten A., Mackay F., Brink R.
    Immunity 28:391-401(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "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."
    Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T., Yoshimura A.
    J. Biol. Chem. 283:33858-33864(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAFD1.
  12. "Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-kappaB signaling."
    Vallabhapurapu S., Matsuzawa A., Zhang W., Tseng P.H., Keats J.J., Wang H., Vignali D.A., Bergsagel P.L., Karin M.
    Nat. Immunol. 9:1364-1370(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN A COMPLEX WITH TRAF2; BIRC3 AND MAP3K14, UBIQUITINATION, TISSUE SPECIFICITY.
  13. "Noncanonical NF-kappaB activation requires coordinated assembly of a regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and the kinase NIK."
    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.
    Nat. Immunol. 9:1371-1378(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAP3K14.
  14. "TRAF2 and TRAF3 independently mediate Ig class switching driven by CD40."
    Jabara H.H., Weng Y., Sannikova T., Geha R.S.
    Int. Immunol. 21:477-488(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines."
    Tseng P.H., Matsuzawa A., Zhang W., Mino T., Vignali D.A., Karin M.
    Nat. Immunol. 11:70-75(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, E3 PROTEIN-UBIQUITIN LIGASE ACTIVITY, MUTAGENESIS OF CYS-67 AND HIS-69, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TLR4, IDENTIFICATION IN A COMPLEX WITH TLR4; TRAF6; MAP3K7; MYD88; IKBKG; TICAM1; BIRC2; BIRC3 AND UBE2N, UBIQUITINATION, TISSUE SPECIFICITY.
  16. "OTUD7B controls non-canonical NF-kappaB activation through deubiquitination of TRAF3."
    Hu H., Brittain G.C., Chang J.H., Puebla-Osorio N., Jin J., Zal A., Xiao Y., Cheng X., Chang M., Fu Y.X., Zal T., Zhu C., Sun S.C.
    Nature 494:371-374(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY OTUD7B.

Entry informationi

Entry nameiTRAF3_MOUSE
AccessioniPrimary (citable) accession number: Q60803
Secondary accession number(s): B2RPW3, Q62380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi