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Q9BUZ4

- TRAF4_HUMAN

UniProt

Q9BUZ4 - TRAF4_HUMAN

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Protein
TNF receptor-associated factor 4
Gene
TRAF4, CART1, MLN62, RNF83
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Adapter protein and signal transducer that links members of the tumor necrosis factor receptor (TNFR) family to different signaling pathways. Plays a role in the activation of NF-kappa-B and JNK, and in the regulation of cell survival and apoptosis. Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for normal skeleton development, and for normal development of the respiratory tract By similarity. Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri18 – 5841RING-type
Add
BLAST
Zinc fingeri102 – 15453TRAF-type 1
Add
BLAST
Zinc fingeri155 – 20854TRAF-type 2
Add
BLAST
Zinc fingeri209 – 26658TRAF-type 3
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. WW domain binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. thioesterase binding Source: UniProtKB
  5. tumor necrosis factor receptor binding Source: UniProt
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. ubiquitin-protein transferase activity Source: InterPro
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. activation of NF-kappaB-inducing kinase activity Source: InterPro
  2. apoptotic process Source: UniProtKB-KW
  3. positive regulation of JNK cascade Source: UniProtKB
  4. positive regulation of protein homodimerization activity Source: UniProtKB
  5. positive regulation of protein kinase activity Source: UniProtKB
  6. regulation of apoptotic process Source: InterPro
  7. respiratory gaseous exchange Source: Ensembl
  8. respiratory tube development Source: Ensembl
  9. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ9BUZ4.

Names & Taxonomyi

Protein namesi
Recommended name:
TNF receptor-associated factor 4
Alternative name(s):
Cysteine-rich domain associated with RING and Traf domains protein 1
Metastatic lymph node gene 62 protein
Short name:
MLN 62
RING finger protein 83
Gene namesi
Name:TRAF4
Synonyms:CART1, MLN62, RNF83
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:12034. TRAF4.

Subcellular locationi

Cytoplasm. Nucleus. Cytoplasmperinuclear region. Cell junctiontight junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton Inferred 6 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
  4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB-SubCell
  6. tight junction Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36711.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470TNF receptor-associated factor 4
PRO_0000056403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei426 – 4261Phosphoserine2 Publications

Post-translational modificationi

Polyubiquitinated, leading to its proteasomal degradation.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9BUZ4.
PaxDbiQ9BUZ4.
PeptideAtlasiQ9BUZ4.
PRIDEiQ9BUZ4.

PTM databases

PhosphoSiteiQ9BUZ4.

Expressioni

Tissue specificityi

Expressed in epithelial cells of thymus, dendritic cells of lymph node, and in the basal cell layer of epithelia such as epidermis, nasopharynx, respiratory tract, salivary gland, and esophagus.2 Publications

Inductioni

Up-regulated by bacterial lipopolysaccharides (LPS) and by single-stranded CpG oligodeoxynucleotide.1 Publication

Gene expression databases

ArrayExpressiQ9BUZ4.
BgeeiQ9BUZ4.
CleanExiHS_TRAF4.
GenevestigatoriQ9BUZ4.

Organism-specific databases

HPAiCAB009055.
HPA052377.

Interactioni

Subunit structurei

Homotrimer Inferred. Interacts with LTBR/TNFRSF3, NGFR/TNFRSF16, RPS6KB1 and TGFB1I1. Interacts with SMURF1. Interacts (via TRAF domain) with MAP3K4 (via kinase domain). Interacts with NCF1, TICAM1, IRAK1 and TRAF6, and is probably part of a complex containing TRAF4, NCF1, TICAM1, IRAK1 and TRAF6.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NgfrP071743EBI-3650647,EBI-1038810From a different organism.

Protein-protein interaction databases

BioGridi114979. 54 interactions.
DIPiDIP-40910N.
IntActiQ9BUZ4. 12 interactions.
MINTiMINT-107471.
STRINGi9606.ENSP00000262395.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi123 – 1264
Turni127 – 1326
Beta strandi142 – 1443
Helixi150 – 1556
Turni156 – 1583
Beta strandi192 – 1943
Beta strandi196 – 1983
Beta strandi201 – 2033
Helixi204 – 21310
Beta strandi215 – 2206
Beta strandi229 – 2313
Turni232 – 2343
Helixi235 – 2406
Beta strandi243 – 2453
Helixi286 – 30116
Beta strandi309 – 3146
Helixi317 – 32610
Beta strandi337 – 3404
Beta strandi345 – 3517
Helixi356 – 3583
Turni359 – 3613
Beta strandi362 – 3709
Helixi375 – 3773
Beta strandi386 – 3905
Turni396 – 3983
Beta strandi404 – 4085
Helixi415 – 4173
Beta strandi434 – 4418
Helixi442 – 4454
Turni446 – 4505
Beta strandi455 – 4628

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EODNMR-A190-248[»]
2YUCNMR-A102-164[»]
3ZJBX-ray1.84A/B/C283-470[»]
4K8UX-ray2.30A/B/C281-470[»]
4M4EX-ray2.60A/B/C292-466[»]
ProteinModelPortaliQ9BUZ4.
SMRiQ9BUZ4. Positions 3-164, 190-248, 291-468.

Miscellaneous databases

EvolutionaryTraceiQ9BUZ4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini307 – 462156MATH
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili277 – 30933 Reviewed prediction
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 MATH domain.

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG321306.
HOGENOMiHOG000004841.
HOVERGENiHBG103438.
InParanoidiQ9BUZ4.
KOiK09848.
OMAiEAFESHE.
OrthoDBiEOG7966G5.
PhylomeDBiQ9BUZ4.
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.
IPR027138. TRAF4.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view]
PANTHERiPTHR10131:SF71. PTHR10131:SF71. 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. 3 hits.
PROSITEiPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BUZ4-1) [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

MPGFDYKFLE KPKRRLLCPL CGKPMREPVQ VSTCGHRFCD TCLQEFLSEG    50
VFKCPEDQLP LDYAKIYPDP ELEVQVLGLP IRCIHSEEGC RWSGPLRHLQ 100
GHLNTCSFNV IPCPNRCPMK LSRRDLPAHL QHDCPKRRLK CEFCGCDFSG 150
EAYESHEGMC PQESVYCENK CGARMMRRLL AQHATSECPK RTQPCTYCTK 200
EFVFDTIQSH QYQCPRLPVA CPNQCGVGTV AREDLPGHLK DSCNTALVLC 250
PFKDSGCKHR CPKLAMARHV EESVKPHLAM MCALVSRQRQ ELQELRRELE 300
ELSVGSDGVL IWKIGSYGRR LQEAKAKPNL ECFSPAFYTH KYGYKLQVSA 350
FLNGNGSGEG THLSLYIRVL PGAFDNLLEW PFARRVTFSL LDQSDPGLAK 400
PQHVTETFHP DPNWKNFQKP GTWRGSLDES SLGFGYPKFI SHQDIRKRNY 450
VRDDAVFIRA AVELPRKILS 470
Length:470
Mass (Da):53,543
Last modified:June 1, 2001 - v1
Checksum:iA3F57E0E1081AB88
GO
Isoform 2 (identifier: Q9BUZ4-2) [UniParc]FASTAAdd to Basket

Also known as: TRAF4 variant 5

The sequence of this isoform differs from the canonical sequence as follows:
     157-428: Missing.

Show »
Length:198
Mass (Da):22,841
Checksum:i1571EDE9630E7398
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti173 – 1731A → T.1 Publication
Corresponds to variant rs35932778 [ dbSNP | Ensembl ].
VAR_025805
Natural varianti178 – 1781R → G.1 Publication
Corresponds to variant rs1044066 [ dbSNP | Ensembl ].
VAR_052150

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei157 – 428272Missing in isoform 2.
VSP_007403Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80200 mRNA. Translation: CAA56491.1.
AF082185 mRNA. Translation: AAC32376.1.
AY937224 mRNA. Translation: AAY16990.1.
DQ323999 Genomic DNA. Translation: ABC40750.1.
AC010761 Genomic DNA. No translation available.
BC001769 mRNA. Translation: AAH01769.1.
CCDSiCCDS11243.1. [Q9BUZ4-1]
PIRiI38026.
RefSeqiNP_004286.2. NM_004295.3. [Q9BUZ4-1]
UniGeneiHs.8375.

Genome annotation databases

EnsembliENST00000262395; ENSP00000262395; ENSG00000076604. [Q9BUZ4-1]
ENST00000262396; ENSP00000262396; ENSG00000076604.
GeneIDi9618.
KEGGihsa:9618.
UCSCiuc002hcq.1. human. [Q9BUZ4-2]
uc002hcs.3. human. [Q9BUZ4-1]

Polymorphism databases

DMDMi30580636.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80200 mRNA. Translation: CAA56491.1 .
AF082185 mRNA. Translation: AAC32376.1 .
AY937224 mRNA. Translation: AAY16990.1 .
DQ323999 Genomic DNA. Translation: ABC40750.1 .
AC010761 Genomic DNA. No translation available.
BC001769 mRNA. Translation: AAH01769.1 .
CCDSi CCDS11243.1. [Q9BUZ4-1 ]
PIRi I38026.
RefSeqi NP_004286.2. NM_004295.3. [Q9BUZ4-1 ]
UniGenei Hs.8375.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EOD NMR - A 190-248 [» ]
2YUC NMR - A 102-164 [» ]
3ZJB X-ray 1.84 A/B/C 283-470 [» ]
4K8U X-ray 2.30 A/B/C 281-470 [» ]
4M4E X-ray 2.60 A/B/C 292-466 [» ]
ProteinModelPortali Q9BUZ4.
SMRi Q9BUZ4. Positions 3-164, 190-248, 291-468.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114979. 54 interactions.
DIPi DIP-40910N.
IntActi Q9BUZ4. 12 interactions.
MINTi MINT-107471.
STRINGi 9606.ENSP00000262395.

PTM databases

PhosphoSitei Q9BUZ4.

Polymorphism databases

DMDMi 30580636.

Proteomic databases

MaxQBi Q9BUZ4.
PaxDbi Q9BUZ4.
PeptideAtlasi Q9BUZ4.
PRIDEi Q9BUZ4.

Protocols and materials databases

DNASUi 9618.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262395 ; ENSP00000262395 ; ENSG00000076604 . [Q9BUZ4-1 ]
ENST00000262396 ; ENSP00000262396 ; ENSG00000076604 .
GeneIDi 9618.
KEGGi hsa:9618.
UCSCi uc002hcq.1. human. [Q9BUZ4-2 ]
uc002hcs.3. human. [Q9BUZ4-1 ]

Organism-specific databases

CTDi 9618.
GeneCardsi GC17P027071.
HGNCi HGNC:12034. TRAF4.
HPAi CAB009055.
HPA052377.
MIMi 602464. gene.
neXtProti NX_Q9BUZ4.
PharmGKBi PA36711.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG321306.
HOGENOMi HOG000004841.
HOVERGENi HBG103438.
InParanoidi Q9BUZ4.
KOi K09848.
OMAi EAFESHE.
OrthoDBi EOG7966G5.
PhylomeDBi Q9BUZ4.
TreeFami TF321154.

Enzyme and pathway databases

SignaLinki Q9BUZ4.

Miscellaneous databases

ChiTaRSi TRAF4. human.
EvolutionaryTracei Q9BUZ4.
GeneWikii TRAF4.
GenomeRNAii 9618.
NextBioi 36083.
PROi Q9BUZ4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BUZ4.
Bgeei Q9BUZ4.
CleanExi HS_TRAF4.
Genevestigatori Q9BUZ4.

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.
IPR027138. TRAF4.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
IPR001293. Znf_TRAF.
[Graphical view ]
PANTHERi PTHR10131:SF71. PTHR10131:SF71. 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. 3 hits.
PROSITEi PS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17."
    Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P., Lidereau R., Basset P., Rio M.-C.
    Genomics 28:367-376(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-178.
    Tissue: Mammary tumor.
  2. "TRAF4 expression in proliferating cells."
    Miller H.G., Pullen S.P., White H.E., Phipps R.P., Kehry M.R., Crute J.J.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Lung.
  3. Cai C.L., Li R., Wang R.S., Miao S.Y., Wang L.F.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cervix carcinoma.
  4. NIEHS SNPs program
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-173.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Retinoblastoma.
  7. "Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor-associated protein family, which is expressed in breast carcinoma."
    Regnier C.H., Tomasetto C., Moog-Lutz C., Chenard M.-P., Wendling C., Basset P., Rio M.-C.
    J. Biol. Chem. 270:25715-25721(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "TRAF-4 expression in epithelial progenitor cells. Analysis in normal adult, fetal, and tumor tissues."
    Krajewska M., Krajewski S., Zapata J.M., VanArsdale T., Gascoyne R.D., Berern K., McFadden D., Shabaik A., Hugh J., Reynolds A., Clevenger C.V., Reed J.C.
    Am. J. Pathol. 152:1549-1561(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LTBR AND TNFRSDF16, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "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.
  10. "Involvement of TRAF4 in oxidative activation of c-Jun N-terminal kinase."
    Xu Y.C., Wu R.F., Gu Y., Yang Y.S., Yang M.C., Nwariaku F.E., Terada L.S.
    J. Biol. Chem. 277:28051-28057(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCF1, SUBCELLULAR LOCATION.
  11. "Tumor necrosis factor receptor-associated factor (TRAF) 4 is a new binding partner for the p70S6 serine/threonine kinase."
    Fleckenstein D.S., Dirks W.G., Drexler H.G., Quentmeier H.
    Leuk. Res. 27:687-694(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPS6KB1.
  12. "TRAF4 acts as a silencer in TLR-mediated signaling through the association with TRAF6 and TRIF."
    Takeshita F., Ishii K.J., Kobiyama K., Kojima Y., Coban C., Sasaki S., Ishii N., Klinman D.M., Okuda K., Akira S., Suzuki K.
    Eur. J. Immunol. 35:2477-2485(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCF1; TICAM1; IRAK1 AND TRAF6, INDUCTION.
  13. "MEKK4 is an effector of the embryonic TRAF4 for JNK activation."
    Abell A.N., Johnson G.L.
    J. Biol. Chem. 280:35793-35796(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K4.
  14. "Subcellular targeting of oxidants during endothelial cell migration."
    Wu R.F., Xu Y.C., Ma Z., Nwariaku F.E., Sarosi G.A. Jr., Terada L.S.
    J. Cell Biol. 171:893-904(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  15. "TRAF4 is potently induced by TAp63 isoforms and localised according to differentiation in SCCHN."
    Gu X., Coates P.J., MacCallum S.F., Boldrup L., Sjostrom B., Nylander K.
    Cancer Biol. Ther. 6:1986-1990(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Tumor necrosis factor receptor-associated factor 4 is a dynamic tight junction-related shuttle protein involved in epithelium homeostasis."
    Kedinger V., Alpy F., Baguet A., Polette M., Stoll I., Chenard M.P., Tomasetto C., Rio M.C.
    PLoS ONE 3:E3518-E3518(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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: FUNCTION, INTERACTION WITH SMURF1, UBIQUITINATION.
  19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Solution structure of TRAF-type zinc finger domains from human TNF receptor-associated factor 4."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 101-248.

Entry informationi

Entry nameiTRAF4_HUMAN
AccessioniPrimary (citable) accession number: Q9BUZ4
Secondary accession number(s): O75615
, Q14848, Q2KJU4, Q2PJN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 132 of the entry and version 1 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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