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Q9BUZ4

- TRAF4_HUMAN

UniProt

Q9BUZ4 - TRAF4_HUMAN

Protein

TNF receptor-associated factor 4

Gene

TRAF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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.By similarity6 Publications

    Regions

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

    GO - Molecular functioni

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

    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

    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

    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 4PRO_0000056403Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Polyubiquitinated, leading to its proteasomal degradation.1 Publication

    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 Probable. 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 PublicationsCurated

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi114979. 54 interactions.
    DIPiDIP-40910N.
    IntActiQ9BUZ4. 13 interactions.
    MINTiMINT-107471.
    STRINGi9606.ENSP00000262395.

    Structurei

    Secondary structure

    1
    470
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BUZ4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini307 – 462156MATHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili277 – 30933Sequence AnalysisAdd
    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.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 3 TRAF-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

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

    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. 2 PublicationsVSP_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. 13 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

    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: October 1, 2014
    This is version 133 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