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O00463

- TRAF5_HUMAN

UniProt

O00463 - TRAF5_HUMAN

Protein

TNF receptor-associated factor 5

Gene

TRAF5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri45 – 8541RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri127 – 18155TRAF-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri182 – 23958TRAF-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. signal transducer activity Source: Ensembl
    3. thioesterase binding Source: UniProtKB
    4. ubiquitin protein ligase binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: InterPro
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. positive regulation of cell proliferation Source: Ensembl
    3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    5. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    6. regulation of apoptotic process Source: InterPro
    7. signal transduction Source: ProtInc

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiO00463.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TNF receptor-associated factor 5
    Alternative name(s):
    RING finger protein 84
    Gene namesi
    Name:TRAF5
    Synonyms:RNF84
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12035. TRAF5.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. centrosome Source: UniProtKB
    3. cytoplasm Source: HPA
    4. cytoplasmic side of plasma membrane Source: BHF-UCL
    5. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36712.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 557557TNF receptor-associated factor 5PRO_0000056405Add
    BLAST

    Proteomic databases

    MaxQBiO00463.
    PaxDbiO00463.
    PRIDEiO00463.

    PTM databases

    PhosphoSiteiO00463.

    Expressioni

    Tissue specificityi

    Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, and peripheral blood.

    Gene expression databases

    ArrayExpressiO00463.
    BgeeiO00463.
    CleanExiHS_TRAF5.
    GenevestigatoriO00463.

    Organism-specific databases

    HPAiCAB010277.
    HPA008052.

    Interactioni

    Subunit structurei

    Homotrimer Probable. Heteromer with TRAF3. Associates with TNFRSF5/CD40 through interaction with TRAF3. Associates with LTBR/TNFRSF3, TNFRSF4, TNFRSF8/CD30, TNFRSF11A/RANK, TNFRSF13B/TACI, TNFRSF14, TNFRSF17, TNFRSF19/TROY, RIPK2, MAP3K14, MAP3K5, and TRAF and TNF receptor associated protein TDP2. Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain).15 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SRSF1Q079552EBI-523498,EBI-398920
    TNFRSF14Q929565EBI-523498,EBI-1056653
    TRAF6Q9Y4K33EBI-523498,EBI-359276

    Protein-protein interaction databases

    BioGridi113040. 45 interactions.
    IntActiO00463. 24 interactions.
    MINTiMINT-1535869.
    STRINGi9606.ENSP00000261464.

    Structurei

    3D structure databases

    ProteinModelPortaliO00463.
    SMRiO00463. Positions 32-189, 346-556.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini403 – 549147MATHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni345 – 557213Interaction with EIF2AK2/PKRAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili237 – 342106Sequence AnalysisAdd
    BLAST

    Domaini

    The MATH/TRAF domain binds to receptor cytoplasmic domains.

    Sequence similaritiesi

    Contains 1 MATH domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 2 TRAF-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri45 – 8541RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri127 – 18155TRAF-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri182 – 23958TRAF-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG239194.
    HOVERGENiHBG058222.
    InParanoidiO00463.
    KOiK09849.
    OMAiIDKSAWL.
    OrthoDBiEOG7966G5.
    PhylomeDBiO00463.
    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.
    IPR027130. TRAF5.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    IPR001293. Znf_TRAF.
    [Graphical view]
    PANTHERiPTHR10131:SF66. PTHR10131:SF66. 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. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00463-1) [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

    MAYSEEHKGM PCGFIRQNSG NSISLDFEPS IEYQFVERLE ERYKCAFCHS    50
    VLHNPHQTGC GHRFCQHCIL SLRELNTVPI CPVDKEVIKS QEVFKDNCCK 100
    REVLNLYVYC SNAPGCNAKV ILGRYQDHLQ QCLFQPVQCS NEKCREPVLR 150
    KDLKEHLSAS CQFRKEKCLY CKKDVVVINL QNHEENLCPE YPVFCPNNCA 200
    KIILKTEVDE HLAVCPEAEQ DCPFKHYGCA VTDKRRNLQQ HEHSALREHM 250
    RLVLEKNVQL EEQISDLHKS LEQKESKIQQ LAETIKKLEK EFKQFAQLFG 300
    KNGSFLPNIQ VFASHIDKSA WLEAQVHQLL QMVNQQQNKF DLRPLMEAVD 350
    TVKQKITLLE NNDQRLAVLE EETNKHDTHI NIHKAQLSKN EERFKLLEGT 400
    CYNGKLIWKV TDYKMKKREA VDGHTVSIFS QSFYTSRCGY RLCARAYLNG 450
    DGSGRGSHLS LYFVVMRGEF DSLLQWPFRQ RVTLMLLDQS GKKNIMETFK 500
    PDPNSSSFKR PDGEMNIASG CPRFVAHSVL ENAKNAYIKD DTLFLKVAVD 550
    LTDLEDL 557
    Length:557
    Mass (Da):64,406
    Last modified:November 1, 1998 - v2
    Checksum:i86EB3724CE111176
    GO
    Isoform 2 (identifier: O00463-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         126-126: Q → QQVPLACCYLLQ

    Note: No experimental confirmation available.

    Show »
    Length:568
    Mass (Da):65,638
    Checksum:i6FDF94A0E03DA62A
    GO
    Isoform 3 (identifier: O00463-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         127-232: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:451
    Mass (Da):52,158
    Checksum:i82936A6A81BA59AF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti120 – 1201V → G.
    Corresponds to variant rs3946808 [ dbSNP | Ensembl ].
    VAR_052151
    Natural varianti186 – 1861N → H.
    Corresponds to variant rs2271458 [ dbSNP | Ensembl ].
    VAR_020117
    Natural varianti268 – 2681H → Y.1 Publication
    Corresponds to variant rs200398415 [ dbSNP | Ensembl ].
    VAR_071060
    Natural varianti358 – 3581L → V.
    Corresponds to variant rs2230780 [ dbSNP | Ensembl ].
    VAR_052152

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei126 – 1261Q → QQVPLACCYLLQ in isoform 2. 1 PublicationVSP_055449
    Alternative sequencei127 – 232106Missing in isoform 3. 1 PublicationVSP_055450Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000509 mRNA. Translation: BAA25262.1.
    AK295766 mRNA. Translation: BAG58591.1.
    AK303286 mRNA. Translation: BAG64364.1.
    CR536557 mRNA. Translation: CAG38794.1.
    AL590101 Genomic DNA. Translation: CAH72434.1.
    CH471100 Genomic DNA. Translation: EAW93420.1.
    CH471100 Genomic DNA. Translation: EAW93422.1.
    BC029600 mRNA. Translation: AAH29600.1.
    U69108 mRNA. Translation: AAC51329.1.
    CCDSiCCDS1497.1.
    PIRiJC6539.
    RefSeqiNP_001029082.1. NM_001033910.2.
    NP_004610.1. NM_004619.3.
    NP_665702.1. NM_145759.2.
    UniGeneiHs.523930.

    Genome annotation databases

    EnsembliENST00000261464; ENSP00000261464; ENSG00000082512. [O00463-1]
    ENST00000336184; ENSP00000336825; ENSG00000082512. [O00463-1]
    ENST00000367004; ENSP00000355971; ENSG00000082512. [O00463-1]
    GeneIDi7188.
    KEGGihsa:7188.
    UCSCiuc001hih.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000509 mRNA. Translation: BAA25262.1 .
    AK295766 mRNA. Translation: BAG58591.1 .
    AK303286 mRNA. Translation: BAG64364.1 .
    CR536557 mRNA. Translation: CAG38794.1 .
    AL590101 Genomic DNA. Translation: CAH72434.1 .
    CH471100 Genomic DNA. Translation: EAW93420.1 .
    CH471100 Genomic DNA. Translation: EAW93422.1 .
    BC029600 mRNA. Translation: AAH29600.1 .
    U69108 mRNA. Translation: AAC51329.1 .
    CCDSi CCDS1497.1.
    PIRi JC6539.
    RefSeqi NP_001029082.1. NM_001033910.2.
    NP_004610.1. NM_004619.3.
    NP_665702.1. NM_145759.2.
    UniGenei Hs.523930.

    3D structure databases

    ProteinModelPortali O00463.
    SMRi O00463. Positions 32-189, 346-556.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113040. 45 interactions.
    IntActi O00463. 24 interactions.
    MINTi MINT-1535869.
    STRINGi 9606.ENSP00000261464.

    PTM databases

    PhosphoSitei O00463.

    Proteomic databases

    MaxQBi O00463.
    PaxDbi O00463.
    PRIDEi O00463.

    Protocols and materials databases

    DNASUi 7188.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261464 ; ENSP00000261464 ; ENSG00000082512 . [O00463-1 ]
    ENST00000336184 ; ENSP00000336825 ; ENSG00000082512 . [O00463-1 ]
    ENST00000367004 ; ENSP00000355971 ; ENSG00000082512 . [O00463-1 ]
    GeneIDi 7188.
    KEGGi hsa:7188.
    UCSCi uc001hih.3. human.

    Organism-specific databases

    CTDi 7188.
    GeneCardsi GC01P211499.
    HGNCi HGNC:12035. TRAF5.
    HPAi CAB010277.
    HPA008052.
    MIMi 602356. gene.
    neXtProti NX_O00463.
    PharmGKBi PA36712.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239194.
    HOVERGENi HBG058222.
    InParanoidi O00463.
    KOi K09849.
    OMAi IDKSAWL.
    OrthoDBi EOG7966G5.
    PhylomeDBi O00463.
    TreeFami TF321154.

    Enzyme and pathway databases

    SignaLinki O00463.

    Miscellaneous databases

    ChiTaRSi TRAF5. human.
    GeneWikii TRAF5.
    GenomeRNAii 7188.
    NextBioi 28184.
    PROi O00463.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00463.
    Bgeei O00463.
    CleanExi HS_TRAF5.
    Genevestigatori O00463.

    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.
    IPR027130. TRAF5.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    IPR001293. Znf_TRAF.
    [Graphical view ]
    PANTHERi PTHR10131:SF66. PTHR10131:SF66. 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. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a cDNA encoding the human homolog of tumor necrosis factor receptor-associated factor 5 (TRAF5)."
      Mizushima S., Fujita M., Ishida T., Azuma S., Kato K., Hirai M., Otsuka M., Yamamoto T., Inoue J.
      Gene 207:135-140(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5; TNFRSF8 AND LTBR.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANT TYR-268.
      Tissue: Hippocampus and Thymus.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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: Testis.
    7. "Human TNF receptor-associated factor 5 (TRAF5): cDNA cloning, expression and assignment of the TRAF5 gene to chromosome 1q32."
      Nakano H., Shindo M., Yamada K., Yoshida M.C., Santee S.M., Ware C.F., Jenkins N.A., Gilbert D.J., Yagita H., Copeland N.G., Okumura K.
      Genomics 42:26-32(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-557 (ISOFORM 1).
    8. "The TNF-receptor-associated factor family: scaffold molecules for cytokine receptors, kinases and their regulators."
      Wajant H., Henkler F., Scheurich P.
      Cell. Signal. 13:389-400(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    9. "Tumor necrosis factor receptor-associated factors (TRAFs)."
      Bradley J.R., Pober J.S.
      Oncogene 20:6482-6491(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    10. "Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1."
      Marsters S.A., Ayres T.M., Skubatch M., Gray C.L., Rothe M., Ashkenazi A.
      J. Biol. Chem. 272:14029-14032(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF14.
    11. "ATAR, a novel tumor necrosis factor receptor family member, signals through TRAF2 and TRAF5."
      Hsu H., Solovyev I., Colombero A., Elliott R., Kelley M., Boyle W.J.
      J. Biol. Chem. 272:13471-13474(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF14.
    12. "Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2."
      Song H.Y., Regnier C.H., Kirschning C.J., Goeddel D.V., Rothe M.
      Proc. Natl. Acad. Sci. U.S.A. 94:9792-9796(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K14.
    13. "Tumor necrosis factor receptor-associated factor (TRAF) 5 and TRAF2 are involved in CD30-mediated NFkappaB activation."
      Aizawa S., Nakano H., Ishida T., Horie R., Nagai M., Ito K., Yagita H., Okumura K., Inoue J., Watanabe T.
      J. Biol. Chem. 272:2042-2045(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF8.
    14. Cited for: INTERACTION WITH MAP3K5.
    15. "CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions: regulation of CD40 signaling through multiple TRAF binding sites and TRAF hetero-oligomerization."
      Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J., Kehry M.R.
      Biochemistry 37:11836-11845(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF5 AND TRAF3.
    16. "Activation of OX40 signal transduction pathways leads to tumor necrosis factor receptor-associated factor (TRAF) 2- and TRAF5-mediated NF-kappaB activation."
      Kawamata S., Hori T., Imura A., Takaori-Kondo A., Uchiyama T.
      J. Biol. Chem. 273:5808-5814(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF4.
    17. "RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase."
      McCarthy J.V., Ni J., Dixit V.M.
      J. Biol. Chem. 273:16968-16975(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIPK2.
    18. "TAJ, a novel member of the tumor necrosis factor receptor family, activates the c-Jun N-terminal kinase pathway and mediates caspase-independent cell death."
      Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.
      J. Biol. Chem. 275:15336-15342(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF19.
    19. "The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor."
      Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.
      J. Biol. Chem. 273:28355-28359(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF11A.
    20. "TTRAP, a novel protein that associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that inhibits nuclear factor-kappa B activation."
      Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I., Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.
      J. Biol. Chem. 275:18586-18593(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TDP2.
    21. "TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation."
      Xia X.-Z., Treanor J., Senaldi G., Khare S.D., Boone T., Kelley M., Theill L.E., Colombero A., Solovyev I., Lee F., McCabe S., Elliott R., Miner K., Hawkins N., Guo J., Stolina M., Yu G., Wang J.
      , Delaney J., Meng S.-Y., Boyle W.J., Hsu H.
      J. Exp. Med. 192:137-143(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF13B.
    22. "B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1."
      Shu H.-B., Johnson H.
      Proc. Natl. Acad. Sci. U.S.A. 97:9156-9161(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF17.
    23. Cited for: FUNCTION, INTERACTION WITH EIF2AK2, SUBCELLULAR LOCATION.
    24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiTRAF5_HUMAN
    AccessioniPrimary (citable) accession number: O00463
    Secondary accession number(s): B4DIS9, B4E0A2, Q6FHY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3