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O00463 (TRAF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TNF receptor-associated factor 5
Alternative name(s):
RING finger protein 84
Gene names
Name:TRAF5
Synonyms:RNF84
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.22

Subunit structure

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). Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Subcellular location

Cytoplasm Probable. Cytoplasmcytosol Ref.22.

Tissue specificity

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

Domain

The MATH/TRAF domain binds to receptor cytoplasmic domains.

Sequence similarities

Belongs to the TNF receptor-associated factor family. A subfamily.

Contains 1 MATH domain.

Contains 1 RING-type zinc finger.

Contains 2 TRAF-type zinc fingers.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.22. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 12296995. Source: BHF-UCL

regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentCD40 receptor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Inferred from direct assay Ref.22. Source: UniProtKB

   Molecular_functionsignal transducer activity

Inferred from electronic annotation. Source: Ensembl

thioesterase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557TNF receptor-associated factor 5
PRO_0000056405

Regions

Domain403 – 549147MATH
Zinc finger45 – 8541RING-type
Zinc finger127 – 18155TRAF-type 1
Zinc finger182 – 23958TRAF-type 2
Region345 – 557213Interaction with EIF2AK2/PKR
Coiled coil237 – 342106 Potential

Natural variations

Natural variant1201V → G.
Corresponds to variant rs3946808 [ dbSNP | Ensembl ].
VAR_052151
Natural variant1861N → H.
Corresponds to variant rs2271458 [ dbSNP | Ensembl ].
VAR_020117
Natural variant3581L → V.
Corresponds to variant rs2230780 [ dbSNP | Ensembl ].
VAR_052152

Sequences

Sequence LengthMass (Da)Tools
O00463 [UniParc].

Last modified November 1, 1998. Version 2.
Checksum: 86EB3724CE111176

FASTA55764,406
        10         20         30         40         50         60 
MAYSEEHKGM PCGFIRQNSG NSISLDFEPS IEYQFVERLE ERYKCAFCHS VLHNPHQTGC 

        70         80         90        100        110        120 
GHRFCQHCIL SLRELNTVPI CPVDKEVIKS QEVFKDNCCK REVLNLYVYC SNAPGCNAKV 

       130        140        150        160        170        180 
ILGRYQDHLQ QCLFQPVQCS NEKCREPVLR KDLKEHLSAS CQFRKEKCLY CKKDVVVINL 

       190        200        210        220        230        240 
QNHEENLCPE YPVFCPNNCA KIILKTEVDE HLAVCPEAEQ DCPFKHYGCA VTDKRRNLQQ 

       250        260        270        280        290        300 
HEHSALREHM RLVLEKNVQL EEQISDLHKS LEQKESKIQQ LAETIKKLEK EFKQFAQLFG 

       310        320        330        340        350        360 
KNGSFLPNIQ VFASHIDKSA WLEAQVHQLL QMVNQQQNKF DLRPLMEAVD TVKQKITLLE 

       370        380        390        400        410        420 
NNDQRLAVLE EETNKHDTHI NIHKAQLSKN EERFKLLEGT CYNGKLIWKV TDYKMKKREA 

       430        440        450        460        470        480 
VDGHTVSIFS QSFYTSRCGY RLCARAYLNG DGSGRGSHLS LYFVVMRGEF DSLLQWPFRQ 

       490        500        510        520        530        540 
RVTLMLLDQS GKKNIMETFK PDPNSSSFKR PDGEMNIASG CPRFVAHSVL ENAKNAYIKD 

       550 
DTLFLKVAVD LTDLEDL 

« Hide

References

« Hide 'large scale' references
[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], INTERACTION WITH TNFRSF5; TNFRSF8 AND LTBR.
[2]"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].
[3]"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. expand/collapse author list , 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].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Testis.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"ASK1 is essential for JNK/SAPK activation by TRAF2."
Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M., Miyazono K., Ichijo H.
Mol. Cell 2:389-395(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP3K5.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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. expand/collapse author list , 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.
[21]"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.
[22]"TRAF family proteins link PKR with NF-kappa B activation."
Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J., Nakano H., Alcami J., Esteban M.
Mol. Cell. Biol. 24:4502-4512(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EIF2AK2, SUBCELLULAR LOCATION.
[23]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB000509 mRNA. Translation: BAA25262.1.
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.
PIRJC6539.
RefSeqNP_001029082.1. NM_001033910.2.
NP_004610.1. NM_004619.3.
NP_665702.1. NM_145759.2.
UniGeneHs.523930.

3D structure databases

ProteinModelPortalO00463.
SMRO00463. Positions 32-219, 346-556.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113040. 45 interactions.
IntActO00463. 23 interactions.
MINTMINT-1535869.
STRING9606.ENSP00000261464.

PTM databases

PhosphoSiteO00463.

Proteomic databases

PaxDbO00463.
PRIDEO00463.

Protocols and materials databases

DNASU7188.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261464; ENSP00000261464; ENSG00000082512.
ENST00000336184; ENSP00000336825; ENSG00000082512.
ENST00000367004; ENSP00000355971; ENSG00000082512.
GeneID7188.
KEGGhsa:7188.
UCSCuc001hih.3. human.

Organism-specific databases

CTD7188.
GeneCardsGC01P211499.
HGNCHGNC:12035. TRAF5.
HPACAB010277.
HPA008052.
MIM602356. gene.
neXtProtNX_O00463.
PharmGKBPA36712.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239194.
HOVERGENHBG058222.
InParanoidO00463.
KOK09849.
OMAIDKSAWL.
OrthoDBEOG7966G5.
PhylomeDBO00463.
TreeFamTF321154.

Enzyme and pathway databases

SignaLinkO00463.

Gene expression databases

ArrayExpressO00463.
BgeeO00463.
CleanExHS_TRAF5.
GenevestigatorO00463.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.90.890.10. 1 hit.
InterProIPR002083. 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]
PANTHERPTHR10131:SF23. PTHR10131:SF23. 1 hit.
PfamPF00917. MATH. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PIRSFPIRSF015614. TRAF. 1 hit.
SMARTSM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49599. SSF49599. 3 hits.
PROSITEPS50144. MATH. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
PS50145. ZF_TRAF. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRAF5. human.
GeneWikiTRAF5.
GenomeRNAi7188.
NextBio28184.
PROO00463.
SOURCESearch...

Entry information

Entry nameTRAF5_HUMAN
AccessionPrimary (citable) accession number: O00463
Secondary accession number(s): Q6FHY1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM