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O00463

- TRAF5_HUMAN

UniProt

O00463 - TRAF5_HUMAN

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Protein
TNF receptor-associated factor 5
Gene
TRAF5, RNF84
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 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-type
Add
BLAST
Zinc fingeri127 – 18155TRAF-type 1
Add
BLAST
Zinc fingeri182 – 23958TRAF-type 2
Add
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
Complete GO annotation...

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  3. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  4. positive regulation of cell proliferation Source: Ensembl
  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
Complete GO annotation...

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 Inferred. 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
Complete GO annotation...

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 5
PRO_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 Inferred. 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 Publications

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. 23 interactions.
MINTiMINT-1535869.
STRINGi9606.ENSP00000261464.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini403 – 549147MATH
Add
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili237 – 342106 Reviewed prediction
Add
BLAST

Domaini

The MATH/TRAF domain binds to receptor cytoplasmic domains.

Sequence similaritiesi

Contains 1 MATH domain.

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.
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.
VSP_055449
Alternative sequencei127 – 232106Missing in isoform 3.
VSP_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.
ENST00000336184; ENSP00000336825; ENSG00000082512.
ENST00000367004; ENSP00000355971; ENSG00000082512.
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...

Protein-protein interaction databases

BioGridi 113040. 45 interactions.
IntActi O00463. 23 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 .
ENST00000336184 ; ENSP00000336825 ; ENSG00000082512 .
ENST00000367004 ; ENSP00000355971 ; ENSG00000082512 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 142 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

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