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P25942

- TNR5_HUMAN

UniProt

P25942 - TNR5_HUMAN

Protein

Tumor necrosis factor receptor superfamily member 5

Gene

CD40

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    Receptor for TNFSF5/CD40LG. Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion.

    GO - Molecular functioni

    1. antigen binding Source: Ensembl
    2. enzyme binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. receptor activity Source: ProtInc
    5. signal transducer activity Source: ProtInc
    6. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. B cell proliferation Source: UniProtKB
    2. cellular calcium ion homeostasis Source: BHF-UCL
    3. cellular response to lipopolysaccharide Source: Ensembl
    4. cellular response to mechanical stimulus Source: UniProtKB
    5. defense response to virus Source: Ensembl
    6. immune response-regulating cell surface receptor signaling pathway Source: Ensembl
    7. inflammatory response Source: ProtInc
    8. platelet activation Source: UniProtKB
    9. positive regulation of B cell proliferation Source: Ensembl
    10. positive regulation of Cdc42 GTPase activity Source: BHF-UCL
    11. positive regulation of endothelial cell apoptotic process Source: BHF-UCL
    12. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    13. positive regulation of interleukin-12 production Source: Ensembl
    14. positive regulation of isotype switching to IgG isotypes Source: Ensembl
    15. positive regulation of MAP kinase activity Source: BHF-UCL
    16. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
    17. positive regulation of protein kinase C signaling Source: BHF-UCL
    18. positive regulation of protein phosphorylation Source: BHF-UCL
    19. positive regulation of Rac GTPase activity Source: BHF-UCL
    20. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    21. positive regulation of tyrosine phosphorylation of Stat1 protein Source: BHF-UCL
    22. protein complex assembly Source: ProtInc
    23. regulation of immune response Source: Reactome
    24. regulation of immunoglobulin secretion Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor necrosis factor receptor superfamily member 5
    Alternative name(s):
    B-cell surface antigen CD40
    Bp50
    CD40L receptor
    CDw40
    CD_antigen: CD40
    Gene namesi
    Name:CD40
    Synonyms:TNFRSF5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11919. CD40.

    Subcellular locationi

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cytoplasm Source: Ensembl
    3. external side of plasma membrane Source: Ensembl
    4. extracellular space Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. integral component of plasma membrane Source: ProtInc
    7. intracellular membrane-bounded organelle Source: Ensembl
    8. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Immunodeficiency with hyper-IgM 3 (HIGM3) [MIM:606843]: A rare immunodeficiency syndrome characterized by normal or elevated serum IgM levels with absence of IgG, IgA, and IgE. It results in a profound susceptibility to bacterial infections.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti83 – 831C → R in HIGM3. 1 Publication
    Corresponds to variant rs28931586 [ dbSNP | Ensembl ].
    VAR_013628

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi606843. phenotype.
    Orphaneti101090. Hyper-IgM syndrome type 3.
    PharmGKBiPA36612.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20203 PublicationsAdd
    BLAST
    Chaini21 – 277257Tumor necrosis factor receptor superfamily member 5PRO_0000034559Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 37
    Disulfide bondi38 ↔ 51
    Disulfide bondi41 ↔ 59
    Disulfide bondi62 ↔ 77
    Disulfide bondi83 ↔ 103
    Disulfide bondi105 ↔ 119
    Disulfide bondi111 ↔ 116
    Disulfide bondi125 ↔ 143
    Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP25942.
    PaxDbiP25942.
    PRIDEiP25942.

    PTM databases

    PhosphoSiteiP25942.

    Miscellaneous databases

    PMAP-CutDBP25942.

    Expressioni

    Tissue specificityi

    B-cells and in primary carcinomas.

    Gene expression databases

    ArrayExpressiP25942.
    BgeeiP25942.
    CleanExiHS_CD40.
    GenevestigatoriP25942.

    Organism-specific databases

    HPAiCAB002495.
    HPA031567.
    HPA031568.

    Interactioni

    Subunit structurei

    Monomer and homodimer. The variant form found in the bladder carcinoma cell line Hu549 does not form homodimers. Interacts with TRAF1, TRAF2, TRAF3, TRAF5 and TRAF6. Interacts with TRAF6 and MAP3K8; the interaction is required for ERK activation.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TRAF3Q131143EBI-525714,EBI-357631
    TRAF6Q9Y4K32EBI-525714,EBI-359276

    Protein-protein interaction databases

    BioGridi107396. 42 interactions.
    DIPiDIP-3014N.
    IntActiP25942. 5 interactions.
    MINTiMINT-1505936.
    STRINGi9606.ENSP00000361359.

    Structurei

    Secondary structure

    1
    277
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 385
    Beta strandi64 – 674
    Beta strandi70 – 723
    Helixi85 – 873
    Beta strandi89 – 935
    Beta strandi102 – 1054
    Beta strandi109 – 1157
    Beta strandi119 – 1213
    Beta strandi234 – 2363
    Beta strandi258 – 2603

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CDFmodel-A24-144[»]
    1CZZX-ray2.70D/E250-258[»]
    1D00X-ray2.00I/J/K/L/M/N/O/P250-254[»]
    1FLLX-ray3.50X/Y246-266[»]
    1LB6X-ray1.80B230-236[»]
    3QD6X-ray3.50R/S/T/U21-190[»]
    ProteinModelPortaliP25942.
    SMRiP25942. Positions 21-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25942.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 193173ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini216 – 27762CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei194 – 21522HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati25 – 6036TNFR-Cys 1Add
    BLAST
    Repeati61 – 10343TNFR-Cys 2Add
    BLAST
    Repeati104 – 14441TNFR-Cys 3Add
    BLAST
    Repeati145 – 18743TNFR-Cys 4Add
    BLAST

    Sequence similaritiesi

    Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG28193.
    HOVERGENiHBG005117.
    InParanoidiP25942.
    KOiK03160.
    OMAiEKCHPWT.
    OrthoDBiEOG786H2Q.
    PhylomeDBiP25942.
    TreeFamiTF331157.

    Family and domain databases

    InterProiIPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR020435. TNFR_5.
    [Graphical view]
    PfamiPF00020. TNFR_c6. 1 hit.
    [Graphical view]
    PRINTSiPR01922. TNFACTORR5.
    SMARTiSM00208. TNFR. 4 hits.
    [Graphical view]
    PROSITEiPS00652. TNFR_NGFR_1. 1 hit.
    PS50050. TNFR_NGFR_2. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform I (identifier: P25942-1) [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

    MVRLPLQCVL WGCLLTAVHP EPPTACREKQ YLINSQCCSL CQPGQKLVSD    50
    CTEFTETECL PCGESEFLDT WNRETHCHQH KYCDPNLGLR VQQKGTSETD 100
    TICTCEEGWH CTSEACESCV LHRSCSPGFG VKQIATGVSD TICEPCPVGF 150
    FSNVSSAFEK CHPWTSCETK DLVVQQAGTN KTDVVCGPQD RLRALVVIPI 200
    IFGILFAILL VLVFIKKVAK KPTNKAPHPK QEPQEINFPD DLPGSNTAAP 250
    VQETLHGCQP VTQEDGKESR ISVQERQ 277
    Length:277
    Mass (Da):30,619
    Last modified:May 1, 1992 - v1
    Checksum:iBC8776EC2C4A5680
    GO
    Isoform II (identifier: P25942-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         166-203: SCETKDLVVQ...ALVVIPIIFG → RSPGSAESPG...YQKGGQEANQ
         204-277: Missing.

    Show »
    Length:203
    Mass (Da):22,259
    Checksum:i07399D5F79D59A4F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti112 – 1121T → A in BAD96616. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261C → Q in bladder carcinoma cell line Hu549; requires 2 nucleotide substitutions. 1 Publication
    VAR_039301
    Natural varianti35 – 351S → G in bladder carcinoma cell line Hu549. 1 Publication
    VAR_039302
    Natural varianti39 – 391S → T in bladder carcinoma cell line Hu549. 1 Publication
    VAR_039303
    Natural varianti83 – 831C → R in HIGM3. 1 Publication
    Corresponds to variant rs28931586 [ dbSNP | Ensembl ].
    VAR_013628
    Natural varianti124 – 1241S → L.1 Publication
    Corresponds to variant rs11569321 [ dbSNP | Ensembl ].
    VAR_018751
    Natural varianti227 – 2271P → A.1 Publication
    Corresponds to variant rs11086998 [ dbSNP | Ensembl ].
    VAR_018752

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei166 – 20338SCETK…PIIFG → RSPGSAESPGGDPHHLRDPV CHPLGAGLYQKGGQEANQ in isoform II. 1 PublicationVSP_006472Add
    BLAST
    Alternative sequencei204 – 27774Missing in isoform II. 1 PublicationVSP_006473Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60592 mRNA. Translation: CAA43045.1.
    AJ300189 mRNA. Translation: CAC29424.1.
    BT019901 mRNA. Translation: AAV38704.1.
    AK222896 mRNA. Translation: BAD96616.1.
    AY504960 Genomic DNA. Translation: AAR84238.1.
    EF064754 Genomic DNA. Translation: ABK41937.1.
    AL035662 Genomic DNA. Translation: CAC17670.1.
    AL035662 Genomic DNA. Translation: CAI42973.1.
    CH471077 Genomic DNA. Translation: EAW75758.1.
    CH471077 Genomic DNA. Translation: EAW75760.1.
    CH471077 Genomic DNA. Translation: EAW75762.1.
    BC012419 mRNA. Translation: AAH12419.1.
    AY225405 mRNA. Translation: AAO43990.1.
    CCDSiCCDS13393.1. [P25942-1]
    CCDS13394.1. [P25942-2]
    PIRiB60771.
    S04460. A60771.
    RefSeqiNP_001241.1. NM_001250.4. [P25942-1]
    NP_690593.1. NM_152854.2. [P25942-2]
    UniGeneiHs.472860.

    Genome annotation databases

    EnsembliENST00000372276; ENSP00000361350; ENSG00000101017. [P25942-2]
    ENST00000372285; ENSP00000361359; ENSG00000101017. [P25942-1]
    GeneIDi958.
    KEGGihsa:958.
    UCSCiuc002xrf.1. human. [P25942-2]
    uc002xrg.1. human. [P25942-1]

    Polymorphism databases

    DMDMi116000.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    CD40base

    CD40 mutation db

    NIEHS-SNPs
    Wikipedia

    CD40 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60592 mRNA. Translation: CAA43045.1 .
    AJ300189 mRNA. Translation: CAC29424.1 .
    BT019901 mRNA. Translation: AAV38704.1 .
    AK222896 mRNA. Translation: BAD96616.1 .
    AY504960 Genomic DNA. Translation: AAR84238.1 .
    EF064754 Genomic DNA. Translation: ABK41937.1 .
    AL035662 Genomic DNA. Translation: CAC17670.1 .
    AL035662 Genomic DNA. Translation: CAI42973.1 .
    CH471077 Genomic DNA. Translation: EAW75758.1 .
    CH471077 Genomic DNA. Translation: EAW75760.1 .
    CH471077 Genomic DNA. Translation: EAW75762.1 .
    BC012419 mRNA. Translation: AAH12419.1 .
    AY225405 mRNA. Translation: AAO43990.1 .
    CCDSi CCDS13393.1. [P25942-1 ]
    CCDS13394.1. [P25942-2 ]
    PIRi B60771.
    S04460. A60771.
    RefSeqi NP_001241.1. NM_001250.4. [P25942-1 ]
    NP_690593.1. NM_152854.2. [P25942-2 ]
    UniGenei Hs.472860.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CDF model - A 24-144 [» ]
    1CZZ X-ray 2.70 D/E 250-258 [» ]
    1D00 X-ray 2.00 I/J/K/L/M/N/O/P 250-254 [» ]
    1FLL X-ray 3.50 X/Y 246-266 [» ]
    1LB6 X-ray 1.80 B 230-236 [» ]
    3QD6 X-ray 3.50 R/S/T/U 21-190 [» ]
    ProteinModelPortali P25942.
    SMRi P25942. Positions 21-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107396. 42 interactions.
    DIPi DIP-3014N.
    IntActi P25942. 5 interactions.
    MINTi MINT-1505936.
    STRINGi 9606.ENSP00000361359.

    Chemistry

    BindingDBi P25942.
    ChEMBLi CHEMBL1250358.
    DrugBanki DB00641. Simvastatin.
    GuidetoPHARMACOLOGYi 1874.

    PTM databases

    PhosphoSitei P25942.

    Polymorphism databases

    DMDMi 116000.

    Proteomic databases

    MaxQBi P25942.
    PaxDbi P25942.
    PRIDEi P25942.

    Protocols and materials databases

    DNASUi 958.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372276 ; ENSP00000361350 ; ENSG00000101017 . [P25942-2 ]
    ENST00000372285 ; ENSP00000361359 ; ENSG00000101017 . [P25942-1 ]
    GeneIDi 958.
    KEGGi hsa:958.
    UCSCi uc002xrf.1. human. [P25942-2 ]
    uc002xrg.1. human. [P25942-1 ]

    Organism-specific databases

    CTDi 958.
    GeneCardsi GC20P044746.
    HGNCi HGNC:11919. CD40.
    HPAi CAB002495.
    HPA031567.
    HPA031568.
    MIMi 109535. gene.
    606843. phenotype.
    neXtProti NX_P25942.
    Orphaneti 101090. Hyper-IgM syndrome type 3.
    PharmGKBi PA36612.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG28193.
    HOVERGENi HBG005117.
    InParanoidi P25942.
    KOi K03160.
    OMAi EKCHPWT.
    OrthoDBi EOG786H2Q.
    PhylomeDBi P25942.
    TreeFami TF331157.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

    Miscellaneous databases

    EvolutionaryTracei P25942.
    GeneWikii CD40_(protein).
    GenomeRNAii 958.
    NextBioi 3990.
    PMAP-CutDB P25942.
    PROi P25942.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25942.
    Bgeei P25942.
    CleanExi HS_CD40.
    Genevestigatori P25942.

    Family and domain databases

    InterProi IPR001368. TNFR/NGFR_Cys_rich_reg.
    IPR020435. TNFR_5.
    [Graphical view ]
    Pfami PF00020. TNFR_c6. 1 hit.
    [Graphical view ]
    PRINTSi PR01922. TNFACTORR5.
    SMARTi SM00208. TNFR. 4 hits.
    [Graphical view ]
    PROSITEi PS00652. TNFR_NGFR_1. 1 hit.
    PS50050. TNFR_NGFR_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A B-lymphocyte activation molecule related to the nerve growth factor receptor and induced by cytokines in carcinomas."
      Stamenkovic I., Clark E.A., Seed B.
      EMBO J. 8:1403-1410(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
    2. "Regulation of CD40 function by its isoforms generated through alternative splicing."
      Tone M., Tone Y., Fairchild P.J., Wykes M., Waldmann H.
      Proc. Natl. Acad. Sci. U.S.A. 98:1751-1756(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
      Tissue: Kidney.
    5. NIEHS SNPs program
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-124 AND ALA-227.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 I).
      Tissue: Ovary.
    10. "Transcripts of CD40 isoform in peripheral mononuclear cells."
      He X., Xu L., Zeng Y.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-223 (ISOFORM I).
      Tissue: Leukocyte.
    11. "Biochemical characteristics and partial amino acid sequence of the receptor-like human B cell and carcinoma antigen CDw40."
      Braesch-Andersen S., Paulie S., Koho H., Nika H., Aspenstroem P., Perlmann P.
      J. Immunol. 142:562-567(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-50, SUBUNIT, VARIANTS GLN-26; GLY-35 AND THR-39.
      Tissue: Lymphoma and Urinary bladder carcinoma.
    12. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-35.
    13. "Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells."
      Khandekar S.S., Silverman C., Wells-Marani J., Bacon A.M., Birrell H., Brigham-Burke M., DeMarini D.J., Jonak Z.L., Camilleri P., Fishman-Lobell J.
      Protein Expr. Purif. 23:301-310(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-30.
    14. "A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40."
      Sato T., Irie S., Reed J.C.
      FEBS Lett. 358:113-118(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF3.
    15. "Involvement of CRAF1, a relative of TRAF, in CD40 signaling."
      Cheng G., Cleary A.M., Ye Z.S., Hong D.I., Lederman S., Baltimore D.
      Science 267:1494-1498(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF3.
    16. "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 TRAF1; TRAF2; TRAF3 AND TRAF5.
    17. "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: INTERACTION WITH TRAF5.
    18. "Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates extracellular signal-regulated kinase (ERK) activity in CD40 signaling along a ras-independent pathway."
      Kashiwada M., Shirakata Y., Inoue J., Nakano H., Okazaki K., Okumura K., Yamamoto T., Nagaoka H., Takemori T.
      J. Exp. Med. 187:237-244(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF6.
    19. "Construction and analysis of a detailed three-dimensional model of the ligand binding domain of the human B cell receptor CD40."
      Bajorath J., Aruffo A.
      Proteins 27:59-70(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 24-144.
    20. "The role of polar interactions in the molecular recognition of CD40L with its receptor CD40."
      Singh J., Garber E., van Vlijmen H., Karpsusas M., Hsu Y.-M., Zheng Z., Naismith J.H., Thomas D.
      Protein Sci. 7:1124-1135(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 26-186 IN COMPLEX WITH CD40LG.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 247-266 IN COMPLEX WITH TRAF3.
    22. "Downstream regulator TANK binds to the CD40 recognition site on TRAF3."
      Li C., Ni C.Z., Havert M.L., Cabezas E., He J., Kaiser D., Reed J.C., Satterthwait A.C., Cheng G., Ely K.R.
      Structure 10:403-411(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 178-195 IN COMPLEX WITH TRAF3.
    23. Cited for: VARIANT HIGM3 ARG-83.

    Entry informationi

    Entry nameiTNR5_HUMAN
    AccessioniPrimary (citable) accession number: P25942
    Secondary accession number(s): E1P5S9
    , Q53GN5, Q5JY15, Q5U007, Q7M4Q8, Q86YK5, Q9BYU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 173 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3