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P29965

- CD40L_HUMAN

UniProt

P29965 - CD40L_HUMAN

Protein

CD40 ligand

Gene

CD40LG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL-4. Involved in immunoglobulin class switching.1 Publication
    Release of soluble CD40L from platelets is partially regulated by GP IIb/IIIa, actin polymerization, and an matrix metalloproteinases (MMP) inhibitor-sensitive pathway.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei112 – 1132Cleavage

    GO - Molecular functioni

    1. CD40 receptor binding Source: UniProtKB

    GO - Biological processi

    1. B cell differentiation Source: Ensembl
    2. B cell proliferation Source: UniProtKB
    3. immunoglobulin secretion Source: Ensembl
    4. inflammatory response Source: UniProtKB
    5. isotype switching Source: UniProtKB
    6. leukocyte cell-cell adhesion Source: UniProtKB
    7. negative regulation of apoptotic process Source: UniProtKB
    8. platelet activation Source: UniProtKB
    9. positive regulation of endothelial cell apoptotic process Source: BHF-UCL
    10. positive regulation of interleukin-12 production Source: UniProtKB
    11. regulation of immune response Source: Reactome
    12. regulation of immunoglobulin secretion Source: Ensembl

    Keywords - Molecular functioni

    Cytokine

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CD40 ligand
    Short name:
    CD40-L
    Alternative name(s):
    T-cell antigen Gp39
    TNF-related activation protein
    Short name:
    TRAP
    Tumor necrosis factor ligand superfamily member 5
    CD_antigen: CD154
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CD40LG
    Synonyms:CD40L, TNFSF5, TRAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11935. CD40LG.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular space Source: UniProtKB-KW
    3. integral component of membrane Source: UniProtKB
    4. integral component of plasma membrane Source: ProtInc
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    X-linked immunodeficiency with hyper-IgM 1 (HIGM1) [MIM:308230]: Immunoglobulin isotype switch defect characterized by elevated concentrations of serum IgM and decreased amounts of all other isotypes. Affected males present at an early age (usually within the first year of life) recurrent bacterial and opportunistic infections, including Pneumocystis carinii pneumonia and intractable diarrhea due to cryptosporidium infection. Despite substitution treatment with intravenous immunoglobulin, the overall prognosis is rather poor, with a death rate of about 10% before adolescence.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361M → R in HIGM1. 2 Publications
    VAR_007513
    Natural varianti38 – 381G → R in HIGM1. 1 Publication
    VAR_017925
    Natural varianti116 – 1161G → R in HIGM1.
    VAR_017929
    Natural varianti116 – 1161G → S in HIGM1. 1 Publication
    VAR_017930
    Natural varianti123 – 1231A → E in HIGM1. 1 Publication
    VAR_007514
    Natural varianti125 – 1251H → R in HIGM1. 1 Publication
    VAR_017926
    Natural varianti126 – 1261V → A in HIGM1. 1 Publication
    VAR_007515
    Natural varianti126 – 1261V → D in HIGM1.
    VAR_017931
    Natural varianti128 – 1292SE → RG in HIGM1.
    VAR_007516
    Natural varianti140 – 1401W → C in HIGM1. 1 Publication
    VAR_007517
    Natural varianti140 – 1401W → G in HIGM1. 1 Publication
    VAR_007518
    Natural varianti140 – 1401W → R in HIGM1. 1 Publication
    VAR_007519
    Natural varianti143 – 1431K → T in HIGM1.
    VAR_017932
    Natural varianti144 – 1441G → E in HIGM1. 1 Publication
    VAR_007520
    Natural varianti147 – 1471T → N in HIGM1. 1 Publication
    VAR_017922
    Natural varianti155 – 1551L → P in HIGM1. 2 Publications
    VAR_007521
    Natural varianti170 – 1701Y → C in HIGM1. 1 Publication
    VAR_017923
    Natural varianti173 – 1731A → D in HIGM1.
    VAR_017933
    Natural varianti174 – 1741Q → R in HIGM1. 1 Publication
    VAR_017927
    Natural varianti176 – 1761T → I in HIGM1.
    VAR_017934
    Natural varianti195 – 1951L → P in HIGM1.
    VAR_017935
    Natural varianti208 – 2081A → D in HIGM1.
    VAR_017936
    Natural varianti211 – 2111T → N in HIGM1. 1 Publication
    VAR_007522
    Natural varianti224 – 2241H → Y in HIGM1.
    VAR_017937
    Natural varianti226 – 2261G → A in HIGM1.
    VAR_017938
    Natural varianti227 – 2271G → V in HIGM1. 3 Publications
    VAR_007524
    Natural varianti227 – 2271Missing in HIGM1. 1 Publication
    VAR_007525
    Natural varianti231 – 2311L → S in HIGM1. 2 Publications
    VAR_007526
    Natural varianti235 – 2351A → P in HIGM1. 2 Publications
    VAR_007527
    Natural varianti237 – 2371V → E in HIGM1. 1 Publication
    VAR_017939
    Natural varianti254 – 2541T → M in HIGM1. 2 Publications
    VAR_007528
    Natural varianti257 – 2571G → D in HIGM1.
    VAR_017940
    Natural varianti257 – 2571G → S in HIGM1. 1 Publication
    VAR_017928
    Natural varianti258 – 2581L → S in HIGM1. 1 Publication
    VAR_017924

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi308230. phenotype.
    Orphaneti101088. X-linked hyper-IgM syndrome.
    PharmGKBiPA36626.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261CD40 ligand, membrane formPRO_0000034484Add
    BLAST
    Chaini113 – 261149CD40 ligand, soluble formPRO_0000034485Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi178 ↔ 218Sequence Analysis
    Glycosylationi240 – 2401N-linked (GlcNAc...) (high mannose and complex)CAR_000229

    Post-translational modificationi

    The soluble form derives from the membrane form by proteolytic processing.1 Publication
    N-linked glycan is a mixture of high mannose and complex type. Glycan structure does not influence binding affinity to CD40.
    Not O-glycosylated.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP29965.
    PaxDbiP29965.
    PRIDEiP29965.

    PTM databases

    PhosphoSiteiP29965.
    UniCarbKBiP29965.

    Miscellaneous databases

    PMAP-CutDBP29965.

    Expressioni

    Tissue specificityi

    Specifically expressed on activated CD4+ T-lymphocytes.

    Gene expression databases

    ArrayExpressiP29965.
    BgeeiP29965.
    CleanExiHS_CD40LG.
    GenevestigatoriP29965.

    Organism-specific databases

    HPAiHPA045827.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    BioGridi107397. 10 interactions.
    DIPiDIP-3013N.
    STRINGi9606.ENSP00000359663.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi123 – 1286
    Beta strandi132 – 1343
    Beta strandi140 – 1423
    Beta strandi153 – 1564
    Turni157 – 1593
    Beta strandi160 – 1656
    Beta strandi167 – 17913
    Turni181 – 1833
    Beta strandi186 – 19510
    Beta strandi203 – 2119
    Beta strandi218 – 23215
    Beta strandi237 – 2426
    Helixi244 – 2463
    Beta strandi251 – 26010

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ALYX-ray2.00A116-261[»]
    1I9RX-ray3.10A/B/C116-261[»]
    3LKJX-ray2.50A/B/C121-261[»]
    3QD6X-ray3.50A/B/C/D/E/F116-261[»]
    ProteinModelPortaliP29965.
    SMRiP29965. Positions 116-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29965.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini47 – 261215ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei23 – 4624Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tumor necrosis factor family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG39330.
    HOGENOMiHOG000111291.
    HOVERGENiHBG079629.
    InParanoidiP29965.
    KOiK03161.
    OMAiFLITQMI.
    OrthoDBiEOG7ZPNKR.
    PhylomeDBiP29965.
    TreeFamiTF332169.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR021184. TNF_CS.
    IPR006052. TNF_dom.
    IPR003263. TNF_ligand_5.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF00229. TNF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016527. TNF_5. 1 hit.
    PRINTSiPR01702. CD40LIGAND.
    SMARTiSM00207. TNF. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.
    PROSITEiPS00251. TNF_1. 1 hit.
    PS50049. TNF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29965-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIETYNQTSP RSAATGLPIS MKIFMYLLTV FLITQMIGSA LFAVYLHRRL    50
    DKIEDERNLH EDFVFMKTIQ RCNTGERSLS LLNCEEIKSQ FEGFVKDIML 100
    NKEETKKENS FEMQKGDQNP QIAAHVISEA SSKTTSVLQW AEKGYYTMSN 150
    NLVTLENGKQ LTVKRQGLYY IYAQVTFCSN REASSQAPFI ASLCLKSPGR 200
    FERILLRAAN THSSAKPCGQ QSIHLGGVFE LQPGASVFVN VTDPSQVSHG 250
    TGFTSFGLLK L 261
    Length:261
    Mass (Da):29,274
    Last modified:April 1, 1993 - v1
    Checksum:i16F5CEB093BCC2BB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361M → R in HIGM1. 2 Publications
    VAR_007513
    Natural varianti38 – 381G → R in HIGM1. 1 Publication
    VAR_017925
    Natural varianti116 – 1161G → R in HIGM1.
    VAR_017929
    Natural varianti116 – 1161G → S in HIGM1. 1 Publication
    VAR_017930
    Natural varianti123 – 1231A → E in HIGM1. 1 Publication
    VAR_007514
    Natural varianti125 – 1251H → R in HIGM1. 1 Publication
    VAR_017926
    Natural varianti126 – 1261V → A in HIGM1. 1 Publication
    VAR_007515
    Natural varianti126 – 1261V → D in HIGM1.
    VAR_017931
    Natural varianti128 – 1292SE → RG in HIGM1.
    VAR_007516
    Natural varianti140 – 1401W → C in HIGM1. 1 Publication
    VAR_007517
    Natural varianti140 – 1401W → G in HIGM1. 1 Publication
    VAR_007518
    Natural varianti140 – 1401W → R in HIGM1. 1 Publication
    VAR_007519
    Natural varianti143 – 1431K → T in HIGM1.
    VAR_017932
    Natural varianti144 – 1441G → E in HIGM1. 1 Publication
    VAR_007520
    Natural varianti147 – 1471T → N in HIGM1. 1 Publication
    VAR_017922
    Natural varianti155 – 1551L → P in HIGM1. 2 Publications
    VAR_007521
    Natural varianti170 – 1701Y → C in HIGM1. 1 Publication
    VAR_017923
    Natural varianti173 – 1731A → D in HIGM1.
    VAR_017933
    Natural varianti174 – 1741Q → R in HIGM1. 1 Publication
    VAR_017927
    Natural varianti176 – 1761T → I in HIGM1.
    VAR_017934
    Natural varianti195 – 1951L → P in HIGM1.
    VAR_017935
    Natural varianti208 – 2081A → D in HIGM1.
    VAR_017936
    Natural varianti211 – 2111T → N in HIGM1. 1 Publication
    VAR_007522
    Natural varianti219 – 2191G → R.1 Publication
    Corresponds to variant rs148594123 [ dbSNP | Ensembl ].
    VAR_007523
    Natural varianti224 – 2241H → Y in HIGM1.
    VAR_017937
    Natural varianti226 – 2261G → A in HIGM1.
    VAR_017938
    Natural varianti227 – 2271G → V in HIGM1. 3 Publications
    VAR_007524
    Natural varianti227 – 2271Missing in HIGM1. 1 Publication
    VAR_007525
    Natural varianti231 – 2311L → S in HIGM1. 2 Publications
    VAR_007526
    Natural varianti235 – 2351A → P in HIGM1. 2 Publications
    VAR_007527
    Natural varianti237 – 2371V → E in HIGM1. 1 Publication
    VAR_017939
    Natural varianti254 – 2541T → M in HIGM1. 2 Publications
    VAR_007528
    Natural varianti257 – 2571G → D in HIGM1.
    VAR_017940
    Natural varianti257 – 2571G → S in HIGM1. 1 Publication
    VAR_017928
    Natural varianti258 – 2581L → S in HIGM1. 1 Publication
    VAR_017924

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68550 mRNA. Translation: CAA48554.1.
    Z15017 mRNA. Translation: CAA78737.1.
    X67878 mRNA. Translation: CAA48077.1.
    L07414 mRNA. Translation: AAA35662.1.
    D31797 Genomic DNA. Translation: BAA06599.1.
    BC071754 mRNA. Translation: AAH71754.1.
    BC074950 mRNA. Translation: AAH74950.1.
    CCDSiCCDS14659.1.
    PIRiS28017. I53476.
    RefSeqiNP_000065.1. NM_000074.2.
    UniGeneiHs.592244.

    Genome annotation databases

    EnsembliENST00000370629; ENSP00000359663; ENSG00000102245.
    GeneIDi959.
    KEGGihsa:959.
    UCSCiuc004faa.3. human.

    Polymorphism databases

    DMDMi231718.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    CD40Lbase

    CD40L defect database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68550 mRNA. Translation: CAA48554.1 .
    Z15017 mRNA. Translation: CAA78737.1 .
    X67878 mRNA. Translation: CAA48077.1 .
    L07414 mRNA. Translation: AAA35662.1 .
    D31797 Genomic DNA. Translation: BAA06599.1 .
    BC071754 mRNA. Translation: AAH71754.1 .
    BC074950 mRNA. Translation: AAH74950.1 .
    CCDSi CCDS14659.1.
    PIRi S28017. I53476.
    RefSeqi NP_000065.1. NM_000074.2.
    UniGenei Hs.592244.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ALY X-ray 2.00 A 116-261 [» ]
    1I9R X-ray 3.10 A/B/C 116-261 [» ]
    3LKJ X-ray 2.50 A/B/C 121-261 [» ]
    3QD6 X-ray 3.50 A/B/C/D/E/F 116-261 [» ]
    ProteinModelPortali P29965.
    SMRi P29965. Positions 116-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107397. 10 interactions.
    DIPi DIP-3013N.
    STRINGi 9606.ENSP00000359663.

    Chemistry

    DrugBanki DB01076. Atorvastatin.

    PTM databases

    PhosphoSitei P29965.
    UniCarbKBi P29965.

    Polymorphism databases

    DMDMi 231718.

    Proteomic databases

    MaxQBi P29965.
    PaxDbi P29965.
    PRIDEi P29965.

    Protocols and materials databases

    DNASUi 959.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370629 ; ENSP00000359663 ; ENSG00000102245 .
    GeneIDi 959.
    KEGGi hsa:959.
    UCSCi uc004faa.3. human.

    Organism-specific databases

    CTDi 959.
    GeneCardsi GC0XP135730.
    GeneReviewsi CD40LG.
    HGNCi HGNC:11935. CD40LG.
    HPAi HPA045827.
    MIMi 300386. gene.
    308230. phenotype.
    neXtProti NX_P29965.
    Orphaneti 101088. X-linked hyper-IgM syndrome.
    PharmGKBi PA36626.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39330.
    HOGENOMi HOG000111291.
    HOVERGENi HBG079629.
    InParanoidi P29965.
    KOi K03161.
    OMAi FLITQMI.
    OrthoDBi EOG7ZPNKR.
    PhylomeDBi P29965.
    TreeFami TF332169.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P29965.
    GeneWikii CD154.
    GenomeRNAii 959.
    NextBioi 3996.
    PMAP-CutDB P29965.
    PROi P29965.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29965.
    Bgeei P29965.
    CleanExi HS_CD40LG.
    Genevestigatori P29965.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR021184. TNF_CS.
    IPR006052. TNF_dom.
    IPR003263. TNF_ligand_5.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00229. TNF. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016527. TNF_5. 1 hit.
    PRINTSi PR01702. CD40LIGAND.
    SMARTi SM00207. TNF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS00251. TNF_1. 1 hit.
    PS50049. TNF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The human T cell antigen gp39, a member of the TNF gene family, is a ligand for the CD40 receptor: expression of a soluble form of gp39 with B cell co-stimulatory activity."
      Hollenbaugh D., Grosmaire L.S., Kullas C.D., Chalupny J.N., Braesch-Andersen S., Noelle R.J., Stamenkovic I., Ledbetter J.A., Aruffo A.
      EMBO J. 11:4313-4321(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The CD40 ligand, gp39, is defective in activated T cells from patients with X-linked hyper-IgM syndrome."
      Aruffo A., Farrington M., Hollenbaugh D., Li X., Milatovich A., Nonoyama S., Bajorath J., Grosmaire L.S., Stenkamp R., Neubauer M., Roberts R.L., Noelle R.J., Ledbetter J.A., Francke U., Ochs H.D.
      Cell 72:291-300(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIGM1 128-ARG-GLY-129 AND PRO-235.
    4. "Recombinant human CD40 ligand stimulates B cell proliferation and immunoglobulin E secretion."
      Spriggs M.K., Armitage R.J., Strockbine L., Clifford K.N., Macduff B.M., Sato T.A., Maliszewski C.R., Fanslow W.C.
      J. Exp. Med. 176:1543-1550(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Human CD40-ligand: molecular cloning, cellular distribution and regulation of expression by factors controlling IgE production."
      Gauchat J.-F., Aubry J.-P., Mazzei G.J., Life P., Jomotte T., Elson G., Bonnefoy J.-Y.
      FEBS Lett. 315:259-266(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Structural organization of the gene for CD40 ligand: molecular analysis for diagnosis of X-linked hyper-IgM syndrome."
      Shimadzu M., Nunoi H., Terasaki H., Ninomiya R., Iwata M., Kanegasaka S., Matsuda I.
      Biochim. Biophys. Acta 1260:67-72(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "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: Blood.
    8. "Human native soluble CD40L is a biologically active trimer, processed inside microsomes."
      Pietravalle F., Lecoanet-Henchoz S., Blasey H., Aubry J.-P., Elson G., Edgerton M.D., Bonnefoy J.-Y., Gauchat J.-F.
      J. Biol. Chem. 271:5965-5967(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 113-117, PROTEOLYTIC PROCESSING.
    9. "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: STRUCTURE OF CARBOHYDRATE ON ASN-240, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Release of soluble CD40L from platelets is regulated by glycoprotein IIb/IIIa and actin polymerization."
      Furman M.I., Krueger L.A., Linden M.D., Barnard M.R., Frelinger A.L. III, Michelson A.D.
      J. Am. Coll. Cardiol. 43:2319-2325(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "2-A crystal structure of an extracellular fragment of human CD40 ligand."
      Karpsusas M., Hsu Y.-M., Wang J.-H., Thompson J., Lederman S., Chess L., Thomas D.
      Structure 3:1031-1039(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 116-261.
    12. "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 COMPLEX WITH CD40.
    13. "Defective expression of T-cell CD40 ligand causes X-linked immunodeficiency with hyper-IgM."
      Korthaeuer U., Graf D., Mages H.W., Briere F., Padayachee M., Malcolm S., Ugazio A.G., Notarangelo L.D., Levinsky R.J., Kroczek R.A.
      Nature 361:539-541(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIGM1 ARG-36 AND GLY-140.
    14. "CD40 ligand mutations in X-linked immunodeficiency with hyper-IgM."
      Disanto J.P., Bonnefoy J.-Y., Gauchat J.-F., Fischer A., de Saint Basile G.
      Nature 361:541-543(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HIGM1 GLU-123.
    15. Cited for: VARIANTS HIGM1 PRO-155; ASN-211 AND VAL-227.
    16. "Characterization of nine novel mutations in the CD40 ligand gene in patients with X-linked hyper IgM syndrome of various ancestry."
      Macchi P., Villa A., Strina D., Sacco M.G., Morali F., Brugnoni D., Giliani S., Mantuano E., Fasth A., Andersson B., Zegers B.J.M., Cavagni G., Reznick I., Levy J., Zan-Bar I., Porat Y., Airo P., Plebani A., Vezzoni P., Notarangelo L.D.
      Am. J. Hum. Genet. 56:898-906(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIGM1 ALA-126; ARG-140 AND GLU-144.
    17. "Signaling through CD40 rescues IgE but not IgG or IgA secretion in X-linked immunodeficiency with hyper-IgM."
      Saiki O., Tanaka T., Wada Y., Uda H., Inoue A., Katada Y., Izeki M., Iwata M., Nunoi H., Matsuda I.
      J. Clin. Invest. 95:510-514(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HIGM1 GLU-237.
    18. "Mutation analysis in CD40 ligand deficiency leading to X-linked hypogammaglobulinemia with hyper IgM syndrome."
      Katz F., Hinshelwood S., Rutland P., Jones A., Kinnon C., Morgan G.
      Hum. Mutat. 8:223-228(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIGM1 ARG-38; ARG-125; ARG-174 AND SER-257.
    19. "A single strand conformation polymorphism study of CD40 ligand. Efficient mutation analysis and carrier detection for X-linked hyper IgM syndrome."
      Lin Q., Rohrer J., Allen R.C., Larche M., Greene J.M., Shigeoka A.O., Gatti R.A., Derauf D.C., Belmont J.W., Conley M.E.
      J. Clin. Invest. 97:196-201(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIGM1 PRO-155 AND VAL-227, VARIANT ARG-219.
    20. "Mutations of the CD40 ligand gene in 13 Japanese patients with X-linked hyper-IgM syndrome."
      Nonoyama S., Shimadzu M., Toru H., Seyama K., Nunoi H., Neubauer M., Yata J., Och H.D.
      Hum. Genet. 99:624-627(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIGM1 ARG-36; CYS-140; GLY-227 DEL; SER-231 AND MET-254.
    21. "Mutations of the CD40 ligand gene and its effect on CD40 ligand expression in patients with X-linked hyper IgM syndrome."
      Seyama K., Nonoyama S., Gangsaas I., Hollenbaugh D., Pabst H.F., Aruffo A., Ochs H.D.
      Blood 92:2421-2434(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIGM1 SER-116; ASN-147; CYS-170; VAL-227; SER-231; PRO-235; MET-254 AND SER-258.

    Entry informationi

    Entry nameiCD40L_HUMAN
    AccessioniPrimary (citable) accession number: P29965
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    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 X
      Human chromosome X: 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

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