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P29965

- CD40L_HUMAN

UniProt

P29965 - CD40L_HUMAN

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Protein

CD40 ligand

Gene

CD40LG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP29965.
CleanExiHS_CD40LG.
ExpressionAtlasiP29965. baseline.
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.
GeneTreeiENSGT00510000048489.
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

        10         20         30         40         50
MIETYNQTSP RSAATGLPIS MKIFMYLLTV FLITQMIGSA LFAVYLHRRL
60 70 80 90 100
DKIEDERNLH EDFVFMKTIQ RCNTGERSLS LLNCEEIKSQ FEGFVKDIML
110 120 130 140 150
NKEETKKENS FEMQKGDQNP QIAAHVISEA SSKTTSVLQW AEKGYYTMSN
160 170 180 190 200
NLVTLENGKQ LTVKRQGLYY IYAQVTFCSN REASSQAPFI ASLCLKSPGR
210 220 230 240 250
FERILLRAAN THSSAKPCGQ QSIHLGGVFE LQPGASVFVN VTDPSQVSHG
260
TGFTSFGLLK L
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.

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.
GeneTreei ENSGT00510000048489.
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

Bgeei P29965.
CleanExi HS_CD40LG.
ExpressionAtlasi P29965. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 174 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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