Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P25942 (TNR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 5
Alternative name(s):
B-cell surface antigen CD40
Bp50
CD40L receptor
CDw40
CD_antigen=CD40
Gene names
Name:CD40
Synonyms:TNFRSF5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Isoform I: Cell membrane; Single-pass type I membrane protein.

Isoform II: Secreted.

Tissue specificity

B-cells and in primary carcinomas.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Contains 4 TNFR-Cys repeats.

Ontologies

Keywords
   Biological processImmunity
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell proliferation

Non-traceable author statement PubMed 8605945. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

defense response to virus

Inferred from electronic annotation. Source: Ensembl

immune response-regulating cell surface receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement Ref.1. Source: ProtInc

platelet activation

Non-traceable author statement PubMed 9468137. Source: UniProtKB

positive regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of Cdc42 GTPase activity

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

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

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

positive regulation of Rac GTPase activity

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

positive regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 12885753. Source: BHF-UCL

positive regulation of interleukin-12 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of isotype switching to IgG isotypes

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase C signaling

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

positive regulation of tyrosine phosphorylation of Stat1 protein

Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL

protein complex assembly

Traceable author statement PubMed 10748139. Source: ProtInc

regulation of immune response

Traceable author statement. Source: Reactome

regulation of immunoglobulin secretion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentCD40 receptor complex

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

cytoplasm

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of plasma membrane

Traceable author statement PubMed 10748139. Source: ProtInc

intracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Ensembl

plasma membrane

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

   Molecular_functionantigen binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction PubMed 12223522. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 9468137. Source: UniProtKB

receptor activity

Traceable author statement PubMed 10092834. Source: ProtInc

signal transducer activity

Traceable author statement PubMed 9671306. Source: ProtInc

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRAF3Q131143EBI-525714,EBI-357631
TRAF6Q9Y4K32EBI-525714,EBI-359276

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform I (identifier: P25942-1)

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.
Isoform II (identifier: P25942-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.11 Ref.12 Ref.13
Chain21 – 277257Tumor necrosis factor receptor superfamily member 5
PRO_0000034559

Regions

Topological domain21 – 193173Extracellular Potential
Transmembrane194 – 21522Helical; Potential
Topological domain216 – 27762Cytoplasmic Potential
Repeat25 – 6036TNFR-Cys 1
Repeat61 – 10343TNFR-Cys 2
Repeat104 – 14441TNFR-Cys 3
Repeat145 – 18743TNFR-Cys 4

Amino acid modifications

Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 37
Disulfide bond38 ↔ 51
Disulfide bond41 ↔ 59
Disulfide bond62 ↔ 77
Disulfide bond83 ↔ 103
Disulfide bond105 ↔ 119
Disulfide bond111 ↔ 116
Disulfide bond125 ↔ 143

Natural variations

Alternative sequence166 – 20338SCETK…PIIFG → RSPGSAESPGGDPHHLRDPV CHPLGAGLYQKGGQEANQ in isoform II.
VSP_006472
Alternative sequence204 – 27774Missing in isoform II.
VSP_006473
Natural variant261C → Q in bladder carcinoma cell line Hu549; requires 2 nucleotide substitutions. Ref.11
VAR_039301
Natural variant351S → G in bladder carcinoma cell line Hu549. Ref.11
VAR_039302
Natural variant391S → T in bladder carcinoma cell line Hu549. Ref.11
VAR_039303
Natural variant831C → R in HIGM3. Ref.23
Corresponds to variant rs28931586 [ dbSNP | Ensembl ].
VAR_013628
Natural variant1241S → L. Ref.5
Corresponds to variant rs11569321 [ dbSNP | Ensembl ].
VAR_018751
Natural variant2271P → A. Ref.5
Corresponds to variant rs11086998 [ dbSNP | Ensembl ].
VAR_018752

Experimental info

Sequence conflict1121T → A in BAD96616. Ref.4

Secondary structure

..................... 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform I [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: BC8776EC2C4A5680

FASTA27730,619
        10         20         30         40         50         60 
MVRLPLQCVL WGCLLTAVHP EPPTACREKQ YLINSQCCSL CQPGQKLVSD CTEFTETECL 

        70         80         90        100        110        120 
PCGESEFLDT WNRETHCHQH KYCDPNLGLR VQQKGTSETD TICTCEEGWH CTSEACESCV 

       130        140        150        160        170        180 
LHRSCSPGFG VKQIATGVSD TICEPCPVGF FSNVSSAFEK CHPWTSCETK DLVVQQAGTN 

       190        200        210        220        230        240 
KTDVVCGPQD RLRALVVIPI IFGILFAILL VLVFIKKVAK KPTNKAPHPK QEPQEINFPD 

       250        260        270 
DLPGSNTAAP VQETLHGCQP VTQEDGKESR ISVQERQ 

« Hide

Isoform II [UniParc].

Checksum: 07399D5F79D59A4F
Show »

FASTA20322,259

References

« Hide 'large scale' references
[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]Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]"Molecular basis for CD40 signaling mediated by TRAF3."
Ni C.Z., Welsh K., Leo E., Chiou C.K., Wu H., Reed J.C., Ely K.R.
Proc. Natl. Acad. Sci. U.S.A. 97:10395-10399(2000) [PubMed] [Europe PMC] [Abstract]
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]"Mutations of CD40 gene cause an autosomal recessive form of immunodeficiency with hyper IgM."
Ferrari S., Giliani S., Insalaco A., Al-Ghonaium A., Soresina A.R., Loubser M., Avanzini M.A., Marconi M., Badolato R., Ugazio A.G., Levy Y., Catalan N., Durandy A., Tbakhi A., Notarangelo L.D., Plebani A.
Proc. Natl. Acad. Sci. U.S.A. 98:12614-12619(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIGM3 ARG-83.
+Additional computationally mapped references.

Web resources

CD40base

CD40 mutation db

NIEHS-SNPs
Wikipedia

CD40 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13393.1. [P25942-1]
CCDS13394.1. [P25942-2]
PIRB60771.
A60771. S04460.
RefSeqNP_001241.1. NM_001250.4. [P25942-1]
NP_690593.1. NM_152854.2. [P25942-2]
UniGeneHs.472860.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP25942.
SMRP25942. Positions 21-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107396. 42 interactions.
DIPDIP-3014N.
IntActP25942. 5 interactions.
MINTMINT-1505936.
STRING9606.ENSP00000361359.

Chemistry

BindingDBP25942.
ChEMBLCHEMBL1250358.
DrugBankDB00641. Simvastatin.
GuidetoPHARMACOLOGY1874.

PTM databases

PhosphoSiteP25942.

Polymorphism databases

DMDM116000.

Proteomic databases

MaxQBP25942.
PaxDbP25942.
PRIDEP25942.

Protocols and materials databases

DNASU958.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372276; ENSP00000361350; ENSG00000101017. [P25942-2]
ENST00000372285; ENSP00000361359; ENSG00000101017. [P25942-1]
GeneID958.
KEGGhsa:958.
UCSCuc002xrf.1. human. [P25942-2]
uc002xrg.1. human. [P25942-1]

Organism-specific databases

CTD958.
GeneCardsGC20P044746.
HGNCHGNC:11919. CD40.
HPACAB002495.
HPA031567.
HPA031568.
MIM109535. gene.
606843. phenotype.
neXtProtNX_P25942.
Orphanet101090. Hyper-IgM syndrome type 3.
PharmGKBPA36612.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG28193.
HOVERGENHBG005117.
InParanoidP25942.
KOK03160.
OMAEKCHPWT.
OrthoDBEOG786H2Q.
PhylomeDBP25942.
TreeFamTF331157.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP25942.
BgeeP25942.
CleanExHS_CD40.
GenevestigatorP25942.

Family and domain databases

InterProIPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020435. TNFR_5.
[Graphical view]
PfamPF00020. TNFR_c6. 1 hit.
[Graphical view]
PRINTSPR01922. TNFACTORR5.
SMARTSM00208. TNFR. 4 hits.
[Graphical view]
PROSITEPS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25942.
GeneWikiCD40_(protein).
GenomeRNAi958.
NextBio3990.
PMAP-CutDBP25942.
PROP25942.
SOURCESearch...

Entry information

Entry nameTNR5_HUMAN
AccessionPrimary (citable) accession number: P25942
Secondary accession number(s): E1P5S9 expand/collapse secondary AC list , Q53GN5, Q5JY15, Q5U007, Q7M4Q8, Q86YK5, Q9BYU0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries