P25942 (TNR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CD40
Synonyms:	TNFRSF5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for TNFSF5/CD40LG.
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. 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
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B 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 mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB defense response to virus Inferred from electronic annotation. Source: Compara immune response-regulating cell surface receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of Cdc42 GTPase activity Inferred from mutant phenotype PubMed 21410936. Source: BHF-UCL positive regulation of I-kappaB kinase/NF-kappaB cascade 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: Compara positive regulation of isotype switching to IgG isotypes Inferred from electronic annotation. Source: Compara positive regulation of protein kinase C signaling cascade 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: Compara
Cellular_component	CD40 receptor complex Inferred from sequence or structural similarity. Source: BHF-UCL external side of plasma membrane Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular membrane-bounded organelle Inferred from electronic annotation. Source: Compara
Molecular_function	receptor activity Traceable author statement PubMed 10092834. Source: ProtInc signal transducer activity Traceable author statement PubMed 9671306. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRAF3	Q13114	3	EBI-525714,EBI-357631
TRAF6	Q9Y4K3	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.11 Ref.12 Ref.13

Chain

21 – 277

257

Tumor necrosis factor receptor superfamily member 5

PRO_0000034559

Regions

Topological domain

21 – 193

173

Extracellular Potential

Transmembrane

194 – 215

22

Helical; Potential

Topological domain

216 – 277

62

Cytoplasmic Potential

Repeat

25 – 60

36

TNFR-Cys 1

Repeat

61 – 103

43

TNFR-Cys 2

Repeat

104 – 144

41

TNFR-Cys 3

Repeat

145 – 187

43

TNFR-Cys 4

Amino acid modifications

Modified residue

272

1

Phosphoserine By similarity

Glycosylation

153

1

N-linked (GlcNAc...) Potential

Glycosylation

180

1

N-linked (GlcNAc...) Potential

Disulfide bond

26 ↔ 37

Disulfide bond

38 ↔ 51

Disulfide bond

41 ↔ 59

Disulfide bond

62 ↔ 77

Disulfide bond

83 ↔ 103

Disulfide bond

105 ↔ 119

Disulfide bond

111 ↔ 116

Disulfide bond

125 ↔ 143

Natural variations

Alternative sequence

166 – 203

38

SCETK…PIIFG → RSPGSAESPGGDPHHLRDPV CHPLGAGLYQKGGQEANQ in isoform II.

VSP_006472

Alternative sequence

204 – 277

74

Missing in isoform II.

VSP_006473

Natural variant

26

1

C → Q in bladder carcinoma cell line Hu549; requires 2 nucleotide substitutions. Ref.11

VAR_039301

Natural variant

35

1

S → G in bladder carcinoma cell line Hu549. Ref.11

VAR_039302

Natural variant

39

1

S → T in bladder carcinoma cell line Hu549. Ref.11

VAR_039303

Natural variant

83

1

C → R in HIGM3. Ref.23
Corresponds to variant rs28931586 [ dbSNP | Ensembl ].

VAR_013628

Natural variant

124

1

S → L. Ref.5
Corresponds to variant rs11569321 [ dbSNP | Ensembl ].

VAR_018751

Natural variant

227

1

P → A. Ref.5
Corresponds to variant rs11086998 [ dbSNP | Ensembl ].

VAR_018752

Experimental info

Sequence conflict

112

1

T → A in BAD96616. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

277

Helix Strand Turn

Details...

Beta strand

34 – 38

5

Beta strand

64 – 67

4

Beta strand

70 – 72

3

Helix

85 – 87

3

Beta strand

89 – 93

5

Beta strand

102 – 105

4

Beta strand

109 – 115

7

Beta strand

119 – 121

3

Beta strand

234 – 236

3

Beta strand

258 – 260

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform I [UniParc]. Last modified May 1, 1992. Version 1. Checksum: BC8776EC2C4A5680	FASTA	277	30,619
	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
	Isoform II [UniParc]. Checksum: 07399D5F79D59A4F	FASTA	203	22,259
	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 CHPWTRSPGS AESPGGDPHH 190 200 LRDPVCHPLG AGLYQKGGQE ANQ

References

	« Hide 'large scale' referencesShow '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. , 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. , 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

GeneReviews

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.

IPI

IPI00018282.
IPI00218464.

PIR

B60771.
A60771. S04460.

RefSeq

NP_001241.1. NM_001250.4.
NP_690593.1. NM_152854.2.

UniGene

Hs.472860.

3D structure databases

PDBe
RCSB PDB
PDBj

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	247-266	[»]
1LB6	X-ray	1.80	B	230-236	[»]
3QD6	X-ray	3.50	R/S/T/U	21-190	[»]

ProteinModelPortal

P25942.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3014N.
DIP-6221N.

IntAct

P25942. 5 interactions.

MINT

MINT-1505936.

STRING

9606.ENSP00000361359.

PTM databases

PhosphoSite

P25942.

Polymorphism databases

DMDM

116000.

Proteomic databases

PaxDb

P25942.

PRIDE

P25942.

Protocols and materials databases

DNASU

958.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000372276; ENSP00000361350; ENSG00000101017.
ENST00000372285; ENSP00000361359; ENSG00000101017.

GeneID

958.

KEGG

hsa:958.

UCSC

uc002xrf.1. human.
uc002xrg.1. human.

Organism-specific databases

CTD

958.

GeneCards

GC20P044746.

HGNC

HGNC:11919. CD40.

HPA

CAB002495.

MIM

109535. gene.
606843. phenotype.

neXtProt

NX_P25942.

Orphanet

101090. Hyper-IgM syndrome type 3.

PharmGKB

PA36612.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG28193.

HOVERGEN

HBG005117.

InParanoid

P25942.

KO

K03160.

OMA

EKCHPWT.

OrthoDB

EOG49PB0W.

PhylomeDB

P25942.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P25942.

Bgee

P25942.

CleanEx

HS_CD40.

Genevestigator

P25942.

GermOnline

ENSG00000101017. Homo sapiens.

Family and domain databases

InterPro

IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR020435. TNFR_5.
[Graphical view]

Pfam

PF00020. TNFR_c6. 1 hit.
[Graphical view]

PRINTS

PR01922. TNFACTORR5.

SMART

SM00208. TNFR. 4 hits.
[Graphical view]

PROSITE

PS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P25942.

ChEMBL

CHEMBL1250358.

DrugBank

DB00641. Simvastatin.

EvolutionaryTrace

P25942.

GenomeRNAi

958.

NextBio

3990.

PMAP-CutDB

P25942.

SOURCE

Search...

Entry information

Entry name

TNR5_HUMAN

Accession

Primary (citable) accession number: P25942
Secondary accession number(s): E1P5S9 , Q53GN5, Q5JY15, Q5U007, Q7M4Q8, Q86YK5, Q9BYU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 29, 2013
This is version 160 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.