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CD104 (integrin-beta 4, GP150, ITGB4)
Function:
- associates with integrin alpha 6 (integrin alpha-6/beta-4)
- signalling through the integrin beta-4 cytoplasmic domain may induce expression of p21WAF1/Cip1 [2]
Structure:
- the fibronectin type-III-like domains bind BPAG1 & plectin & probably also recruit BP230
- belongs to the integrin beta chain family
- contains 1 calx-beta domain
- contains 4 fibronectin F3 modules
- contains 1 VWFA domain
Compartment: membrane
Expression:
- thymocytes, epithelial cells
- isoform beta-4D is also expressed in colon & placenta
- isoform beta-4E is also expressed in epidermis, lung, duodenum, heart, spleen & stomach
Pathology:
- mutations associated with
- epidermolysis bullosa letalis with pyloric atresia (junctional epidermolysis bullosa with pyloric atresia or aplasia cutis congenita with gastrointestinal atresia)
- generalized atrophic benign epidermolysis bullosa
Interactions
molecular events
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
glycoprotein
integrin-beta
Properties
SIZE: entity length = 788 aa
MW = 87 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-26}
cysteine residue {C31}
MODIFICATION: cysteine residue {C461}
cysteine residue {C39}
MODIFICATION: cysteine residue {C49}
cysteine residue {C42}
MODIFICATION: cysteine residue {C75}
cysteine residue {C49}
MODIFICATION: cysteine residue {C39}
cysteine residue {C52}
MODIFICATION: cysteine residue {C64}
cysteine residue {C64}
MODIFICATION: cysteine residue {C52}
cysteine residue {C75}
MODIFICATION: cysteine residue {C42}
N-glycosylation site {N125}
VWFA domain {135-377}
MOTIF: cysteine residue {C203}
MODIFICATION: cysteine residue {C210}
cysteine residue {C210}
MODIFICATION: cysteine residue {C203}
cysteine residue {C258}
MODIFICATION: cysteine residue {C299}
cysteine residue {C299}
MODIFICATION: cysteine residue {C258}
N-glycosylation site {N346}
N-glycosylation site {N397}
cysteine residue {C400}
MODIFICATION: cysteine residue {C412}
cysteine residue {C412}
MODIFICATION: cysteine residue {C400}
cysteine residue {C432}
MODIFICATION: cysteine residue {C681}
cysteine residue {C459}
MODIFICATION: cysteine residue {C463}
cysteine residue {C461}
MODIFICATION: cysteine residue {C31}
Cysteine-rich tandem repeats {463-629}
MOTIF: consensus repeat {463-511}
cysteine residue {C463}
MODIFICATION: cysteine residue {C459}
cysteine residue {C474}
MODIFICATION: cysteine residue {C486}
N-glycosylation site {N478}
cysteine residue {C483}
MODIFICATION: cysteine residue {C521}
cysteine residue {C486}
MODIFICATION: cysteine residue {C474}
cysteine residue {C488}
MODIFICATION: cysteine residue {C497}
cysteine residue {C497}
MODIFICATION: cysteine residue {C488}
cysteine residue {C499}
MODIFICATION: cysteine residue {C512}
consensus repeat {512-553}
cysteine residue {C512}
MODIFICATION: cysteine residue {C499}
cysteine residue {C521}
MODIFICATION: cysteine residue {C483}
cysteine residue {C527}
MODIFICATION: cysteine residue {C532}
cysteine residue {C529}
MODIFICATION: cysteine residue {C562}
cysteine residue {C532}
MODIFICATION: cysteine residue {C527}
cysteine residue {C534}
MODIFICATION: cysteine residue {C547}
cysteine residue {C547}
MODIFICATION: cysteine residue {C534}
cysteine residue {C549}
MODIFICATION: cysteine residue {C554}
consensus repeat {554-592}
cysteine residue {C554}
MODIFICATION: cysteine residue {C549}
cysteine residue {C562}
MODIFICATION: cysteine residue {C529}
cysteine residue {C568}
MODIFICATION: cysteine residue {C573}
cysteine residue {C570}
MODIFICATION: cysteine residue {C601}
cysteine residue {C573}
MODIFICATION: cysteine residue {C568}
cysteine residue {C575}
MODIFICATION: cysteine residue {C584}
cysteine residue {C584}
MODIFICATION: cysteine residue {C575}
N-glycosylation site {N585}
cysteine residue {C586}
MODIFICATION: cysteine residue {C593}
consensus repeat {593-629}
cysteine residue {C593}
MODIFICATION: cysteine residue {C586}
cysteine residue {C601}
MODIFICATION: cysteine residue {C570}
cysteine residue {C607}
MODIFICATION: cysteine residue {C612}
cysteine residue {C609}
MODIFICATION: cysteine residue {C657}
cysteine residue {C612}
MODIFICATION: cysteine residue {C607}
cysteine residue {C614}
MODIFICATION: cysteine residue {C624}
cysteine residue {C624}
MODIFICATION: cysteine residue {C614}
cysteine residue {C627}
MODIFICATION: cysteine residue {C630}
cysteine residue {C630}
MODIFICATION: cysteine residue {C627}
cysteine residue {C634}
MODIFICATION: cysteine residue {C643}
cysteine residue {C640}
MODIFICATION: cysteine residue {C713}
cysteine residue {C643}
MODIFICATION: cysteine residue {C634}
cysteine residue {C657}
MODIFICATION: cysteine residue {C609}
cysteine residue {C661}
MODIFICATION: cysteine residue {C689}
N-glycosylation site {N680}
cysteine residue {C681}
MODIFICATION: cysteine residue {C432}
cysteine residue {C689}
MODIFICATION: cysteine residue {C661}
cysteine residue {C713}
MODIFICATION: cysteine residue {C640}
transmembrane domain {719-741}
Tyr phosphorylation site {Y773}
Thr phosphorylation site {T779}
Tyr phosphorylation site {Y785}
Database Correlations
OMIM correlations
MORBIDMAP 173470
UniProt P16144
PFAM correlations
Entrez Gene 3691
Kegg hsa:3690
References
- Clarke et al J Biol Chem 270:22673 1995
- Entrez Gene :accession 3691
- http://www.pathologyoutlines.com/cd100247.html
21 June 2005
- Uniprot :accession P16144
- GeneReviews
https://www.genecards.org/cgi-bin/carddisp.pl?gene=ITGB4
Component-of
molecular complex