Search
laminin beta-1 (laminin-B1, LAMB1)
Function:
- laminin-beta
- subunit of laminin-1 (EHS laminin), laminin-2 (merosin), & laminin-6 (K-laminin)
Structure:
- the alpha-helical domains I & II are thought to interact with other laminin chains to form a coiled coil structure
- domains VI & IV are globular
- contains 13 laminin EGF-like domains
- contains 1 laminin IV type B domain
- contains 1 laminin N-terminal domain
Compartment:
- secreted, extracellular space, extracellular matrix
- basement membrane, major component
General
laminin-beta (laminin B1)
Properties
SIZE: entity length = 1786 aa
MW = 198 kD
MOTIF: signal sequence {1-21}
Laminin N-terminal {31-270}
MOTIF: N-glycosylation site {N120}
EGF domain {271-334}
MOTIF: cysteine residue {C271}
MODIFICATION: cysteine residue {C280}
cysteine residue {C273}
MODIFICATION: cysteine residue {C298}
cysteine residue {C280}
MODIFICATION: cysteine residue {C271}
cysteine residue {C298}
MODIFICATION: cysteine residue {C273}
cysteine residue {C300}
MODIFICATION: cysteine residue {C309}
cysteine residue {C309}
MODIFICATION: cysteine residue {C300}
cysteine residue {C312}
MODIFICATION: cysteine residue {C332}
cysteine residue {C332}
MODIFICATION: cysteine residue {C312}
EGF domain {335-397}
MOTIF: cysteine residue {C335}
MODIFICATION: cysteine residue {C344}
cysteine residue {C337}
MODIFICATION: cysteine residue {C362}
cysteine residue {C344}
MODIFICATION: cysteine residue {C335}
N-glycosylation site {N356}
cysteine residue {C362}
MODIFICATION: cysteine residue {C337}
cysteine residue {C365}
MODIFICATION: cysteine residue {C374}
cysteine residue {C374}
MODIFICATION: cysteine residue {C365}
cysteine residue {C377}
MODIFICATION: cysteine residue {C395}
cysteine residue {C395}
MODIFICATION: cysteine residue {C377}
EGF domain {398-457}
MOTIF: cysteine residue {C398}
MODIFICATION: cysteine residue {C411}
cysteine residue {C400}
MODIFICATION: cysteine residue {C426}
cysteine residue {C411}
MODIFICATION: cysteine residue {C398}
cysteine residue {C426}
MODIFICATION: cysteine residue {C400}
cysteine residue {C428}
MODIFICATION: cysteine residue {C437}
cysteine residue {C437}
MODIFICATION: cysteine residue {C428}
cysteine residue {C440}
MODIFICATION: cysteine residue {C455}
cysteine residue {C455}
MODIFICATION: cysteine residue {C440}
EGF domain {458-509}
MOTIF: cysteine residue {C458}
MODIFICATION: cysteine residue {C472}
cysteine residue {C460}
MODIFICATION: cysteine residue {C479}
cysteine residue {C472}
MODIFICATION: cysteine residue {C458}
cysteine residue {C479}
MODIFICATION: cysteine residue {C460}
cysteine residue {C481}
MODIFICATION: cysteine residue {C490}
cysteine residue {C490}
MODIFICATION: cysteine residue {C481}
cysteine residue {C493}
MODIFICATION: cysteine residue {C507}
cysteine residue {C507}
MODIFICATION: cysteine residue {C493}
EGF domain {510-540}
MOTIF: cysteine residue {C510}
MODIFICATION: cysteine residue {C522}
cysteine residue {C512}
MODIFICATION: cysteine residue {C529}
N-glycosylation site {N519}
cysteine residue {C522}
MODIFICATION: cysteine residue {C510}
cysteine residue {C529}
MODIFICATION: cysteine residue {C512}
cysteine residue {C531}
MODIFICATION: cysteine residue {C540}
cysteine residue {C540}
MODIFICATION: cysteine residue {C531}
Laminin IV type B {549-767}
MOTIF: N-glycosylation site {N677}
EGF domain {773-820}
MOTIF: cysteine residue {C773}
MODIFICATION: cysteine residue {C785}
cysteine residue {C775}
MODIFICATION: cysteine residue {C792}
cysteine residue {C785}
MODIFICATION: cysteine residue {C773}
cysteine residue {C792}
MODIFICATION: cysteine residue {C775}
cysteine residue {C794}
MODIFICATION: cysteine residue {C803}
cysteine residue {C803}
MODIFICATION: cysteine residue {C794}
cysteine residue {C806}
MODIFICATION: cysteine residue {C818}
cysteine residue {C818}
MODIFICATION: cysteine residue {C806}
EGF domain {821-866}
MOTIF: cysteine residue {C821}
MODIFICATION: cysteine residue {C833}
cysteine residue {C823}
MODIFICATION: cysteine residue {C840}
cysteine residue {C833}
MODIFICATION: cysteine residue {C821}
cysteine residue {C840}
MODIFICATION: cysteine residue {C823}
cysteine residue {C842}
MODIFICATION: cysteine residue {C851}
cysteine residue {C851}
MODIFICATION: cysteine residue {C842}
cysteine residue {C854}
MODIFICATION: cysteine residue {C864}
cysteine residue {C864}
MODIFICATION: cysteine residue {C854}
EGF domain {867-916}
MOTIF: cysteine residue {C867}
MODIFICATION: cysteine residue {C876}
cysteine residue {C869}
MODIFICATION: cysteine residue {C883}
cysteine residue {C876}
MODIFICATION: cysteine residue {C867}
cysteine residue {C883}
MODIFICATION: cysteine residue {C869}
cysteine residue {C886}
MODIFICATION: cysteine residue {C895}
cysteine residue {C895}
MODIFICATION: cysteine residue {C886}
cysteine residue {C898}
MODIFICATION: cysteine residue {C914}
cysteine residue {C914}
MODIFICATION: cysteine residue {C898}
EGF domain {917-975}
MOTIF: cysteine residue {C917}
MODIFICATION: cysteine residue {C933}
cysteine residue {C919}
MODIFICATION: cysteine residue {C944}
cysteine residue {C933}
MODIFICATION: cysteine residue {C917}
cysteine residue {C944}
MODIFICATION: cysteine residue {C919}
cysteine residue {C946}
MODIFICATION: cysteine residue {C955}
cysteine residue {C955}
MODIFICATION: cysteine residue {C946}
cysteine residue {C958}
MODIFICATION: cysteine residue {C973}
cysteine residue {C973}
MODIFICATION: cysteine residue {C958}
EGF domain {976-1027}
MOTIF: cysteine residue {C976}
MODIFICATION: cysteine residue {C990}
cysteine residue {C978}
MODIFICATION: cysteine residue {C997}
cysteine residue {C990}
MODIFICATION: cysteine residue {C976}
cysteine residue {C997}
MODIFICATION: cysteine residue {C978}
cysteine residue {C1000}
MODIFICATION: cysteine residue {C1009}
cysteine residue {C1009}
MODIFICATION: cysteine residue {C1000}
cysteine residue {C1012}
MODIFICATION: cysteine residue {C1025}
cysteine residue {C1025}
MODIFICATION: cysteine residue {C1012}
EGF domain {1028-1083}
MOTIF: cysteine residue {C1028}
MODIFICATION: cysteine residue {C1040}
cysteine residue {C1030}
MODIFICATION: cysteine residue {C1054}
cysteine residue {C1040}
MODIFICATION: cysteine residue {C1028}
N-glycosylation site {N1041}
cysteine residue {C1054}
MODIFICATION: cysteine residue {C1030}
cysteine residue {C1056}
MODIFICATION: cysteine residue {C1065}
cysteine residue {C1065}
MODIFICATION: cysteine residue {C1056}
cysteine residue {C1068}
MODIFICATION: cysteine residue {C1081}
cysteine residue {C1081}
MODIFICATION: cysteine residue {C1068}
EGF domain {1084-1131}
MOTIF: cysteine residue {C1084}
MODIFICATION: cysteine residue {C1096}
cysteine residue {C1086}
MODIFICATION: cysteine residue {C1103}
cysteine residue {C1096}
MODIFICATION: cysteine residue {C1084}
cysteine residue {C1103}
MODIFICATION: cysteine residue {C1086}
cysteine residue {C1105}
MODIFICATION: cysteine residue {C1114}
cysteine residue {C1114}
MODIFICATION: cysteine residue {C1105}
cysteine residue {C1117}
MODIFICATION: cysteine residue {C1129}
cysteine residue {C1129}
MODIFICATION: cysteine residue {C1117}
EGF domain {1132-1178}
MOTIF: cysteine residue {C1132}
MODIFICATION: cysteine residue {C1144}
cysteine residue {C1134}
MODIFICATION: cysteine residue {C1151}
cysteine residue {C1144}
MODIFICATION: cysteine residue {C1132}
cysteine residue {C1151}
MODIFICATION: cysteine residue {C1134}
cysteine residue {C1153}
MODIFICATION: cysteine residue {C1162}
cysteine residue {C1162}
MODIFICATION: cysteine residue {C1153}
cysteine residue {C1165}
MODIFICATION: cysteine residue {C1176}
cysteine residue {C1176}
MODIFICATION: cysteine residue {C1165}
Domain II {1179-1397}
MOTIF: cysteine residue {C1179}
MODIFICATION: cysteine residue {C-INTERCHAIN}
cysteine residue {C1182}
MODIFICATION: cysteine residue {C-INTERCHAIN}
N-glycosylation site {N1195}
coiled coil {1216-1315}
N-glycosylation site {N1279}
N-glycosylation site {N1336}
N-glycosylation site {N1343}
coiled coil {1353-1388}
Domain alpha {1398-1430}
Domain I {1431-1786}
MOTIF: coiled coil {1442-1781}
N-glycosylation site {N1487}
N-glycosylation site {N1542}
cysteine residue {C1785}
MODIFICATION: cysteine residue {C-INTERCHAIN}
Database Correlations
OMIM 150240
UniProt P07942
PFAM correlations
Entrez Gene 3912
Kegg hsa:3912
References
- Molecular Cell Biology (2nd ed) Darnell J; Lodish H
& Baltimore D (eds), Scientific American Books,
WH Freeman, NY 1990, pg 920
- Schachner M, Martini R.
Glycans and the modulation of neural-recognition molecule function.
Trends Neurosci. 1995 Apr;18(4):183-91. Review.
PMID: 7539963
- Entrez Gene :accession 3912
- UniProt :accession P07942
Component-of
laminin-5