Version 5.4
Homo sapiens Gene: LAMB2
Summary
InnateDB Gene IDBG-34423.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol LAMB2
Gene Name laminin, beta 2 (laminin S)
Synonyms LAMS; NPHS5
Species Homo sapiens
Ensembl Gene ENSG00000172037
Encoded Proteins
IDBP-34425
laminin, beta 2 (laminin S)
IDBP-377052
laminin, beta 2 (laminin S)
IDBP-584665
laminin, beta 2 (laminin S)
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 2. The beta 2 chain contains the 7 structural domains typical of beta chains of laminin, including the short alpha region. However, unlike beta 1 chain, beta 2 has a more restricted tissue distribution. It is enriched in the basement membrane of muscles at the neuromuscular junctions, kidney glomerulus and vascular smooth muscle. Transgenic mice in which the beta 2 chain gene was inactivated by homologous recombination, showed defects in the maturation of neuromuscular junctions and impairment of glomerular filtration. Alternative splicing involving a non consensus 5' splice site (gc) in the 5' UTR of this gene has been reported. It was suggested that inefficient splicing of this first intron, which does not change the protein sequence, results in a greater abundance of the unspliced form of the transcript than the spliced form. The full-length nature of the spliced transcript is not known. [provided by RefSeq, Aug 2011]
Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 2. The beta 2 chain contains the 7 structural domains typical of beta chains of laminin, including the short alpha region. However, unlike beta 1 chain, beta 2 has a more restricted tissue distribution. It is enriched in the basement membrane of muscles at the neuromuscular junctions, kidney glomerulus and vascular smooth muscle. Transgenic mice in which the beta 2 chain gene was inactivated by homologous recombination, showed defects in the maturation of neuromuscular junctions and impairment of glomerular filtration. Alternative splicing involving a non consensus 5\' splice site (gc) in the 5\' UTR of this gene has been reported. It was suggested that inefficient splicing of this first intron, which does not change the protein sequence, results in a greater abundance of the unspliced form of the transcript than the spliced form. The full-length nature of the spliced transcript is not known. [provided by RefSeq, Aug 2011]
Gene Information
Type Protein coding
Genomic Location Chromosome 3:49121114-49133118
Strand Reverse strand
Band p21.31
Transcripts
ENST00000305544 ENSP00000307156
ENST00000418109 ENSP00000388325
ENST00000467506
ENST00000484713
ENST00000498377
ENST00000469665
ENST00000477225
ENST00000480640
ENST00000462930
ENST00000464891
ENST00000483057
ENST00000486298
ENST00000477701
ENST00000493571
ENST00000488638
ENST00000483321
ENST00000494831 ENSP00000444751
ENST00000538659
ENST00000542580
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 13 experimentally validated interaction(s) in this database.
Experimentally validated
Total 13 [view]
Protein-Protein 13 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0005178 integrin binding
GO:0005198 structural molecule activity
GO:0005515 protein binding
Biological Process
GO:0000904 cell morphogenesis involved in differentiation
GO:0007155 cell adhesion
GO:0007411 axon guidance
GO:0007528 neuromuscular junction development
GO:0007601 visual perception
GO:0014002 astrocyte development
GO:0014044 Schwann cell development
GO:0030198 extracellular matrix organization
GO:0031175 neuron projection development
GO:0048677 axon extension involved in regeneration
GO:0050808 synapse organization
GO:0060041 retina development in camera-type eye
GO:0072249 metanephric glomerular visceral epithelial cell development
GO:0072274 metanephric glomerular basement membrane development
Cellular Component
GO:0005576 extracellular region
GO:0005604 basement membrane
GO:0005605 basal lamina
GO:0005608 laminin-3 complex
GO:0031012 extracellular matrix
GO:0043256 laminin complex
GO:0043260 laminin-11 complex
GO:0045202 synapse
GO:0070062 extracellular vesicular exosome
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000052911
View Gene Order
ENSBTAG00000022635
Not yet available
Pathways
NETPATH
NetPath_1
Alpha6Beta4Integrin pathway
REACTOME
REACT_118779
Extracellular matrix organization pathway
REACT_163906
ECM proteoglycans pathway
REACT_163874
Non-integrin membrane-ECM interactions pathway
REACT_169262
Laminin interactions pathway
KEGG
hsa04512
ECM-receptor interaction pathway
hsa05222
Small cell lung cancer pathway
hsa04510
Focal adhesion pathway
hsa05200
Pathways in cancer pathway
hsa05146
Amoebiasis pathway
hsa05145
Toxoplasmosis pathway
INOH
PID NCI
integrin1_pathway
Beta1 integrin cell surface interactions
integrin4_pathway
Alpha6 beta4 integrin-ligand interactions
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Hs.439726
RefSeq NM_002292 XM_005265127
HUGO
OMIM
CCDS CCDS2789
HPRD 01034
IMGT
EMBL
GenPept
RNA Seq Atlas

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca