Laminin, beta 1

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Available structures
PDBOrtholog search: PDBe RCSB
AliasesLAMB1, CLM, LIS5, Laminin, beta 1, laminin subunit beta 1
External IDsOMIM: 150240 MGI: 96743 HomoloGene: 1722 GeneCards: LAMB1
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for LAMB1
Genomic location for LAMB1
Band7q31.1Start107,923,799 bp[1]
End108,003,187 bp[1]
RNA expression pattern
PBB GE LAMB1 211651 s at fs.png

PBB GE LAMB1 201505 at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 7: 107.92 – 108 MbChr 12: 31.27 – 31.33 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene.[5][6][7][8]

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 are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they 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 1. The beta 1 chain has 7 structurally distinct domains, which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.[8]

5′-UTR of Laminin-B1 harbors IRES (internal ribosome entry site) between −293 and −1 upstream of the start codon. IRES are involved in cancer malignancy. [Petz 2011 [1]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000091136 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000002900 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Ikonen J, Pikkarainen T, Savolainen ER, Tryggvason K (Feb 1989). "A Hpa I polymorphism in the human laminin B1 chain gene on 7q22". Nucleic Acids Res. 17 (1): 473. doi:10.1093/nar/17.1.473. PMC 331592. PMID 2563160.
  6. ^ Roche KB, Moore JW, Surana RB, Wilson BE (May 1989). "Aortic root dilatation associated with partial trisomy 7(q31.2----qter)". Pediatr Cardiol. 10 (1): 53–5. doi:10.1007/BF02328637. PMID 2704655.
  7. ^ Bonneau D, Huret JL, Godeau G, Couet D, Putterman M, Tanzer J, Babin P, Larregue M (Sep 1991). "Recurrent ctb(7)(q31.3) and possible laminin involvement in a neonatal cutis laxa with a Marfan phenotype". Hum Genet. 87 (3): 317–9. doi:10.1007/bf00200911. PMID 1864606.
  8. ^ a b "Entrez Gene: LAMB1 laminin, beta 1".

Further reading[edit]