Laminin, beta 3

LAMB3

Identifiers

LAMB3, BM600-125KDA, LAM5, LAMNB1, AI1A, Laminin, beta 3, laminin subunit beta 3, JEB1B, JEB1A

External IDs

OMIM: 150310 MGI: 99915 HomoloGene: 191 GeneCards: LAMB3

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1q32.2	Start	209,614,870 bp^[1]
Band	1q32.2	End	209,652,425 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)^[2]

Band	1 H6\|1 97.71 cM	Start	192,890,007 bp^[2]
Band	1 H6\|1 97.71 cM	End	193,026,186 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

periodontal fiber

jejunal mucosa

skin of abdomen

minor salivary gland

palpebral conjunctiva

islet of Langerhans

duodenum

upper lobe of left lung

lactiferous duct

cavity of mouth

Top expressed in

molar

epithelium of stomach

left colon

corneal stroma

left lung

mucous cell of stomach

right lung lobe

pyloric antrum

left lung lobe

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding structural molecule activity protein-containing complex binding extracellular matrix structural constituent
Cellular component	extracellular region basement membrane laminin-5 complex collagen-containing extracellular matrix laminin complex
Biological process	hemidesmosome assembly cell adhesion extracellular matrix organization endodermal cell differentiation brown fat cell differentiation epidermis development animal organ morphogenesis tissue development cell migration substrate adhesion-dependent cell spreading basement membrane assembly
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


3914


16780

Ensembl


ENSG00000196878


ENSMUSG00000026639

UniProt


Q13751


Q61087

RefSeq (mRNA)


NM_000228 NM_001017402 NM_001127641


NM_001277928 NM_008484

RefSeq (protein)


NP_000219 NP_001017402 NP_001121113


NP_001264857 NP_032510

Location (UCSC)

Chr 1: 209.61 – 209.65 Mb

Chr 1: 192.89 – 193.03 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Laminin subunit beta-3 is a protein that in humans is encoded by the LAMB3 gene.^[5]^[6]^[7]

LAMB3 encodes the beta 3 subunit of laminin. Laminin is composed of three subunits (alpha, beta, and gamma), and refers to a family of basement membrane proteins. For example, LAMB3 serves as the beta chain in laminin-5. Mutations in LAMB3 have been identified as the cause of various types of epidermolysis bullosa. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.^[7]

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References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000196878 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026639 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Vailly J, Szepetowski P, Mattei MG, Pedeutour F, Burgeson R, Ortonne JP, Meneguzzi G (Oct 1994). "The genes for nicein/kalinin 125- and 100-kDa subunits, candidates for junctional epidermolysis bullosa, map to chromosomes 1q32 and 1q25-q31". Genomics. 21 (1): 286–8. doi:10.1006/geno.1994.1263. PMID 8088808.
^ Pulkkinen L, Gerecke DR, Christiano AM, Wagman DW, Burgeson RE, Uitto J (Jul 1995). "Cloning of the beta 3 chain gene (LAMB3) of human laminin 5, a candidate gene in junctional epidermolysis bullosa". Genomics. 25 (1): 192–8. doi:10.1016/0888-7543(95)80125-6. PMID 7774918.
^ ^a ^b "Entrez Gene: LAMB3 laminin, beta 3".

Gerecke DR, Wagman DW, Champliaud MF, Burgeson RE (1994). "The complete primary structure for a novel laminin chain, the laminin B1k chain". J. Biol. Chem. 269 (15): 11073–80. doi:10.1016/S0021-9258(19)78093-4. PMID 7512558.
Pulkkinen L, McGrath JA, Christiano AM, Uitto J (1995). "Detection of sequence variants in the gene encoding the beta 3 chain of laminin 5 (LAMB3)". Hum. Mutat. 6 (1): 77–84. doi:10.1002/humu.1380060115. PMID 7550237. S2CID 42814229.
McGrath JA, Gatalica B, Christiano AM, et al. (1995). "Mutations in the 180-kD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa". Nat. Genet. 11 (1): 83–6. doi:10.1038/ng0995-83. PMID 7550320. S2CID 23732185.
Pulkkinen L, Christiano AM, Gerecke D, et al. (1995). "A homozygous nonsense mutation in the beta 3 chain gene of laminin 5 (LAMB3) in Herlitz junctional epidermolysis bullosa". Genomics. 24 (2): 357–60. doi:10.1006/geno.1994.1627. PMID 7698759.
McGrath JA, Pulkkinen L, Christiano AM, et al. (1995). "Altered laminin 5 expression due to mutations in the gene encoding the beta 3 chain (LAMB3) in generalized atrophic benign epidermolysis bullosa". J. Invest. Dermatol. 104 (4): 467–74. doi:10.1111/1523-1747.ep12605904. PMID 7706760.
Rousselle P, Golbik R, van der Rest M, Aumailley M (1995). "Structural requirement for cell adhesion to kalinin (laminin-5)". J. Biol. Chem. 270 (23): 13766–70. doi:10.1074/jbc.270.23.13766. PMID 7775432.
Morishima Y, Ariyama T, Yamanishi K, et al. (1996). "Chromosomal loci of 50 human keratinocyte cDNAs assigned by fluorescence in situ hybridization". Genomics. 28 (2): 273–9. doi:10.1006/geno.1995.1141. PMID 8530036.
Kivirikko S, McGrath JA, Pulkkinen L, et al. (1996). "Mutational hotspots in the LAMB3 gene in the lethal (Herlitz) type of junctional epidermolysis bullosa". Hum. Mol. Genet. 5 (2): 231–7. doi:10.1093/hmg/5.2.231. PMID 8824879.
Ashton GH, Mellerio JE, Dunnill MG, et al. (1997). "A recurrent laminin 5 mutation in British patients with lethal (Herlitz) junctional epidermolysis bullosa: evidence for a mutational hotspot rather than propagation of an ancestral allele". Br. J. Dermatol. 136 (5): 674–7. doi:10.1111/j.1365-2133.1997.tb03650.x. PMID 9205497.
Pulkkinen L, Meneguzzi G, McGrath JA, et al. (1997). "Predominance of the recurrent mutation R635X in the LAMB3 gene in European patients with Herlitz junctional epidermolysis bullosa has implications for mutation detection strategy". J. Invest. Dermatol. 109 (2): 232–7. doi:10.1111/1523-1747.ep12319752. PMID 9242513.
Takizawa Y, Shimizu H, Pulkkinen L, et al. (1998). "Novel mutations in the LAMB3 gene shared by two Japanese unrelated families with Herlitz junctional epidermolysis bullosa, and their application for prenatal testing". J. Invest. Dermatol. 110 (2): 174–8. doi:10.1046/j.1523-1747.1998.00105.x. PMID 9457915.
Posteraro P, Sorvillo S, Gagnoux-Palacios L, et al. (1998). "Compound heterozygosity for an out-of-frame deletion and a splice site mutation in the LAMB3 gene causes nonlethal junctional epidermolysis bullosa". Biochem. Biophys. Res. Commun. 243 (3): 758–64. doi:10.1006/bbrc.1998.8180. PMID 9501007.
Takizawa Y, Pulkkinen L, Shimizu H, et al. (1998). "Maternal uniparental meroisodisomy in the LAMB3 region of chromosome 1 results in lethal junctional epidermolysis bullosa". J. Invest. Dermatol. 110 (5): 828–31. doi:10.1046/j.1523-1747.1998.00186.x. PMID 9579554.
Mellerio JE, Eady RA, Atherton DJ, et al. (1999). "E210K mutation in the gene encoding the beta3 chain of laminin-5 (LAMB3) is predictive of a phenotype of generalized atrophic benign epidermolysis bullosa". Br. J. Dermatol. 139 (2): 325–31. doi:10.1046/j.1365-2133.1998.02377.x. PMID 9767254. S2CID 32996449.
Aho S, Uitto J (1999). "Two-hybrid analysis reveals multiple direct interactions for thrombospondin 1". Matrix Biol. 17 (6): 401–12. doi:10.1016/S0945-053X(98)90100-7. PMID 9840442.
Pulkkinen L, Uitto J (1999). "Heterozygosity for premature termination codon mutations in LAMB3 in siblings with non-lethal junctional epidermolysis bullosa". J. Invest. Dermatol. 111 (6): 1244–6. doi:10.1046/j.1523-1747.1998.00399.x. PMID 9856855.
Chen M, Marinkovich MP, Jones JC, et al. (1999). "NC1 domain of type VII collagen binds to the beta3 chain of laminin 5 via a unique subdomain within the fibronectin-like repeats". J. Invest. Dermatol. 112 (2): 177–83. doi:10.1046/j.1523-1747.1999.00491.x. PMID 9989793.
Floeth M, Bruckner-Tuderman L (2000). "Digenic junctional epidermolysis bullosa: mutations in COL17A1 and LAMB3 genes". Am. J. Hum. Genet. 65 (6): 1530–7. doi:10.1086/302672. PMC 1288363. PMID 10577906.

Protein: scleroproteins

Extracellular
matrix

Collagen

Fibril forming	type I COL1A1 COL1A2 type II (COL2A1) type III type V COL5A1 COL5A2 COL5A3 COL24A1 COL26A1
Other	FACIT: type IX COL9A1 COL9A2 COL9A3 type XII (COL12A1) COL14A1 COL16A1 COL19A1 COL20A1 COL21A1 COL22A1 basement membrane: type IV COL4A1 COL4A2 COL4A3 COL4A4 COL4A5 COL4A6 multiplexin: COL15A1 type XVIII COL18A1 Endostatin transmembrane: COL13A1 COL17A1 COL23A1 COL25A1 other: type VI COL6A1 COL6A2 COL6A3 COL6A5 type VII (COL7A1) type VIII COL8A1 COL8A2 type X (COL10A1) type XI COL11A1 COL11A2 COL27A1 COL28A1
Enzymes	Prolyl hydroxylase/Lysyl hydroxylase Cartilage associated protein/Leprecan ADAMTS2 Procollagen peptidase Lysyl oxidase

Laminin

alpha
- LAMA1
- LAMA2
- LAMA3
- LAMA4
- LAMA5
beta
- LAMB1
- LAMB2
- LAMB3
- LAMB4
gamma
- LAMC1
- LAMC2
- LAMC3

Other

See also: diseases

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

This page was last edited on 29 January 2023, at 23:05

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References

Further reading