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Details on Person UniProt:P07942 LAMB1
| Class:Id | ReferenceGeneProduct:58619 |
|---|---|
| _chainChangeLog | signal peptide:1-21 added on Fri February 6 2015;chain:22-1786 added on Fri February 6 2015 |
| _displayName | UniProt:P07942 LAMB1 |
| _timestamp | 2026-02-20 22:00:41 |
| chain | signal peptide:1-21 chain:22-1786 |
| checksum | 8F8EF96E765B9A0D |
| comment | FUNCTION Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of the cerebral cortex (PubMed:23472759). It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons (By similarity). Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface (By similarity). As a subunit of laminin-1 (also known as laminin-111 or EHS laminin), it is involved in the stimulation of agrin-induced receptor clustering through a MuSK-independent pathway (By similarity).SUBUNIT Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213). Interacts with ITGB1 (By similarity).INTERACTION Major component.DOMAIN The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.DOMAIN Domains VI and IV are globular.DISEASE The disease is caused by variants affecting the gene represented in this entry. |
| description | recommendedName: Laminin subunit beta-1 alternativeName: Laminin B1 chain alternativeName: Laminin-1 subunit beta alternativeName: Laminin-10 subunit beta alternativeName: Laminin-12 subunit beta alternativeName: Laminin-2 subunit beta alternativeName: Laminin-6 subunit beta alternativeName: Laminin-8 subunit beta |
| geneName | LAMB1 |
| identifier | P07942 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Basement membrane Cell adhesion Coiled coil Disulfide bond Extracellular matrix Glycoprotein Laminin EGF-like domain Lissencephaly Phosphoprotein Proteomics identification Reference proteome Repeat Secreted Signal |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | LAMB1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8960170] ENSEMBL:ENSG00000091136 LAMB1 [Homo sapiens] |
| secondaryIdentifier | LAMB1_HUMAN Q14D91 |
| sequenceLength | 1786 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:215959] LAMB1 [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:2533844] LAMB1(22-?) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:2533954] LAMB1(?-1786) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:8956706] LAMB1 [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:8956889] p-LAMB1 [endoplasmic reticulum lumen] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:8956981] phosphorylated residue at unknown position |
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No pathways have been reviewed or authored by UniProt:P07942 LAMB1 (58619)
