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http://www.biopax.org/relea... | |
http://www.biopax.org/relea... |
Laminin subunit beta-1
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http://www.biopax.org/relea... |
LAMB1_HUMAN
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http://www.biopax.org/relea... | |
http://www.biopax.org/relea... |
Laminin B1 chain,
Laminin-1 subunit beta,
Laminin-10 subunit beta,
Laminin-12 subunit beta,
Laminin-2 subunit beta,
Laminin-6 subunit beta,
Laminin-8 subunit beta
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http://www.biopax.org/relea... |
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. 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). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=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. SIMILARITY: Contains 13 laminin EGF-like domains. SIMILARITY: Contains 1 laminin IV type B domain. SIMILARITY: Contains 1 laminin N-terminal domain. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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