cpath:CPATH-125027 | rdf:type | http://www.biopax.org/relea... | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | cpath:CPATH-LOCAL-516385 | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | cpath:CPATH-LOCAL-516386 | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | cpath:CPATH-LOCAL-516387 | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | cpath:CPATH-LOCAL-516388 | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | cpath:CPATH-LOCAL-517385 | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | Laminin subunit alpha-1 | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | LAMA1_HUMAN | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | cpath:CPATH-LOCAL-516383 | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | S-laminin subunit alpha | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | Laminin A chain | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | Laminin-1 subunit alpha | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | S-LAM alpha | lld:biogrid |
cpath:CPATH-125027 | http://www.biopax.org/relea... | Laminin-3 subunit alpha | lld:biogrid |
cpath:CPATH-125027 | 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. Alpha-1 is a subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3 (laminin-121 or S-laminin). 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, IV and G are globular. SIMILARITY: Contains 17 laminin EGF-like domains. SIMILARITY: Contains 5 laminin G-like domains. SIMILARITY: Contains 2 laminin IV type A domains. SIMILARITY: Contains 1 laminin N-terminal domain. GENE SYNONYMS: LAMA. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License. | lld:biogrid |
cpath:CPATH-125027 | skos:exactMatch | uniprot-protein:P25391 | lld:mappings |
cpath:CPATH-125027 | skos:closeMatch | entrez-gene:284217 | lld:mappings |
cpath:CPATH-LOCAL-11148249 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11158105 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11490309 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11499490 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11510275 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11514024 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11568834 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11637159 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11646400 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |
cpath:CPATH-LOCAL-11709549 | http://www.biopax.org/relea... | cpath:CPATH-125027 | lld:biogrid |