| http://purl.uniprot.org/citations/15574431 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15574431 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15574431 | http://www.w3.org/2000/01/rdf-schema#comment | "CIB1 (CIB) is an EF-hand-containing protein that binds multiple effector proteins, including the platelet alphaIIbbeta3 integrin and several serine/threonine kinases and potentially modulates their function. The crystal structure for Ca(2+)-bound CIB1 has been determined at 2.0 A resolution and reveals a compact alpha-helical protein containing four EF-hands, the last two of which bind calcium ions in the standard fashion seen in many other EF-hand proteins. CIB1 shares high structural similarity with calcineurin B and the neuronal calcium sensor (NCS) family of EF-hand-containing proteins. Most importantly, like calcineurin B and NCS proteins, which possess a large hydrophobic pocket necessary for ligand binding, CIB1 contains a hydrophobic pocket that has been implicated in ligand binding by previous mutational analysis. However, unlike several NCS proteins, Ca(2+)-bound CIB1 is largely monomeric whether bound to a relevant peptide ligand or ligand-free. Differences in structure, oligomeric state, and phylogeny define a new family of CIB1-related proteins that extends from arthropods to humans."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m411515200"xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m411515200"xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Singer A.U."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Singer A.U."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Yang C."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Yang C."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Sondek J."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Sondek J."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Betts L."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Betts L."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Parise L.V."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Parise L.V."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Ferrara J.D."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Ferrara J.D."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Gentry H.R."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/author | "Gentry H.R."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/pages | "8407-8415"xsd:string |
| http://purl.uniprot.org/citations/15574431 | http://purl.uniprot.org/core/pages | "8407-8415"xsd:string |