| http://purl.uniprot.org/citations/14517229 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14517229 | http://www.w3.org/2000/01/rdf-schema#comment | "The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact betabetaalpha-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/cdg475"xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/author | "Inagaki F."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/author | "Ito T."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/author | "Ogura K."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/author | "Sumimoto H."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/author | "Takeya R."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/author | "Yoshinaga S."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/author | "Yokochi M."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/author | "Kohjima M."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/name | "EMBO J"xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/pages | "4888-4897"xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/title | "The PB1 domain and the PC motif-containing region are structurally similar protein binding modules."xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://purl.uniprot.org/core/volume | "22"xsd:string |
| http://purl.uniprot.org/citations/14517229 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14517229 |
| http://purl.uniprot.org/citations/14517229 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/14517229 |
| http://purl.uniprot.org/uniprot/#_O75004-mappedCitation-14517229 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14517229 |
| http://purl.uniprot.org/uniprot/#_P11433-mappedCitation-14517229 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14517229 |
| http://purl.uniprot.org/uniprot/#_P29366-mappedCitation-14517229 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/14517229 |
| http://purl.uniprot.org/uniprot/P29366 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14517229 |
| http://purl.uniprot.org/uniprot/P11433 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14517229 |
| http://purl.uniprot.org/uniprot/O75004 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/14517229 |