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http://purl.uniprot.org/citations/11410595http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11410595http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11410595http://www.w3.org/2000/01/rdf-schema#comment"Atp11p and Atp12p were first described as proteins required for assembly of the F(1) component of the mitochondrial ATP synthase in Saccharomyces cerevisiae (Ackerman, S. H., and Tzagoloff, A. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 4986-4990). Here we report the isolation of the cDNAs and the characterization of the human genes for Atp11p and Atp12p and show that the human proteins function like their yeast counterparts. Human ATP11 spans 24 kilobase pairs in 9 exons and maps to 1p32.3-p33, while ATP12 contains > or =8 exons and localizes to 17p11.2. Both genes are broadly conserved in eukaryotes and are expressed in a wide range of tissues, which suggests that Atp11p and Atp12p are essential housekeeping proteins of human cells. The information reported herein will be useful in the evaluation of patients with ascertained deficiencies in the ATP synthase, in which the underlying biochemical defect is unknown and may reside in a protein that influences the assembly of the enzyme."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m104133200"xsd:string
http://purl.uniprot.org/citations/11410595http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m104133200"xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/author"White P.S."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/author"White P.S."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/author"Ackerman S.H."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/author"Ackerman S.H."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/author"Wang Z.-G."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/author"Wang Z.-G."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/pages"30773-30778"xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/pages"30773-30778"xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/title"Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/title"Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria."xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11410595http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11410595http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11410595
http://purl.uniprot.org/citations/11410595http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11410595
http://purl.uniprot.org/citations/11410595http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11410595
http://purl.uniprot.org/citations/11410595http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11410595