Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1995-1-26
pubmed:abstractText
KIN28, a member of the p34cdc2/CDC28 family of protein kinases, is identified as a subunit of yeast RNA polymerase transcription factor IIH (TFIIH) on the basis of sequence determination, immunological reactivity, and copurification. KIN28 is, moreover, one of three subunits of TFIIK, a subassembly of TFIIH with protein kinase activity directed toward the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II. Itself a phosphoprotein, KIN28 interacts specifically with the two largest subunits of RNA polymerase II. Previous work of others points to two further associations: KIN28 interacts in vivo with the cyclin CCL1, and KIN28 and CCL1 are homologous to human MO15 and cyclin H, which form the cyclin-dependent kinase-activating kinase (CAK). We show that human CAK possesses the CTD kinase activity characteristic of TFIIH.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Cyclins, http://linkedlifedata.com/resource/pubmed/chemical/Kin28 protein kinase, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TAF6 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/TATA-Binding Protein Associated..., http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIH, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, TFII, http://linkedlifedata.com/resource/pubmed/chemical/cyclin-dependent kinase-activating...
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1103-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8001136-Amino Acid Sequence, pubmed-meshheading:8001136-Base Sequence, pubmed-meshheading:8001136-Blotting, Western, pubmed-meshheading:8001136-Cell-Free System, pubmed-meshheading:8001136-Cyclin-Dependent Kinases, pubmed-meshheading:8001136-Cyclins, pubmed-meshheading:8001136-Humans, pubmed-meshheading:8001136-Molecular Sequence Data, pubmed-meshheading:8001136-Phosphoric Monoester Hydrolases, pubmed-meshheading:8001136-Protein Binding, pubmed-meshheading:8001136-Protein Biosynthesis, pubmed-meshheading:8001136-Protein-Serine-Threonine Kinases, pubmed-meshheading:8001136-RNA Polymerase II, pubmed-meshheading:8001136-Recombinant Proteins, pubmed-meshheading:8001136-Saccharomyces cerevisiae Proteins, pubmed-meshheading:8001136-Sequence Analysis, pubmed-meshheading:8001136-Sequence Homology, Amino Acid, pubmed-meshheading:8001136-TATA-Binding Protein Associated Factors, pubmed-meshheading:8001136-Transcription Factor TFIID, pubmed-meshheading:8001136-Transcription Factor TFIIH, pubmed-meshheading:8001136-Transcription Factors, pubmed-meshheading:8001136-Transcription Factors, TFII
pubmed:year
1994
pubmed:articleTitle
Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK.
pubmed:affiliation
Department of Structural Biology, Stanford University School of Medicine, California 94305.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't