Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1991-9-26
pubmed:databankReference
pubmed:abstractText
We have isolated cDNAs encoding kinases from a murine pre-B cell line by screening a lambda gt11 cDNA expression library with anti-phosphotyrosine antibodies. One cDNA was identified to encode the previously isolated tyrosine kinase c-lyn. Among the remaining clones, we have characterized a cDNA encoding a novel kinase which we have designated TIK. Sequence analysis of this cDNA indicates that the TIK enzyme lacks the features thought to be conserved among protein tyrosine kinases. Although isolated on the basis of its reactivity with the anti-phosphotyrosine antibody, the TIK enzyme was found to have only serine and threonine kinase activity. The amino-terminal portion of the TIK protein contains a cdc2 phosphorylation consensus sequence. Three mRNA transcripts derived from the TIK gene are detected in a variety of adult murine tissues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16073-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
TIK, a novel serine/threonine kinase, is recognized by antibodies directed against phosphotyrosine.
pubmed:affiliation
Department of Medicine, University of Ottawa, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't