Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.10.1 (ERK)
 95,504 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have identified human and rat DNAs encoding two novel members of the eph subclass of putative receptor protein-tyrosine kinases. Rat cDNA clones encoding eek (eph- and elk-related kinase) were isolated from a brain cDNA library probed with DNA encoding the kinase region of the insulin receptor-related receptor. The predicted eek protein contains all the amino acid residues conserved in the catalytic domains of protein-tyrosine kinases and is most similar to two putative receptor protein-tyrosine kinases of the eph subclass, elk (69%) and eph (57%). Human genomic DNAs encoding part of eek (EEK) as well as another putative protein-tyrosine kinase most similar to elk (90%), ERK (elk-related kinase), were isolated and partially characterized. The novel identity of these two eph-family genes was further supported by Southern blot analyses and localization to human chromosome 1. In Northern blot analysis of rat RNA, DNAs encoding rat eek and human ERK hybridized to transcripts most abundant in brain and lung, respectively. These two new members of the eph subclass of receptor protein-tyrosine kinases, eek and erk, may therefore have tissue-specific functions distinct from those of other eph family members.
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PMID:eek and erk, new members of the eph subclass of receptor protein-tyrosine kinases. 164 1

A human epithelial (HeLa) cDNA library was screened with degenerate oligonucleotides designed to hybridize to highly conserved regions of protein-tyrosine kinases. One cDNA from this screen was shown to contain a putative protein-tyrosine kinase catalytic domain and subsequently used to isolate another cDNA from a human keratinocyte library that encompasses the entire coding region of a 976-amino-acid polypeptide. The predicted protein has an external domain of 534 amino acids with a presumptive N-terminal signal peptide, a transmembrane domain, and a cytoplasmic domain of 418 amino acids that includes a canonical protein-tyrosine kinase catalytic domain. Molecular phylogeny indicates that this protein kinase is closely related to eph and elk and that this receptor family is more closely related to the non-receptor protein-tyrosine kinase families than to other receptor protein-tyrosine kinases. Antibodies raised against a TrpE fusion protein immunoprecipitated a 130-kDa protein that became phosphorylated on tyrosine in immune complex kinase assays, indicating that this protein is a bona fide protein-tyrosine kinase. Analysis of RNA from 13 adult rat organs showed that the eck gene is expressed most highly in tissues that contain a high proportion of epithelial cells, e.g., skin, intestine, lung, and ovary. Several cell lines of epithelial origin were found to express the eck protein kinase at the protein and RNA levels. Immunohistochemical analysis of several rat organs also showed staining in epithelial cells. These observations prompted us to name this protein kinase eck, for epithelial cell kinase.
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PMID:cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases. 217 5