Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04626 (erbB-2)
 5,251 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The epidermal growth factor (EGF) receptor is a tyrosine-specific protein kinase with autophosphorylating activity. A 300 amino acid-long region of the receptor's cytoplasmic domain matches (35-90% homology) sequences of transforming proteins from the src family and includes a putative nucleotide binding site. Several of the src transforming proteins have tyrosine kinase activity, but v-erb-B, which appears to be a truncated EGF receptor, is virtually identical to the receptor over this region and yet lacks detectable kinase activity. To locate possible acceptor sites in the v-erb-B protein, we have mapped these sites in the human EGF receptor. We report here that three tyrosine sites near the C-terminus are phosphorylated in vitro. In intact cells, we find that EGF stimulates phosphorylation of several sites, the tyrosine 14 residues from the C-terminus being modified the most extensively. The equivalent site is absent in the v-erb-B protein of avian erythroblastosis virus (AEV) and may influence tyrosine kinase activity.
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PMID:Autophosphorylation sites on the epidermal growth factor receptor. 609 Sep 45

The recently discovered similarity between the human epidermal growth factor (EGF) receptor and the avian erythroblastosis virus v-erb-B protein supports the hypothesis that viral oncogenes share a common evolutionary origin with genes encoding growth-regulating cell-surface receptors. To elucidate the relationship between receptors and malignant transformation, we have now used a fragment of v-erb-B as a probe to screen a cDNA library of mRNA from A431 human carcinoma cells, which possess a large number of EGF receptors. Of the six clones isolated, the largest (pE7) contains an insert of 2.4 kilobase pairs (kbp) whose deduced amino acid sequence is homologous to the v-erb-B protein and identical to reported EGF receptor peptide sequences. This pE7 cDNA hybridized to three prominent RNAs of approximately 10, 5.6 and 2.9 kilobases (kb), and to three minor species of 6.3, 4.6 and 3.3 kb. All were present in elevated levels in A431 cells. The prominent 2.9-kb RNA was homologous only to the 5' portion of the pE7 insert. This result raises the possibility that differential RNA processing is used by A431 cells to generate a variety of RNAs.
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PMID:Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells. 633 May 63