|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5192
|
|
pubmed:dateCreated |
1995-1-13
|
|
pubmed:abstractText |
Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that participate in signaling by growth factors and oncogenes. A protein domain was identified that bound specifically to the tyrosine-phosphorylated form of its target protein but differs from known SH2 sequences. Phosphotyrosine-binding (PTB) domains were found in two proteins: SHC, a protein implicated in signaling through Ras; and SCK, encoded by a previously uncharacterized gene. The PTB domain of SHC specifically bound to a tyrosine-phosphorylated 145-kilodalton protein. PTB domains are an alternative to SH2 domains for specifically recruiting tyrosine-phosphorylated proteins into signaling complexes and are likely to take part in signaling by many growth factors.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet-Derived Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SHC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Shc Signaling Adaptor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Shc1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0036-8075
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
16
|
|
pubmed:volume |
266
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1862-5
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:7527937-3T3 Cells,
pubmed-meshheading:7527937-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:7527937-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:7527937-Amino Acid Sequence,
pubmed-meshheading:7527937-Animals,
pubmed-meshheading:7527937-Cell Line,
pubmed-meshheading:7527937-Humans,
pubmed-meshheading:7527937-Mice,
pubmed-meshheading:7527937-Molecular Sequence Data,
pubmed-meshheading:7527937-Phosphoproteins,
pubmed-meshheading:7527937-Phosphorylation,
pubmed-meshheading:7527937-Phosphotyrosine,
pubmed-meshheading:7527937-Platelet-Derived Growth Factor,
pubmed-meshheading:7527937-Protein Binding,
pubmed-meshheading:7527937-Protein-Tyrosine Kinases,
pubmed-meshheading:7527937-Proteins,
pubmed-meshheading:7527937-Shc Signaling Adaptor Proteins,
pubmed-meshheading:7527937-Signal Transduction,
pubmed-meshheading:7527937-Tyrosine
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
An alternative to SH2 domains for binding tyrosine-phosphorylated proteins.
|
|
pubmed:affiliation |
Department of Medicine, University of California, San Francisco 94143.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
