Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1996-7-9
|
| pubmed:databankReference | |
| pubmed:abstractText |
Src homology 2 (SH2) domains are structural modules that function in the assembly of multicomponent signaling complexes by binding to specific phosphopeptides. The tetratricopeptide repeat (TPR) is a distinct structural motif that has been suggested to mediate protein-protein interactions. Among SH2-binding phosphoproteins purified from the mouse B cell lymphoma A20, a 150-kDa species was identified and the corresponding complementary DNA (cDNA) was molecularly cloned. This protein encoded by this cDNA, which we have termed p150TSP (for TPR-containing, SH2-binding phosphoprotein), is located predominantly in the nucleus and is highly conserved in evolution. The gene encoding p150TSP (Tsp) was mapped to chromosome 7 of the mouse with gene order: centromere-Tyr-Wnt11-Tsp-Zp2. The amino-terminal two-thirds of p150TSP consist almost entirely of tandemly arranged TPR units, which mediate specific, homotypic protein interactions in transfected cells. The carboxyl-terminal third of p150TSP, which is serine- and glutamic acid-rich, is essential for SH2 binding; this interaction is dependent on serine/threonine phosphorylation but independent of tyrosine phosphorylation. The sequence and binding properties of p150TSP suggest that it may mediate interactions between TPR-containing and SH2-containing proteins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/RNA
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
22
|
| pubmed:volume |
271
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6952-62
|
| pubmed:dateRevised |
2007-5-17
|
| pubmed:meshHeading |
pubmed-meshheading:8636124-Amino Acid Sequence,
pubmed-meshheading:8636124-Animals,
pubmed-meshheading:8636124-Base Sequence,
pubmed-meshheading:8636124-Cell Line,
pubmed-meshheading:8636124-Cell Nucleus,
pubmed-meshheading:8636124-Chromatography, Affinity,
pubmed-meshheading:8636124-Cloning, Molecular,
pubmed-meshheading:8636124-DNA, Complementary,
pubmed-meshheading:8636124-Humans,
pubmed-meshheading:8636124-Hydrogen-Ion Concentration,
pubmed-meshheading:8636124-Molecular Sequence Data,
pubmed-meshheading:8636124-Nuclear Proteins,
pubmed-meshheading:8636124-Peptides,
pubmed-meshheading:8636124-Phosphoproteins,
pubmed-meshheading:8636124-Phosphorylation,
pubmed-meshheading:8636124-Phosphotyrosine,
pubmed-meshheading:8636124-Protein Binding,
pubmed-meshheading:8636124-RNA,
pubmed-meshheading:8636124-Sequence Homology, Amino Acid,
pubmed-meshheading:8636124-src Homology Domains
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
p150TSP, a conserved nuclear phosphoprotein that contains multiple tetratricopeptide repeats and binds specifically to SH2 domains.
|
| pubmed:affiliation |
Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|