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PMID: 9007998 Published · ppublish English Journal Article

SAM as a protein interaction domain involved in developmental regulation.

Protein science : a publication of the Protein Society ·Vol. 6 ·No. 1 ·1997-01-00 ·Pages 249-53

Schultz J, Ponting CP, Hofmann K, Bork P

Abstract

More than 60 previously undetected SAM domain-containing proteins have been identified using profile searching methods. Among these are over 40 EPH-related receptor tyrosine kinases (RPTK), Drosophila bicaudal-C, a p53 from Loligo forbesi, and diacyglycerol-kinase isoform delta. This extended dataset suggests that SAM is an evolutionary conserved protein binding domain that is involved in the regulation of numerous developmental processes among diverse eukaryotes. A conserved tyrosine in the SAM sequences of the EPH related RPTKs is likely to mediate cell-cell initiated signal transduction via the binding of SH2 containing proteins to phosphotyrosine.

MeSH Terms
Amino Acid Sequence Animals Gene Expression Regulation, Developmental Humans Molecular Sequence Data Protein Conformation Sequence Homology, Amino Acid
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schultz J
EMBL, Heidelberg, Germany.
Ponting C P
Hofmann K
Bork P
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29 references, click to expand
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
DOI
10.1002/pro.5560060128
Published
1997-01-00
Pages
249-53
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2143507
Subset
IM
Databases
GENBANK
D73409, D86982, P23567, P28829, P36622, P38041, P39769, P39969, S73882, U00046, U03277, U03288, U13645, U15635, U15928, U20158, U20159, U22815, U32174, U40953, U43595, U49739, U52426, U61952, Z31590, Z48367, Z49936, Z50794, Z68337, Z78546
External Links
PubMed source DOI: 10.1002/pro.5560060128 PMC Full Text View journal details
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