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SAM as a protein interaction domain involved in developmental regulation

Open access
Schultz, Jörg, Bork, Peer, Ponting, Christopher P., Hofmann, Kay·1997·Protein Science

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 diacylglycerol‐kinase isoform δ. 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.

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Metadata

Authors
Schultz, J., Bork, P., Ponting, C. P., & Hofmann, K.
Venue
Protein Science
Publisher
Wiley
Published
1997-01
Volume
6
Issue
1
Pages
249-253
ISSN
  • 0961-8368 (ISSN-L)
  • 1469-896X
OpenAlex
W2103785126
Cited by
300
References
1
FWCI
6.20
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: SAM as a protein interaction domain involved in developmental regulation. https://app.cochat.ai/papers/10.1002/pro.5560060128
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Schultz, J., Bork, P., Ponting, C. P., & Hofmann, K. (1997). SAM as a protein interaction domain involved in developmental regulation. Protein Science. https://doi.org/10.1002/pro.5560060128

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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