Relations between 'Arrestin, N-terminal' and 'Arrestin, conserved site'

This is a known relation: The relation among these concepts has been integrated in BioGraph's knowledge base as a known relation.

In the context of Arrestin, N-terminal, Arrestin, conserved site has rank 1 out of 11924 'Domain' concepts (top 0.01%) in BioGraph's knowledge base. (Show more ranking information)

Publications

The BioGraph contains no references to the literature for this relation.^?Note that not all databases contain references to the literature (e.g., for gene ontology annotations, pathway memberships, disease relatedness, protein domain annotations, ...)

Literature search on PubMed for this relation:

• Song et al., Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites. (2007)
• Houslay et al., The role of ERK2 docking and phosphorylation of PDE4 cAMP phosphodiesterase isoforms in mediating cross-talk between the cAMP and ERK signalling pathways. (2003)
• Miller et al., Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3. (2001)
• Teo et al., The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors. (2001)
• Vishnivetskiy et al., An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation. (2000)

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Resource databases

The following database(s) have been used to integrate this relation into our knowledge base:

Putative functional relations

The following trails provide putative functional links between Arrestin, N-terminal (context) and Arrestin, conserved site (target)

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