Summary: EBP50, C-terminal
EBP50, C-terminal Provide feedback
This C terminal domain allows interaction of EBP50 with FERM (four-point one ERM) domains, resulting in the activation of Ezrin-radixin-moesin (ERM), with subsequent cytoskeletal modulation and cellular growth control .
Finnerty CM, Chambers D, Ingraffea J, Faber HR, Karplus PA, Bretscher A; , J Cell Sci. 2004;117:1547-1552.: The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain. PUBMED:15020681 EPMC:15020681
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This tab holds annotation information from the InterPro database.
InterPro entry IPR015098
This C-terminal domain allows interaction of EBP50 with FERM (four-point one ERM) domains, resulting in the activation of Ezrin-radixin-moesin (ERM), with subsequent cytoskeletal modulation and cellular growth control [PUBMED:15020681].
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This example describes an architecture with one
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Curation and family details
|Author:||Mistry J, Sammut SJ|
|Number in seed:||6|
|Number in full:||149|
|Average length of the domain:||40.90 aa|
|Average identity of full alignment:||60 %|
|Average coverage of the sequence by the domain:||12.56 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the EBP50_C-term domain has been found. There are 9 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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