Group:MUZIC:XIN: Difference between revisions

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Xin directly binds the EVH1 domain proteins Mena and VASP <ref name="pmid16631741">.
Xin directly binds the EVH1 domain proteins Mena and VASP <ref name="pmid16631741">.
Xin binds the unique insertion of filamin c containing Ig domain 20.
Xin binds the unique insertion of filamin c containing Ig domain 20.
Xin directly binds F-actin <ref name="pmid15454575">.
Xin directly binds F-actin <ref name="pmid15454575">.</nowiki>
 
 


<blockquote>
This section complements the article on [http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb106_1.html Poly(A) Polymerase] in the
[http://www.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] Series. See also [[Teaching Scenes, Tutorials, and Educators' Pages]].
</blockquote>


==Additional Resources==
For additional information, see: [[Translation]] <br/>
For additional examples of transferases, see: [[Transferase]]


== References ==
== References ==
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Revision as of 00:19, 12 July 2011

Xin actin-binding repeat-containing protein 1 (Alternative name: Cardiomyopathy-associated protein 1) is coded by the gene (Synonyms:CMYA1, XIN) and has an actin-binding domain (ABD). It crosslinks actin filaments and participates in anchoring of membrane proteins. Intraexogic splicing leads to a least three different isoforms.

Sequence Annotation


Interactions with other proteins/ Function

Xin and Mena/VASP colocalize with filamin c in intercalated discs (ICD, structure at the end of the myocytes that transduce force from the myofibrils via the cell membranes to the extracelluar matrix and neighboring cells) in the adult heart [1].

Xin directly binds the EVH1 domain proteins Mena and VASP <ref name="pmid16631741">. Xin binds the unique insertion of filamin c containing Ig domain 20. Xin directly binds F-actin <ref name="pmid15454575">.</nowiki>



References

  1. ↑ Clark AR, Sawyer GM, Robertson SP, Sutherland-Smith AJ. Skeletal dysplasias due to filamin A mutations result from a gain-of-function mechanism distinct from allelic neurological disorders. Hum Mol Genet. 2009 Dec 15;18(24):4791-800. Epub 2009 Sep 22. PMID:19773341 doi:10.1093/hmg/ddp442

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Proteopedia Page Contributors and Editors (what is this?)

Georg Mlynek, Jaime Prilusky, Nikos Pinotsis