Group:MUZIC:XIN: Difference between revisions
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Xin directly binds F-actin <ref name="pmid15454575">. | Xin directly binds F-actin <ref name="pmid15454575">. | ||
<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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<references /> | <references /> | ||
Revision as of 00:17, 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][1](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">.
This section complements the article on Poly(A) Polymerase in the Molecule of the Month Series. See also Teaching Scenes, Tutorials, and Educators' Pages.
Additional Resources
For additional information, see: Translation
For additional examples of transferases, see: Transferase
References
- ↑ 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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