Ankyrin
From Proteopedia
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| - | < | + | <StructureSection load='1n11' size='350' side='right' scene='45/454440/Cv/1' caption='Human ankyrin-1 ankyrin repeat region (containing 12 repeats) complex with Cl- (green) and Br- (dark red) ions [[1n11]]'> |
| - | '''Ankyrins''' (ANK) are proteins which mediate the attachment of membrane proteins to the membrane skeleton. | + | |
| - | Kemp et.al cloned mouse Ankrd2 and obtained a partial human ANKRD2 cDNA. | + | |
| + | == Function == | ||
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| + | '''Ankyrins''' (ANK) are proteins which mediate the attachment of membrane proteins to the membrane skeleton. '''ANKRD2''' belongs to the conserved muscle ankyrin repeat protein (MARP) family.Also known as Arpp or '''stretch responsive muscle''' ANKRD2 gene contains 9 exons and spans about 12 kb. The 5-prime flanking region contains a TATA box and binding motifs for the muscle-specific transcription factors MYOD and for NF-kappa-B. | ||
| + | Kemp et.al cloned mouse Ankrd2 and obtained a partial human ANKRD2 cDNA. Northern blot and PCR analyses detected expression of mouse Ankrd2 only in tissues containing striated muscle. In situ hybridization of mouse embryos showed that Ankrd2 expression was restricted to the myotome of somites at day 9.5. At later developmental stages, Ankrd2 expression was stronger in outer back muscles than intercostal muscles, and it was not expressed in heart. See also <br /> | ||
*[[Group:MUZIC:ANKRD2]]<br /> | *[[Group:MUZIC:ANKRD2]]<br /> | ||
*[[Group:MUZIC:CARP]]<br /> | *[[Group:MUZIC:CARP]]<br /> | ||
*[[Group:MUZIC:DARP]]. | *[[Group:MUZIC:DARP]]. | ||
| - | __NOTOC__ | ||
| - | == | + | In mammals ANK is encoded by 3 genes: ANK1, ANK2 and ANK3.<br /> |
| + | *'''ANK1''' or '''ankyrin-R''' is found in erythrocytes, brain and muscle.<br /> | ||
| + | *'''ANK2''' or '''ankyrin-B''' is found in brain and muscle.<br /> | ||
| + | *'''ANK3''' or '''ankyrin-G''' is found in the nervous system and associates with Na channels.<br /> | ||
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| + | '''Gankyrin''' or '''26S proteasome non-ATPase regulatory subunit 10''' (GANK) is an oncoprotein which is a component of the 19S cap of the proteasome. GANK contains ankyrin repeats. | ||
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| + | == Disease == | ||
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| + | Mutations in erythrocyte ANK1 are associated with spherocytosis. Mutations in ANK2 are associated with cardiac arrhythmia syndrome. Mutations in ANK3 are associated with bipolar disorder. | ||
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| + | == Relevance == | ||
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| + | GANK is overexpressed in hepatocellular carcinoma. | ||
| - | + | == Structural highlights == | |
| - | + | Ankyrin contains four domains: the N terminal which contains 24 ankyrin repeats, a spectrin-binding domain, a death domain which binds to proteins involved in apoptosis and a C terminal regulatory domain. The full-length 328-amino acid mouse protein contains an ATP/GTP-binding domain in its N-terminal half and an ankyrin repeat region in its C-terminal half. It also has a nuclear localization signal, 2 protein-destabilizing PEST sequences, and 2 phosphorylation sites. The '''ankyrin repeat''' is a protein-protein interaction motif. It is a 33 residue segment consisting of a helix-loop-helix motif. The long ankyrin repeat in human ankyrin-R contains 12 ankyrin repeats (residues 402-827) and is called D34 region. <scene name='45/454440/Cv/2'>Click here to see 12 ankyrin repeats</scene>. <ref>PMID:12456646</ref> <scene name='45/454440/Cv/3'>One ankyrin repeat</scene> from [[1n0r]]. <ref>PMID:12461176</ref> | |
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| - | == | + | == 3D Structures of ankyrin == |
| - | [[ | + | [[Ankyrin 3D structures]] |
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| - | + | </StructureSection> | |
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646
- ↑ Mosavi LK, Minor DL Jr, Peng ZY. Consensus-derived structural determinants of the ankyrin repeat motif. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16029-34. Epub 2002 Dec 2. PMID:12461176 doi:http://dx.doi.org/10.1073/pnas.252537899
