Structural highlightsFunction[CAMP1_HUMAN] Probable microtubule-binding protein that plays a role in the regulation of cell morphology and cytoskeletal organization. Through interaction with spectrin may regulate neurite outgrowth.[1] [2] [3] [TBB5_HUMAN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [TBA1B_HUMAN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
References
- ↑ Baines AJ, Bignone PA, King MD, Maggs AM, Bennett PM, Pinder JC, Phillips GW. The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins. Mol Biol Evol. 2009 Sep;26(9):2005-14. doi: 10.1093/molbev/msp115. Epub 2009 Jun , 9. PMID:19508979 doi:http://dx.doi.org/10.1093/molbev/msp115
- ↑ Bai SW, Herrera-Abreu MT, Rohn JL, Racine V, Tajadura V, Suryavanshi N, Bechtel S, Wiemann S, Baum B, Ridley AJ. Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration. BMC Biol. 2011 Aug 11;9:54. doi: 10.1186/1741-7007-9-54. PMID:21834987 doi:10.1186/1741-7007-9-54
- ↑ King MD, Phillips GW, Bignone PA, Hayes NV, Pinder JC, Baines AJ. A conserved sequence in calmodulin regulated spectrin-associated protein 1 links its interaction with spectrin and calmodulin to neurite outgrowth. J Neurochem. 2014 Feb;128(3):391-402. doi: 10.1111/jnc.12462. Epub 2013 Oct 24. PMID:24117850 doi:http://dx.doi.org/10.1111/jnc.12462
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