Ankyrins
(Redirected from Ankyrin B)
ankyrin 1, erythrocytic | |
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Identifiers | |
Symbol | ANK1 |
Alt. symbols | ANK |
Entrez | 286 |
HUGO | 492 |
OMIM | 182900 |
RefSeq | NM_000037 |
UniProt | P16157 |
Other data | |
Locus | Chr. 8 p21.1-11.2 |
ankyrin 2, neuronal | |
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Identifiers | |
Symbol | ANK2 |
Alt. symbols | LQT4 |
Entrez | 287 |
HUGO | 493 |
OMIM | 106410 |
RefSeq | NM_001148 |
UniProt | Q01484 |
Other data | |
Locus | Chr. 4 q25-q27 |
ankyrin 3, node of Ranvier (ankyrin G) | |
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Identifiers | |
Symbol | ANK3 |
Entrez | 288 |
HUGO | 494 |
OMIM | 600465 |
RefSeq | NM_020987 |
UniProt | Q12955 |
Other data | |
Locus | Chr. 10 q21 |
Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]
Associate Editor-In-Chief: Cafer Zorkun, M.D., Ph.D. [2]
Overview
Ankyrins are a family of proteins that mediates the attachment of integral membrane proteins to the cytoskeleton.[1]
Ankyrin 1, was first discovered in the erythrocytes but also later found to be expressed in the brain and muscles. In erythrocytes, Ankyrin 1 links membrane receptor CD44 to inositol triphosphate and the cytoskeleton.[2]
Ankyrin contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD) consisting of 22–24 tandem repeats of 33 amino acids, a spectrin binding domain and a variably sized C-terminal regulatory domain.
Ankyrin was discovered by Dr. G. Vann Bennett (M.D., PhD.) in 1976.
References
- ↑ Hryniewicz-Jankowska A, Czogalla A, Bok E, Sikorsk AF (2002). "Ankyrins, multifunctional proteins involved in many cellular pathways". Folia Histochem Cytobiol. 40 (3): 239–49. PMID 12219834.
- ↑ Singleton PA, Bourguignon LY (2004). "CD44 interaction with ankyrin and IP3 receptor in lipid rafts promotes hyaluronan-mediated Ca2+ signaling leading to nitric oxide production and endothelial cell adhesion and proliferation". Exp Cell Res. 295 (1): 102–18. PMID 15051494.
External links
- Ankyrins at the US National Library of Medicine Medical Subject Headings (MeSH)