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Ankyrin



Ribbon diagram of a fragment of the membrane-binding domain of ankyrin 1. From PDB 1N11.
ankyrin 1, erythrocytic
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
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)
Identifiers
Symbol ANK3
Entrez 288
HUGO 494
OMIM 600465
RefSeq NM_020987
UniProt Q12955
Other data
Locus Chr. 10 q21

Ankyrins are a family of proteins that mediates the attachment of integral membrane proteins to the cytoskeleton.[1]

Additional recommended knowledge

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

  1. ^ 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.
  2. ^ 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.
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Ankyrin". A list of authors is available in Wikipedia.
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