Ankyrins

ankyrin 1, erythrocytic
Ribbon diagram of a fragment of the membrane-binding domain of ankyrin 1. From PDB: 1N11​.
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

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.

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.

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.

External links

• Ankyrins at the US National Library of Medicine Medical Subject Headings (MeSH)

de:Ankyrin

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