Ankyrins

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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

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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.[1]

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

External links



de:Ankyrin

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Acknowledgement and Attribution Regarding Sources of Content

Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .

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