Ankyrin

ANK1, erythrocytic
Ribbon diagram of a fragment of the membrane-binding domain of ankyrin R.[1]
Identifiers
SymbolANK1
Alt. symbolsAnkyrinR, Band2.1
NCBI gene286
HGNC492
OMIM182900
PDB1N11
RefSeqNM_000037
UniProtP16157
Other data
LocusChr. 8 p21.1-11.2
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StructuresSwiss-model
DomainsInterPro
Ankyrin repeat
Identifiers
SymbolAnk
PfamPF00023
InterProIPR002110
SMARTSM00248
PROSITEPDOC50088
SCOP21awc / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
ANK2, neuronal
Identifiers
SymbolANK2
Alt. symbolsAnkyrinB
NCBI gene287
HGNC493
OMIM106410
RefSeqNM_001148
UniProtQ01484
Other data
LocusChr. 4 q25-q27
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ANK3, node of Ranvier
Identifiers
SymbolANK3
Alt. symbolsAnkyrinG
NCBI gene288
HGNC494
OMIM600465
RefSeqNM_020987
UniProtQ12955
Other data
LocusChr. 10 q21
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StructuresSwiss-model
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Ankyrins are a family of proteins that mediate the attachment of integral membrane proteins to the spectrin-actin based membrane cytoskeleton.[2] Ankyrins have binding sites for the beta subunit of spectrin and at least 12 families of integral membrane proteins. This linkage is required to maintain the integrity of the plasma membranes and to anchor specific ion channels, ion exchangers and ion transporters in the plasma membrane. The name is derived from the Greek word ἄγκυρα (ankyra) for "anchor".

  1. ^ PDB: 1N11​; Michaely P, Tomchick DR, Machius M, Anderson RG (December 2002). "Crystal structure of a 12 ANK repeat stack from human ankyrinR". The EMBO Journal. 21 (23): 6387–96. doi:10.1093/emboj/cdf651. PMC 136955. PMID 12456646.
  2. ^ Bennett V, Baines AJ (July 2001). "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues". Physiological Reviews. 81 (3): 1353–92. doi:10.1152/physrev.2001.81.3.1353. PMID 11427698. S2CID 15307181.