MGP Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins
MGP000150

UniProt Annotations

Entry Information
Gene Nameankyrin 3, node of Ranvier (ankyrin G)
Protein EntryANK3_HUMAN
UniProt IDQ12955
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q12955-3; Sequence=Displayed; Name=2; IsoId=Q12955-4; Sequence=VSP_044349, VSP_044350, VSP_044351, VSP_044352, VSP_044353, VSP_044354; Name=3; IsoId=Q12955-5; Sequence=VSP_044348, VSP_044351, VSP_044352, VSP_044353, VSP_044354; Name=4; IsoId=Q12955-6; Sequence=VSP_046885, VSP_046886, VSP_044351, VSP_044352, VSP_044353, VSP_044354; Note=Ref.3 (CAB66645) sequence(s) differ(s) from that shown due to (a) frameshift(s) in position(s) 810.; Name=5; Synonyms=AnkG119, Golgi ankyrin; IsoId=Q12955-7; Sequence=VSP_053753, VSP_053754, VSP_053755, VSP_053756, VSP_053757, VSP_044351, VSP_053758, VSP_053759; Note=Avidly binds beta spectrin.;
Developmental StageUp-regulated during muscle cell differentiation. {ECO:0000269|PubMed:21223964}.
DiseaseMental retardation, autosomal recessive 37 (MRT37) [MIM:615493]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT37 patients manifest delayed global development with speech delay, hypotonia, spasticity, and a sleep disorder. Severe behavioral abnormalities include aggression, hyperactivity, and grinding of the teeth. Note=The disease is caused by mutations affecting the gene represented in this entry. A homozygous deletion in ANK3 predicted to result in frameshift and premature truncation, has been shown to be the cause of moderate intellectual disability, an ADHD-like phenotype and behavioral problems in a consanguineous family (PubMed:23390136). {ECO:0000269|PubMed:23390136}.
DiseaseNote=Genetic variations in ANK3 may be associated with autism spectrum disorders susceptibility.
DomainThe tandem configuration of the two ZU5 and the UPA domains forms a structural supramodule termed ZZU. ZU5-1 mediates interaction with beta-spectrin, and the ZU5-1/UPA interface is required for ankyrin's function other than binding to spectrin (By similarity). {ECO:0000250}.
FunctionIn skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. {ECO:0000250}.
FunctionIsoform 5: May be part of a Golgi-specific membrane cytoskeleton in association with beta-spectrin.
InteractionQ15796:SMAD2; NbExp=2; IntAct=EBI-2691178, EBI-1040141;
SimilarityContains 1 death domain. {ECO:0000255|PROSITE- ProRule:PRU00064}.
SimilarityContains 23 ANK repeats. {ECO:0000255|PROSITE- ProRule:PRU00023}.
SimilarityContains 2 ZU5 domains. {ECO:0000255|PROSITE- ProRule:PRU00485}.
Subcellular LocationCytoplasm, cytoskeleton {ECO:0000269|PubMed:21223964}. Cell projection, axon {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000269|PubMed:21223964}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}. Lysosome {ECO:0000250}. Note=In skeletal muscle, localized at costameres and neuromuscular junctions. In macrophages, associated with lysosomes. {ECO:0000250}.
Subcellular LocationIsoform 5: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8666667}. Golgi apparatus {ECO:0000269|PubMed:8666667}.
SubunitDirectly interacts with DMD and betaDAG1. This interaction does not interfere with binding between DMD and betaDAG1. It is also required for DMD and betaDAG1 retention at costameres (By similarity). Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 5 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs) (By similarity). May be a constituent of a neurofascin/NRCAM/ankyrin G complex. Interacts with RHBG. Interacts with PLEC and FLNC. {ECO:0000250, ECO:0000269|PubMed:15611082, ECO:0000269|PubMed:21223964}.
Tissue SpecificityExpressed in brain, neurons, muscles and other tissues. {ECO:0000269|PubMed:21223964, ECO:0000269|PubMed:7836469}.
Web ResourceName=Wikipedia; Note=Ankyrin entry; URL="http://en.wikipedia.org/wiki/Ankyrin";
  logo