Aliases for PPFIA2 Gene
- PTPRF Interacting Protein Alpha 2 2 3 5
- Protein Tyrosine Phosphatase, Receptor Type, F Polypeptide (PTPRF), Interacting Protein (Liprin), Alpha 2 2 3
- Liprin-Alpha-2 3 4
- Protein Tyrosine Phosphatase Receptor Type F Polypeptide-Interacting Protein Alpha-2 4
- PTPRF-Interacting Protein Alpha-2 4
- Liprin-Alpha2 2
External Ids for PPFIA2 Gene
Previous GeneCards Identifiers for PPFIA2 Gene
The protein encoded by this gene is a member of the LAR protein-tyrosine phosphatase-interacting protein (liprin) family. Liprins interact with members of LAR family of transmembrane protein tyrosine phosphatases, which are known to be important for axon guidance and mammary gland development. It has been proposed that liprins are multivalent proteins that form complex structures and act as scaffolds for the recruitment and anchoring of LAR family of tyrosine phosphatases. This protein has been shown to bind the calcium/calmodulin-dependent serine protein kinase (MAGUK family) protein (also known as CASK) and proposed to regulate higher-order brain functions in mammals. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2013]
GeneCards Summary for PPFIA2 Gene
PPFIA2 (PTPRF Interacting Protein Alpha 2) is a Protein Coding gene. Diseases associated with PPFIA2 include Myopia and Non-Syndromic X-Linked Intellectual Disability. Among its related pathways are Neurotransmitter Release Cycle and Transmission across Chemical Synapses. Gene Ontology (GO) annotations related to this gene include nucleotide binding. An important paralog of this gene is PPFIA1.
UniProtKB/Swiss-Prot Summary for PPFIA2 Gene
Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates. In neuronal cells, is a scaffolding protein in the dendritic spines which acts as immobile postsynaptic post able to recruit KIF1A-driven dense core vesicles to dendritic spines (PubMed:30021165).