CAV2
entrez
858
canonical
uniprot
P51636
canonical
ensembl
ENSG00000105971
resolver
ensp
ENSP00000222693
resolver
ensp
ENSP00000345679
resolver
genesymbol
CAV2
resolver
hgnc
HGNC:1528
resolver
uniprot
A4D0U2
resolver
uniprot
Q53X57
resolver
uniprot
Q9UGM7
resolver
uniprot_entry
CAV2_HUMAN
resolver
uniprot_entry
Q53X57_HUMAN
resolver
uniprot_sec
A4D0U2
resolver
uniprot_sec
Q9UGM7
resolver
amino_acid_sequence
MGLETEKADVQLFMDDDSYSHHSGLEYADPEKFADSDQDRDPHRLNSHLKLGFEDVIAEPVTTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVIIAPLCTSVGRCFSSVSLQLSQD
uniprot
proteins
function
FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity). {ECO:0000250, ECO:0000269|PubMed:15504032, ECO:0000269|PubMed:18081315}.
uniprot
proteins
mass_dalton
18291
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="Y->A: Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated tyrosine phosphorylation and binding to RASA1, SRC and NCK1; when associated with A-27."; /evidence="ECO:0000269|PubMed:15504032"; MUTAGEN 23; /note="S->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:18081315"; MUTAGEN 27; /note="Y->A: Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated phosphorylation and binding of RASA1, SRC and NCK1; when associated with A-19."; /evidence="ECO:0000269|PubMed:15504032"; MUTAGEN 36; /note="S->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:18081315
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity). Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
Caveolin family
uniprot
proteins
pubmed
10218480
uniprot
proteins
pubmed
12091389
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15504032
uniprot
proteins
pubmed
18081315
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
8552590
uniprot
proteins
pubmed
9361015
uniprot
proteins
pubmed
9738464
uniprot
proteins
sequence_length
162
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments. {ECO:0000250}.
uniprot
proteins