Cav2
entrez
363425
canonical
uniprot
Q2IBC5
canonical
ensembl
ENSRNOG00055018134
resolver
ensembl
ENSRNOG00060000798
resolver
ensembl
ENSRNOG00065007760
resolver
ensp
ENSRNOP00055024704
resolver
ensp
ENSRNOP00060000299
resolver
ensp
ENSRNOP00065008897
resolver
enst
ENSRNOT00055030712
resolver
enst
ENSRNOT00060000977
resolver
enst
ENSRNOT00065012168
resolver
genesymbol
Cav2
resolver
uniprot
Q6P6R8
resolver
uniprot
Q8VIK7
resolver
uniprot_entry
CAV2_RAT
resolver
uniprot_sec
Q6P6R8
resolver
uniprot_sec
Q8VIK7
resolver
amino_acid_sequence
MGLETEKADVQLFMADDAYSHHSVVDYTDPEKYVDSSQDRDPHQLNSHLKLGFEDLIAEPPTTHSFDKVWICSHALFEISKYVIYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVVIGPLCTSVGRIFSSVSMQLSHD
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. {ECO:0000269|PubMed:19427337, ECO:0000269|PubMed:19778377}.
uniprot
proteins
mass_dalton
18266
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="Y->A: Abolishes phosphorylation, insulin-stimulated interaction with phosphorylated MAPK1, MAPK1 nuclear translocation and activation, reduction of insulin-induced DNA binding of STAT3 but no effect on 'S-727' phosphorylation of STAT3. Completely abolishes phosphorylation, decreases insulin-induced DNA binding and impairs nuclear location of STAT3, inhibits insulin-induced 'S-727' phosphorylation of STAT3, and eliminates binding to RASA1, SRC and NCK1; when associated with A-27."; /evidence="ECO:0000269|PubMed:19427337, ECO:0000269|PubMed:19778377"; MUTAGEN 27; /note="Y->A: Abolishes phosphorylation and insulin-induced nuclear location, but no effect on insulin-induced 'S-727' phosphorylation of STAT3 nor on MAPK1 phosphorylation. Completely abolishes insulin-induced phosphorylation, nuclear location, nuclear translocation of MAPK1 and STAT3 and 'S-727' phosphorylation of STAT3 and MAPK1 phosphorylation; when associated with A-19."; /evidence="ECO:0000269|PubMed:19427337
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which 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. {ECO:0000250, ECO:0000269|PubMed:19427337, ECO:0000269|PubMed:19778377}.
uniprot
proteins
protein_family
Caveolin family
uniprot
proteins
pubmed
11883949
uniprot
proteins
pubmed
12917688
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16645331
uniprot
proteins
pubmed
19427337
uniprot
proteins
pubmed
19778377
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, in response to insulin, is translocated to the nucleus in complex with MAPK1. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. The CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. The Ser-36-phosphorylated form resides in intracellular compartments (By similarity). {ECO:0000250}.
uniprot
proteins