extrinsic component of cytoplasmic side of plasma membrane
Golgi membrane
plasma membrane
integral component of plasma membrane
intracellular anatomical structure
transport vesicle
acrosomal membrane
perinuclear region of cytoplasm
caveola
membrane raft
cytoplasmic vesicle
nucleus
protein-containing complex
sarcolemma
Biological process
insulin receptor signaling pathway
positive regulation of endothelial cell proliferation
caveola assembly
vesicle organization
mitochondrion organization
negative regulation of transforming growth factor beta receptor signaling pathway
positive regulation of dopamine receptor signaling pathway
endoplasmic reticulum organization
negative regulation of endothelial cell proliferation
vesicle docking
positive regulation of GTPase activity
positive regulation by host of viral process
skeletal muscle fiber development
protein complex oligomerization
receptor-mediated endocytosis of virus by host cell
vesicle fusion
positive regulation of MAPK cascade
regulation of mitotic nuclear division
negative regulation of cell population proliferation
cell differentiation
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
858
12390
Ensembl
ENSG00000105971
ENSMUSG00000000058
UniProt
P51636
Q9WVC3
RefSeq (mRNA)
NM_001206747 NM_001206748 NM_001233 NM_198212
NM_001277756 NM_016900
RefSeq (protein)
NP_001193676 NP_001193677 NP_001224 NP_937855
NP_001264685 NP_058596
Location (UCSC)
Chr 7: 116.29 – 116.51 Mb
Chr 6: 17.28 – 17.29 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Caveolin-2 is a protein that in humans is encoded by the CAV2 gene.[5][6][7]
The protein encoded by this gene is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. This protein may function as a tumor suppressor. The CAV1 and CAV2 genes are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex,[7][8] which can be disrupted by Src-mediated phosphorylation of tyrosine 19 on caveolin-2.[9] Two transcript variants encoding distinct isoforms have been identified for this gene. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by one transcript.[7]
^ abcGRCh38: Ensembl release 89: ENSG00000105971 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000000058 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Scherer PE, Okamoto T, Chun M, Nishimoto I, Lodish HF, Lisanti MP (Feb 1996). "Identification, sequence, and expression of caveolin-2 defines a caveolin gene family". Proc Natl Acad Sci U S A. 93 (1): 131–5. Bibcode:1996PNAS...93..131S. doi:10.1073/pnas.93.1.131. PMC 40192. PMID 8552590.
^Fra AM, Mastroianni N, Mancini M, Pasqualetto E, Sitia R (May 1999). "Human caveolin-1 and caveolin-2 are closely linked genes colocalized with WI-5336 in a region of 7q31 frequently deleted in tumors". Genomics. 56 (3): 355–6. doi:10.1006/geno.1998.5723. PMID 10087206.
^ abc"Entrez Gene: CAV2 caveolin 2".
^Scherer PE, Lewis R Y, Volonte D, Engelman J A, Galbiati F, Couet J, Kohtz D S, van Donselaar E, Peters P, Lisanti M P (Nov 1997). "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo". J. Biol. Chem. 272 (46). UNITED STATES: 29337–46. doi:10.1074/jbc.272.46.29337. ISSN 0021-9258. PMID 9361015.
^Lee H, Park David S, Wang Xiao Bo, Scherer Philipp E, Schwartz Phillip E, Lisanti Michael P (Sep 2002). "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1". J. Biol. Chem. 277 (37). United States: 34556–67. doi:10.1074/jbc.M204367200. ISSN 0021-9258. PMID 12091389.
Caveolin-2 is a protein that in humans is encoded by the CAV2 gene. The protein encoded by this gene is a major component of the inner surface of caveolae...
proteins caveolin-1, caveolin-2, and caveolin-3, respectively. All three members are membrane proteins with similar structure. Caveolin forms oligomers and...
Caveolin-1 is a protein that in humans is encoded by the CAV1 gene. The scaffolding protein encoded by this gene is the main component of the caveolae...
discovered the clathrin coat molecule in 1976. Caveolin proteins like caveolin-1 (CAV1), caveolin-2 (CAV2), and caveolin-3 (CAV3), play significant roles in the...
possibly related to overexpression (hypomethylation) of caveolin 1 and caveolin2. Caveolin is, paradoxically, tumour-promoting in IBC. NF-κB pathway...
aeruginosa, from invading murine lung epithelial cells by knocking down the caveolin-2 (CAV2) gene. Thus, though bacteria cannot be directly targeted by siRNA...
Mediates Bacterial Invasion through Ku70 in an Actin, c-Cbl, Clathrin and Caveolin2-Dependent Manner". Cellular Microbiology. 11 (4): 629–644. doi:10.1111/j...
their product. One of these cases is tyrosine phosphorylation of caveolin2 (Cav-2) that negatively regulates the anti-proliferative function of transforming...
caveolins associate with lipid rafts and form oligomers (14-16 molecules). These oligomerized caveolins form the caveolae. The presence of caveolin leads...
MP (September 2002). "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains...
and direct interaction of eNOS with caveolin-1. The binding of calcium-activated calmodulin to eNOS displaces caveolin-1 and activates eNOS. However, more...
Caveolin-3 is a protein that in humans is encoded by the CAV3 gene. Alternative splicing has been identified for this locus, with inclusion or exclusion...
microRNA-103/107 may affect insulin sensitivity by targeting caveolin-1. The blockmir CD5-2 has been shown to inhibit the interaction between miR-27 and...
of molecules within a vesicle. Examples include: Archain ARFs Clathrin Caveolin Dynamin and related proteins, such as the EHD protein family Rab proteins...
perhaps larger oligomers. It can also has been shown to interact with Caveolin 3 in skeletal muscle, and this interaction is thought to retain dysferlin...
protein, caveolin-3. Caveolins form specific membrane domains called caveolae in which voltage-gated sodium channels sit. Similar to LQT3, these caveolin variants...
5.2 kb. The virion adheres to cell surface receptors of MHC class I by the virion glycoprotein VP1. Penetration into the cell is through a caveolin vesicle...
S2CID 22056818. Pflug, BR; Reiter, RE; Nelson, JB (1 September 1999). "Caveolin expression is decreased following androgen deprivation in human prostate...
as well as in hepatocytes; it blocks aminopeptidase N and interrupts a caveolin 1–annexin A2 complex involved in trafficking cholesterol. Within 4–12 hours...
Global Information
