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Protein Page:
Caveolin-1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Caveolin-1 May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Involved in the costimulatory signal essential for T-cell receptor (TCR)- mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3- dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway. Homooligomer. Interacts with GLIPR2, NOSTRIN, SNAP25 and syntaxin. Interacts with rotavirus A NSP4. Interacts (via the N- terminus) with DPP4; the interaction is direct. Interacts with CTNNB1, CDH1 and JUP. Interacts with BMX and BTK. Expressed in muscle and lung, less so in liver, brain and kidney. Belongs to the caveolin family. 2 isoforms of the human protein are produced by alternative initiation. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; Adaptor/scaffold; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 7q31.1
Cellular Component: acrosomal membrane; apical plasma membrane; basal plasma membrane; basolateral plasma membrane; caveola; cell cortex; cell surface; cilium; cytoplasmic vesicle; cytosol; early endosome membrane; endoplasmic reticulum; endoplasmic reticulum membrane; endosome; focal adhesion; Golgi membrane; integral to plasma membrane; intracellular; lipid particle; lipid raft; membrane; mitochondrion; perinuclear region of cytoplasm; peroxisomal membrane; plasma membrane; protein complex
Molecular Function: ATPase binding; cholesterol binding; enzyme binding; identical protein binding; nitric-oxide synthase binding; patched binding; protease activator activity; protein binding; protein binding, bridging; protein complex scaffold; protein heterodimerization activity; protein kinase binding; Rac GTPase binding; receptor binding; structural molecule activity; syntaxin binding
Biological Process: angiogenesis; blood coagulation; calcium ion homeostasis; calcium ion transport; cellular calcium ion homeostasis; cellular response to starvation; cholesterol efflux; cholesterol homeostasis; cholesterol transport; cytosolic calcium ion homeostasis; inactivation of MAPK activity; lactation; leukocyte migration; maintenance of cellular protein localization; mammary gland development; mammary gland involution; MAPKKK cascade; membrane depolarization; microtubule polymerization; negative regulation of BMP signaling pathway; negative regulation of cytokine and chemokine mediated signaling pathway; negative regulation of endothelial cell proliferation; negative regulation of epithelial cell differentiation; negative regulation of JAK-STAT cascade; negative regulation of MAPKKK cascade; negative regulation of neuron differentiation; negative regulation of nitric oxide biosynthetic process; negative regulation of nitric-oxide synthase activity; negative regulation of peptidyl-serine phosphorylation; negative regulation of pinocytosis; negative regulation of protein binding; negative regulation of protein ubiquitination; negative regulation of smooth muscle cell proliferation; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transforming growth factor beta receptor signaling pathway; negative regulation of tyrosine phosphorylation of Stat5 protein; nitric oxide homeostasis; nitric oxide metabolic process; organ regeneration; positive regulation of endocytosis; positive regulation of endothelial cell proliferation; positive regulation of metalloenzyme activity; positive regulation of microtubule polymerization; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein binding; positive regulation of protein ubiquitination; positive regulation of toll-like receptor 3 signaling pathway; positive regulation of vasoconstriction; protein homooligomerization; protein localization; receptor internalization; receptor mediated endocytosis of virus by host; regulation of blood coagulation; regulation of fatty acid metabolic process; regulation of nitric-oxide synthase activity; regulation of peptidase activity; regulation of smooth muscle contraction; regulation of the force of heart contraction by chemical signal; response to bacterium; response to calcium ion; response to drug; response to estrogen stimulus; response to gamma radiation; response to glucocorticoid stimulus; response to hypoxia; response to nutrient; response to progesterone stimulus; sequestering of lipid; skeletal muscle development; T cell costimulation; triacylglycerol metabolic process; vascular endothelial growth factor receptor signaling pathway; vasculogenesis; vasoconstriction; vesicle organization and biogenesis
Disease: Lipodystrophy, Congenital Generalized, Type 3; Partial Lipodystrophy, Congenital Cataracts, And Neurodegeneration Syndrome; Pulmonary Hypertension, Primary, 3
Reference #:  Q03135 (UniProtKB)
Alt. Names/Synonyms: BSCL3; CAV; CAV1; caveolin 1, caveolae protein, 22kDa; Caveolin-1; cell growth-inhibiting protein 32; CGL3; MSTP085; VIP21
Gene Symbols: CAV1
Molecular weight: 20,472 Da
Basal Isoelectric point: 5.64  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics  |  ErbB/HER Signaling  |  Insulin Receptor Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Caveolin-1

Protein Structure Not Found.


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Sites Implicated In
apoptosis, induced: Y14‑p
cell adhesion, altered: Y14‑p
cell cycle regulation: Y14‑p
cell growth, altered: Y14‑p
cell growth, induced: Y14‑p
cell motility, altered: Y14‑p
cell motility, induced: Y14‑p
cytoskeletal reorganization: Y14‑p
transcription, altered: Y14‑p
activity, induced: Y14‑p
intracellular localization: Y14‑p
molecular association, regulation: Y14‑p
phosphorylation: Y14‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 6 S2‑p ______MsGGkyVDs
0 3 K5‑ac ___MsGGkyVDsEGH
1 3 K5‑ub ___MsGGkyVDsEGH
2 90 Y6‑p __MsGGkyVDsEGHL
0 13 S9‑p sGGkyVDsEGHLytV
37 844 Y14‑p VDsEGHLytVPIREQ
0 127 T15‑p DsEGHLytVPIREQG
2 106 Y25‑p IREQGNIykPNNkAM
0 1 K26 REQGNIyKPNNkAMA
1 9 K26‑ub REQGNIykPNNkAMA
0 1 K30 NIykPNNKAMADELs
1 8 K30‑ub NIykPNNkAMADELs
0 53 S37‑p kAMADELsEkQVyDA
0 1 K39 MADELsEKQVyDAHt
1 19 K39‑ub MADELsEkQVyDAHt
1 79 Y42‑p ELsEkQVyDAHtkEI
0 6 T46‑p kQVyDAHtkEIDLVN
0 1 K47 QVyDAHtKEIDLVNR
1 3 K47‑ub QVyDAHtkEIDLVNR
1 3 K57‑ub DLVNRDPkHLNDDVV
0 1 K65‑ub HLNDDVVkIDFEDVI
2 0 S80‑p AEPEGTHsFDGIWKA
1 0 S88 FDGIWKASFTTFTVT
0 2 K176‑ub NVRINLQkEI_____
  mouse

 
S2‑p ______MsGGkyVDs
K5 ___MsGGKyVDsEGH
K5‑ub ___MsGGkyVDsEGH
Y6‑p __MsGGkyVDsEGHL
S9‑p sGGkyVDsEGHLytV
Y14‑p VDsEGHLytVPIREQ
T15‑p DsEGHLytVPIREQG
Y25‑p IREQGNIykPNNkAM
K26 REQGNIyKPNNkAMA
K26‑ub REQGNIykPNNkAMA
K30 NIykPNNKAMADEVt
K30‑ub NIykPNNkAMADEVt
T37‑p kAMADEVtEkQVyDA
K39 MADEVtEKQVyDAHt
K39‑ub MADEVtEkQVyDAHt
Y42‑p EVtEkQVyDAHtkEI
T46‑p kQVyDAHtkEIDLVN
K47 QVyDAHtKEIDLVNR
K47‑ub QVyDAHtkEIDLVNR
K57‑ub DLVNRDPkHLNDDVV
K65 HLNDDVVKIDFEDVI
S80 AEPEGTHSFDGIWKA
S88 FDGIWKASFTTFTVT
K176‑ub NIRISTQkEI_____
3251 : Phospho-Caveolin-1 (Tyr14) Antibody
  rat

 
S2‑p ______MsGGkYVDs
K5‑ac ___MsGGkYVDsEGH
K5 ___MsGGKYVDsEGH
Y6 __MsGGkYVDsEGHL
S9‑p sGGkYVDsEGHLyTV
Y14‑p VDsEGHLyTVPIREQ
T15 DsEGHLyTVPIREQG
Y25 IREQGNIYkPNNkAM
K26‑ac REQGNIYkPNNkAMA
K26 REQGNIYKPNNkAMA
K30‑ac NIYkPNNkAMADEVN
K30 NIYkPNNKAMADEVN
N37 kAMADEVNEkQVYDA
K39‑ac MADEVNEkQVYDAHT
K39 MADEVNEKQVYDAHT
Y42 EVNEkQVYDAHTkEI
T46 kQVYDAHTkEIDLVN
K47‑ac QVYDAHTkEIDLVNR
K47 QVYDAHTKEIDLVNR
K57 DLVNRDPKHLNDDVV
K65 HLNDDVVKIDFEDVI
S80 AEPEGTHSFDGIWKA
S88 FDGIWKASFTTFTVT
E176 NIRISTQEEI_____
3251 : Phospho-Caveolin-1 (Tyr14) Antibody
  dog

 
S2 ______MSGGKYVDS
K5 ___MSGGKYVDSEGH
K5 ___MSGGKYVDSEGH
Y6 __MSGGKYVDSEGHL
S9 SGGKYVDSEGHLyTV
Y14‑p VDSEGHLyTVPIREQ
T15 DSEGHLyTVPIREQG
Y25 IREQGNIYKPNNKAM
K26 REQGNIYKPNNKAMA
K26 REQGNIYKPNNKAMA
K30 NIYKPNNKAMAEEMS
K30 NIYKPNNKAMAEEMS
S37 KAMAEEMSEKQVYDA
K39 MAEEMSEKQVYDAHT
K39 MAEEMSEKQVYDAHT
Y42 EMSEKQVYDAHTKEI
T46 KQVYDAHTKEIDLVN
K47 QVYDAHTKEIDLVNR
K47 QVYDAHTKEIDLVNR
K57 DLVNRDPKHLNDDVV
K65 HLNDDVVKIDFEDVI
S80‑p AEPEGTHsFDGIWKA
S88‑p FDGIWKAsFTTFTVT
K176 NIRINMQKET_____
  sheep

 
S2 ______MSGGKYVDS
K5 ___MSGGKYVDSEGH
K5 ___MSGGKYVDSEGH
Y6 __MSGGKYVDSEGHL
S9 SGGKYVDSEGHLyTV
Y14‑p VDSEGHLyTVPIREQ
T15 DSEGHLyTVPIREQG
Y25 IREQGNIYKPNNKAM
K26 REQGNIYKPNNKAMA
K26 REQGNIYKPNNKAMA
K30 NIYKPNNKAMAEEMN
K30 NIYKPNNKAMAEEMN
N37 KAMAEEMNEKQVYDA
K39 MAEEMNEKQVYDAHT
K39 MAEEMNEKQVYDAHT
Y42 EMNEKQVYDAHTKEI
T46 KQVYDAHTKEIDLVN
K47 QVYDAHTKEIDLVNR
K47 QVYDAHTKEIDLVNR
K57 DLVNRDPKHLNDDVV
K65 HLNDDVVKIDFEDVI
S80 AEPEGTHSFDGIWKA
S88 FDGIWKASFTTFTVT
K176 NIRINTQKEI_____
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