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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 Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
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: Adaptor/scaffold; Nuclear receptor co-regulator; Motility/polarity/chemotaxis
Cellular Component: protein complex; integral to plasma membrane; endoplasmic reticulum; basolateral plasma membrane; lipid particle; cell cortex; caveola; acrosomal membrane; cilium; lipid raft; Golgi membrane; perinuclear region of cytoplasm; apical plasma membrane; plasma membrane; intracellular; cytoplasmic vesicle; endosome
Molecular Function: protein binding; enzyme binding; protease activator activity; cholesterol binding; patched binding; protein complex scaffold; nitric-oxide synthase binding; structural molecule activity; receptor binding
Biological Process: mammary gland involution; viral reproduction; negative regulation of epithelial cell differentiation; negative regulation of tyrosine phosphorylation of Stat5 protein; nitric oxide homeostasis; negative regulation of BMP signaling pathway; calcium ion homeostasis; protein localization; sequestering of lipid; regulation of the force of heart contraction by chemical signal; regulation of fatty acid metabolic process; negative regulation of protein binding; inactivation of MAPK activity; regulation of smooth muscle contraction; maintenance of cellular protein localization; skeletal muscle development; cytosolic calcium ion homeostasis; negative regulation of nitric-oxide synthase activity; cellular response to starvation; membrane depolarization; cholesterol homeostasis; response to estrogen stimulus; negative regulation of endothelial cell proliferation; T cell costimulation; negative regulation of protein ubiquitination; regulation of nitric-oxide synthase activity; response to calcium ion; response to progesterone stimulus; leukocyte migration; negative regulation of JAK-STAT cascade; lactation; vesicle organization and biogenesis; negative regulation of peptidyl-serine phosphorylation; negative regulation of transcription from RNA polymerase II promoter; negative regulation of pinocytosis; nitric oxide metabolic process; mammary gland development; calcium ion transport; negative regulation of cytokine and chemokine mediated signaling pathway; angiogenesis; vasculogenesis; protein homooligomerization; vasoconstriction; cholesterol transport; negative regulation of MAPKKK cascade; negative regulation of nitric oxide biosynthetic process; MAPKKK cascade; positive regulation of metalloenzyme activity; positive regulation of peptidyl-serine phosphorylation; regulation of peptidase activity; cellular calcium ion homeostasis; triacylglycerol metabolic process; regulation of blood coagulation; response to hypoxia; positive regulation of vasoconstriction; blood coagulation
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 motility, altered: 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


 SS 

SS: 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.


 MS 

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


       human

 
0 2 K5-ac ___MSGGkyVDsEGH
1 3 K5-ub ___MSGGkyVDsEGH
2 67 Y6-p __MSGGkyVDsEGHL
0 7 S9-p SGGkyVDsEGHLytV
35 803 Y14-p VDsEGHLytVPIREQ
0 121 T15-p DsEGHLytVPIREQG
2 95 Y25-p IREQGNIykPNNkAM
1 9 K26-ub REQGNIykPNNkAMA
1 8 K30-ub NIykPNNkAMADELs
0 41 S37-p kAMADELsEkQVyDA
1 20 K39-ub MADELsEkQVyDAHt
1 77 Y42-p ELsEkQVyDAHtkEI
0 4 T46-p kQVyDAHtkEIDLVN
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_____
3251 : Phospho-Caveolin-1 (Tyr14) Antibody
  mouse

 
K5 ___MSGGKyVDsEGH
K5-ub ___MSGGkyVDsEGH
Y6-p __MSGGkyVDsEGHL
S9-p SGGkyVDsEGHLytV
Y14-p VDsEGHLytVPIREQ
T15-p DsEGHLytVPIREQG
Y25-p IREQGNIykPNNkAM
K26-ub REQGNIykPNNkAMA
K30-ub NIykPNNkAMADEVt
T37-p kAMADEVtEkQVyDA
K39-ub MADEVtEkQVyDAHT
Y42-p EVtEkQVyDAHTkEI
T46 kQVyDAHTkEIDLVN
K47-ub QVyDAHTkEIDLVNR
K57-ub DLVNRDPkHLNDDVV
K65 HLNDDVVKIDFEDVI
S80 AEPEGTHSFDGIWKA
S88 FDGIWKASFTTFTVT
K176-ub NIRISTQkEI_____
3251 : Phospho-Caveolin-1 (Tyr14) Antibody
  rat

 
K5 ___MSGGKYVDSEGH
K5 ___MSGGKYVDSEGH
Y6 __MSGGKYVDSEGHL
S9 SGGKYVDSEGHLyTV
Y14-p VDSEGHLyTVPIREQ
T15 DSEGHLyTVPIREQG
Y25 IREQGNIYKPNNKAM
K26 REQGNIYKPNNKAMA
K30 NIYKPNNKAMADEVN
N37 KAMADEVNEKQVYDA
K39 MADEVNEKQVYDAHT
Y42 EVNEKQVYDAHTKEI
T46 KQVYDAHTKEIDLVN
K47 QVYDAHTKEIDLVNR
K57 DLVNRDPKHLNDDVV
K65 HLNDDVVKIDFEDVI
S80 AEPEGTHSFDGIWKA
S88 FDGIWKASFTTFTVT
E176 NIRISTQEEI_____
3251 : Phospho-Caveolin-1 (Tyr14) Antibody
  dog

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

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