UniProt Accession

 CAV1_HUMAN; Q03135; Q9UGP1; Q9UNG1; Q9UQH6 

Genbank Protein ID

 Z18951; AF095593; AF095591; AF095592; AJ133269; AF125348; BT007143; BC009685; BC082246 

Genbank Nucleotide ID

 CAA79476.1; AAD23745.1; AAD23745.1; AAD23745.1; CAB63654.1; AAD34722.1; AAP35807.1; AAH09685.1; AAH82246.1 

Protein Name

 Caveolin-1 

Protein Synonyms/Alias

  

Gene Name

 CAV1 

Gene Synonyms/Alias

 CAV 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MSGGKYVDSEGH	acetylation	[1, 2]
5	***MSGGKYVDSEGH	ubiquitination	[3, 4, 5, 6]
26	REQGNIYKPNNKAMA	ubiquitination	[4, 5, 6, 7, 8]
30	NIYKPNNKAMADELS	ubiquitination	[4, 6, 7, 8]
39	MADELSEKQVYDAHT	ubiquitination	[3, 4, 5, 6, 7, 8]
47	QVYDAHTKEIDLVNR	ubiquitination	[4, 5, 6, 7]
57	DLVNRDPKHLNDDVV	ubiquitination	[3, 6, 7]
65	HLNDDVVKIDFEDVI	ubiquitination	[8]
176	NVRINLQKEI*****	ubiquitination	[7]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

 May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). 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. 

Sequence Annotation

 MOD_RES 2 2 N-acetylserine.
 MOD_RES 5 5 N6-acetyllysine.
 MOD_RES 6 6 Phosphotyrosine.
 MOD_RES 14 14 Phosphotyrosine; by ABL1.
 MOD_RES 25 25 Phosphotyrosine.
 MOD_RES 37 37 Phosphoserine.
 MOD_RES 42 42 Phosphotyrosine.
 LIPID 133 133 S-palmitoyl cysteine (By similarity).
 LIPID 143 143 S-palmitoyl cysteine (By similarity).
 LIPID 156 156 S-palmitoyl cysteine (By similarity).  

Keyword

 Acetylation; Alternative initiation; Cell membrane; Complete proteome; Congenital generalized lipodystrophy; Direct protein sequencing; Disease mutation; Golgi apparatus; Host-virus interaction; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 178 AA 

Protein Sequence

Gene Ontology

 GO:0002080; C:acrosomal membrane; IEA:Compara.
 GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
 GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
 GO:0005901; C:caveola; IDA:UniProtKB.
 GO:0005938; C:cell cortex; IEA:Compara.
 GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
 GO:0005783; C:endoplasmic reticulum; IDA:HGNC.
 GO:0005768; C:endosome; IDA:UniProtKB.
 GO:0000139; C:Golgi membrane; IDA:HGNC.
 GO:0005887; C:integral to plasma membrane; IEA:Compara.
 GO:0005811; C:lipid particle; TAS:Reactome.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0015485; F:cholesterol binding; TAS:HGNC.
 GO:0016504; F:peptidase activator activity; ISS:BHF-UCL.
 GO:0032947; F:protein complex scaffold; TAS:BHF-UCL.
 GO:0001525; P:angiogenesis; IEA:Compara.
 GO:0097190; P:apoptotic signaling pathway; IMP:UniProtKB.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0006816; P:calcium ion transport; ISS:BHF-UCL.
 GO:0070836; P:caveola assembly; IMP:BHF-UCL.
 GO:0072584; P:caveolin-mediated endocytosis; IDA:UniProtKB.
 GO:0071455; P:cellular response to hyperoxia; IMP:UniProtKB.
 GO:0009267; P:cellular response to starvation; IEP:BHF-UCL.
 GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
 GO:0030301; P:cholesterol transport; TAS:HGNC.
 GO:0051480; P:cytosolic calcium ion homeostasis; IDA:BHF-UCL.
 GO:0000188; P:inactivation of MAPK activity; ISS:BHF-UCL.
 GO:0007595; P:lactation; IEA:Compara.
 GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO:0019915; P:lipid storage; ISS:BHF-UCL.
 GO:0032507; P:maintenance of protein location in cell; ISS:BHF-UCL.
 GO:0060056; P:mammary gland involution; ISS:BHF-UCL.
 GO:0000165; P:MAPK cascade; IEA:Compara.
 GO:0051899; P:membrane depolarization; ISS:BHF-UCL.
 GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
 GO:0030514; P:negative regulation of BMP signaling pathway; IDA:BHF-UCL.
 GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; ISS:UniProtKB.
 GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IEA:Compara.
 GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:BHF-UCL.
 GO:0030857; P:negative regulation of epithelial cell differentiation; ISS:BHF-UCL.
 GO:0046426; P:negative regulation of JAK-STAT cascade; ISS:BHF-UCL.
 GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
 GO:0051001; P:negative regulation of nitric-oxide synthase activity; IEA:Compara.
 GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
 GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
 GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0042524; P:negative regulation of tyrosine phosphorylation of Stat5 protein; IEA:Compara.
 GO:0033484; P:nitric oxide homeostasis; ISS:BHF-UCL.
 GO:0046209; P:nitric oxide metabolic process; TAS:Reactome.
 GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISS:BHF-UCL.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
 GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
 GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
 GO:0048554; P:positive regulation of metalloenzyme activity; ISS:BHF-UCL.
 GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
 GO:0045907; P:positive regulation of vasoconstriction; ISS:BHF-UCL.
 GO:0051260; P:protein homooligomerization; ISS:BHF-UCL.
 GO:2000286; P:receptor internalization involved in canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
 GO:0030193; P:regulation of blood coagulation; IMP:BHF-UCL.
 GO:0019217; P:regulation of fatty acid metabolic process; ISS:BHF-UCL.
 GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
 GO:0006940; P:regulation of smooth muscle contraction; ISS:BHF-UCL.
 GO:0003057; P:regulation of the force of heart contraction by chemical signal; IEA:Compara.
 GO:0051592; P:response to calcium ion; ISS:BHF-UCL.
 GO:0043627; P:response to estrogen stimulus; IDA:MGI.
 GO:0001666; P:response to hypoxia; ISS:BHF-UCL.
 GO:0002931; P:response to ischemia; IEA:Compara.
 GO:0032570; P:response to progesterone stimulus; IDA:MGI.
 GO:0007519; P:skeletal muscle tissue development; ISS:BHF-UCL.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0031295; P:T cell costimulation; IDA:UniProtKB.
 GO:0006641; P:triglyceride metabolic process; ISS:BHF-UCL.
 GO:0001570; P:vasculogenesis; ISS:BHF-UCL.
 GO:0042310; P:vasoconstriction; IEA:Compara.
 GO:0016050; P:vesicle organization; IDA:BHF-UCL.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR001612; Caveolin.
 IPR015504; Caveolin_1.
 IPR018361; Caveolin_CS. 

Pfam

 PF01146; Caveolin 

SMART

  

PROSITE

 PS01210; CAVEOLIN 

PRINTS