Q03135 (CAV1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caveolin-1

Gene names

Name:	CAV1
Synonyms:	CAV

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	178 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.17
Subunit structure	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 By similarity. Interacts with BMX and BTK. Ref.8 Ref.9 Ref.14 Ref.15 Ref.17
Subcellular location	Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane › caveola; Peripheral membrane protein. Membrane raft. Note: Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Ref.6 Ref.8 Ref.17
Tissue specificity	Expressed in muscle and lung, less so in liver, brain and kidney.
Post-translational modification	The initiator methionine for isoform Beta is removed during or just after translation. The new N-terminal amino acid is then N-acetylated. Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. Ref.6 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Involvement in disease	Defects in CAV1 are the cause of congenital generalized lipodystrophy type 3 (CGL3) [MIM:612526]; also called Berardinelli-Seip congenital lipodystrophy type 3 (BSCL3). Congenital generalized lipodystrophies are autosomal recessive disorders characterized by a near absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes. Ref.25
Sequence similarities	Belongs to the caveolin family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell membrane Golgi apparatus Membrane
Coding sequence diversity	Alternative initiation
Disease	Congenital generalized lipodystrophy Disease mutation
PTM	Acetylation Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	T cell costimulation Inferred from direct assay Ref.17. Source: UniProtKB blood coagulation Traceable author statement. Source: Reactome calcium ion transport Inferred from sequence or structural similarity. Source: BHF-UCL caveola assembly Inferred from mutant phenotype. Source: BHF-UCL cellular response to hyperoxia Inferred from mutant phenotype. Source: UniProtKB cellular response to starvation Inferred from expression pattern. Source: BHF-UCL cholesterol homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL cytosolic calcium ion homeostasis Inferred from direct assay. Source: BHF-UCL inactivation of MAPK activity Inferred from sequence or structural similarity. Source: BHF-UCL induction of apoptosis by extracellular signals Inferred from mutant phenotype. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW leukocyte migration Traceable author statement. Source: Reactome lipid storage Inferred from sequence or structural similarity. Source: BHF-UCL maintenance of protein location in cell Inferred from sequence or structural similarity. Source: BHF-UCL mammary gland involution Inferred from sequence or structural similarity. Source: BHF-UCL membrane depolarization Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of BMP signaling pathway Inferred from direct assay. Source: BHF-UCL negative regulation of canonical Wnt receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of endothelial cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of epithelial cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of nitric oxide biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of peptidyl-serine phosphorylation Inferred from direct assay. Source: BHF-UCL negative regulation of protein binding Inferred from direct assay. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB nitric oxide homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL nitric oxide metabolic process Traceable author statement. Source: Reactome positive regulation of calcium ion transport into cytosol Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype. Source: BHF-UCL positive regulation of metalloenzyme activity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of peptidyl-serine phosphorylation Inferred from direct assay. Source: BHF-UCL positive regulation of vasoconstriction Inferred from sequence or structural similarity. Source: BHF-UCL protein homooligomerization Inferred from sequence or structural similarity. Source: BHF-UCL receptor internalization involved in canonical Wnt receptor signaling pathway Inferred from mutant phenotype. Source: BHF-UCL regulation of blood coagulation Inferred from mutant phenotype. Source: BHF-UCL regulation of fatty acid metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL regulation of nitric-oxide synthase activity Traceable author statement. Source: Reactome regulation of smooth muscle contraction Inferred from sequence or structural similarity. Source: BHF-UCL response to calcium ion Inferred from sequence or structural similarity. Source: BHF-UCL response to estrogen stimulus Inferred from direct assay. Source: MGI response to hypoxia Inferred from sequence or structural similarity. Source: BHF-UCL response to progesterone stimulus Inferred from direct assay. Source: MGI skeletal muscle tissue development Inferred from sequence or structural similarity. Source: BHF-UCL triglyceride metabolic process Inferred from sequence or structural similarity. Source: BHF-UCL vasculogenesis Inferred from sequence or structural similarity. Source: BHF-UCL vesicle organization Inferred from direct assay. Source: BHF-UCL
Cellular component	Golgi membrane Inferred from direct assay. Source: HGNC apical plasma membrane Inferred from direct assay. Source: BHF-UCL basolateral plasma membrane Inferred from direct assay. Source: BHF-UCL caveola Inferred from direct assay Ref.6. Source: UniProtKB cytosol Inferred from direct assay. Source: GOC endocytic vesicle membrane Traceable author statement. Source: Reactome endoplasmic reticulum Inferred from direct assay. Source: HGNC endosome Inferred from direct assay. Source: UniProtKB lipid particle Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	cholesterol binding Traceable author statement. Source: HGNC nitric-oxide synthase binding Inferred from physical interaction. Source: BHF-UCL peptidase activator activity Inferred from sequence or structural similarity. Source: BHF-UCL protein binding Inferred from physical interaction. Source: BHF-UCL protein complex scaffold Traceable author statement. Source: BHF-UCL receptor binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BID	P55957	3	EBI-603614,EBI-519672
F2R	P25116	3	EBI-603614,EBI-2803960
FAS	P25445	3	EBI-603614,EBI-494743
ID1	P41134	6	EBI-603614,EBI-1215527
SCP2	P22307	3	EBI-603614,EBI-1050999

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Alpha (identifier: Q03135-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Beta (identifier: Q03135-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Note: Met-1 is removed. Acetylated on Ala-2.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 178	177	Caveolin-1		PRO_0000004764
Regions
	Topological domain	2 – 104	103	Cytoplasmic Potential
	Intramembrane	105 – 125	21	Helical; Potential
	Topological domain	126 – 178	53	Cytoplasmic Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.6
	Modified residue	5	1	N6-acetyllysine Ref.23
	Modified residue	6	1	Phosphotyrosine Ref.11 Ref.18 Ref.21
	Modified residue	14	1	Phosphotyrosine; by ABL1 Ref.10 Ref.11 Ref.12 Ref.16 Ref.18 Ref.21
	Modified residue	25	1	Phosphotyrosine Ref.11 Ref.21
	Modified residue	37	1	Phosphoserine Ref.13 Ref.19 Ref.20 Ref.22
	Modified residue	42	1	Phosphotyrosine Ref.21
	Lipidation	133	1	S-palmitoyl cysteine By similarity
	Lipidation	143	1	S-palmitoyl cysteine By similarity
	Lipidation	156	1	S-palmitoyl cysteine By similarity
Natural variations
	Alternative sequence	1 – 31	31	Missing in isoform Beta.		VSP_018692
	Natural variant	132	1	P → L in breast cancer; seems to form misfolded oligomers that are retained within the Golgi complex and are not targeted to caveolae or the plasma membrane. Ref.24		VAR_015103
Experimental info
	Sequence conflict	82	1	D → H in CAA79476. Ref.1
	Sequence conflict	144	1	I → T in CAA79476. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 2424DE9B5E6521D5	FASTA	178	20,472
	10 20 30 40 50 60 MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADELSEKQ VYDAHTKEID LVNRDPKHLN 70 80 90 100 110 120 DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSALFGIP MALIWGIYFA 130 140 150 160 170 ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTVCDPLF EAVGKIFSNV RINLQKEI
	Isoform Beta [UniParc]. Checksum: 1A7D806312F72A47	FASTA	147	17,023
	10 20 30 40 50 60 MADELSEKQV YDAHTKEIDL VNRDPKHLND DVVKIDFEDV IAEPEGTHSF DGIWKASFTT 70 80 90 100 110 120 FTVTKYWFYR LLSALFGIPM ALIWGIYFAI LSFLHIWAVV PCIKSFLIEI QCISRVYSIY 130 140 VHTVCDPLFE AVGKIFSNVR INLQKEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles." Glenney J.R. Jr. FEBS Lett. 314:45-48(1992) [PubMed: 1360410] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[2]	"Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines." Hurlstone A.F., Reid G., Reeves J.R., Fraser J., Strathdee G., Rahilly M., Parkinson E.K., Black D.M. Oncogene 18:1881-1890(1999) [PubMed: 10086342] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines." Engelman J.A., Zhang X.L., Lisanti M.P. FEBS Lett. 448:221-230(1999) [PubMed: 10218480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Lung.
[6]	"N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes." Vainonen J.P., Aboulaich N., Turkina M.V., Stralfors P., Vener A.V. Biochem. Biophys. Res. Commun. 320:480-486(2004) [PubMed: 15219854] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-66, SUBCELLULAR LOCATION, ACETYLATION AT SER-2, PHOSPHORYLATION. Tissue: Adipose tissue.
[7]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed: 15242332] [Abstract] Cited for: PROTEIN SEQUENCE OF 58-65. Tissue: Adipocyte.
[8]	"Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx." Vargas L., Nore B.F., Berglof A., Heinonen J.E., Mattsson P.T., Smith C.I., Mohamed A.J. J. Biol. Chem. 277:9351-9357(2002) [PubMed: 11751885] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BMX AND BTK.
[9]	"Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex." Eberle H.B., Serrano R.L., Fuellekrug J., Schlosser A., Lehmann W.D., Lottspeich F., Kaloyanova D., Wieland F.T., Helms J.B. J. Cell Sci. 115:827-838(2002) [PubMed: 11865038] [Abstract] Cited for: INTERACTION WITH GLIPR2. Tissue: Brain.
[10]	"c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14." Sanguinetti A.R., Mastick C.C. Cell. Signal. 15:289-298(2003) [PubMed: 12531427] [Abstract] Cited for: PHOSPHORYLATION AT TYR-14.
[11]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6; TYR-14 AND TYR-25, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[12]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-14, MASS SPECTROMETRY.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN." Schilling K., Opitz N., Wiesenthal A., Oess S., Tikkanen R., Mueller-Esterl W., Icking A. Mol. Biol. Cell 17:3870-3880(2006) [PubMed: 16807357] [Abstract] Cited for: INTERACTION WITH NOSTRIN.
[15]	"The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1." Parr R.D., Storey S.M., Mitchell D.M., McIntosh A.L., Zhou M., Mir K.D., Ball J.M. J. Virol. 80:2842-2854(2006) [PubMed: 16501093] [Abstract] Cited for: INTERACTION WITH ROTAVIRUS A NSP4.
[16]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-14, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[17]	"Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1." Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C. J. Biol. Chem. 282:10117-10131(2007) [PubMed: 17287217] [Abstract] Cited for: FUNCTION, INTERACTION WITH DPP4, SUBCELLULAR LOCATION.
[18]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6 AND TYR-14, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[19]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6; TYR-14; TYR-25 AND TYR-42, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[22]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5, MASS SPECTROMETRY.
[24]	"Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia." Lee H., Park D.S., Razani B., Russell R.G., Pestell R.G., Lisanti M.P. Am. J. Pathol. 161:1357-1369(2002) [PubMed: 12368209] [Abstract] Cited for: VARIANT LEU-132.
[25]	"Association of a homozygous nonsense caveolin-1 mutation with Berardinelli-Seip congenital lipodystrophy." Kim C.A., Delepine M., Boutet E., El Mourabit H., Le Lay S., Meier M., Nemani M., Bridel E., Leite C.C., Bertola D.R., Semple R.K., O'Rahilly S., Dugail I., Capeau J., Lathrop M., Magre J. J. Clin. Endocrinol. Metab. 93:1129-1134(2008) [PubMed: 18211975] [Abstract] Cited for: INVOLVEMENT IN CGL3.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Caveolin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z18951 mRNA. Translation: CAA79476.1. AF095593, AF095591, AF095592 Genomic DNA. Translation: AAD23745.1. AJ133269 Genomic DNA. Translation: CAB63654.1. AF125348 Genomic DNA. Translation: AAD34722.1. BT007143 mRNA. Translation: AAP35807.1. BC009685 mRNA. Translation: AAH09685.1. BC082246 mRNA. Translation: AAH82246.1.
IPI	IPI00009236. IPI00759683.
PIR	S26884.
RefSeq	NP_001744.2. NM_001753.4.
UniGene	Hs.74034.
3D structure databases
ProteinModelPortal	Q03135.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5960N.
IntAct	Q03135. 16 interactions.
MINT	MINT-152933.
STRING	Q03135.
PTM databases
PhosphoSite	Q03135.
Polymorphism databases
DMDM	13637934.
Proteomic databases
PeptideAtlas	Q03135.
PRIDE	Q03135.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341049; ENSP00000339191; ENSG00000105974.
GeneID	857.
KEGG	hsa:857.
UCSC	uc003vif.1. human. uc003vih.2. human.
Organism-specific databases
CTD	857.
GeneCards	GC07P116164.
H-InvDB	HIX0007018.
HGNC	HGNC:1527. CAV1.
HPA	CAB003791.
MIM	601047. gene. 612526. phenotype.
neXtProt	NX_Q03135.
Orphanet	528. Berardinelli-Seip congenital lipodystrophy.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11341.
HOVERGEN	HBG003422.
InParanoid	Q03135.
OMA	VHTFCDP.
OrthoDB	EOG4JQ3ZP.
PhylomeDB	Q03135.
Enzyme and pathway databases
Pathway_Interaction_DB	insulin_pathway. Insulin Pathway. pdgfrapathway. PDGFR-alpha signaling pathway. ptp1bpathway. Signaling events mediated by PTP1B. vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2. tgfbrpathway. TGF-beta receptor signaling. tnfpathway. TNF receptor signaling pathway. vegfr1_pathway. VEGFR1 specific signals.
Reactome	REACT_111217. Metabolism. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q03135.
Bgee	Q03135.
CleanEx	HS_CAV1.
Genevestigator	Q03135.
GermOnline	ENSG00000105974. Homo sapiens.
Family and domain databases
InterPro	IPR001612. Caveolin. IPR015504. Caveolin_1. IPR018361. Caveolin_CS. [Graphical view]
KO	K06278.
PANTHER	PTHR10844. Caveolin. 1 hit. PTHR10844:SF5. Caveolin_1. 1 hit.
Pfam	PF01146. Caveolin. 1 hit. [Graphical view]
PROSITE	PS01210. CAVEOLIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	3556.
SOURCE	Search...

Entry information

Entry name

CAV1_HUMAN

Accession

Primary (citable) accession number: Q03135
Secondary accession number(s): Q9UGP1, Q9UNG1, Q9UQH6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 137 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.