ID CAV2_HUMAN Reviewed; 162 AA. AC P51636; A4D0U2; Q9UGM7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 04-NOV-2026, entry version 221. DE RecName: Full=Caveolin-2; GN Name=CAV2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). RX PubMed=8552590; DOI=10.1073/pnas.93.1.131; RA Scherer P.E., Okamoto T., Chun M., Nishimoto I., Lodish H.F., Lisanti M.P.; RT "Identification, sequence, and expression of caveolin-2 defines a caveolin RT gene family."; RL Proc. Natl. Acad. Sci. U.S.A. 93:131-135(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INTERACTION WITH CAV1, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9361015; DOI=10.1074/jbc.272.46.29337; RA Scherer P.E., Lewis R.Y., Volonte D., Engelman J.A., Galbiati F., Couet J., RA Kohtz D.S., van Donselaar E., Peters P., Lisanti M.P.; RT "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 RT co-localize and form a stable hetero-oligomeric complex in vivo."; RL J. Biol. Chem. 272:29337-29346(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10218480; DOI=10.1016/s0014-5793(99)00365-8; RA Engelman J.A., Zhang X.L., Lisanti M.P.; RT "Sequence and detailed organization of the human caveolin-1 and -2 genes RT located near the D7S522 locus (7q31.1). Methylation of a CpG island in the RT 5' promoter region of the caveolin-1 gene in human breast cancer cell RT lines."; RL FEBS Lett. 448:221-230(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C). RC TISSUE=Hepatoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH CAV1, ALTERNATIVE PRODUCTS, AND SUBCELLULAR LOCATION. RX PubMed=9738464; DOI=10.1016/s0014-5793(98)00945-4; RA Li S., Galbiati F., Volonte D., Sargiacomo M., Engelman J.A., Das K., RA Scherer P.E., Lisanti M.P.; RT "Mutational analysis of caveolin-induced vesicle formation. Expression of RT caveolin-1 recruits caveolin-2 to caveolae membranes."; RL FEBS Lett. 434:127-134(1998). RN [9] RP PHOSPHORYLATION AT TYR-19, SUBCELLULAR LOCATION, AND INTERACTION WITH CAV1; RP SRC; RASA1 AND NCK1. RX PubMed=12091389; DOI=10.1074/jbc.m204367200; RA Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.; RT "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho- RT caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated RT with lipid rafts/caveolae, but no longer forms a high molecular mass RT hetero-oligomer with caveolin-1."; RL J. Biol. Chem. 277:34556-34567(2002). RN [10] RP PHOSPHORYLATION AT TYR-19 AND TYR-27, SUBCELLULAR LOCATION, INTERACTION RP WITH CAV1; NCK1; RASA1 AND SRC, FUNCTION, AND MUTAGENESIS OF TYR-19 AND RP TYR-27. RX PubMed=15504032; DOI=10.1021/bi049295+; RA Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., RA Campos-Gonzalez R., Lisanti M.P.; RT "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the RT spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."; RL Biochemistry 43:13694-13706(2004). RN [11] RP PHOSPHORYLATION AT SER-23 AND SER-36, FUNCTION, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF SER-23 AND SER-36. RX PubMed=18081315; DOI=10.1021/bi701709s; RA Sowa G., Xie L., Xu L., Sessa W.C.; RT "Serine 23 and 36 phosphorylation of caveolin-2 is differentially regulated RT by targeting to lipid raft/caveolae and in mitotic endothelial cells."; RL Biochemistry 47:101-111(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes. CC Interacts directly with G protein alpha subunits and can functionally CC regulate their activity. Acts as an accessory protein in conjunction CC with CAV1 in targeting to lipid rafts and driving caveolae formation. CC The Ser-36 phosphorylated form has a role in modulating mitosis in CC endothelial cells. Positive regulator of cellular mitogenesis of the CC MAPK signaling pathway. Required for the insulin-stimulated nuclear CC translocation and activation of MAPK1 and STAT3, and the subsequent CC regulation of cell cycle progression (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:15504032, ECO:0000269|PubMed:18081315}. CC -!- SUBUNIT: Monomer or homodimer. Interacts with CAV1; the interaction CC forms a stable heterooligomeric complex that is required for targeting CC to lipid rafts and for caveolae formation. Tyrosine phosphorylated CC forms do not form heterooligomers with the Tyr-19-phosphorylated form CC existing as a monomer or dimer, and the Tyr-27-form as a monomer only. CC Interacts (tyrosine phosphorylated form) with the SH2 domain-containing CC proteins, RASA1, NCK1 and SRC. Interacts (tyrosine phosphorylated form) CC with INSR, the interaction (Tyr-27-phosphorylated form) is increased on CC insulin stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1 CC (phosphorylated form); the interaction, promoted by insulin, leads to CC nuclear location and MAPK1 activation. Interacts with STAT3; the CC interaction is increased on insulin-induced tyrosine phosphorylation CC leading to STAT activation (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC P51636; Q03135: CAV1; NbExp=5; IntAct=EBI-603607, EBI-603614; CC P51636; P00533: EGFR; NbExp=3; IntAct=EBI-603607, EBI-297353; CC P51636; O00560: SDCBP; NbExp=3; IntAct=EBI-603607, EBI-727004; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Golgi apparatus membrane; CC Peripheral membrane protein. Cell membrane; Peripheral membrane CC protein. Membrane, caveola; Peripheral membrane protein. Note=Potential CC hairpin-like structure in the membrane. Membrane protein of caveolae. CC Tyr-19-phosphorylated form is enriched at sites of cell-cell contact CC and is translocated to the nucleus in complex with MAPK1 in response to CC insulin (By similarity). Tyr-27-phosphorylated form is located both in CC the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated CC form locates to the plasma membrane. Ser-36-phosphorylated form resides CC in intracellular compartments. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Name=Alpha; CC IsoId=P51636-1; Sequence=Displayed; CC Name=Beta; CC IsoId=P51636-2; Sequence=VSP_018696; CC Name=C; CC IsoId=P51636-3; Sequence=VSP_038114, VSP_038115; CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells, smooth muscle CC cells, skeletal myoblasts and fibroblasts. CC {ECO:0000269|PubMed:9361015}. CC -!- PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes CC phosphorylation on Ser-23 which then targets the complex to the plasma CC membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears CC to modulate mitosis in endothelial cells (By similarity). CC Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin- CC induced 'Ser-727' phosphorylation of STAT3 and its activation. CC Phosphorylation on Tyr-19 is required for insulin-induced CC phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine CC phosphorylation is induced by both EGF and insulin (By similarity). CC {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform Beta]: Produced by alternative initiation. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform C]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Caveolin entry; CC URL="https://en.wikipedia.org/wiki/Caveolin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF035752; AAB88492.1; -; mRNA. DR EMBL; AJ133269; CAB63653.1; -; Genomic_DNA. DR EMBL; BT007051; AAP35700.1; -; mRNA. DR EMBL; BC005256; AAH05256.1; -; mRNA. DR EMBL; AJ242718; CAB65090.1; -; Genomic_DNA. DR EMBL; AK310786; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CH236947; EAL24361.1; -; Genomic_DNA. DR CCDS; CCDS5765.1; -. [P51636-3] DR CCDS; CCDS5766.1; -. [P51636-1] DR RefSeq; NP_001193676.1; NM_001206747.2. [P51636-2] DR RefSeq; NP_001193677.1; NM_001206748.2. DR RefSeq; NP_001224.1; NM_001233.5. [P51636-1] DR RefSeq; NP_937855.1; NM_198212.3. [P51636-3] DR AlphaFoldDB; P51636; -. DR SMR; P51636; -. DR BioGRID; 107306; 141. DR DIP; DIP-34929N; -. DR FunCoup; P51636; 920. DR IntAct; P51636; 102. DR NDEx; IQUERY-CP-CAV2; 7 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000222693; -. DR TCDB; 8.A.104.1.11; the 5'-amp-activated protein kinase (ampk) family. DR iPTMnet; P51636; -. DR PhosphoSitePlus; P51636; -. DR SwissPalm; P51636; -. DR BioMuta; CAV2; -. DR jPOST; P51636; -. DR MassIVE; P51636; -. DR PaxDb; 9606-ENSP00000222693; -. DR PeptideAtlas; P51636; -. DR ProteomicsDB; 56353; -. [P51636-1] DR ProteomicsDB; 56354; -. [P51636-2] DR ProteomicsDB; 56355; -. [P51636-3] DR Pumba; P51636; -. DR Antibodypedia; 4606; 515 antibodies from 42 providers. DR DNASU; 858; -. DR Ensembl; ENST00000222693.5; ENSP00000222693.4; ENSG00000105971.16. [P51636-1] DR Ensembl; ENST00000343213.2; ENSP00000345679.2; ENSG00000105971.16. [P51636-3] DR GeneID; 858; -. DR KEGG; hsa:858; -. DR MANE-Select; ENST00000222693.5; ENSP00000222693.4; NM_001233.5; NP_001224.1. DR UCSC; uc003vie.4; human. [P51636-1] DR AGR; HGNC:1528; -. DR ClinPGx; PA26108; -. DR CTD; 858; -. DR DisGeNET; 858; -. DR GeneCards; CAV2; -. DR HGNC; HGNC:1528; CAV2. DR HPA; ENSG00000105971; Tissue enhanced (adipose). DR MalaCards; CAV2; -. DR MIM; 601048; gene. DR OpenTargets; ENSG00000105971; -. DR VEuPathDB; HostDB:ENSG00000105971; -. DR eggNOG; ENOG502RZYX; Eukaryota. DR GeneTree; ENSGT00950000183006; -. DR HOGENOM; CLU_2145024_0_0_1; -. DR InParanoid; P51636; -. DR OMA; ADCFWFQ; -. DR OrthoDB; 5917823at2759; -. DR PAN-GO; P51636; 13 GO annotations based on evolutionary models. DR PhylomeDB; P51636; -. DR PathwayCommons; P51636; -. DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling. DR SignaLink; P51636; -. DR SIGNOR; P51636; -. DR Agora; ENSG00000105971; -. DR BioGRID-ORCS; 858; 11 hits in 1158 CRISPR screens. DR ChiTaRS; CAV2; human. DR GeneWiki; Caveolin_2; -. DR GenomeRNAi; 858; -. DR Pharos; P51636; Tbio. DR PRO; PR:P51636; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P51636; protein. DR Bgee; ENSG00000105971; Expressed in lower lobe of lung and 212 other cell types or tissues. DR ExpressionAtlas; P51636; baseline and differential. DR GO; GO:0005901; C:caveola; IDA:BHF-UCL. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI. DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045121; C:membrane raft; IDA:HGNC-UCL. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0044853; C:plasma membrane raft; IDA:BHF-UCL. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central. DR GO; GO:0030133; C:transport vesicle; IDA:LIFEdb. DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:BHF-UCL. DR GO; GO:0032795; F:heterotrimeric G-protein binding; IDA:BHF-UCL. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IDA:MGI. DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl. DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl. DR GO; GO:0070836; P:caveola assembly; IDA:BHF-UCL. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0044794; P:host-mediated activation of viral process; IMP:AgBase. DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB. DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL. DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IGI:CACAO. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central. DR GO; GO:0007088; P:regulation of mitotic nuclear division; IDA:BHF-UCL. DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB. DR GO; GO:0006906; P:vesicle fusion; IDA:BHF-UCL. DR GO; GO:0016050; P:vesicle organization; IDA:BHF-UCL. DR GO; GO:0019076; P:viral release from host cell; IMP:AgBase. DR InterPro; IPR001612; Caveolin. DR InterPro; IPR018361; Caveolin_CS. DR PANTHER; PTHR10844; CAVEOLIN; 1. DR PANTHER; PTHR10844:SF3; CAVEOLIN-2; 1. DR Pfam; PF01146; Caveolin; 1. DR PROSITE; PS01210; CAVEOLIN; 1. PE 1: Evidence at protein level; KW Alternative initiation; Alternative splicing; Cell membrane; Cytoplasm; KW Golgi apparatus; Membrane; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome. FT CHAIN 1..162 FT /note="Caveolin-2" FT /id="PRO_0000004772" FT TOPO_DOM 1..86 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT INTRAMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 108..162 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOD_RES 19 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000269|PubMed:12091389, FT ECO:0000269|PubMed:15504032" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WVC3" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18081315" FT MOD_RES 27 FT /note="Phosphotyrosine; by SRC" FT /evidence="ECO:0000269|PubMed:15504032" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18081315" FT VAR_SEQ 1..13 FT /note="Missing (in isoform Beta)" FT /evidence="ECO:0000305" FT /id="VSP_018696" FT VAR_SEQ 51..112 FT /note="LGFEDVIAEPVTTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGI FT LFATLSCLHI -> DFNAFCKDLPNGSAFSADNMEECDRCYHCSIVYERRTMLLFCQPA FT TEPGLNTWTPGLEIGIL (in isoform C)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038114" FT VAR_SEQ 113..162 FT /note="Missing (in isoform C)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038115" FT VARIANT 130 FT /note="Q -> E (in dbSNP:rs8940)" FT /id="VAR_012071" FT MUTAGEN 19 FT /note="Y->A: Greatly reduced Src-mediated phosphorylation FT and binding of RASA1, SRC and NCK1. Completely eliminates FT Src-mediated tyrosine phosphorylation and binding to RASA1, FT SRC and NCK1; when associated with A-27." FT /evidence="ECO:0000269|PubMed:15504032" FT MUTAGEN 23 FT /note="S->A: Abolishes phosphorylation." FT /evidence="ECO:0000269|PubMed:18081315" FT MUTAGEN 27 FT /note="Y->A: Greatly reduced Src-mediated phosphorylation FT and binding of RASA1, SRC and NCK1. Completely eliminates FT Src-mediated phosphorylation and binding of RASA1, SRC and FT NCK1; when associated with A-19." FT /evidence="ECO:0000269|PubMed:15504032" FT MUTAGEN 36 FT /note="S->A: Abolishes phosphorylation." FT /evidence="ECO:0000269|PubMed:18081315" SQ SEQUENCE 162 AA; 18291 MW; 89FDEDA861330B87 CRC64; MGLETEKADV QLFMDDDSYS HHSGLEYADP EKFADSDQDR DPHRLNSHLK LGFEDVIAEP VTTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA GILFATLSCL HIWILMPFVK TCLMVLPSVQ TIWKSVTDVI IAPLCTSVGR CFSSVSLQLS QD //