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P51636

- CAV2_HUMAN

UniProt

P51636 - CAV2_HUMAN

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Protein

Caveolin-2

Gene

CAV2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity).By similarity

GO - Molecular functioni

  1. D1 dopamine receptor binding Source: BHF-UCL
  2. protein homodimerization activity Source: MGI

GO - Biological processi

  1. caveola assembly Source: BHF-UCL
  2. endoplasmic reticulum organization Source: UniProtKB
  3. mitochondrion organization Source: UniProtKB
  4. negative regulation of endothelial cell proliferation Source: UniProtKB
  5. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  6. positive regulation of dopamine receptor signaling pathway Source: BHF-UCL
  7. positive regulation of endothelial cell proliferation Source: Ensembl
  8. protein oligomerization Source: Ensembl
  9. regulation of mitosis Source: BHF-UCL
  10. skeletal muscle fiber development Source: UniProtKB
  11. synaptic transmission Source: Ensembl
  12. vesicle docking Source: BHF-UCL
  13. vesicle fusion Source: BHF-UCL
  14. vesicle organization Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiP51636.

Names & Taxonomyi

Protein namesi
Recommended name:
Caveolin-2
Gene namesi
Name:CAV2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:1528. CAV2.

Subcellular locationi

Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membranecaveola; Peripheral membrane protein
Note: Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8686CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei87 – 10721HelicalSequence AnalysisAdd
BLAST
Topological domaini108 – 16255CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. acrosomal membrane Source: Ensembl
  2. caveola Source: BHF-UCL
  3. cell surface Source: Ensembl
  4. cytoplasmic vesicle Source: MGI
  5. cytosol Source: Ensembl
  6. extrinsic component of cytoplasmic side of plasma membrane Source: BHF-UCL
  7. Golgi apparatus Source: BHF-UCL
  8. integral component of plasma membrane Source: MGI
  9. intracellular Source: BHF-UCL
  10. lipid particle Source: Ensembl
  11. membrane Source: BHF-UCL
  12. membrane raft Source: HGNC
  13. nucleus Source: UniProtKB-KW
  14. perinuclear region of cytoplasm Source: BHF-UCL
  15. plasma membrane Source: BHF-UCL
  16. protein complex Source: MGI
  17. transport vesicle Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191Y → A: Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated tyrosine phosphorylation and binding to RASA1, SRC and NCK1; when associated with A-27. 1 Publication
Mutagenesisi23 – 231S → A: Abolishes phosphorylation. 1 Publication
Mutagenesisi27 – 271Y → A: Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated phosphorylation and binding of RASA1, SRC and NCK1; when associated with A-19. 1 Publication
Mutagenesisi36 – 361S → A: Abolishes phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA26108.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Caveolin-2PRO_0000004772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphotyrosine; by SRC2 Publications
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei27 – 271Phosphotyrosine; by SRC1 Publication
Modified residuei36 – 361Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity). Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP51636.
PaxDbiP51636.
PRIDEiP51636.

PTM databases

PhosphoSiteiP51636.

Expressioni

Tissue specificityi

Expressed in endothelial cells, smooth muscle cells, skeletal myoblasts and fibroblasts.1 Publication

Gene expression databases

BgeeiP51636.
CleanExiHS_CAV2.
ExpressionAtlasiP51636. baseline and differential.
GenevestigatoriP51636.

Organism-specific databases

HPAiCAB013488.
HPA044810.

Interactioni

Subunit structurei

Monomer or homodimer. Interacts with CAV1; the interaction forms a stable heterooligomeric complex that is required for targeting to lipid rafts and for caveolae formation. Tyrosine phosphorylated forms do not form heterooligomers with the Tyr-19-phosphorylated form existing as a monomer or dimer, and the Tyr-27-form as a monomer only. Interacts (tyrosine phosphorylated form) with the SH2 domain-containing proteins, RASA1, NCK1 and SRC. Interacts (tyrosine phosphorylated form) with INSR, the interaction (Tyr-27-phosphorylated form) is increased on insulin stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1 (phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with STAT3; the interaction is increased on insulin-induced tyrosine phosphorylation leading to STAT activation (By similarity).By similarity

Protein-protein interaction databases

BioGridi107306. 12 interactions.
DIPiDIP-34929N.
IntActiP51636. 6 interactions.
MINTiMINT-1403441.
STRINGi9606.ENSP00000222693.

Structurei

3D structure databases

ProteinModelPortaliP51636.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the caveolin family.Curated

Phylogenomic databases

eggNOGiNOG74268.
GeneTreeiENSGT00390000014924.
HOGENOMiHOG000036550.
HOVERGENiHBG003422.
InParanoidiP51636.
KOiK12958.
OMAiSTHSFDK.
OrthoDBiEOG7V1FSD.
PhylomeDBiP51636.
TreeFamiTF315736.

Family and domain databases

InterProiIPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERiPTHR10844. PTHR10844. 1 hit.
PfamiPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEiPS01210. CAVEOLIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative initiation. Align

Isoform Alpha (identifier: P51636-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGLETEKADV QLFMDDDSYS HHSGLEYADP EKFADSDQDR DPHRLNSHLK
60 70 80 90 100
LGFEDVIAEP VTTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA
110 120 130 140 150
GILFATLSCL HIWILMPFVK TCLMVLPSVQ TIWKSVTDVI IAPLCTSVGR
160
CFSSVSLQLS QD
Length:162
Mass (Da):18,291
Last modified:July 15, 1999 - v2
Checksum:i89FDEDA861330B87
GO
Isoform Beta (identifier: P51636-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.

Note: Produced by alternative initiation.

Show »
Length:149
Mass (Da):16,829
Checksum:i0706B574F5E1AAD8
GO
Isoform C (identifier: P51636-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     51-112: LGFEDVIAEP...LFATLSCLHI → DFNAFCKDLP...WTPGLEIGIL
     113-162: Missing.

Note: Produced by alternative splicing.

Show »
Length:112
Mass (Da):12,780
Checksum:i7C60DC5ABD6B0105
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti130 – 1301Q → E.
Corresponds to variant rs8940 [ dbSNP | Ensembl ].
VAR_012071

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313Missing in isoform Beta. CuratedVSP_018696Add
BLAST
Alternative sequencei51 – 11262LGFED…SCLHI → DFNAFCKDLPNGSAFSADNM EECDRCYHCSIVYERRTMLL FCQPATEPGLNTWTPGLEIG IL in isoform C. 1 PublicationVSP_038114Add
BLAST
Alternative sequencei113 – 16250Missing in isoform C. 1 PublicationVSP_038115Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035752 mRNA. Translation: AAB88492.1.
AJ133269 Genomic DNA. Translation: CAB63653.1.
BT007051 mRNA. Translation: AAP35700.1.
BC005256 mRNA. Translation: AAH05256.1.
AJ242718 Genomic DNA. Translation: CAB65090.1.
AK310786 mRNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24361.1.
CCDSiCCDS5765.1. [P51636-3]
CCDS5766.1. [P51636-1]
RefSeqiNP_001193676.1. NM_001206747.1. [P51636-2]
NP_001193677.1. NM_001206748.1.
NP_001224.1. NM_001233.4. [P51636-1]
NP_937855.1. NM_198212.2. [P51636-3]
UniGeneiHs.212332.
Hs.603096.

Genome annotation databases

EnsembliENST00000222693; ENSP00000222693; ENSG00000105971. [P51636-1]
ENST00000343213; ENSP00000345679; ENSG00000105971. [P51636-3]
GeneIDi858.
KEGGihsa:858.
UCSCiuc003vid.3. human. [P51636-1]
uc003vie.3. human. [P51636-3]
uc022akj.1. human. [P51636-2]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Caveolin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035752 mRNA. Translation: AAB88492.1 .
AJ133269 Genomic DNA. Translation: CAB63653.1 .
BT007051 mRNA. Translation: AAP35700.1 .
BC005256 mRNA. Translation: AAH05256.1 .
AJ242718 Genomic DNA. Translation: CAB65090.1 .
AK310786 mRNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24361.1 .
CCDSi CCDS5765.1. [P51636-3 ]
CCDS5766.1. [P51636-1 ]
RefSeqi NP_001193676.1. NM_001206747.1. [P51636-2 ]
NP_001193677.1. NM_001206748.1.
NP_001224.1. NM_001233.4. [P51636-1 ]
NP_937855.1. NM_198212.2. [P51636-3 ]
UniGenei Hs.212332.
Hs.603096.

3D structure databases

ProteinModelPortali P51636.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107306. 12 interactions.
DIPi DIP-34929N.
IntActi P51636. 6 interactions.
MINTi MINT-1403441.
STRINGi 9606.ENSP00000222693.

PTM databases

PhosphoSitei P51636.

Proteomic databases

MaxQBi P51636.
PaxDbi P51636.
PRIDEi P51636.

Protocols and materials databases

DNASUi 858.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222693 ; ENSP00000222693 ; ENSG00000105971 . [P51636-1 ]
ENST00000343213 ; ENSP00000345679 ; ENSG00000105971 . [P51636-3 ]
GeneIDi 858.
KEGGi hsa:858.
UCSCi uc003vid.3. human. [P51636-1 ]
uc003vie.3. human. [P51636-3 ]
uc022akj.1. human. [P51636-2 ]

Organism-specific databases

CTDi 858.
GeneCardsi GC07P115926.
HGNCi HGNC:1528. CAV2.
HPAi CAB013488.
HPA044810.
MIMi 601048. gene.
neXtProti NX_P51636.
PharmGKBi PA26108.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG74268.
GeneTreei ENSGT00390000014924.
HOGENOMi HOG000036550.
HOVERGENi HBG003422.
InParanoidi P51636.
KOi K12958.
OMAi STHSFDK.
OrthoDBi EOG7V1FSD.
PhylomeDBi P51636.
TreeFami TF315736.

Enzyme and pathway databases

SignaLinki P51636.

Miscellaneous databases

ChiTaRSi CAV2. human.
GeneWikii Caveolin_2.
GenomeRNAii 858.
NextBioi 3560.
PROi P51636.
SOURCEi Search...

Gene expression databases

Bgeei P51636.
CleanExi HS_CAV2.
ExpressionAtlasi P51636. baseline and differential.
Genevestigatori P51636.

Family and domain databases

InterProi IPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view ]
PANTHERi PTHR10844. PTHR10844. 1 hit.
Pfami PF01146. Caveolin. 1 hit.
[Graphical view ]
PROSITEi PS01210. CAVEOLIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, sequence, and expression of caveolin-2 defines a caveolin gene family."
    Scherer P.E., Okamoto T., Chun M., Nishimoto I., Lodish H.F., Lisanti M.P.
    Proc. Natl. Acad. Sci. U.S.A. 93:131-135(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
  2. "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo."
    Scherer P.E., Lewis R.Y., Volonte D., Engelman J.A., Galbiati F., Couet J., Kohtz D.S., van Donselaar E., Peters P., Lisanti M.P.
    J. Biol. Chem. 272:29337-29346(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INTERACTION WITH CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  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] [Europe PMC] [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] (ISOFORM ALPHA).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Tissue: Hepatoma.
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    Tissue: Kidney.
  8. "Mutational analysis of caveolin-induced vesicle formation. Expression of caveolin-1 recruits caveolin-2 to caveolae membranes."
    Li S., Galbiati F., Volonte D., Sargiacomo M., Engelman J.A., Das K., Scherer P.E., Lisanti M.P.
    FEBS Lett. 434:127-134(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV1, ALTERNATIVE PRODUCTS, SUBCELLULAR LOCATION.
  9. "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
    Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
    J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-19, SUBCELLULAR LOCATION, INTERACTION WITH CAV1; SRC; RASA1 AND NCK1.
  10. "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."
    Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P.
    Biochemistry 43:13694-13706(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-19 AND TYR-27, SUBCELLULAR LOCATION, INTERACTION WITH CAV1; NCK1; RASA1 AND SRC, FUNCTION, MUTAGENESIS OF TYR-19 AND TYR-27.
  11. "Serine 23 and 36 phosphorylation of caveolin-2 is differentially regulated by targeting to lipid raft/caveolae and in mitotic endothelial cells."
    Sowa G., Xie L., Xu L., Sessa W.C.
    Biochemistry 47:101-111(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-23 AND SER-36, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-23 AND SER-36.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAV2_HUMAN
AccessioniPrimary (citable) accession number: P51636
Secondary accession number(s): A4D0U2, Q9UGM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1999
Last modified: October 29, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3