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P49817

- CAV1_MOUSE

UniProt

P49817 - CAV1_MOUSE

Protein

Caveolin-1

Gene

Cav1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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. May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway.1 Publication

    GO - Molecular functioni

    1. peptidase activator activity Source: MGI
    2. protein binding Source: UniProtKB
    3. structural molecule activity Source: Ensembl

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. apoptotic signaling pathway Source: Ensembl
    3. calcium ion homeostasis Source: MGI
    4. calcium ion transport Source: MGI
    5. caveola assembly Source: MGI
    6. caveolin-mediated endocytosis Source: Ensembl
    7. cellular calcium ion homeostasis Source: MGI
    8. cellular response to hyperoxia Source: Ensembl
    9. cellular response to starvation Source: Ensembl
    10. cholesterol homeostasis Source: MGI
    11. cytosolic calcium ion homeostasis Source: Ensembl
    12. endocytosis Source: MGI
    13. inactivation of MAPK activity Source: MGI
    14. lactation Source: MGI
    15. lipid storage Source: MGI
    16. mammary gland development Source: MGI
    17. mammary gland involution Source: MGI
    18. MAPK cascade Source: MGI
    19. membrane depolarization Source: MGI
    20. negative regulation of anoikis Source: UniProtKB
    21. negative regulation of BMP signaling pathway Source: Ensembl
    22. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
    23. negative regulation of cell proliferation Source: MGI
    24. negative regulation of cytokine-mediated signaling pathway Source: MGI
    25. negative regulation of endothelial cell proliferation Source: MGI
    26. negative regulation of epithelial cell differentiation Source: MGI
    27. negative regulation of JAK-STAT cascade Source: MGI
    28. negative regulation of MAPK cascade Source: MGI
    29. negative regulation of MAP kinase activity Source: MGI
    30. negative regulation of nitric oxide biosynthetic process Source: MGI
    31. negative regulation of nitric-oxide synthase activity Source: MGI
    32. negative regulation of peptidyl-serine phosphorylation Source: Ensembl
    33. negative regulation of protein binding Source: Ensembl
    34. negative regulation of protein ubiquitination Source: UniProtKB
    35. negative regulation of signal transduction Source: MGI
    36. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    37. negative regulation of tyrosine phosphorylation of Stat5 protein Source: MGI
    38. nitric oxide homeostasis Source: MGI
    39. positive regulation of calcium ion transport into cytosol Source: BHF-UCL
    40. positive regulation of canonical Wnt signaling pathway Source: Ensembl
    41. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    42. positive regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    43. positive regulation of metalloenzyme activity Source: MGI
    44. positive regulation of peptidase activity Source: GOC
    45. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
    46. positive regulation of vasoconstriction Source: MGI
    47. protein homooligomerization Source: MGI
    48. protein localization Source: MGI
    49. protein oligomerization Source: MGI
    50. receptor internalization involved in canonical Wnt signaling pathway Source: Ensembl
    51. regulation of blood coagulation Source: Ensembl
    52. regulation of fatty acid metabolic process Source: MGI
    53. regulation of peptidase activity Source: MGI
    54. regulation of smooth muscle contraction Source: MGI
    55. regulation of the force of heart contraction Source: MGI
    56. regulation of the force of heart contraction by chemical signal Source: MGI
    57. response to calcium ion Source: BHF-UCL
    58. response to estrogen Source: MGI
    59. response to hypoxia Source: MGI
    60. response to ischemia Source: MGI
    61. response to progesterone Source: MGI
    62. skeletal muscle tissue development Source: MGI
    63. T cell costimulation Source: UniProtKB
    64. triglyceride metabolic process Source: MGI
    65. vasculogenesis Source: MGI
    66. vasoconstriction Source: MGI
    67. vesicle organization Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_211508. Basigin interactions.
    REACT_215995. NOSTRIN mediated eNOS trafficking.
    REACT_221264. eNOS activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caveolin-1
    Gene namesi
    Name:Cav1
    Synonyms:Cav
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:102709. Cav1.

    Subcellular locationi

    Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity. Membranecaveola 1 Publication; Peripheral membrane protein 1 Publication. Membrane raft By similarity
    Note: Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae By similarity.By similarity

    GO - Cellular componenti

    1. acrosomal membrane Source: MGI
    2. apical plasma membrane Source: Ensembl
    3. basolateral plasma membrane Source: Ensembl
    4. caveola Source: UniProtKB
    5. cell cortex Source: MGI
    6. cilium Source: MGI
    7. cytoplasmic vesicle Source: MGI
    8. endoplasmic reticulum Source: HGNC
    9. endosome Source: UniProtKB
    10. Golgi apparatus Source: MGI
    11. Golgi membrane Source: HGNC
    12. integral component of membrane Source: MGI
    13. integral component of plasma membrane Source: MGI
    14. membrane Source: MGI
    15. membrane raft Source: MGI
    16. perinuclear region of cytoplasm Source: MGI
    17. plasma membrane Source: MGI
    18. protein complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 178177Caveolin-1PRO_0000004766Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei5 – 51N6-acetyllysine1 Publication
    Modified residuei6 – 61PhosphotyrosineBy similarity
    Modified residuei14 – 141Phosphotyrosine; by ABL1 and INSR2 Publications
    Modified residuei25 – 251PhosphotyrosineBy similarity
    Modified residuei42 – 421PhosphotyrosineBy similarity
    Lipidationi133 – 1331S-palmitoyl cysteineBy similarity
    Lipidationi143 – 1431S-palmitoyl cysteineBy similarity
    Lipidationi156 – 1561S-palmitoyl cysteineBy similarity

    Post-translational modificationi

    The N-terminus of both isoforms are blocked.
    Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress.2 Publications

    Keywords - PTMi

    Acetylation, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP49817.
    PaxDbiP49817.
    PRIDEiP49817.

    PTM databases

    PhosphoSiteiP49817.

    Expressioni

    Gene expression databases

    ArrayExpressiP49817.
    BgeeiP49817.
    CleanExiMM_CAV1.
    GenevestigatoriP49817.

    Interactioni

    Subunit structurei

    Homooligomer By similarity. Interacts (via the N-terminus) with DPP4; the interaction is direct By similarity. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Interacts with BMX, BTK, CTNNB1, CDH1, GLIPR2, JUP, NOSTRIN, SNAP25 and STX1A. Interacts with SLC7A9 By similarity. Interacts with PACSIN2.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MCL1Q078203EBI-1161338,EBI-1003422From a different organism.
    SCP2P223073EBI-1161338,EBI-1050999From a different organism.

    Protein-protein interaction databases

    BioGridi198514. 9 interactions.
    DIPiDIP-35140N.
    IntActiP49817. 11 interactions.
    MINTiMINT-1542313.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 104103CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini126 – 17853CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei105 – 12521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the caveolin family.Curated

    Phylogenomic databases

    eggNOGiNOG86001.
    GeneTreeiENSGT00390000014924.
    HOGENOMiHOG000036550.
    HOVERGENiHBG003422.
    InParanoidiP49817.
    KOiK06278.
    OMAiRINMQKE.
    OrthoDBiEOG7V1FSD.
    PhylomeDBiP49817.
    TreeFamiTF315736.

    Family and domain databases

    InterProiIPR001612. Caveolin.
    IPR015504. Caveolin_1.
    IPR018361. Caveolin_CS.
    [Graphical view]
    PANTHERiPTHR10844. PTHR10844. 1 hit.
    PTHR10844:SF5. PTHR10844:SF5. 1 hit.
    PfamiPF01146. Caveolin. 1 hit.
    [Graphical view]
    PROSITEiPS01210. CAVEOLIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P49817-1) [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

    MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADEVTEKQ VYDAHTKEID    50
    LVNRDPKHLN DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY 100
    RLLSTIFGIP MALIWGIYFA ILSFLHIWAV VPCIKSFLIE IQCISRVYSI 150
    YVHTFCDPLF EAIGKIFSNI RISTQKEI 178
    Length:178
    Mass (Da):20,539
    Last modified:October 1, 1996 - v1
    Checksum:iCF88FE9B1D3D67AE
    GO
    Isoform 2 (identifier: P49817-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-31: Missing.

    Show »
    Length:148
    Mass (Da):17,221
    Checksum:iF19874C9347CDD0C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti170 – 1701I → F in BAC29118. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 3130Missing in isoform 2. 2 PublicationsVSP_018693Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07645 mRNA. Translation: AAA85784.1.
    AB029929 mRNA. Translation: BAA89461.1.
    AB029930 mRNA. Translation: BAA89462.1.
    AB029931 Genomic DNA. Translation: BAA89463.1.
    AY439333 mRNA. Translation: AAR99702.1.
    AK003489 mRNA. Translation: BAB22817.1.
    AK028738 mRNA. Translation: BAC26091.1.
    AK035592 mRNA. Translation: BAC29118.1.
    AK090074 mRNA. Translation: BAC41079.1.
    BC038280 mRNA. Translation: AAH38280.1.
    BC052859 mRNA. Translation: AAH52859.1.
    CCDSiCCDS19924.1. [P49817-1]
    PIRiI48976.
    RefSeqiNP_001229993.1. NM_001243064.1.
    NP_031642.1. NM_007616.4. [P49817-1]
    XP_006505037.1. XM_006504974.1. [P49817-1]
    XP_006505038.1. XM_006504975.1.
    XP_006505039.1. XM_006504976.1.
    UniGeneiMm.28278.

    Genome annotation databases

    EnsembliENSMUST00000007799; ENSMUSP00000007799; ENSMUSG00000007655. [P49817-1]
    ENSMUST00000115453; ENSMUSP00000111113; ENSMUSG00000007655.
    ENSMUST00000115454; ENSMUSP00000111114; ENSMUSG00000007655.
    ENSMUST00000115456; ENSMUSP00000111116; ENSMUSG00000007655. [P49817-1]
    GeneIDi12389.
    KEGGimmu:12389.
    UCSCiuc009azo.2. mouse. [P49817-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07645 mRNA. Translation: AAA85784.1 .
    AB029929 mRNA. Translation: BAA89461.1 .
    AB029930 mRNA. Translation: BAA89462.1 .
    AB029931 Genomic DNA. Translation: BAA89463.1 .
    AY439333 mRNA. Translation: AAR99702.1 .
    AK003489 mRNA. Translation: BAB22817.1 .
    AK028738 mRNA. Translation: BAC26091.1 .
    AK035592 mRNA. Translation: BAC29118.1 .
    AK090074 mRNA. Translation: BAC41079.1 .
    BC038280 mRNA. Translation: AAH38280.1 .
    BC052859 mRNA. Translation: AAH52859.1 .
    CCDSi CCDS19924.1. [P49817-1 ]
    PIRi I48976.
    RefSeqi NP_001229993.1. NM_001243064.1.
    NP_031642.1. NM_007616.4. [P49817-1 ]
    XP_006505037.1. XM_006504974.1. [P49817-1 ]
    XP_006505038.1. XM_006504975.1.
    XP_006505039.1. XM_006504976.1.
    UniGenei Mm.28278.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198514. 9 interactions.
    DIPi DIP-35140N.
    IntActi P49817. 11 interactions.
    MINTi MINT-1542313.

    PTM databases

    PhosphoSitei P49817.

    Proteomic databases

    MaxQBi P49817.
    PaxDbi P49817.
    PRIDEi P49817.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000007799 ; ENSMUSP00000007799 ; ENSMUSG00000007655 . [P49817-1 ]
    ENSMUST00000115453 ; ENSMUSP00000111113 ; ENSMUSG00000007655 .
    ENSMUST00000115454 ; ENSMUSP00000111114 ; ENSMUSG00000007655 .
    ENSMUST00000115456 ; ENSMUSP00000111116 ; ENSMUSG00000007655 . [P49817-1 ]
    GeneIDi 12389.
    KEGGi mmu:12389.
    UCSCi uc009azo.2. mouse. [P49817-1 ]

    Organism-specific databases

    CTDi 857.
    MGIi MGI:102709. Cav1.

    Phylogenomic databases

    eggNOGi NOG86001.
    GeneTreei ENSGT00390000014924.
    HOGENOMi HOG000036550.
    HOVERGENi HBG003422.
    InParanoidi P49817.
    KOi K06278.
    OMAi RINMQKE.
    OrthoDBi EOG7V1FSD.
    PhylomeDBi P49817.
    TreeFami TF315736.

    Enzyme and pathway databases

    Reactomei REACT_211508. Basigin interactions.
    REACT_215995. NOSTRIN mediated eNOS trafficking.
    REACT_221264. eNOS activation.

    Miscellaneous databases

    NextBioi 281122.
    PROi P49817.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49817.
    Bgeei P49817.
    CleanExi MM_CAV1.
    Genevestigatori P49817.

    Family and domain databases

    InterProi IPR001612. Caveolin.
    IPR015504. Caveolin_1.
    IPR018361. Caveolin_CS.
    [Graphical view ]
    PANTHERi PTHR10844. PTHR10844. 1 hit.
    PTHR10844:SF5. PTHR10844:SF5. 1 hit.
    Pfami PF01146. Caveolin. 1 hit.
    [Graphical view ]
    PROSITEi PS01210. CAVEOLIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary sequence of murine caveolin reveals a conserved consensus site for phosphorylation by protein kinase C."
      Tang Z., Scherer P.E., Lisanti M.P.
      Gene 147:299-300(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    2. "Caveolin-1 isoforms are encoded in distinct mRNAs: identification of mouse caveolin-1 mRNA variants caused by alternative transcription initiation and splicing."
      Kogo H., Fujimoto T.
      FEBS Lett. 465:119-123(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
    3. "Met gene is a candidate for the mouse pulmonary adenoma resistance 4 (Par4) locus."
      Zaffaroni D., Dragani T.A.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: SWR/J.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Embryo, Skin and Urinary bladder.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C3H/He.
      Tissue: Mesenchymal cell.
    6. "Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe."
      Scherer P.E., Tang Z., Chun M., Sargiacomo M., Lodish H.F., Lisanti M.P.
      J. Biol. Chem. 270:16395-16401(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-26; 47-77 AND 165-176.
    7. "Caveolin-1 expression inhibits Wnt/beta-catenin/Lef-1 signaling by recruiting beta-catenin to caveolae membrane domains."
      Galbiati F., Volonte D., Brown A.M., Weinstein D.E., Ben-Ze'ev A., Pestell R.G., Lisanti M.P.
      J. Biol. Chem. 275:23368-23377(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1."
      Kimura A., Mora S., Shigematsu S., Pessin J.E., Saltiel A.R.
      J. Biol. Chem. 277:30153-30158(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-14.
    9. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-14.
    10. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    12. "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting."
      Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.
      J. Cell Sci. 124:2032-2040(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PACSIN2, SUBCELLULAR LOCATION.
    13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-5, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiCAV1_MOUSE
    AccessioniPrimary (citable) accession number: P49817
    Secondary accession number(s): Q8C1X7
    , Q8CBP4, Q9QYH3, Q9QYH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3