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Accession Number: | Q03135 |
Protein Name: | Caveolin-1 |
Length: | 178 |
Molecular Weight: | 20472.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 2 |
Location1 / Topology2 / Orientation3: | Golgi apparatus membrane1 / Peripheral membrane protein2 |
Substrate |
Cross database links:
DIP: | DIP-5960N |
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Entrez Gene ID: | 857 |
Pfam: | PF01146 |
KEGG: | hsa:857 |
Gene Ontology
GO:0016324
C:apical plasma membrane
GO:0016323
C:basolateral plasma membrane
GO:0005901
C:caveola
GO:0005829
C:cytosol
GO:0030666
C:endocytic vesicle membrane
GO:0005783
C:endoplasmic reticulum
GO:0005768
C:endosome
GO:0000139
C:Golgi membrane
GO:0005811
C:lipid particle
GO:0048471
C:perinuclear region of cytoplasm
GO:0015485
F:cholesterol binding
GO:0050998
F:nitric-oxide synthase binding
GO:0016504
F:peptidase activator activity
GO:0005515
F:protein binding
GO:0032947
F:protein complex scaffold
GO:0005102
F:receptor binding
GO:0007596
P:blood coagulation
GO:0006816
P:calcium ion transport
GO:0070836
P:caveola assembly
GO:0071455
P:cellular response to hyperoxia
GO:0009267
P:cellular response to starvation
GO:0042632
P:cholesterol homeostasis
GO:0051480
P:cytosolic calcium ion homeostasis
GO:0000188
P:inactivation of MAPK activity
GO:0008624
P:induction of apoptosis by extracellular signals
GO:0044419
P:interspecies interaction between organisms
GO:0050900
P:leukocyte migration
GO:0019915
P:lipid storage
GO:0032507
P:maintenance of protein location in cell
GO:0060056
P:mammary gland involution
GO:0051899
P:membrane depolarization
GO:0030514
P:negative regulation of BMP signaling pathway
GO:0090090
P:negative regulation of canonical Wnt receptor signaling pathway
GO:0001937
P:negative regulation of endothelial cell proliferation
GO:0030857
P:negative regulation of epithelial cell differentiation
GO:0045019
P:negative regulation of nitric oxide biosynthetic process
GO:0033137
P:negative regulation of peptidyl-serine phosphorylation
GO:0032091
P:negative regulation of protein binding
GO:0000122
P:negative regulation of transcription from RNA polymerase II promoter
GO:0033484
P:nitric oxide homeostasis
GO:0046209
P:nitric oxide metabolic process
GO:0010524
P:positive regulation of calcium ion transport into cytosol
GO:0090263
P:positive regulation of canonical Wnt receptor signaling pathway
GO:0048554
P:positive regulation of metalloenzyme activity
GO:0033138
P:positive regulation of peptidyl-serine phosphorylation
GO:0045907
P:positive regulation of vasoconstriction
GO:0051260
P:protein homooligomerization
GO:2000286
P:receptor internalization involved in canonical Wnt receptor signaling pathway
GO:0030193
P:regulation of blood coagulation
GO:0019217
P:regulation of fatty acid metabolic process
GO:0050999
P:regulation of nitric-oxide synthase activity
GO:0006940
P:regulation of smooth muscle contraction
GO:0051592
P:response to calcium ion
GO:0043627
P:response to estrogen stimulus
GO:0001666
P:response to hypoxia
GO:0032570
P:response to progesterone stimulus
GO:0007519
P:skeletal muscle tissue development
GO:0031295
P:T cell costimulation
GO:0006641
P:triglyceride metabolic process
GO:0001570
P:vasculogenesis
GO:0016050
P:vesicle organization
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References (24)[1] “The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles.” Glenney J.R. Jr.et.al. 1360410 [2] “Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines.” Hurlstone A.F.et.al. 10086342 [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.et.al. 10218480 [4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [5] “N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes.” Vainonen J.P.et.al. 15219854 [6] “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.et.al. 15242332 [7] “Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx.” Vargas L.et.al. 11751885 [8] “Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex.” Eberle H.B.et.al. 11865038 [9] “c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14.” Sanguinetti A.R.et.al. 12531427 [10] “Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.” Zhang Y.et.al. 15951569 [11] “Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.” Rush J.et.al. 15592455 [12] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.” Olsen J.V.et.al. 17081983 [13] “Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN.” Schilling K.et.al. 16807357 [14] “The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1.” Parr R.D.et.al. 16501093 [15] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.” Rikova K.et.al. 18083107 [16] “Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1.” Ohnuma K.et.al. 17287217 [17] “Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks.” Wolf-Yadlin A.et.al. 17389395 [18] “Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis.” Wang B.et.al. 19007248 [19] “A quantitative atlas of mitotic phosphorylation.” Dephoure N.et.al. 18669648 [20] “An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells.” Heibeck T.H.et.al. 19534553 [21] “Large-scale proteomics analysis of the human kinome.” Oppermann F.S.et.al. 19369195 [22] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.” Choudhary C.et.al. 19608861 [23] “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.et.al. 12368209 [24] “Association of a homozygous nonsense caveolin-1 mutation with Berardinelli-Seip congenital lipodystrophy.” Kim C.A.et.al. 18211975
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External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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1: MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADELSEKQ VYDAHTKEID LVNRDPKHLN 61: DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSALFGIP MALIWGIYFA 121: ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTVCDPLF EAVGKIFSNV RINLQKEI