CAV1 | ENSG00000105974 | NCBI 857

Details for: CAV1

Gene ID: 857

Symbol: CAV1

Ensembl ID: ENSG00000105974

Description: caveolin 1

Associated with

Basigin interactions
(R-HSA-210991)
Cdc42 gtpase cycle
(R-HSA-9013148)
Cell surface interactions at the vascular wall
(R-HSA-202733)
Disassembly of the destruction complex and recruitment of axin to the membrane
(R-HSA-4641262)
Disease
(R-HSA-1643685)
Enos activation
(R-HSA-203615)
Esr-mediated signaling
(R-HSA-8939211)
Extra-nuclear estrogen signaling
(R-HSA-9009391)
Foxo-mediated transcription
(R-HSA-9614085)
Foxo-mediated transcription of cell cycle genes
(R-HSA-9617828)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hemostasis
(R-HSA-109582)
Infectious disease
(R-HSA-5663205)
Metabolism
(R-HSA-1430728)
Metabolism of lipids
(R-HSA-556833)
Metabolism of nitric oxide: nos3 activation and regulation
(R-HSA-202131)
Nostrin mediated enos trafficking
(R-HSA-203641)
Rac1 gtpase cycle
(R-HSA-9013149)
Rac2 gtpase cycle
(R-HSA-9013404)
Rac3 gtpase cycle
(R-HSA-9013423)
Rhoa gtpase cycle
(R-HSA-8980692)
Rhob gtpase cycle
(R-HSA-9013026)
Rhoc gtpase cycle
(R-HSA-9013106)
Rhod gtpase cycle
(R-HSA-9013405)
Rhof gtpase cycle
(R-HSA-9035034)
Rhog gtpase cycle
(R-HSA-9013408)
Rho gtpase cycle
(R-HSA-9012999)
Rhoh gtpase cycle
(R-HSA-9013407)
Rhoj gtpase cycle
(R-HSA-9013409)
Rhoq gtpase cycle
(R-HSA-9013406)
Rna polymerase ii transcription
(R-HSA-73857)
Rnd1 gtpase cycle
(R-HSA-9696273)
Rnd2 gtpase cycle
(R-HSA-9696270)
Rnd3 gtpase cycle
(R-HSA-9696264)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-1 targets host intracellular signalling and regulatory pathways
(R-HSA-9735871)
Sars-cov-1-host interactions
(R-HSA-9692914)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov-2 targets host intracellular signalling and regulatory pathways
(R-HSA-9755779)
Sars-cov-2-host interactions
(R-HSA-9705683)
Sars-cov infections
(R-HSA-9679506)
Signaling by nuclear receptors
(R-HSA-9006931)
Signaling by receptor tyrosine kinases
(R-HSA-9006934)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signaling by vegf
(R-HSA-194138)
Signaling by wnt
(R-HSA-195721)
Signal transduction
(R-HSA-162582)
Tcf dependent signaling in response to wnt
(R-HSA-201681)
Triglyceride catabolism
(R-HSA-163560)
Triglyceride metabolism
(R-HSA-8979227)
Vegfa-vegfr2 pathway
(R-HSA-4420097)
Vegfr2 mediated vascular permeability
(R-HSA-5218920)
Viral infection pathways
(R-HSA-9824446)
Angiogenesis
(GO:0001525)
Atpase binding
(GO:0051117)
Calcium ion transport
(GO:0006816)
Cellular response to starvation
(GO:0009267)
Cholesterol binding
(GO:0015485)
Endothelial cell proliferation
(GO:0001935)
Enzyme binding
(GO:0019899)
Glandular epithelial cell differentiation
(GO:0002067)
Identical protein binding
(GO:0042802)
Intracellular calcium ion homeostasis
(GO:0006874)
Inward rectifier potassium channel inhibitor activity
(GO:0070320)
Lactation
(GO:0007595)
Mapk cascade
(GO:0000165)
Molecular adaptor activity
(GO:0060090)
Negative regulation of cytokine-mediated signaling pathway
(GO:0001960)
Negative regulation of endothelial cell proliferation
(GO:0001937)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Nitric-oxide synthase binding
(GO:0050998)
Nitric oxide biosynthetic process
(GO:0006809)
Oxysterol binding
(GO:0008142)
Patched binding
(GO:0005113)
Peptidase activator activity
(GO:0016504)
Protein-containing complex binding
(GO:0044877)
Protein-macromolecule adaptor activity
(GO:0030674)
Protein binding
(GO:0005515)
Protein heterodimerization activity
(GO:0046982)
Protein kinase binding
(GO:0019901)
Protein localization
(GO:0008104)
Protein sequestering activity
(GO:0140311)
Protein tyrosine kinase inhibitor activity
(GO:0030292)
Regulation of smooth muscle contraction
(GO:0006940)
Regulation of the force of heart contraction by chemical signal
(GO:0003057)
Response to bacterium
(GO:0009617)
Response to hypoxia
(GO:0001666)
Response to ischemia
(GO:0002931)
Signaling receptor binding
(GO:0005102)
Skeletal muscle tissue development
(GO:0007519)
Small gtpase binding
(GO:0031267)
Transmembrane transporter binding
(GO:0044325)
Triglyceride metabolic process
(GO:0006641)
Vasculogenesis
(GO:0001570)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 359.6382
Cell Significance Index: -55.9400
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 221.8469
Cell Significance Index: -56.2700
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 142.4210
Cell Significance Index: -58.6700
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 108.0969
Cell Significance Index: -51.0400
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 107.6166
Cell Significance Index: -43.7200
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 45.9286
Cell Significance Index: -43.8500
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 45.3706
Cell Significance Index: -55.9400
Cell Name: stem cell of epidermis (CL1000428)
Fold Change: 26.3819
Cell Significance Index: 78.4600
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 14.1458
Cell Significance Index: -55.8200
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: 12.9702
Cell Significance Index: 229.2000
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 9.2609
Cell Significance Index: 482.3900
Cell Name: perivascular cell (CL4033054)
Fold Change: 7.7103
Cell Significance Index: 35.6000
Cell Name: oral mucosa squamous cell (CL1001576)
Fold Change: 6.8207
Cell Significance Index: 58.6100
Cell Name: enteric smooth muscle cell (CL0002504)
Fold Change: 6.2542
Cell Significance Index: 32.9100
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 6.0165
Cell Significance Index: 68.3500
Cell Name: prostate gland microvascular endothelial cell (CL2000059)
Fold Change: 3.4740
Cell Significance Index: 24.9500
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 3.1745
Cell Significance Index: 91.0000
Cell Name: pulmonary interstitial fibroblast (CL0002241)
Fold Change: 2.9482
Cell Significance Index: 18.2400
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: 2.4464
Cell Significance Index: 35.1900
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 2.3124
Cell Significance Index: 1022.3500
Cell Name: endothelial cell of uterus (CL0009095)
Fold Change: 2.1225
Cell Significance Index: 13.2900
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 1.8534
Cell Significance Index: 254.5200
Cell Name: preadipocyte (CL0002334)
Fold Change: 1.5059
Cell Significance Index: 29.3900
Cell Name: adipocyte of breast (CL0002617)
Fold Change: 1.4318
Cell Significance Index: 18.0300
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 1.4020
Cell Significance Index: 63.5500
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 1.2625
Cell Significance Index: 96.8800
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: 1.1663
Cell Significance Index: 37.3600
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 1.1122
Cell Significance Index: 211.6500
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: 1.1007
Cell Significance Index: 6.6500
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 1.0804
Cell Significance Index: 76.4100
Cell Name: fallopian tube secretory epithelial cell (CL4030006)
Fold Change: 0.9346
Cell Significance Index: 14.4600
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.8146
Cell Significance Index: 21.7500
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.6486
Cell Significance Index: 585.6200
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.5621
Cell Significance Index: 306.9700
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 0.5485
Cell Significance Index: 14.9300
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.4492
Cell Significance Index: 21.1100
Cell Name: lactocyte (CL0002325)
Fold Change: 0.3773
Cell Significance Index: 48.7500
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.3643
Cell Significance Index: 19.1300
Cell Name: ovarian surface epithelial cell (CL2000064)
Fold Change: 0.3444
Cell Significance Index: 1.6800
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.3417
Cell Significance Index: 42.0200
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.2297
Cell Significance Index: 37.3600
Cell Name: granulosa cell (CL0000501)
Fold Change: 0.1457
Cell Significance Index: 3.8300
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.1124
Cell Significance Index: 11.1200
Cell Name: extravillous trophoblast (CL0008036)
Fold Change: 0.0644
Cell Significance Index: 0.4000
Cell Name: abnormal cell (CL0001061)
Fold Change: 0.0306
Cell Significance Index: 3.1300
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.0174
Cell Significance Index: 13.1700
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0082
Cell Significance Index: -5.1500
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: -0.0154
Cell Significance Index: -29.0800
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.0164
Cell Significance Index: -1.9100
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0268
Cell Significance Index: -36.4100
Cell Name: odontoblast (CL0000060)
Fold Change: -0.0283
Cell Significance Index: -3.6300
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: -0.0316
Cell Significance Index: -3.4400
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0320
Cell Significance Index: -23.7200
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0331
Cell Significance Index: -60.9900
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0385
Cell Significance Index: -59.2400
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0407
Cell Significance Index: -18.4800
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0439
Cell Significance Index: -27.9100
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: -0.0475
Cell Significance Index: -1.3700
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: -0.0500
Cell Significance Index: -0.4200
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0571
Cell Significance Index: -32.2200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -0.0600
Cell Significance Index: -1.5000
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0626
Cell Significance Index: -45.8900
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: -0.0668
Cell Significance Index: -12.0400
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.0914
Cell Significance Index: -1.3500
Cell Name: epithelial cell of esophagus (CL0002252)
Fold Change: -0.0934
Cell Significance Index: -0.6200
Cell Name: neoplastic cell (CL0001063)
Fold Change: -0.1123
Cell Significance Index: -22.2900
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: -0.1250
Cell Significance Index: -44.8500
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.1633
Cell Significance Index: -27.8900
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.1742
Cell Significance Index: -2.9200
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.1777
Cell Significance Index: -51.1200
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.2133
Cell Significance Index: -2.9100
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.2136
Cell Significance Index: -44.9900
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.2310
Cell Significance Index: -26.4600
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: -0.2339
Cell Significance Index: -46.9200
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.3517
Cell Significance Index: -51.1300
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.3549
Cell Significance Index: -21.7600
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.3591
Cell Significance Index: -7.7800
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.3778
Cell Significance Index: -43.1300
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: -0.4582
Cell Significance Index: -54.0300
Cell Name: peg cell (CL4033014)
Fold Change: -0.4848
Cell Significance Index: -11.2000
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -0.4862
Cell Significance Index: -33.6300
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.5131
Cell Significance Index: -53.4300
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -0.5673
Cell Significance Index: -34.0600
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.5767
Cell Significance Index: -42.9800
Cell Name: pulmonary capillary endothelial cell (CL4028001)
Fold Change: -0.6120
Cell Significance Index: -8.3800
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.6506
Cell Significance Index: -32.8800
Cell Name: early pro-B cell (CL0002046)
Fold Change: -0.8161
Cell Significance Index: -52.6500
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.8328
Cell Significance Index: -52.4900
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.8632
Cell Significance Index: -58.0400
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.9086
Cell Significance Index: -55.8500
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: -0.9388
Cell Significance Index: -19.6500
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: -1.0581
Cell Significance Index: -21.9500
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -1.0711
Cell Significance Index: -60.1100
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -1.1464
Cell Significance Index: -53.4500
Cell Name: theca cell (CL0000503)
Fold Change: -1.2391
Cell Significance Index: -7.2800
Cell Name: supporting cell (CL0000630)
Fold Change: -1.2427
Cell Significance Index: -5.7400
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -1.2663
Cell Significance Index: -65.7800
Cell Name: lens fiber cell (CL0011004)
Fold Change: -1.2830
Cell Significance Index: -40.5800
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -1.3070
Cell Significance Index: -47.9800
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -1.3187
Cell Significance Index: -58.3300

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** CAV1 is a 18-kDa protein that is highly conserved across species. Its unique structure consists of four caveolin repeats, which are amphipathic helices that interact with cholesterol and other lipids. CAV1 is also characterized by its ability to bind to a wide range of signaling molecules, including G-proteins, receptors, and kinases. The protein's binding properties allow it to modulate various signaling pathways, including those involved in cell proliferation, differentiation, and survival. **Pathways and Functions** CAV1 is involved in numerous signaling pathways, including: 1. **Endothelial cell function**: CAV1 plays a crucial role in the regulation of endothelial cell function, including cell proliferation, differentiation, and survival. It interacts with G-proteins and receptors to modulate signaling pathways involved in these processes. 2. **Cell signaling**: CAV1 is involved in various cell signaling pathways, including those mediated by G-proteins, receptors, and kinases. It modulates the activity of these signaling molecules to regulate cellular processes. 3. **Gene expression**: CAV1 is involved in the regulation of gene expression, particularly in endothelial cells. It interacts with transcription factors to modulate the expression of genes involved in cell proliferation and differentiation. 4. **Vascular development**: CAV1 is involved in the regulation of vascular development, including the formation of blood vessels and the maintenance of endothelial cell function. **Clinical Significance** CAV1 has been implicated in various diseases, including: 1. **Atherosclerosis**: CAV1 has been shown to play a role in the development of atherosclerosis, a disease characterized by the buildup of plaques in blood vessels. 2. **Cancer**: CAV1 has been implicated in the development and progression of various cancers, including breast, lung, and colon cancer. 3. **Infectious diseases**: CAV1 has been shown to interact with viral proteins, such as those from SARS-CoV-2, to modulate signaling pathways involved in viral infection. 4. **Neurological disorders**: CAV1 has been implicated in the development of various neurological disorders, including Alzheimer's disease and Parkinson's disease. In conclusion, CAV1 is a multifunctional protein that plays a crucial role in various cellular processes, including cell signaling, membrane trafficking, and gene expression. Its involvement in numerous signaling pathways and diseases makes it an important target for therapeutic intervention.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Genular Protein ID: 978574568

Symbol: CAV1_HUMAN

Name: Caveolin-1

UniProtKB Accession Codes:

Q03135 Q9UGP1 Q9UNG1 Q9UQH6

Database IDs:

Citations:

PubMed ID: 1360410

Title: The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles.

PubMed ID: 1360410

DOI: 10.1016/0014-5793(92)81458-x

PubMed ID: 10086342

Title: Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines.

PubMed ID: 10086342

DOI: 10.1038/sj.onc.1202491

PubMed ID: 10218480

Title: 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.

PubMed ID: 10218480

DOI: 10.1016/s0014-5793(99)00365-8

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 15219854

Title: N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes.

PubMed ID: 15219854

DOI: 10.1016/j.bbrc.2004.05.196

PubMed ID: 15242332

Title: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.

PubMed ID: 15242332

DOI: 10.1042/bj20040647

PubMed ID: 8632005

Title: Phosphorylation of caveolin by src tyrosine kinases. The alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo.

PubMed ID: 8632005

DOI: 10.1074/jbc.271.7.3863

PubMed ID: 11751885

Title: Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx.

PubMed ID: 11751885

DOI: 10.1074/jbc.m108537200

PubMed ID: 11865038

Title: Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex.

PubMed ID: 11865038

DOI: 10.1242/jcs.115.4.827

PubMed ID: 12531427

Title: c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14.

PubMed ID: 12531427

DOI: 10.1016/s0898-6568(02)00090-6

PubMed ID: 16807357

Title: Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN.

PubMed ID: 16807357

DOI: 10.1091/mbc.e05-08-0709

PubMed ID: 16501093

Title: The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1.

PubMed ID: 16501093

DOI: 10.1128/jvi.80.6.2842-2854.2006

PubMed ID: 17287217

Title: Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1.

PubMed ID: 17287217

DOI: 10.1074/jbc.m609157200

PubMed ID: 18211975

Title: Association of a homozygous nonsense caveolin-1 mutation with Berardinelli-Seip congenital lipodystrophy.

PubMed ID: 18211975

DOI: 10.1210/jc.2007-1328

PubMed ID: 18237401

Title: Heterozygous CAV1 frameshift mutations (MIM 601047) in patients with atypical partial lipodystrophy and hypertriglyceridemia.

PubMed ID: 18237401

DOI: 10.1186/1476-511x-7-3

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19262564

Title: SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae function.

PubMed ID: 19262564

DOI: 10.1038/emboj.2009.46

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 20345844

Title: Decreased caveolin-1 levels contribute to fibrosis and deposition of extracellular IGFBP-5.

PubMed ID: 20345844

DOI: 10.1111/j.1582-4934.2010.01063.x

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22474227

Title: Whole exome sequencing to identify a novel gene (caveolin-1) associated with human pulmonary arterial hypertension.

PubMed ID: 22474227

DOI: 10.1161/circgenetics.111.961888

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24576892

Title: Caveolin-1 interacts with ATP binding cassette transporter G1 (ABCG1) and regulates ABCG1-mediated cholesterol efflux.

PubMed ID: 24576892

DOI: 10.1016/j.bbalip.2014.02.002

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25588833

Title: Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of caveolae.

PubMed ID: 25588833

DOI: 10.1242/jcs.161463

PubMed ID: 25893292

Title: Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization.

PubMed ID: 25893292

DOI: 10.1038/onc.2015.100

PubMed ID: 28593998

Title: The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation.

PubMed ID: 28593998

DOI: 10.1038/ncomms15502

PubMed ID: 12368209

Title: 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.

PubMed ID: 12368209

DOI: 10.1016/s0002-9440(10)64412-4

PubMed ID: 21822278

Title: Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations.

PubMed ID: 21822278

DOI: 10.1038/ncb2301

PubMed ID: 23335559

Title: Ubiquitination of the N-terminal region of caveolin-1 regulates endosomal sorting by the VCP/p97 AAA-ATPase.

PubMed ID: 23335559

DOI: 10.1074/jbc.m112.429076

PubMed ID: 25556234

Title: New host factors important for respiratory syncytial virus (RSV) replication revealed by a novel microfluidics screen for interactors of matrix (M) protein.

PubMed ID: 25556234

DOI: 10.1074/mcp.m114.044107

Sequence Information:

Length: 178
Mass: 20472
Checksum: 2424DE9B5E6521D5
Sequence:

MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADELSEKQ VYDAHTKEID LVNRDPKHLN 
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSALFGIP MALIWGIYFA 
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTVCDPLF EAVGKIFSNV RINLQKEI

Genular Protein ID: 4004908550

Symbol: A9XTE5_HUMAN

Name: N/A

UniProtKB Accession Codes:

A9XTE5

Database IDs:

Sequence Information:

Length: 176
Mass: 20068
Checksum: 39A8184FA6C3A71B
Sequence:

HGAVAVGAGH LYTVPIREQG NIYKPNNKAM ADELSEKQVY DAHTKEIDLV NRDPKHLNDD 
VVKIDFEDVI AEPEGTHSFD GIWKASFTTF TVTKYWFYRL LSALFGIPMA LIWGIYFAIL 
SFLHIWAVVP CIKSFLIEIQ CTSRVYSIYV HTVCDPLFEA VGKIFSNVRI NLQKEI

Genular Protein ID: 4202660448

Symbol: Q7Z4F3_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q7Z4F3

Database IDs:

Sequence Information:

Length: 147
Mass: 17011
Checksum: 1A7D908D1C072A47
Sequence:

MADELSEKQV YDAHTKEIDL VNRDPKHLND DVVKIDFEDV IAEPEGTHSF DGIWKASFTT 
FTVTKYWFYR LLSALFGIPM ALIWGIYFAI LSFLHIWAVV PCIKSFLIEI QCTSRVYSIY 
VHTVCDPLFE AVGKIFSNVR INLQKEI

Genular Protein ID: 2883065047

Symbol: Q59E85_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q59E85

Database IDs:

Sequence Information:

Length: 217
Mass: 25069
Checksum: 220BFA69EEDE7BF2
Sequence:

LSERLVRFRA RGFPRRQADF SSLVFLFAFF LPPPLPPSPS WPSALRPLQG HLYTVPIREQ 
GNIYKPNNKA MADELSEKQV YDAHTKEIDL VNRDPKHLND DVVKIDFEDV IAEPEGTHSF 
DGIWKASFTT FTVTKYWFYR LLSALFGIPM ALIWGIYFAI LSFLHIWAVV PCIKSFLIEI 
QCISRVYSIY VHTVCDPLFE AVGKIFSNVR INLQKEI

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: CAV1

Associated with

Cells (max top 100)

Other Information

The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles. PubMed ID: 1360410

Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines. PubMed ID: 10086342

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. PubMed ID: 10218480

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes. PubMed ID: 15219854

Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. PubMed ID: 15242332

Phosphorylation of caveolin by src tyrosine kinases. The alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo. PubMed ID: 8632005

Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx. PubMed ID: 11751885

Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex. PubMed ID: 11865038

c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14. PubMed ID: 12531427

Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN. PubMed ID: 16807357

The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1. PubMed ID: 16501093

Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1. PubMed ID: 17287217

Association of a homozygous nonsense caveolin-1 mutation with Berardinelli-Seip congenital lipodystrophy. PubMed ID: 18211975

Heterozygous CAV1 frameshift mutations (MIM 601047) in patients with atypical partial lipodystrophy and hypertriglyceridemia. PubMed ID: 18237401

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae function. PubMed ID: 19262564

Large-scale proteomics analysis of the human kinome. PubMed ID: 19369195

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Decreased caveolin-1 levels contribute to fibrosis and deposition of extracellular IGFBP-5. PubMed ID: 20345844

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Whole exome sequencing to identify a novel gene (caveolin-1) associated with human pulmonary arterial hypertension. PubMed ID: 22474227

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Caveolin-1 interacts with ATP binding cassette transporter G1 (ABCG1) and regulates ABCG1-mediated cholesterol efflux. PubMed ID: 24576892

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of caveolae. PubMed ID: 25588833

Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization. PubMed ID: 25893292

The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation. PubMed ID: 28593998

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. PubMed ID: 12368209

Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations. PubMed ID: 21822278

Ubiquitination of the N-terminal region of caveolin-1 regulates endosomal sorting by the VCP/p97 AAA-ATPase. PubMed ID: 23335559

New host factors important for respiratory syncytial virus (RSV) replication revealed by a novel microfluidics screen for interactors of matrix (M) protein. PubMed ID: 25556234

Database document:

PubMed ID: 1360410

PubMed ID: 10086342

PubMed ID: 10218480

PubMed ID: 15489334

PubMed ID: 15219854

PubMed ID: 15242332

PubMed ID: 8632005

PubMed ID: 11751885

PubMed ID: 11865038

PubMed ID: 12531427

PubMed ID: 16807357

PubMed ID: 16501093

PubMed ID: 17287217

PubMed ID: 18211975

PubMed ID: 18237401

PubMed ID: 18669648

PubMed ID: 19262564

PubMed ID: 19369195

PubMed ID: 19608861

PubMed ID: 20068231

PubMed ID: 20345844

PubMed ID: 21269460

PubMed ID: 21406692

PubMed ID: 22474227

PubMed ID: 22814378

PubMed ID: 23186163

PubMed ID: 24576892

PubMed ID: 24275569

PubMed ID: 25588833

PubMed ID: 25893292

PubMed ID: 28593998

PubMed ID: 12368209

PubMed ID: 21822278

PubMed ID: 23335559

PubMed ID: 25556234