Q6NZI2 · CAVN1_HUMAN
- ProteinCaveolae-associated protein 1
- GeneCAVIN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids390 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:19726876).
Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876).
The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity).
Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876).
The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | caveola | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | membrane raft | |
Cellular Component | mitochondrion | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | identical protein binding | |
Molecular Function | RNA binding | |
Molecular Function | rRNA primary transcript binding | |
Biological Process | positive regulation of cell motility | |
Biological Process | protein secretion | |
Biological Process | rRNA transcription | |
Biological Process | termination of RNA polymerase I transcription | |
Biological Process | transcription initiation at RNA polymerase I promoter |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCaveolae-associated protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6NZI2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Translocates to the cytoplasm from the caveolae upon insulin stimulation (PubMed:17026959).
Colocalizes with CAV1 in lipid rafts in adipocytes. Localizes in the caveolae in a caveolin-dependent manner (By similarity).
Colocalizes with CAV1 in lipid rafts in adipocytes. Localizes in the caveolae in a caveolin-dependent manner (By similarity).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Lipodystrophy, congenital generalized, 4 (CGL4)
- Note
- DescriptionA form of congenital generalized lipodystrophy, a metabolic disorder characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and diabetes mellitus. CGL4 is characterized by the association of congenital generalized lipodystrophy with muscular dystrophy and cardiac anomalies. Inheritance is autosomal recessive.
- See alsoMIM:613327
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035982 | 14 | in a breast cancer sample; somatic mutation | |||
Sequence: P → T | ||||||
Natural variant | VAR_034416 | 193 | in dbSNP:rs35308568 | |||
Sequence: E → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 550 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000097094 | 1-390 | UniProt | Caveolae-associated protein 1 | |||
Sequence: MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSISKSLKESEALPEKEGEELGEGERPEEDAAALELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLVPAERREKLKTSRDKLRKSFTPDHVVYARSKTAVYKVPPFTFHVKKIREGQVEVLKATEMVEVGADDDEGGAERGEAGDLRRGSSPDVHALLEITEESDAVLVDKSDSD | |||||||
Modified residue | 36 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 40 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 40 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 46 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 116 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 118 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 122 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 156 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 156 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 161 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 161 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 165 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 167 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 169 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 170 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 171 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 171 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 175 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 202 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 203 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 203 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 300 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 302 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 302 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 308 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 316 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 326 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 365 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 366 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 376 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 379 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 387 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 387 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 389 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 389 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated. Present in active and inactive forms. Changes in phosphorylation pattern may alter activity. Phosphorylation at Tyr-156 is essential for its functionin the regulation of ribosomal transcriptional activity.
Five truncated forms are found in the caveolae. These are thought to be the result of proteolysis and may be phosphorylation-dependent.
Monoubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the CAVIN complex composed of CAVIN1, CAVIN2, CAVIN3 and CAVIN4. Homotrimer (By similarity).
Interacts with TTF1 (PubMed:9582279).
Interacts with RNA polymerase I subunit POLR1A/RPA1. Binds the 3' end of pre-rRNA. Interacts with transcription factor ZNF148 (By similarity).
Interacts with LIPE in the adipocyte cytoplasm (PubMed:17026959).
Interacts with CAV1 and CAVIN3 (By similarity).
Interacts with CAVIN2 (PubMed:19525939, PubMed:24567387).
Interacts with CAVIN4 and CAV3 (PubMed:24567387).
Interacts with TTF1 (PubMed:9582279).
Interacts with RNA polymerase I subunit POLR1A/RPA1. Binds the 3' end of pre-rRNA. Interacts with transcription factor ZNF148 (By similarity).
Interacts with LIPE in the adipocyte cytoplasm (PubMed:17026959).
Interacts with CAV1 and CAVIN3 (By similarity).
Interacts with CAVIN2 (PubMed:19525939, PubMed:24567387).
Interacts with CAVIN4 and CAV3 (PubMed:24567387).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-40 | Disordered | ||||
Sequence: MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGS | ||||||
Region | 1-98 | Required for homotrimerization and for interaction with CAVIN2 and CAVIN3 | ||||
Sequence: MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGK | ||||||
Region | 52-62 | Nuclear export signal | ||||
Sequence: VLVLSLLDKII | ||||||
Region | 53-75 | Leucine-zipper 1 | ||||
Sequence: LVLSLLDKIIGAVDQIQLTQAQL | ||||||
Region | 136-152 | Nuclear localization signal | ||||
Sequence: KKLEVNEAELLRRRNFK | ||||||
Region | 166-186 | Leucine-zipper 2 | ||||
Sequence: LSISKSLKESEALPEKEGEEL | ||||||
Region | 172-201 | Disordered | ||||
Sequence: LKESEALPEKEGEELGEGERPEEDAAALEL | ||||||
Compositional bias | 174-198 | Basic and acidic residues | ||||
Sequence: ESEALPEKEGEELGEGERPEEDAAA | ||||||
Coiled coil | 199-282 | |||||
Sequence: LELSSDEAVEVEEVIEESRAERIKRSGLRRVDDFKKAFSKEKMEKTKVRTRENLEKTRLKTKENLEKTRHTLEKRMNKLGTRLV | ||||||
Region | 233-249 | Nuclear localization signal | ||||
Sequence: KKAFSKEKMEKTKVRTR | ||||||
Region | 257-297 | Leucine-zipper 3 | ||||
Sequence: LKTKENLEKTRHTLEKRMNKLGTRLVPAERREKLKTSRDKL | ||||||
Compositional bias | 344-364 | Basic and acidic residues | ||||
Sequence: VGADDDEGGAERGEAGDLRRG | ||||||
Region | 344-366 | Disordered | ||||
Sequence: VGADDDEGGAERGEAGDLRRGSS |
Domain
The leucine-zipper domain 1 is essential for its localization in the caveolae.
Sequence similarities
Belongs to the CAVIN family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6NZI2-1
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.
- Name1
- Length390
- Mass (Da)43,476
- Last updated2004-07-05 v1
- ChecksumE37945A9C9E819D4
Q6NZI2-2
- Name2
- Differences from canonical
- 96-185: Missing
Q6NZI2-3
- Name3
- Differences from canonical
- 1-193: MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSISKSLKESEALPEKEGEELGEGERPE → M
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_051624 | 1-193 | in isoform 3 | |||
Sequence: MEDPTLYIVERPLPGYPDAEAPEPSSAGAQAAEEPSGAGSEELIKSDQVNGVLVLSLLDKIIGAVDQIQLTQAQLEERQAEMEGAVQSIQGELSKLGKAHATTSNTVSKLLEKVRKVSVNVKTVRGSLERQAGQIKKLEVNEAELLRRRNFKVMIYQDEVKLPAKLSISKSLKESEALPEKEGEELGEGERPE → M | ||||||
Sequence conflict | 47 | in Ref. 6; AA sequence | ||||
Sequence: D → V | ||||||
Alternative sequence | VSP_051625 | 96-185 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 174-198 | Basic and acidic residues | ||||
Sequence: ESEALPEKEGEELGEGERPEEDAAA | ||||||
Sequence conflict | 213 | in Ref. 6; AA sequence | ||||
Sequence: I → L | ||||||
Sequence conflict | 219 | in Ref. 1; AAG27093 | ||||
Sequence: E → K | ||||||
Compositional bias | 344-364 | Basic and acidic residues | ||||
Sequence: VGADDDEGGAERGEAGDLRRG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF312393 EMBL· GenBank· DDBJ | AAG27093.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314389 EMBL· GenBank· DDBJ | BAG37014.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471152 EMBL· GenBank· DDBJ | EAW60828.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004295 EMBL· GenBank· DDBJ | AAH04295.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008849 EMBL· GenBank· DDBJ | AAH08849.1 EMBL· GenBank· DDBJ | mRNA | ||
BC066123 EMBL· GenBank· DDBJ | AAH66123.1 EMBL· GenBank· DDBJ | mRNA | ||
BC073759 EMBL· GenBank· DDBJ | AAH73759.1 EMBL· GenBank· DDBJ | mRNA | ||
AF000421 EMBL· GenBank· DDBJ | AAC63404.1 EMBL· GenBank· DDBJ | mRNA |