P49795 · RGS19_HUMAN
- ProteinRegulator of G-protein signaling 19
- GeneRGS19
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids217 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein.
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 | brush border | |
Cellular Component | clathrin-coated vesicle | |
Cellular Component | Golgi apparatus | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | G-protein alpha-subunit binding | |
Molecular Function | GTPase activity | |
Biological Process | autophagy | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | negative regulation of signal transduction | |
Biological Process | response to ethanol | |
Biological Process | small GTPase-mediated signal transduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRegulator of G-protein signaling 19
- Short namesRGS19
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP49795
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 151 | Diminishes gap activity towards G(i)-alpha3 and autophagy in colon cancer cells. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 265 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000204229 | 1-217 | UniProt | Regulator of G-protein signaling 19 | |||
Sequence: MPTPHEAEKQITGPEEADRPPSMSSHDTASPAAPSRNPCCLCWCCCCSCSWNQERRRAWQASRESKLQPLPSCEVCATPSPEEVQSWAQSFDKLMHSPAGRSVFRAFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINKKMQEPSAHTFDDAQLQIYTLMHRDSYPRFLSSPTYRALLLQGPSQSSSEA | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 24 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 97 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 143 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 151 | UniProt | Phosphoserine; by MAPK1 and MAPK3 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 215 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Fatty acylated. Heavily palmitoylated in the cysteine string motif.
Phosphorylated, mainly on serine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with GIPC PDZ domain. Interacts with GNAO1 (PubMed:34685729).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P49795 | ALPP P05187 | 3 | EBI-874907, EBI-1211484 | |
BINARY | P49795 | CATSPER1 Q8NEC5 | 3 | EBI-874907, EBI-744545 | |
XENO | P49795 | Gnai3 P08753 | 4 | EBI-874907, EBI-874897 | |
BINARY | P49795 | HOXA1 P49639 | 3 | EBI-874907, EBI-740785 | |
BINARY | P49795 | KRTAP5-6 Q6L8G9 | 3 | EBI-874907, EBI-10250562 | |
BINARY | P49795 | LCE4A Q5TA78 | 3 | EBI-874907, EBI-10246358 | |
BINARY | P49795 | NUFIP2 Q7Z417 | 3 | EBI-874907, EBI-1210753 | |
BINARY | P49795 | OTX1 P32242 | 3 | EBI-874907, EBI-740446 | |
BINARY | P49795 | POU4F2 Q12837 | 3 | EBI-874907, EBI-17236143 | |
BINARY | P49795 | PSMA1 P25786 | 3 | EBI-874907, EBI-359352 | |
BINARY | P49795 | VASN Q6EMK4 | 3 | EBI-874907, EBI-10249550 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MPTPHEAEKQITGPE | ||||||
Region | 1-29 | Disordered | ||||
Sequence: MPTPHEAEKQITGPEEADRPPSMSSHDTA | ||||||
Domain | 90-206 | RGS | ||||
Sequence: SFDKLMHSPAGRSVFRAFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINKKMQEPSAHTFDDAQLQIYTLMHRDSYPRFLSSPTYRALL | ||||||
Region | 207-217 | Interaction with GIPC | ||||
Sequence: LQGPSQSSSEA |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length217
- Mass (Da)24,636
- Last updated1996-10-01 v1
- Checksum925A5687DC222CBD
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MPTPHEAEKQITGPE | ||||||
Sequence conflict | 204 | in Ref. 2; AAM12653 | ||||
Sequence: A → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X91809 EMBL· GenBank· DDBJ | CAA62919.1 EMBL· GenBank· DDBJ | mRNA | ||
AF493939 EMBL· GenBank· DDBJ | AAM12653.1 EMBL· GenBank· DDBJ | mRNA | ||
AY585188 EMBL· GenBank· DDBJ | AAS94232.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009804 EMBL· GenBank· DDBJ | AAP88806.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290081 EMBL· GenBank· DDBJ | BAF82770.1 EMBL· GenBank· DDBJ | mRNA | ||
AL590548 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW75166.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW75167.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001318 EMBL· GenBank· DDBJ | AAH01318.1 EMBL· GenBank· DDBJ | mRNA | ||
BC054337 EMBL· GenBank· DDBJ | AAH54337.1 EMBL· GenBank· DDBJ | mRNA | ||
BC063010 EMBL· GenBank· DDBJ | AAH63010.1 EMBL· GenBank· DDBJ | mRNA |