Rgs19
entrez
59293
canonical
uniprot
O70521
canonical
ensembl
ENSRNOG00000016547
resolver
ensembl
ENSRNOG00055001222
resolver
ensembl
ENSRNOG00060001420
resolver
ensembl
ENSRNOG00065014006
resolver
ensp
ENSRNOP00000022451
resolver
ensp
ENSRNOP00000099010
resolver
ensp
ENSRNOP00055001612
resolver
ensp
ENSRNOP00060001283
resolver
ensp
ENSRNOP00065018012
resolver
enst
ENSRNOT00000022451
resolver
enst
ENSRNOT00055002045
resolver
enst
ENSRNOT00060002087
resolver
enst
ENSRNOT00065023124
resolver
genesymbol
Rgs19
resolver
genesymbol_syn
Gaip
resolver
uniprot_entry
RGS19_RAT
resolver
amino_acid_sequence
MPTPHEAEKQHTGPEEADRPPSMSSHDAAPSGPPSRNPCCLCWCCCCSCSWNQERQRAWQVSRESKLQPLPSCEVCTPPSPEEVQSWAQSFDKLMHSPTGRSVFRAFLRTEYSEENMLFWLACEELKTEADRHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINRKMQEPSPHTFDDAQLQIYTLMHRDSYPRFLTSPTYRSLLLQGAPQSSEA
uniprot
proteins
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, predominantly to G(i)-alpha-3. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G protein (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
24738
uniprot
proteins
mutagenesis
MUTAGEN 24; /note="S->A: 50% reduction of phosphorylation."; /evidence="ECO:0000269|PubMed:10760275
uniprot
proteins
post_translational_modification
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity). {ECO:0000250}.; PTM: Phosphorylated, mainly on serine residues. {ECO:0000269|PubMed:10760275}.
uniprot
proteins
pubmed
10760275
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
9571244
uniprot
proteins
sequence_length
216
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
uniprot
proteins