RGS19
entrez
10287
canonical
uniprot
P49795
canonical
ensembl
ENSG00000171700
resolver
ensp
ENSP00000333194
resolver
ensp
ENSP00000378483
resolver
ensp
ENSP00000580449
resolver
ensp
ENSP00000580450
resolver
ensp
ENSP00000580452
resolver
ensp
ENSP00000580453
resolver
ensp
ENSP00000580454
resolver
ensp
ENSP00000606806
resolver
ensp
ENSP00000614585
resolver
enst
ENST00000332298
resolver
enst
ENST00000395042
resolver
enst
ENST00000910390
resolver
enst
ENST00000910391
resolver
enst
ENST00000910393
resolver
enst
ENST00000910394
resolver
enst
ENST00000910395
resolver
enst
ENST00000936747
resolver
enst
ENST00000944526
resolver
genesymbol
RGS19
resolver
genesymbol_syn
GAIP
resolver
genesymbol_syn
GNAI3IP
resolver
hgnc
HGNC:13735
resolver
uniprot
A8K216
resolver
uniprot
B4DP94
resolver
uniprot
E1P5G9
resolver
uniprot
Q53XN0
resolver
uniprot
Q8TD60
resolver
uniprot_entry
B4DP94_HUMAN
resolver
uniprot_entry
RGS19_HUMAN
resolver
uniprot_sec
A8K216
resolver
uniprot_sec
E1P5G9
resolver
uniprot_sec
Q53XN0
resolver
uniprot_sec
Q8TD60
resolver
amino_acid_sequence
MPTPHEAEKQITGPEEADRPPSMSSHDTASPAAPSRNPCCLCWCCCCSCSWNQERRRAWQASRESKLQPLPSCEVCATPSPEEVQSWAQSFDKLMHSPAGRSVFRAFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINKKMQEPSAHTFDDAQLQIYTLMHRDSYPRFLSSPTYRALLLQGPSQSSSEA
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, 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.
uniprot
proteins
mass_dalton
24636
uniprot
proteins
mutagenesis
MUTAGEN 151; /note="S->A: Diminishes gap activity towards G(i)-alpha3 and autophagy in colon cancer cells."; /evidence="ECO:0000269|PubMed:10993892
uniprot
proteins
post_translational_modification
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif. {ECO:0000269|PubMed:8986788}.; PTM: Phosphorylated, mainly on serine residues. {ECO:0000269|PubMed:10993892}.
uniprot
proteins
pubmed
10452897
uniprot
proteins
pubmed
10993892
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
34685729
uniprot
proteins
pubmed
8524874
uniprot
proteins
pubmed
8986788
uniprot
proteins
pubmed
9748280
uniprot
proteins
sequence_length
217
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
uniprot
proteins