RGS2
entrez
5997
canonical
uniprot
P41220
canonical
ensembl
ENSG00000116741
resolver
ensp
ENSP00000235382
resolver
genesymbol
RGS2
resolver
genesymbol_syn
G0S8
resolver
hgnc
HGNC:9998
resolver
uniprot
Q6I9U5
resolver
uniprot_entry
RGS2_HUMAN
resolver
uniprot_sec
Q6I9U5
resolver
amino_acid_sequence
MQSAMFLAVQHDCRPMDKSAGSGHKSEEKREKMKRTLLKDWKTRLSYFLQNSSTPGKPKTGKKSKQQAFIKPSPEEAQLWSEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKTLIAQNIQEATSGCFTTAQKRVYSLMENNSYPRFLESEFYQDLCKKPQITTEPHAT
uniprot
proteins
function
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:11063746, PubMed:19478087). It is involved in the negative regulation of the angiotensin-activated signaling pathway (PubMed:28784619). Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle (By similarity). Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein (PubMed:19736320). {ECO:0000250|UniProtKB:O08849, ECO:0000269|PubMed:11063746, ECO:0000269|PubMed:11278586, ECO:0000269|PubMed:17901199, ECO:0000269|PubMed:19736320, ECO:0000269|PubMed:28784619, ECO:0000305|PubMed:7643615}.
uniprot
proteins
mass_dalton
24382
uniprot
proteins
mutagenesis
MUTAGEN 1; /note="M->L: Loss of isoform 1 expression."; /evidence="ECO:0000269|PubMed:17901199"; MUTAGEN 3; /note="S->A: Expressed at significantly lower levels than WT."; /evidence="ECO:0000269|PubMed:33008920"; MUTAGEN 3; /note="S->D: Complete suppression of the response to proteasome inhibitor MG132."; /evidence="ECO:0000269|PubMed:33008920"; MUTAGEN 5; /note="M->L: Loss of isoform 2 expression."; /evidence="ECO:0000269|PubMed:17901199"; MUTAGEN 16; /note="M->L: Loss of isoform 3 expression."; /evidence="ECO:0000269|PubMed:17901199"; MUTAGEN 33; /note="M->L: Loss of isoform 4 expression."; /evidence="ECO:0000269|PubMed:17901199"; MUTAGEN 37; /note="L->D: Impairs association with plasma membrane."; /evidence="ECO:0000269|PubMed:11278586"; MUTAGEN 38; /note="L->D: Impairs association with plasma membrane."; /evidence="ECO:0000269|PubMed:11278586"; MUTAGEN 41; /note="W->D: Impairs association with plasma membrane."; /evidence="ECO:0000269|PubMed:11278586"; MUTAGEN 45; /note="L->D: Impairs association with plasma membrane."; /evidence="ECO:0000269|PubMed:11278586"; MUTAGEN 48; /note="F->D: Impairs association with plasma membrane."; /evidence="ECO:0000269|PubMed:11278586"; MUTAGEN 49; /note="L->D: Impairs association with plasma membrane."; /evidence="ECO:0000269|PubMed:11278586"; MUTAGEN 79; /note="L->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with E-86; L-87; S-90; K-102; F-105; I-110; E-111 and L-114."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 86; /note="E->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; L-87; S-90; K-102; F-105; I-110; E-111 and L-114."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 87; /note="L->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; S-90; K-102; F-105; I-110; E-111 and L-114."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 90; /note="S->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; K-102; F-105; I-110; E-111 and L-114."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 102; /note="K->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; F-105; I-110; E-111 and L-114."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 105; /note="F->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; I-110; E-111 and L-114."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 106; /note="C->S: Changes specificity and confers GNAI1 binding; when associated with D-184. Strongly increases affinity for GNAI1 and GNAI3; when associated with D-184 and K-191."; /evidence="ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:19478087"; MUTAGEN 110; /note="I->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; E-111 and L-114."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 111; /note="E->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and L-114."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 114; /note="L->A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and E-111."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 149; /note="N->A: Decreases GTPase accelerating function but has no effect on translation inhibitory activity, suggesting that its role in translation is independent of its effects on G proteins."; /evidence="ECO:0000269|PubMed:19736320"; MUTAGEN 184; /note="N->D: Changes specificity and confers GNAI1 binding; when associated with D-184. Strongly increases affinity for GNAI1 and GNAI3; when associated with S-106 and K-191."; /evidence="ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:19478087"; MUTAGEN 191; /note="E->K: Strongly increases affinity for GNAI1 and GNAI3; when associated with S-106 and D-184."; /evidence="ECO:0000269|PubMed:19478087"; MUTAGEN 200; /note="K->R: Complete abolishment of RGS2 ubiquitination."; /evidence="ECO:0000269|PubMed:33008920
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads to activation of RGS2 activity. Phosphorylation of Ser-3 protects RGS2 from FBXO44-mediated proteasomal degradation (PubMed:33008920). {ECO:0000269|PubMed:11063746, ECO:0000269|PubMed:14608379, ECO:0000269|PubMed:33008920}.; PTM: Ubiquitinated by the cullin-RING ligase (CRL) complex composed of CUL4B, DDB1 and FBXO44; ubiquitination leads to RGS2 proteasomal degradation. {ECO:0000269|PubMed:25970626, ECO:0000269|PubMed:33008920}.
uniprot
proteins
pubmed
11063746
uniprot
proteins
pubmed
11278586
uniprot
proteins
pubmed
14608379
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16003176
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17901199
uniprot
proteins
pubmed
18434541
uniprot
proteins
pubmed
19478087
uniprot
proteins
pubmed
19736320
uniprot
proteins
pubmed
25970626
uniprot
proteins
pubmed
27535533
uniprot
proteins
pubmed
28784619
uniprot
proteins
pubmed
33008920
uniprot
proteins
pubmed
7643615
uniprot
proteins
pubmed
8179820
uniprot
proteins
sequence_length
211
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:11278586, ECO:0000269|PubMed:17901199, ECO:0000269|PubMed:28784619}. Cytoplasm {ECO:0000269|PubMed:11278586, ECO:0000269|PubMed:17901199}. Nucleus, nucleolus {ECO:0000269|PubMed:11278586, ECO:0000269|PubMed:17901199}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17901199}. Cytoplasm {ECO:0000269|PubMed:17901199}. Nucleus, nucleolus {ECO:0000269|PubMed:17901199}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:17901199}. Cytoplasm {ECO:0000269|PubMed:17901199}. Nucleus, nucleolus {ECO:0000269|PubMed:17901199}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:17901199}. Mitochondrion {ECO:0000269|PubMed:17901199}.
uniprot
proteins