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Regulator of G-protein signaling 2 (RGS2) (Cell growth-inhibiting gene 31 protein) (G0/G1 switch regulatory protein 8)

 RGS2_HUMAN              Reviewed;         211 AA.
P41220; Q6I9U5;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 170.
RecName: Full=Regulator of G-protein signaling 2;
Short=RGS2;
AltName: Full=Cell growth-inhibiting gene 31 protein;
AltName: Full=G0/G1 switch regulatory protein 8;
Name=RGS2; Synonyms=G0S8; ORFNames=GIG31;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8179820; DOI=10.1089/dna.1994.13.125;
Siderovski D.P., Heximer S.P., Forsdyke D.R.;
"A human gene encoding a putative basic helix-loop-helix
phosphoprotein whose mRNA increases rapidly in cycloheximide-treated
blood mononuclear cells.";
DNA Cell Biol. 13:125-147(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF LEU-37; LEU-38; TRP-41; LEU-45; PHE-48
AND LEU-49.
PubMed=11278586; DOI=10.1074/jbc.M009942200;
Heximer S.P., Lim H., Bernard J.L., Blumer K.J.;
"Mechanisms governing subcellular localization and function of human
RGS2.";
J. Biol. Chem. 276:14195-14203(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION,
SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, AND MUTAGENESIS OF
MET-1; MET-5; MET-16 AND MET-33.
PubMed=17901199; DOI=10.1124/mol.107.036285;
Gu S., Anton A., Salim S., Blumer K.J., Dessauer C.W., Heximer S.P.;
"Alternative translation initiation of human regulators of G-protein
signaling-2 yields a set of functionally distinct proteins.";
Mol. Pharmacol. 73:1-11(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kim J.W., Kim H.K., Shin S.M.;
"Identification of a human cell growth-inhibiting gene.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
TISSUE SPECIFICITY.
PubMed=7643615;
Wu H.-K., Heng H.H.Q., Shi X.-M., Forsdyke D.R., Tsui L.-C., Mak T.W.,
Minden M.D., Siderovski D.P.;
"Differential expression of a basic helix-loop-helix phosphoprotein
gene, G0S8, in acute leukemia and localization to human chromosome
1q31.";
Leukemia 9:1291-1298(1995).
[13]
PHOSPHORYLATION, AND FUNCTION.
PubMed=11063746; DOI=10.1074/jbc.M007699200;
Cunningham M.L., Waldo G.L., Hollinger S., Hepler J.R., Harden T.K.;
"Protein kinase C phosphorylates RGS2 and modulates its capacity for
negative regulation of Galpha 11 signaling.";
J. Biol. Chem. 276:5438-5444(2001).
[14]
PHOSPHORYLATION BY PRKG1, AND INTERACTION WITH PRKG1.
PubMed=14608379; DOI=10.1038/nm958;
Tang K.M., Wang G.R., Lu P., Karas R.H., Aronovitz M., Heximer S.P.,
Kaltenbronn K.M., Blumer K.J., Siderovski D.P., Zhu Y.,
Mendelsohn M.E.;
"Regulator of G-protein signaling-2 mediates vascular smooth muscle
relaxation and blood pressure.";
Nat. Med. 9:1506-1512(2003).
[15]
FUNCTION, INTERACTION WITH EIF2B5, AND MUTAGENESIS OF LEU-79; GLU-86;
LEU-87; SER-90; LYS-102; PHE-105; ILE-110; GLU-111; LEU-114 AND
ASN-149.
PubMed=19736320; DOI=10.1083/jcb.200811058;
Nguyen C.H., Ming H., Zhao P., Hugendubler L., Gros R., Kimball S.R.,
Chidiac P.;
"Translational control by RGS2.";
J. Cell Biol. 186:755-765(2009).
[16]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GNAQ, AND
CHARACTERIZATION OF VARIANTS ARG-2; LEU-2; GLY-3; VAL-4; VAL-5;
ASN-18; ASP-23; TYR-40; HIS-44; LYS-50; LEU-55; HIS-78; GLY-99;
VAL-110; HIS-188 AND ARG-196.
PubMed=28784619; DOI=10.1124/mol.117.109215;
Phan H.T.N., Sjoegren B., Neubig R.R.;
"Human missense mutations in regulator of G protein signaling 2 affect
the protein function through multiple mechanisms.";
Mol. Pharmacol. 92:451-458(2017).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 71-203, INTERACTION WITH
GNAQ, LACK OF INTERACTION WITH GNAI1, AND MUTAGENESIS OF CYS-106 AND
ASN-184.
PubMed=18434541; DOI=10.1073/pnas.0801508105;
Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
"Structural diversity in the RGS domain and its interaction with
heterotrimeric G protein alpha-subunits.";
Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
[18]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 71-209 IN COMPLEXES WITH
GNAQ AND GNAI3, FUNCTION, INTERACTION WITH GNAQ, LACK OF INTERACTION
WITH GNAI1 AND GNAI3, AND MUTAGENESIS OF CYS-106; ASN-184 AND GLU-191.
PubMed=19478087; DOI=10.1074/jbc.M109.024711;
Kimple A.J., Soundararajan M., Hutsell S.Q., Roos A.K., Urban D.J.,
Setola V., Temple B.R., Roth B.L., Knapp S., Willard F.S.,
Siderovski D.P.;
"Structural determinants of G-protein alpha subunit selectivity by
regulator of G-protein signaling 2 (RGS2).";
J. Biol. Chem. 284:19402-19411(2009).
[19]
VARIANTS ARG-2; LEU-2; VAL-5; HIS-44 AND HIS-78.
PubMed=16003176;
Yang J., Kamide K., Kokubo Y., Takiuchi S., Tanaka C., Banno M.,
Miwa Y., Yoshii M., Horio T., Okayama A., Tomoike H., Kawano Y.,
Miyata T.;
"Genetic variations of regulator of G-protein signaling 2 in
hypertensive patients and in the general population.";
J. Hypertens. 23:1497-1505(2005).
[20]
VARIANTS ARG-2; LEU-2; GLY-3; VAL-4; VAL-5; ASN-18; ASP-23; TYR-40;
HIS-44; LYS-50; LEU-55; GLY-99; VAL-110; HIS-188 AND ARG-196.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- 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}.
-!- SUBUNIT: Interacts with GNAQ (PubMed:18434541, PubMed:19478087,
PubMed:28784619). Does not interact with GNAI1 and GNAI3
(PubMed:18434541, PubMed:19478087). Interacts with EIF2B5
(PubMed:19736320). Interacts with PRKG1 (isoform alpha)
(PubMed:14608379). {ECO:0000269|PubMed:14608379,
ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:19478087,
ECO:0000269|PubMed:19736320, ECO:0000269|PubMed:28784619}.
-!- INTERACTION:
P21279:Gnaq (xeno); NbExp=3; IntAct=EBI-16037474, EBI-771975;
Q5S007:LRRK2; NbExp=6; IntAct=EBI-712388, EBI-5323863;
O60337:MARCH6; NbExp=3; IntAct=EBI-16037474, EBI-2684600;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-712388, EBI-742948;
Q5JR59-3:MTUS2; NbExp=3; IntAct=EBI-712388, EBI-11522433;
Q9ULJ8:PPP1R9A; NbExp=3; IntAct=EBI-712388, EBI-2515561;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=4;
Name=1;
IsoId=P41220-1; Sequence=Displayed;
Name=2;
IsoId=P41220-2; Sequence=VSP_041296;
Name=3;
IsoId=P41220-3; Sequence=VSP_041297;
Note=Lacks type V adenylyl cyclase (AC) inhibitory function.;
Name=4;
IsoId=P41220-4; Sequence=VSP_041298;
Note=Lacks type V adenylyl cyclase (AC) inhibitory function.;
-!- TISSUE SPECIFICITY: Expressed in acute myelogenous leukemia (AML)
and in acute lymphoblastic leukemia (ALL).
{ECO:0000269|PubMed:7643615}.
-!- PTM: Phosphorylated by protein kinase C. Phosphorylation by PRKG1
leads to activation of RGS2 activity.
{ECO:0000269|PubMed:11063746, ECO:0000269|PubMed:14608379}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RGS2ID42102ch1q31.html";
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EMBL; L13391; AAA20680.1; -; Genomic_DNA.
EMBL; L13463; AAC37587.1; -; mRNA.
EMBL; AF493926; AAM12640.1; -; mRNA.
EMBL; AY971351; AAY40361.1; -; mRNA.
EMBL; AK313668; BAG36420.1; -; mRNA.
EMBL; BT007065; AAP35728.1; -; mRNA.
EMBL; CR457410; CAG33691.1; -; mRNA.
EMBL; AL035407; CAB62512.1; -; Genomic_DNA.
EMBL; CH471067; EAW91231.1; -; Genomic_DNA.
EMBL; BC007049; AAH07049.1; -; mRNA.
CCDS; CCDS1377.1; -. [P41220-1]
PIR; I53020; I53020.
RefSeq; NP_002914.1; NM_002923.3. [P41220-1]
UniGene; Hs.78944; -.
PDB; 2AF0; X-ray; 2.30 A; A=71-203.
PDB; 2V4Z; X-ray; 2.80 A; B=71-209.
PDB; 4EKC; X-ray; 7.40 A; B/D=72-203.
PDB; 4EKD; X-ray; 2.71 A; B=72-203.
PDBsum; 2AF0; -.
PDBsum; 2V4Z; -.
PDBsum; 4EKC; -.
PDBsum; 4EKD; -.
ProteinModelPortal; P41220; -.
SMR; P41220; -.
BioGrid; 111929; 67.
DIP; DIP-44289N; -.
IntAct; P41220; 49.
MINT; MINT-1380095; -.
STRING; 9606.ENSP00000235382; -.
iPTMnet; P41220; -.
PhosphoSitePlus; P41220; -.
SwissPalm; P41220; -.
BioMuta; RGS2; -.
DMDM; 729545; -.
MaxQB; P41220; -.
PaxDb; P41220; -.
PeptideAtlas; P41220; -.
PRIDE; P41220; -.
DNASU; 5997; -.
Ensembl; ENST00000235382; ENSP00000235382; ENSG00000116741. [P41220-1]
GeneID; 5997; -.
KEGG; hsa:5997; -.
UCSC; uc001gsl.4; human. [P41220-1]
CTD; 5997; -.
DisGeNET; 5997; -.
EuPathDB; HostDB:ENSG00000116741.7; -.
GeneCards; RGS2; -.
HGNC; HGNC:9998; RGS2.
HPA; HPA013385; -.
MIM; 600861; gene.
neXtProt; NX_P41220; -.
OpenTargets; ENSG00000116741; -.
PharmGKB; PA34372; -.
eggNOG; KOG3589; Eukaryota.
eggNOG; ENOG410YMJD; LUCA.
GeneTree; ENSGT00760000118903; -.
HOGENOM; HOG000233512; -.
HOVERGEN; HBG013233; -.
InParanoid; P41220; -.
KO; K18154; -.
OMA; AVQHDCV; -.
OrthoDB; EOG091G0BDG; -.
PhylomeDB; P41220; -.
TreeFam; TF315837; -.
Reactome; R-HSA-416476; G alpha (q) signalling events.
SIGNOR; P41220; -.
ChiTaRS; RGS2; human.
EvolutionaryTrace; P41220; -.
GeneWiki; RGS2; -.
GenomeRNAi; 5997; -.
PRO; PR:P41220; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116741; -.
CleanEx; HS_RGS2; -.
ExpressionAtlas; P41220; baseline and differential.
Genevisible; P41220; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IEA:Ensembl.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:BHF-UCL.
GO; GO:0045744; P:negative regulation of G-protein coupled receptor protein signaling pathway; ISS:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:BHF-UCL.
GO; GO:0010519; P:negative regulation of phospholipase activity; ISS:BHF-UCL.
GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISS:BHF-UCL.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IEA:Ensembl.
GO; GO:0071877; P:regulation of adrenergic receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IMP:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0055119; P:relaxation of cardiac muscle; ISS:BHF-UCL.
GO; GO:0060087; P:relaxation of vascular smooth muscle; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
Gene3D; 1.10.196.10; -; 2.
InterPro; IPR016137; RGS.
InterPro; IPR034947; RGS2.
InterPro; IPR036305; RGS_sf.
InterPro; IPR024066; RGS_subdom1.
PANTHER; PTHR10845:SF43; PTHR10845:SF43; 1.
Pfam; PF00615; RGS; 1.
PRINTS; PR01301; RGSPROTEIN.
SMART; SM00315; RGS; 1.
SUPFAM; SSF48097; SSF48097; 1.
PROSITE; PS50132; RGS; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Cell cycle; Cell membrane;
Complete proteome; Cytoplasm; GTPase activation; Membrane;
Mitochondrion; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Signal transduction inhibitor;
Translation regulation.
CHAIN 1 211 Regulator of G-protein signaling 2.
/FTId=PRO_0000204178.
DOMAIN 83 199 RGS. {ECO:0000255|PROSITE-
ProRule:PRU00171}.
REGION 32 66 Necessary for membrane association.
{ECO:0000269|PubMed:11278586}.
REGION 79 116 Necessary to inhibit protein synthesis.
{ECO:0000269|PubMed:19736320}.
VAR_SEQ 1 32 Missing (in isoform 4).
{ECO:0000303|PubMed:17901199}.
/FTId=VSP_041298.
VAR_SEQ 1 15 Missing (in isoform 3).
{ECO:0000303|PubMed:17901199}.
/FTId=VSP_041297.
VAR_SEQ 1 4 Missing (in isoform 2).
{ECO:0000303|PubMed:17901199}.
/FTId=VSP_041296.
VARIANT 2 2 Q -> L (rare polymorphism; decreased
down-regulation of angiotensin-activated
signaling pathway; decreased RGS2 protein
abundance). {ECO:0000269|PubMed:16003176,
ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079238.
VARIANT 2 2 Q -> R (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:16003176,
ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079239.
VARIANT 3 3 S -> G (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079240.
VARIANT 4 4 A -> V (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079241.
VARIANT 5 5 M -> V (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:16003176,
ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079242.
VARIANT 18 18 K -> N (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079243.
VARIANT 23 23 G -> D (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079244.
VARIANT 40 40 D -> Y (rare polymorphism; decreased
down-regulation of angiotensin-activated
signaling pathway; reduced localization
at the cell membrane).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079245.
VARIANT 44 44 R -> H (rare polymorphism; decreased
down-regulation of angiotensin-activated
signaling pathway; reduced localization
at the cell membrane).
{ECO:0000269|PubMed:16003176,
ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079246.
VARIANT 50 50 Q -> K (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079247.
VARIANT 55 55 P -> L (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079248.
VARIANT 78 78 Q -> H (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:16003176,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079249.
VARIANT 99 99 A -> G (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079250.
VARIANT 110 110 I -> V (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079251.
VARIANT 188 188 R -> H (rare polymorphism; decreased
down-regulation of angiotensin-activated
signaling pathway; reduced interaction
with GNAQ). {ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079252.
VARIANT 196 196 Q -> R (rare polymorphism; no effect on
down-regulation of angiotensin-activated
signaling pathway).
{ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:28784619}.
/FTId=VAR_079253.
MUTAGEN 1 1 M->L: Loss of isoform 1 expression.
{ECO:0000269|PubMed:17901199}.
MUTAGEN 5 5 M->L: Loss of isoform 2 expression.
{ECO:0000269|PubMed:17901199}.
MUTAGEN 16 16 M->L: Loss of isoform 3 expression.
{ECO:0000269|PubMed:17901199}.
MUTAGEN 33 33 M->L: Loss of isoform 4 expression.
{ECO:0000269|PubMed:17901199}.
MUTAGEN 37 37 L->D: Impairs association with plasma
membrane. {ECO:0000269|PubMed:11278586}.
MUTAGEN 38 38 L->D: Impairs association with plasma
membrane. {ECO:0000269|PubMed:11278586}.
MUTAGEN 41 41 W->D: Impairs association with plasma
membrane. {ECO:0000269|PubMed:11278586}.
MUTAGEN 45 45 L->D: Impairs association with plasma
membrane. {ECO:0000269|PubMed:11278586}.
MUTAGEN 48 48 F->D: Impairs association with plasma
membrane. {ECO:0000269|PubMed:11278586}.
MUTAGEN 49 49 L->D: Impairs association with plasma
membrane. {ECO:0000269|PubMed:11278586}.
MUTAGEN 79 79 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 86 86 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 87 87 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 90 90 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 102 102 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 105 105 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 106 106 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.
{ECO:0000269|PubMed:18434541,
ECO:0000269|PubMed:19478087}.
MUTAGEN 110 110 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 111 111 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 114 114 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 149 149 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.
{ECO:0000269|PubMed:19736320}.
MUTAGEN 184 184 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.
{ECO:0000269|PubMed:18434541,
ECO:0000269|PubMed:19478087}.
MUTAGEN 191 191 E->K: Strongly increases affinity for
GNAI1 and GNAI3; when associated with S-
106 and D-184.
{ECO:0000269|PubMed:19478087}.
HELIX 74 79 {ECO:0000244|PDB:2AF0}.
TURN 80 82 {ECO:0000244|PDB:2V4Z}.
HELIX 84 89 {ECO:0000244|PDB:2AF0}.
HELIX 91 103 {ECO:0000244|PDB:2AF0}.
HELIX 108 120 {ECO:0000244|PDB:2AF0}.
HELIX 125 139 {ECO:0000244|PDB:2AF0}.
HELIX 152 161 {ECO:0000244|PDB:2AF0}.
HELIX 162 164 {ECO:0000244|PDB:2AF0}.
TURN 167 170 {ECO:0000244|PDB:2AF0}.
HELIX 171 183 {ECO:0000244|PDB:2AF0}.
HELIX 185 191 {ECO:0000244|PDB:2AF0}.
HELIX 193 199 {ECO:0000244|PDB:2AF0}.
SEQUENCE 211 AA; 24382 MW; EFFE4AE47EF9AD8F CRC64;
MQSAMFLAVQ HDCRPMDKSA GSGHKSEEKR EKMKRTLLKD WKTRLSYFLQ NSSTPGKPKT
GKKSKQQAFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK
KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL
MENNSYPRFL ESEFYQDLCK KPQITTEPHA T


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