Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O08849 (RGS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 2

Short name=RGS2
Gene names
Name:Rgs2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. May play a role in leukemogenesis. Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein.

Subunit structure

Interacts with EIF2B5 By similarity. Interacts with PRKG1 (isoform alpha) By similarity.

Subcellular location

Cell membrane By similarity. Cytoplasm By similarity. Nucleusnucleolus By similarity.

Tissue specificity

Expressed in a wide variety of tissues.

Post-translational modification

Phosphorylated by protein kinase C By similarity. Phosphorylation by PRKG1 leads to activation of RGS2 activity By similarity.

Sequence similarities

Contains 1 RGS domain.

Ontologies

Keywords
   Biological processCell cycle
Translation regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Molecular functionSignal transduction inhibitor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 11342430. Source: MGI

brown fat cell differentiation

Inferred from direct assay PubMed 18492766. Source: MGI

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of G-protein coupled receptor protein signaling pathway

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

negative regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

negative regulation of cardiac muscle hypertrophy

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

negative regulation of phospholipase activity

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

positive regulation of cardiac muscle contraction

Inferred from mutant phenotype PubMed 19127022PubMed 21291891. Source: BHF-UCL

positive regulation of microtubule polymerization

Inferred from electronic annotation. Source: Ensembl

regulation of adrenergic receptor signaling pathway

Inferred from mutant phenotype PubMed 21291891. Source: BHF-UCL

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

relaxation of cardiac muscle

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

relaxation of vascular smooth muscle

Inferred from mutant phenotype PubMed 14608379. Source: UniProtKB

spermatogenesis

Inferred from expression pattern PubMed 14581517. Source: BHF-UCL

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasmic side of plasma membrane

Inferred from direct assay PubMed 21291891. Source: BHF-UCL

cytosol

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement PubMed 11342430. Source: MGI

plasma membrane

Inferred from mutant phenotype PubMed 19127022. Source: BHF-UCL

   Molecular_functionGTPase activator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 17464283. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Regulator of G-protein signaling 2
PRO_0000204179

Regions

Domain83 – 199117RGS
Region32 – 6635Necessary for membrane association By similarity
Region79 – 11638Necessary to inhibit protein synthesis By similarity

Experimental info

Sequence conflict39 – 402KD → NH in AAB50617. Ref.1
Sequence conflict78 – 792QL → DV in AAL28114. Ref.3
Sequence conflict78 – 792QL → HV in AAB50617. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08849 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 5D6E255C2BC7E7FA

FASTA21124,294
        10         20         30         40         50         60 
MQSAMFLAVQ HDCVPMDKSA GNGPKVEEKR EKMKRTLLKD WKTRLSYFLQ NSSAPGKPKT 

        70         80         90        100        110        120 
GKKSKQQTFI KPSPEEAQLW AEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK 

       130        140        150        160        170        180 
KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKSLIAQ NIQEATSGCF TTAQKRVYSL 

       190        200        210 
MENNSYPRFL ESEFYQDLCK KPQITTEPHA T 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast."
Chen C., Zheng B., Han J., Lin S.-C.
J. Biol. Chem. 272:8679-8685(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"RGS molecule expression in murine B lymphocytes and ability to down-regulate chemotaxis to lymphoid chemokines."
Reif K., Cyster J.G.
J. Immunol. 164:4720-4729(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Identification of novel endometrial and embryonic factors involved in mouse embryo implantation."
Shen Q.-X., Wang J., Huang Z.-P.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U67187 mRNA. Translation: AAB50617.1.
AF215668 mRNA. Translation: AAF34625.1.
AF432916 mRNA. Translation: AAL28114.1.
AK031603 mRNA. Translation: BAC27471.1.
AK077922 mRNA. Translation: BAC37065.1.
AK162276 mRNA. Translation: BAE36830.1.
BC023001 mRNA. Translation: AAH23001.1.
CCDSCCDS15347.1.
RefSeqNP_033087.2. NM_009061.4.
UniGeneMm.28262.

3D structure databases

ProteinModelPortalO08849.
SMRO08849. Positions 73-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO08849. 1 interaction.
MINTMINT-4953705.
STRING10090.ENSMUSP00000115558.

PTM databases

PhosphoSiteO08849.

Proteomic databases

PRIDEO08849.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000127206; ENSMUSP00000115558; ENSMUSG00000026360.
GeneID19735.
KEGGmmu:19735.
UCSCuc007cxg.2. mouse.

Organism-specific databases

CTD5997.
MGIMGI:1098271. Rgs2.

Phylogenomic databases

eggNOGNOG252352.
GeneTreeENSGT00750000117382.
HOGENOMHOG000233512.
HOVERGENHBG013233.
InParanoidO08849.
KOK18154.
OMAQQAFIKP.
OrthoDBEOG7VHSZ5.
PhylomeDBO08849.
TreeFamTF315837.

Gene expression databases

BgeeO08849.
CleanExMM_RGS2.
GenevestigatorO08849.

Family and domain databases

Gene3D1.10.196.10. 2 hits.
InterProIPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view]
PfamPF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
PROSITEPS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio297172.
PROO08849.
SOURCESearch...

Entry information

Entry nameRGS2_MOUSE
AccessionPrimary (citable) accession number: O08849
Secondary accession number(s): Q544S7, Q91WX1, Q9JL24
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot