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Protein

Regulator of G-protein signaling 5

Gene

Rgs5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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(i)-alpha and G(o)-alpha, but not to G(s)-alpha.

GO - Molecular functioni

  • GTPase activator activity Source: MGI

GO - Biological processi

  • G-protein coupled receptor signaling pathway Source: MGI
  • positive regulation of GTPase activity Source: GOC
  • termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 5
Short name:
RGS5
Gene namesi
Name:Rgs5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1098434. Rgs5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Regulator of G-protein signaling 5PRO_0000204189Add
BLAST

Proteomic databases

PRIDEiO08850.

PTM databases

PhosphoSiteiO08850.

Expressioni

Tissue specificityi

Expressed in heart and muscle.

Gene expression databases

BgeeiO08850.
CleanExiMM_RGS5.
GenevisibleiO08850. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027997.

Structurei

3D structure databases

ProteinModelPortaliO08850.
SMRiO08850. Positions 44-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 180117RGSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG285261.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiO08850.
KOiK16449.
OMAiPHSCLER.
OrthoDBiEOG7VHSZ5.
PhylomeDBiO08850.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[Graphical view]
PfamiPF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
PROSITEiPS50132. RGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O08850-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCKGLAALPH SCLERAKEIK IKLGILLQKP DSAVDLVIPY NEKPEKPAKA
60 70 80 90 100
HKPSLEEVLQ WRQSLDKLLQ NSYGFASFKS FLKSEFSEEN LEFWVACENY
110 120 130 140 150
KKIKSPIKMA EKAKQIYEEF IQTEAPKEVN IDHFTKDITM KNLVEPSPRS
160 170 180
FDLAQKRIYA LMEKDSLPRF VRSEFYKELI K
Length:181
Mass (Da):21,086
Last modified:August 14, 2001 - v2
Checksum:iB4B561CFE3DA9630
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 502KA → NG in AAB50618 (PubMed:9079700).Curated
Sequence conflicti77 – 771S → T in AAB50618 (PubMed:9079700).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67188 mRNA. Translation: AAB50618.1.
AK004165 mRNA. Translation: BAB23201.1.
AK044096 mRNA. Translation: BAC31773.1.
AK054098 mRNA. Translation: BAC35655.1.
BC037683 mRNA. Translation: AAH37683.1.
CCDSiCCDS15464.1.
RefSeqiNP_033089.2. NM_009063.3.
UniGeneiMm.20954.

Genome annotation databases

EnsembliENSMUST00000027997; ENSMUSP00000027997; ENSMUSG00000026678.
GeneIDi19737.
KEGGimmu:19737.
UCSCiuc007dlm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67188 mRNA. Translation: AAB50618.1.
AK004165 mRNA. Translation: BAB23201.1.
AK044096 mRNA. Translation: BAC31773.1.
AK054098 mRNA. Translation: BAC35655.1.
BC037683 mRNA. Translation: AAH37683.1.
CCDSiCCDS15464.1.
RefSeqiNP_033089.2. NM_009063.3.
UniGeneiMm.20954.

3D structure databases

ProteinModelPortaliO08850.
SMRiO08850. Positions 44-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027997.

PTM databases

PhosphoSiteiO08850.

Proteomic databases

PRIDEiO08850.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027997; ENSMUSP00000027997; ENSMUSG00000026678.
GeneIDi19737.
KEGGimmu:19737.
UCSCiuc007dlm.1. mouse.

Organism-specific databases

CTDi8490.
MGIiMGI:1098434. Rgs5.

Phylogenomic databases

eggNOGiNOG285261.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiO08850.
KOiK16449.
OMAiPHSCLER.
OrthoDBiEOG7VHSZ5.
PhylomeDBiO08850.
TreeFamiTF315837.

Miscellaneous databases

ChiTaRSiRgs5. mouse.
NextBioi297180.
PROiO08850.
SOURCEiSearch...

Gene expression databases

BgeeiO08850.
CleanExiMM_RGS5.
GenevisibleiO08850. MM.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[Graphical view]
PfamiPF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
PROSITEiPS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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.
    , 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: Brain cortex, Embryo and Oviduct.
  3. "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: FVB/N.
    Tissue: Mammary gland.

Entry informationi

Entry nameiRGS5_MOUSE
AccessioniPrimary (citable) accession number: O08850
Secondary accession number(s): Q543B1, Q9D0Z2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: July 22, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.