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Protein

Regulator of G-protein signaling 10

Gene

Rgs10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 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. Associates specifically with the activated forms of the G protein subunits G(i)-alpha and G(z)-alpha but fails to interact with the structurally and functionally distinct G(s)-alpha subunit. Activity on G(z)-alpha is inhibited by palmitoylation of the G-protein (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Enzyme and pathway databases

ReactomeiREACT_331048. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 10
Short name:
RGS10
Gene namesi
Name:Rgs10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1915115. Rgs10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Regulator of G-protein signaling 10PRO_0000204208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi74 – 741S-palmitoyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ9CQE5.
PaxDbiQ9CQE5.
PRIDEiQ9CQE5.

PTM databases

PhosphoSiteiQ9CQE5.

Expressioni

Gene expression databases

BgeeiQ9CQE5.
CleanExiMM_RGS10.
ExpressionAtlasiQ9CQE5. baseline and differential.
GenevestigatoriQ9CQE5.

Interactioni

Protein-protein interaction databases

IntActiQ9CQE5. 1 interaction.
MINTiMINT-4132285.

Structurei

3D structure databases

ProteinModelPortaliQ9CQE5.
SMRiQ9CQE5. Positions 30-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 156116RGSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG271158.
GeneTreeiENSGT00760000119142.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiQ9CQE5.
KOiK16449.
OMAiPKSTAKW.
OrthoDBiEOG7XDBF0.
PhylomeDBiQ9CQE5.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
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.

Q9CQE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTRAVSRLS RKRPPSDIHD GDGSSSSGHQ SLKSTAKWAS SLENLLEDPE
60 70 80 90 100
GVQRFREFLK KEFSEENVLF WLACEDFKKT EDRKQMQEKA KEIYMTFLSN
110 120 130 140 150
KASSQVNVEG QSRLTEKILE EPHPLMFQKL QDQIFNLMKY DSYSRFLKSD
160 170 180
LFLKPKRTEE EEEEPPDAQT AAKRASRIYN T
Length:181
Mass (Da):21,151
Last modified:June 1, 2001 - v1
Checksum:i9897860505962286
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731A → E in BAB30688 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009686 mRNA. Translation: BAB26440.1.
AK009283 mRNA. Translation: BAB26193.1.
AK017314 mRNA. Translation: BAB30688.1.
AK088009 mRNA. Translation: BAC40091.1.
CCDSiCCDS21896.1.
RefSeqiNP_080694.1. NM_026418.2.
UniGeneiMm.18635.

Genome annotation databases

EnsembliENSMUST00000033133; ENSMUSP00000033133; ENSMUSG00000030844.
GeneIDi67865.
KEGGimmu:67865.
UCSCiuc009jyw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009686 mRNA. Translation: BAB26440.1.
AK009283 mRNA. Translation: BAB26193.1.
AK017314 mRNA. Translation: BAB30688.1.
AK088009 mRNA. Translation: BAC40091.1.
CCDSiCCDS21896.1.
RefSeqiNP_080694.1. NM_026418.2.
UniGeneiMm.18635.

3D structure databases

ProteinModelPortaliQ9CQE5.
SMRiQ9CQE5. Positions 30-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CQE5. 1 interaction.
MINTiMINT-4132285.

PTM databases

PhosphoSiteiQ9CQE5.

Proteomic databases

MaxQBiQ9CQE5.
PaxDbiQ9CQE5.
PRIDEiQ9CQE5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033133; ENSMUSP00000033133; ENSMUSG00000030844.
GeneIDi67865.
KEGGimmu:67865.
UCSCiuc009jyw.1. mouse.

Organism-specific databases

CTDi6001.
MGIiMGI:1915115. Rgs10.

Phylogenomic databases

eggNOGiNOG271158.
GeneTreeiENSGT00760000119142.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiQ9CQE5.
KOiK16449.
OMAiPKSTAKW.
OrthoDBiEOG7XDBF0.
PhylomeDBiQ9CQE5.
TreeFamiTF315837.

Enzyme and pathway databases

ReactomeiREACT_331048. G alpha (i) signalling events.

Miscellaneous databases

NextBioi325763.
PROiQ9CQE5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQE5.
CleanExiMM_RGS10.
ExpressionAtlasiQ9CQE5. baseline and differential.
GenevestigatoriQ9CQE5.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
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

  1. "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: Head, Thymus and Tongue.

Entry informationi

Entry nameiRGS10_MOUSE
AccessioniPrimary (citable) accession number: Q9CQE5
Secondary accession number(s): Q9D3L2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: June 1, 2001
Last modified: May 27, 2015
This is version 102 of the entry and version 1 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.