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Protein

Regulator of G-protein signaling 1

Gene

Rgs1

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.

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

Enzyme and pathway databases

ReactomeiREACT_331048. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 1
Short name:
RGS1
Gene namesi
Name:Rgs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1354694. Rgs1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • plasma membrane Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209Regulator of G-protein signaling 1PRO_0000204176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphoserine; by CK2Sequence Analysis
Modified residuei67 – 671Phosphoserine; by PKCSequence Analysis
Modified residuei75 – 751Phosphoserine; by CK2Sequence Analysis
Modified residuei159 – 1591Phosphothreonine; by PKCSequence Analysis
Modified residuei169 – 1691Phosphothreonine; by CK2Sequence Analysis
Modified residuei180 – 1801Phosphoserine; by CK2Sequence Analysis
Modified residuei207 – 2071Phosphothreonine; by PKCSequence Analysis

Post-translational modificationi

Could be phosphorylated. Might be functionally regulated by protein kinase(s) (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9JL25.

PTM databases

PhosphoSiteiQ9JL25.

Expressioni

Gene expression databases

BgeeiQ9JL25.
CleanExiMM_RGS1.
ExpressionAtlasiQ9JL25. baseline and differential.
GenevisibleiQ9JL25. MM.

Interactioni

Protein-protein interaction databases

IntActiQ9JL25. 3 interactions.
MINTiMINT-1572075.
STRINGi10090.ENSMUSP00000130339.

Structurei

3D structure databases

ProteinModelPortaliQ9JL25.
SMRiQ9JL25. Positions 71-204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 200116RGSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG312555.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiQ9JL25.
KOiK16449.
OMAiKIYKAFV.
OrthoDBiEOG7VHSZ5.
PhylomeDBiQ9JL25.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR016137. RGS.
IPR030409. RGS1.
IPR024066. RGS_subdom1.
[Graphical view]
PANTHERiPTHR10845:SF34. PTHR10845:SF34. 1 hit.
PfamiPF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
PROSITEiPS50132. RGS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JL25-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRAAAISMPR LNKMPGMFFS ASPKDSKEHS HSLLDDKKQK KRPKTFGMDV
60 70 80 90 100
KTYLRSMIPH LESGMKSAKS KDILSAEEVM QWSQSLEKLL ANQTGQNVFG
110 120 130 140 150
RFLKSEFSEE NIEFWLACED YKKTETDLLH NKAENIYKAF VHSDAVKQIN
160 170 180 190 200
IDFHTRESTA KKIKTPTPTS FDEAQKVIYS LMEKDSYPRF LKSNIYLNLL

NDLQANTLK
Length:209
Mass (Da):24,107
Last modified:March 24, 2009 - v2
Checksum:iF483A1690A3E2EB0
GO
Isoform 2 (identifier: Q9JL25-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Show »
Length:162
Mass (Da):18,792
Checksum:iA80EC6C3E35287DD
GO

Sequence cautioni

The sequence AAF34624.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH28634.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE23749.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE32557.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE41748.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE42139.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121N → D in BAE42139 (PubMed:16141072).Curated
Sequence conflicti12 – 121N → D in BAE32557 (PubMed:16141072).Curated
Sequence conflicti73 – 731I → M in BAE42139 (PubMed:16141072).Curated
Sequence conflicti73 – 731I → M in BAE32557 (PubMed:16141072).Curated
Sequence conflicti73 – 731I → M in BAE42382 (PubMed:16141072).Curated
Sequence conflicti101 – 1011R → K in BAE42139 (PubMed:16141072).Curated
Sequence conflicti101 – 1011R → K in BAE32557 (PubMed:16141072).Curated
Sequence conflicti101 – 1011R → K in BAE42382 (PubMed:16141072).Curated
Sequence conflicti121 – 1211Y → C in BAE32557 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 2. 1 PublicationVSP_036732Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138688 mRNA. Translation: BAE23749.1. Different initiation.
AK154394 mRNA. Translation: BAE32557.1. Different initiation.
AK170366 mRNA. Translation: BAE41748.1. Different initiation.
AK170957 mRNA. Translation: BAE42139.1. Different initiation.
AK171306 mRNA. Translation: BAE42382.1.
AF215667 mRNA. Translation: AAF34624.1. Different initiation.
BC028634 mRNA. Translation: AAH28634.1. Different initiation.
CCDSiCCDS15349.2. [Q9JL25-1]
RefSeqiNP_056626.2. NM_015811.2. [Q9JL25-1]
UniGeneiMm.103701.

Genome annotation databases

EnsembliENSMUST00000189061; ENSMUSP00000140624; ENSMUSG00000026358. [Q9JL25-1]
GeneIDi50778.
KEGGimmu:50778.
UCSCiuc007cxj.2. mouse. [Q9JL25-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138688 mRNA. Translation: BAE23749.1. Different initiation.
AK154394 mRNA. Translation: BAE32557.1. Different initiation.
AK170366 mRNA. Translation: BAE41748.1. Different initiation.
AK170957 mRNA. Translation: BAE42139.1. Different initiation.
AK171306 mRNA. Translation: BAE42382.1.
AF215667 mRNA. Translation: AAF34624.1. Different initiation.
BC028634 mRNA. Translation: AAH28634.1. Different initiation.
CCDSiCCDS15349.2. [Q9JL25-1]
RefSeqiNP_056626.2. NM_015811.2. [Q9JL25-1]
UniGeneiMm.103701.

3D structure databases

ProteinModelPortaliQ9JL25.
SMRiQ9JL25. Positions 71-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JL25. 3 interactions.
MINTiMINT-1572075.
STRINGi10090.ENSMUSP00000130339.

PTM databases

PhosphoSiteiQ9JL25.

Proteomic databases

PRIDEiQ9JL25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000189061; ENSMUSP00000140624; ENSMUSG00000026358. [Q9JL25-1]
GeneIDi50778.
KEGGimmu:50778.
UCSCiuc007cxj.2. mouse. [Q9JL25-1]

Organism-specific databases

CTDi5996.
MGIiMGI:1354694. Rgs1.

Phylogenomic databases

eggNOGiNOG312555.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiQ9JL25.
KOiK16449.
OMAiKIYKAFV.
OrthoDBiEOG7VHSZ5.
PhylomeDBiQ9JL25.
TreeFamiTF315837.

Enzyme and pathway databases

ReactomeiREACT_331048. G alpha (i) signalling events.

Miscellaneous databases

ChiTaRSiRgs1. mouse.
NextBioi307717.
PROiQ9JL25.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JL25.
CleanExiMM_RGS1.
ExpressionAtlasiQ9JL25. baseline and differential.
GenevisibleiQ9JL25. MM.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR016137. RGS.
IPR030409. RGS1.
IPR024066. RGS_subdom1.
[Graphical view]
PANTHERiPTHR10845:SF34. PTHR10845:SF34. 1 hit.
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. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Thymus.
  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] OF 2-209 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Lymph node.
  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] OF 2-209 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Thymus.

Entry informationi

Entry nameiRGS1_MOUSE
AccessioniPrimary (citable) accession number: Q9JL25
Secondary accession number(s): Q3TBD1
, Q3TC18, Q3TD56, Q3U477
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: March 24, 2009
Last modified: June 24, 2015
This is version 103 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.