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Q9JL25 (RGS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 1

Short name=RGS1
Gene names
Name:Rgs1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length209 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.

Post-translational modification

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

Sequence similarities

Contains 1 RGS domain.

Sequence caution

The sequence AAF34624.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH28634.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE23749.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE32557.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE41748.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE42139.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JL25-1)

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.
Isoform 2 (identifier: Q9JL25-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Regulator of G-protein signaling 1
PRO_0000204176

Regions

Domain85 – 200116RGS

Amino acid modifications

Modified residue321Phosphoserine; by CK2 Potential
Modified residue671Phosphoserine; by PKC Potential
Modified residue751Phosphoserine; by CK2 Potential
Modified residue1591Phosphothreonine; by PKC Potential
Modified residue1691Phosphothreonine; by CK2 Potential
Modified residue1801Phosphoserine; by CK2 Potential
Modified residue2071Phosphothreonine; by PKC Potential

Natural variations

Alternative sequence1 – 4747Missing in isoform 2.
VSP_036732

Experimental info

Sequence conflict121N → D in BAE42139. Ref.1
Sequence conflict121N → D in BAE32557. Ref.1
Sequence conflict731I → M in BAE42139. Ref.1
Sequence conflict731I → M in BAE32557. Ref.1
Sequence conflict731I → M in BAE42382. Ref.1
Sequence conflict1011R → K in BAE42139. Ref.1
Sequence conflict1011R → K in BAE32557. Ref.1
Sequence conflict1011R → K in BAE42382. Ref.1
Sequence conflict1211Y → C in BAE32557. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: F483A1690A3E2EB0

FASTA20924,107
        10         20         30         40         50         60 
MRAAAISMPR LNKMPGMFFS ASPKDSKEHS HSLLDDKKQK KRPKTFGMDV KTYLRSMIPH 

        70         80         90        100        110        120 
LESGMKSAKS KDILSAEEVM QWSQSLEKLL ANQTGQNVFG RFLKSEFSEE NIEFWLACED 

       130        140        150        160        170        180 
YKKTETDLLH NKAENIYKAF VHSDAVKQIN IDFHTRESTA KKIKTPTPTS FDEAQKVIYS 

       190        200 
LMEKDSYPRF LKSNIYLNLL NDLQANTLK 

« Hide

Isoform 2 [UniParc].

Checksum: A80EC6C3E35287DD
Show »

FASTA16218,792

References

« Hide 'large scale' references
[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. 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] (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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS15349.2. [Q9JL25-1]
RefSeqNP_056626.2. NM_015811.2. [Q9JL25-1]
UniGeneMm.103701.

3D structure databases

ProteinModelPortalQ9JL25.
SMRQ9JL25. Positions 71-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JL25. 3 interactions.
MINTMINT-1572075.

PTM databases

PhosphoSiteQ9JL25.

Proteomic databases

PRIDEQ9JL25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000172388; ENSMUSP00000130339; ENSMUSG00000026358. [Q9JL25-1]
GeneID50778.
KEGGmmu:50778.
UCSCuc007cxj.2. mouse. [Q9JL25-1]

Organism-specific databases

CTD5996.
MGIMGI:1354694. Rgs1.

Phylogenomic databases

eggNOGNOG312555.
GeneTreeENSGT00750000117371.
HOGENOMHOG000233512.
HOVERGENHBG013233.
InParanoidQ3U477.
KOK16449.
OMAEVIQWSQ.
OrthoDBEOG7VHSZ5.
PhylomeDBQ9JL25.
TreeFamTF315837.

Gene expression databases

ArrayExpressQ9JL25.
BgeeQ9JL25.
CleanExMM_RGS1.
GenevestigatorQ9JL25.

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

ChiTaRSRGS1. mouse.
NextBio307717.
PROQ9JL25.
SOURCESearch...

Entry information

Entry nameRGS1_MOUSE
AccessionPrimary (citable) accession number: Q9JL25
Secondary accession number(s): Q3TBD1 expand/collapse secondary AC list , Q3TC18, Q3TD56, Q3U477
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: March 24, 2009
Last modified: July 9, 2014
This is version 96 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