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Q9JL25

- RGS1_MOUSE

UniProt

Q9JL25 - RGS1_MOUSE

Protein

Regulator of G-protein signaling 1

Gene

Rgs1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (24 Mar 2009)
      Previous versions | rss
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    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

    1. GTPase activator activity Source: RefGenome

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: MGI
    2. positive regulation of GTPase activity Source: GOC
    3. termination of G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Signal transduction inhibitor

    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: Chromosome 1

    Organism-specific databases

    MGIiMGI:1354694. Rgs1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. plasma membrane Source: RefGenome

    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

    ArrayExpressiQ9JL25.
    BgeeiQ9JL25.
    CleanExiMM_RGS1.
    GenevestigatoriQ9JL25.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9JL25. 3 interactions.
    MINTiMINT-1572075.

    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.
    GeneTreeiENSGT00750000117371.
    HOGENOMiHOG000233512.
    HOVERGENiHBG013233.
    InParanoidiQ3U477.
    KOiK16449.
    OMAiEVIQWSQ.
    OrthoDBiEOG7VHSZ5.
    PhylomeDBiQ9JL25.
    TreeFamiTF315837.

    Family and domain databases

    Gene3Di1.10.196.10. 2 hits.
    InterProiIPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    [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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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

    MRAAAISMPR LNKMPGMFFS ASPKDSKEHS HSLLDDKKQK KRPKTFGMDV    50
    KTYLRSMIPH LESGMKSAKS KDILSAEEVM QWSQSLEKLL ANQTGQNVFG 100
    RFLKSEFSEE NIEFWLACED YKKTETDLLH NKAENIYKAF VHSDAVKQIN 150
    IDFHTRESTA KKIKTPTPTS FDEAQKVIYS LMEKDSYPRF LKSNIYLNLL 200
    NDLQANTLK 209
    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.
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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

    EnsembliENSMUST00000172388; ENSMUSP00000130339; 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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS15349.2. [Q9JL25-1 ]
    RefSeqi NP_056626.2. NM_015811.2. [Q9JL25-1 ]
    UniGenei Mm.103701.

    3D structure databases

    ProteinModelPortali Q9JL25.
    SMRi Q9JL25. Positions 71-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JL25. 3 interactions.
    MINTi MINT-1572075.

    PTM databases

    PhosphoSitei Q9JL25.

    Proteomic databases

    PRIDEi Q9JL25.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000172388 ; ENSMUSP00000130339 ; ENSMUSG00000026358 . [Q9JL25-1 ]
    GeneIDi 50778.
    KEGGi mmu:50778.
    UCSCi uc007cxj.2. mouse. [Q9JL25-1 ]

    Organism-specific databases

    CTDi 5996.
    MGIi MGI:1354694. Rgs1.

    Phylogenomic databases

    eggNOGi NOG312555.
    GeneTreei ENSGT00750000117371.
    HOGENOMi HOG000233512.
    HOVERGENi HBG013233.
    InParanoidi Q3U477.
    KOi K16449.
    OMAi EVIQWSQ.
    OrthoDBi EOG7VHSZ5.
    PhylomeDBi Q9JL25.
    TreeFami TF315837.

    Miscellaneous databases

    ChiTaRSi RGS1. mouse.
    NextBioi 307717.
    PROi Q9JL25.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JL25.
    Bgeei Q9JL25.
    CleanExi MM_RGS1.
    Genevestigatori Q9JL25.

    Family and domain databases

    Gene3Di 1.10.196.10. 2 hits.
    InterProi IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    [Graphical view ]
    Pfami PF00615. RGS. 1 hit.
    [Graphical view ]
    PRINTSi PR01301. RGSPROTEIN.
    SMARTi SM00315. RGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    PROSITEi PS50132. RGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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] (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: October 1, 2014
    This is version 97 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