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Q61017

- GBGT2_MOUSE

UniProt

Q61017 - GBGT2_MOUSE

Protein

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2

Gene

Gngt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
  1. Functioni

    Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

    GO - Molecular functioni

    1. GTPase activity Source: Ensembl
    2. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Transducer

    Enzyme and pathway databases

    ReactomeiREACT_208837. Activation of G protein gated Potassium channels.
    REACT_213947. Regulation of water balance by renal Aquaporins.
    REACT_221970. Ca2+ pathway.
    REACT_226457. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2
    Alternative name(s):
    G gamma-C
    G-gamma-8
    Gene namesi
    Name:Gngt2
    Synonyms:Gng8, Gngt8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:893584. Gngt2.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

    GO - Cellular componenti

    1. heterotrimeric G-protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6666Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2PRO_0000012647Add
    BLAST
    Propeptidei67 – 693Removed in mature formBy similarityPRO_0000012648

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661Cysteine methyl esterBy similarity
    Lipidationi66 – 661S-farnesyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiQ61017.
    PRIDEiQ61017.

    Expressioni

    Gene expression databases

    ArrayExpressiQ61017.
    BgeeiQ61017.
    GenevestigatoriQ61017.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units, alpha, beta and gamma.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61017.
    SMRiQ61017. Positions 5-62.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G protein gamma family.Curated

    Phylogenomic databases

    eggNOGiNOG304504.
    GeneTreeiENSGT00530000063397.
    HOGENOMiHOG000231034.
    HOVERGENiHBG014983.
    InParanoidiQ61017.
    KOiK04549.
    OMAiMISKTGK.
    OrthoDBiEOG7H1JP7.
    PhylomeDBiQ61017.
    TreeFamiTF319909.

    Family and domain databases

    Gene3Di4.10.260.10. 1 hit.
    InterProiIPR015898. G-protein_gamma-like_dom.
    IPR001770. Gprotein-gamma.
    [Graphical view]
    PANTHERiPTHR13809. PTHR13809. 1 hit.
    PfamiPF00631. G-gamma. 1 hit.
    [Graphical view]
    PRINTSiPR00321. GPROTEING.
    SMARTiSM00224. GGL. 1 hit.
    [Graphical view]
    SUPFAMiSSF48670. SSF48670. 1 hit.
    PROSITEiPS50058. G_PROTEIN_GAMMA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q61017-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQDLSEKEL LRMEVEQLKK EVKNPRDLIS KTGKEIKDYV EAQAGTDPLL   50
    KGIPEDKNPF KEKGTCVLS 69
    Length:69
    Mass (Da):7,802
    Last modified:September 27, 2004 - v2
    Checksum:i80A9586CD56BB304
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010554 mRNA. Translation: BAB27023.1.
    U38500 mRNA. Translation: AAB01731.1.
    CCDSiCCDS25284.1.
    RefSeqiNP_001033753.2. NM_001038664.2.
    NP_001271322.1. NM_001284393.1.
    NP_001271326.1. NM_001284397.1.
    NP_075610.1. NM_023121.2.
    XP_006532293.1. XM_006532230.1.
    XP_006532294.1. XM_006532231.1.
    UniGeneiMm.46299.

    Genome annotation databases

    EnsembliENSMUST00000036088; ENSMUSP00000047586; ENSMUSG00000038811.
    ENSMUST00000100532; ENSMUSP00000098101; ENSMUSG00000038811.
    ENSMUST00000107708; ENSMUSP00000103336; ENSMUSG00000038811.
    ENSMUST00000107709; ENSMUSP00000103337; ENSMUSG00000038811.
    ENSMUST00000107711; ENSMUSP00000103339; ENSMUSG00000038811.
    ENSMUST00000107712; ENSMUSP00000103340; ENSMUSG00000038811.
    ENSMUST00000107714; ENSMUSP00000103342; ENSMUSG00000038811.
    GeneIDi14710.
    KEGGimmu:14710.
    UCSCiuc007lau.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010554 mRNA. Translation: BAB27023.1 .
    U38500 mRNA. Translation: AAB01731.1 .
    CCDSi CCDS25284.1.
    RefSeqi NP_001033753.2. NM_001038664.2.
    NP_001271322.1. NM_001284393.1.
    NP_001271326.1. NM_001284397.1.
    NP_075610.1. NM_023121.2.
    XP_006532293.1. XM_006532230.1.
    XP_006532294.1. XM_006532231.1.
    UniGenei Mm.46299.

    3D structure databases

    ProteinModelPortali Q61017.
    SMRi Q61017. Positions 5-62.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    MaxQBi Q61017.
    PRIDEi Q61017.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000036088 ; ENSMUSP00000047586 ; ENSMUSG00000038811 .
    ENSMUST00000100532 ; ENSMUSP00000098101 ; ENSMUSG00000038811 .
    ENSMUST00000107708 ; ENSMUSP00000103336 ; ENSMUSG00000038811 .
    ENSMUST00000107709 ; ENSMUSP00000103337 ; ENSMUSG00000038811 .
    ENSMUST00000107711 ; ENSMUSP00000103339 ; ENSMUSG00000038811 .
    ENSMUST00000107712 ; ENSMUSP00000103340 ; ENSMUSG00000038811 .
    ENSMUST00000107714 ; ENSMUSP00000103342 ; ENSMUSG00000038811 .
    GeneIDi 14710.
    KEGGi mmu:14710.
    UCSCi uc007lau.1. mouse.

    Organism-specific databases

    CTDi 2793.
    MGIi MGI:893584. Gngt2.

    Phylogenomic databases

    eggNOGi NOG304504.
    GeneTreei ENSGT00530000063397.
    HOGENOMi HOG000231034.
    HOVERGENi HBG014983.
    InParanoidi Q61017.
    KOi K04549.
    OMAi MISKTGK.
    OrthoDBi EOG7H1JP7.
    PhylomeDBi Q61017.
    TreeFami TF319909.

    Enzyme and pathway databases

    Reactomei REACT_208837. Activation of G protein gated Potassium channels.
    REACT_213947. Regulation of water balance by renal Aquaporins.
    REACT_221970. Ca2+ pathway.
    REACT_226457. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.

    Miscellaneous databases

    NextBioi 286705.
    PROi Q61017.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61017.
    Bgeei Q61017.
    Genevestigatori Q61017.

    Family and domain databases

    Gene3Di 4.10.260.10. 1 hit.
    InterProi IPR015898. G-protein_gamma-like_dom.
    IPR001770. Gprotein-gamma.
    [Graphical view ]
    PANTHERi PTHR13809. PTHR13809. 1 hit.
    Pfami PF00631. G-gamma. 1 hit.
    [Graphical view ]
    PRINTSi PR00321. GPROTEING.
    SMARTi SM00224. GGL. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48670. SSF48670. 1 hit.
    PROSITEi PS50058. G_PROTEIN_GAMMA. 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].
      Strain: C57BL/6J.
    2. "G protein gene expression during mouse oocyte growth and maturation, and preimplantation embryo development."
      Williams C.J., Schultz R.M., Kopf G.S.
      Mol. Reprod. Dev. 44:315-323(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-54.
      Strain: CF-1 / Harlan.
      Tissue: Retina.

    Entry informationi

    Entry nameiGBGT2_MOUSE
    AccessioniPrimary (citable) accession number: Q61017
    Secondary accession number(s): Q9CWL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 110 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