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P59768

- GBG2_HUMAN

UniProt

P59768 - GBG2_HUMAN

Protein

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Gene

GNG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  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 By similarity.By similarity

    GO - Molecular functioni

    1. G-protein beta-subunit binding Source: UniProt
    2. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. adenylate cyclase-activating dopamine receptor signaling pathway Source: BHF-UCL
    2. blood coagulation Source: Reactome
    3. cell proliferation Source: Ensembl
    4. cellular response to catecholamine stimulus Source: BHF-UCL
    5. cellular response to glucagon stimulus Source: Reactome
    6. cellular response to prostaglandin E stimulus Source: BHF-UCL
    7. energy reserve metabolic process Source: Reactome
    8. platelet activation Source: Reactome
    9. small molecule metabolic process Source: Reactome
    10. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Transducer

    Enzyme and pathway databases

    ReactomeiREACT_15457. G-protein activation.
    REACT_1665. Glucagon signaling in metabolic regulation.
    REACT_172761. Ca2+ pathway.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18283. G alpha (q) signalling events.
    REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.
    REACT_18377. Glucagon-type ligand receptors.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19140. ADP signalling through P2Y purinoceptor 1.
    REACT_19145. G beta:gamma signalling through PLC beta.
    REACT_19231. G alpha (i) signalling events.
    REACT_19290. G beta:gamma signalling through PI3Kgamma.
    REACT_19327. G alpha (s) signalling events.
    REACT_19333. G alpha (z) signalling events.
    REACT_20647. Thromboxane signalling through TP receptor.
    REACT_20653. ADP signalling through P2Y purinoceptor 12.
    REACT_21254. Presynaptic function of Kainate receptors.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_23946. Prostacyclin signalling through prostacyclin receptor.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
    REACT_75831. Activation of G protein gated Potassium channels.
    SignaLinkiP59768.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
    Alternative name(s):
    G gamma-I
    Gene namesi
    Name:GNG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:4404. GNG2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. heterotrimeric G-protein complex Source: BHF-UCL
    3. membrane Source: BHF-UCL
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28784.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 6867Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2PRO_0000012611Add
    BLAST
    Propeptidei69 – 713Removed in mature formBy similarityPRO_0000012612

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei68 – 681Cysteine methyl esterBy similarity
    Lipidationi68 – 681S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP59768.
    PaxDbiP59768.
    PeptideAtlasiP59768.
    PRIDEiP59768.

    PTM databases

    PhosphoSiteiP59768.

    Expressioni

    Tissue specificityi

    Expressed in fetal tissues, including testis, adrenal gland, brain, white blood cells and brain.1 Publication

    Gene expression databases

    ArrayExpressiP59768.
    BgeeiP59768.
    CleanExiHS_GNG2.
    GenevestigatoriP59768.

    Organism-specific databases

    HPAiCAB018380.
    HPA003534.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units, alpha, beta and gamma By similarity. The heterodimer formed by GNB1 and GNG2 interacts with PTH1R (via C-terminus).By similarity

    Protein-protein interaction databases

    BioGridi119933. 18 interactions.
    DIPiDIP-33949N.
    IntActiP59768. 2 interactions.
    MINTiMINT-8189453.
    STRINGi9606.ENSP00000334448.

    Structurei

    Secondary structure

    1
    71
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 2315
    Helixi30 – 4415
    Helixi45 – 473
    Turni49 – 513
    Turni56 – 583
    Beta strandi60 – 623
    Turni63 – 664

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4KFMX-ray3.45G1-68[»]
    ProteinModelPortaliP59768.
    SMRiP59768. Positions 8-64.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP59768.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G protein gamma family.Curated

    Phylogenomic databases

    eggNOGiNOG298292.
    HOVERGENiHBG014983.
    InParanoidiP59768.
    KOiK07826.
    PhylomeDBiP59768.
    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.

    P59768-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL   50
    LTPVPASENP FREKKFFCAI L 71
    Length:71
    Mass (Da):7,850
    Last modified:January 23, 2007 - v2
    Checksum:iEDB74E4135E7A37A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF493870 mRNA. Translation: AAM12584.1.
    AL832878 mRNA. Translation: CAI46198.1.
    CH471078 Genomic DNA. Translation: EAW65663.1.
    BC020774 mRNA. Translation: AAH20774.1.
    BC060856 mRNA. Translation: AAH60856.1.
    CCDSiCCDS32082.1.
    PIRiJC7290. GNG2.
    RefSeqiNP_001230702.1. NM_001243773.1.
    NP_001230703.1. NM_001243774.1.
    NP_444292.1. NM_053064.4.
    XP_006720236.1. XM_006720173.1.
    UniGeneiHs.187772.
    Hs.709082.
    Hs.723399.
    Hs.741081.

    Genome annotation databases

    EnsembliENST00000335281; ENSP00000334448; ENSG00000186469.
    ENST00000554736; ENSP00000452014; ENSG00000186469.
    ENST00000555472; ENSP00000451102; ENSG00000186469.
    ENST00000556752; ENSP00000451576; ENSG00000186469.
    ENST00000556766; ENSP00000451231; ENSG00000186469.
    GeneIDi54331.
    KEGGihsa:54331.
    UCSCiuc001wzi.3. human.

    Polymorphism databases

    DMDMi32699499.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF493870 mRNA. Translation: AAM12584.1 .
    AL832878 mRNA. Translation: CAI46198.1 .
    CH471078 Genomic DNA. Translation: EAW65663.1 .
    BC020774 mRNA. Translation: AAH20774.1 .
    BC060856 mRNA. Translation: AAH60856.1 .
    CCDSi CCDS32082.1.
    PIRi JC7290. GNG2.
    RefSeqi NP_001230702.1. NM_001243773.1.
    NP_001230703.1. NM_001243774.1.
    NP_444292.1. NM_053064.4.
    XP_006720236.1. XM_006720173.1.
    UniGenei Hs.187772.
    Hs.709082.
    Hs.723399.
    Hs.741081.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4KFM X-ray 3.45 G 1-68 [» ]
    ProteinModelPortali P59768.
    SMRi P59768. Positions 8-64.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119933. 18 interactions.
    DIPi DIP-33949N.
    IntActi P59768. 2 interactions.
    MINTi MINT-8189453.
    STRINGi 9606.ENSP00000334448.

    Chemistry

    DrugBanki DB01159. Halothane.

    PTM databases

    PhosphoSitei P59768.

    Polymorphism databases

    DMDMi 32699499.

    Proteomic databases

    MaxQBi P59768.
    PaxDbi P59768.
    PeptideAtlasi P59768.
    PRIDEi P59768.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335281 ; ENSP00000334448 ; ENSG00000186469 .
    ENST00000554736 ; ENSP00000452014 ; ENSG00000186469 .
    ENST00000555472 ; ENSP00000451102 ; ENSG00000186469 .
    ENST00000556752 ; ENSP00000451576 ; ENSG00000186469 .
    ENST00000556766 ; ENSP00000451231 ; ENSG00000186469 .
    GeneIDi 54331.
    KEGGi hsa:54331.
    UCSCi uc001wzi.3. human.

    Organism-specific databases

    CTDi 54331.
    GeneCardsi GC14P052327.
    HGNCi HGNC:4404. GNG2.
    HPAi CAB018380.
    HPA003534.
    MIMi 606981. gene.
    neXtProti NX_P59768.
    PharmGKBi PA28784.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298292.
    HOVERGENi HBG014983.
    InParanoidi P59768.
    KOi K07826.
    PhylomeDBi P59768.
    TreeFami TF319909.

    Enzyme and pathway databases

    Reactomei REACT_15457. G-protein activation.
    REACT_1665. Glucagon signaling in metabolic regulation.
    REACT_172761. Ca2+ pathway.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18283. G alpha (q) signalling events.
    REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.
    REACT_18377. Glucagon-type ligand receptors.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19140. ADP signalling through P2Y purinoceptor 1.
    REACT_19145. G beta:gamma signalling through PLC beta.
    REACT_19231. G alpha (i) signalling events.
    REACT_19290. G beta:gamma signalling through PI3Kgamma.
    REACT_19327. G alpha (s) signalling events.
    REACT_19333. G alpha (z) signalling events.
    REACT_20647. Thromboxane signalling through TP receptor.
    REACT_20653. ADP signalling through P2Y purinoceptor 12.
    REACT_21254. Presynaptic function of Kainate receptors.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_23946. Prostacyclin signalling through prostacyclin receptor.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
    REACT_75831. Activation of G protein gated Potassium channels.
    SignaLinki P59768.

    Miscellaneous databases

    EvolutionaryTracei P59768.
    GeneWikii GNG2.
    GenomeRNAii 54331.
    NextBioi 56571.
    PROi P59768.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P59768.
    Bgeei P59768.
    CleanExi HS_GNG2.
    Genevestigatori P59768.

    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. "Cloning, characterization, and mapping of the gene encoding the human G protein gamma 2 subunit."
      Modarressi M.H., Taylor K.E., Wolfe J.
      Biochem. Biophys. Res. Commun. 272:610-615(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lymph node.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Brain and Skin.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2."
      Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.
      Structure 16:1086-1094(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEXES WITH GNB1 AND PTH1R.
    9. Cited for: RETRACTION.

    Entry informationi

    Entry nameiGBG2_HUMAN
    AccessioniPrimary (citable) accession number: P59768
    Secondary accession number(s): Q5JPE2, Q6P9A9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3