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P63218

- GBG5_HUMAN

UniProt

P63218 - GBG5_HUMAN

Protein

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5

Gene

GNG5

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.

    GO - Molecular functioni

    1. GTPase activity Source: UniProtKB
    2. PDZ domain binding Source: MGI
    3. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to glucagon stimulus Source: Reactome
    2. energy reserve metabolic process Source: Reactome
    3. G-protein coupled receptor signaling pathway Source: UniProtKB
    4. GTP catabolic process Source: GOC
    5. signal transduction Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
    Gene namesi
    Name:GNG5
    Synonyms:GNGT5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4408. GNG5.

    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: UniProtKB
    3. membrane Source: UniProtKB
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28787.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 6564Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5PRO_0000012627Add
    BLAST
    Propeptidei66 – 683Removed in mature formBy similarityPRO_0000012628

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei65 – 651Cysteine methyl esterBy similarity
    Lipidationi65 – 651S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP63218.
    PaxDbiP63218.
    PRIDEiP63218.

    PTM databases

    PhosphoSiteiP63218.

    Expressioni

    Gene expression databases

    BgeeiP63218.
    CleanExiHS_GNG5.
    GenevestigatoriP63218.

    Organism-specific databases

    HPAiCAB032623.
    HPA043651.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi109049. 7 interactions.
    STRINGi9606.ENSP00000359675.

    Structurei

    3D structure databases

    ProteinModelPortaliP63218.
    SMRiP63218. Positions 6-59.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G protein gamma family.Curated

    Phylogenomic databases

    eggNOGiNOG309295.
    HOVERGENiHBG014983.
    InParanoidiP63218.
    KOiK04542.
    OMAiFFNAIET.
    OrthoDBiEOG7H1JP7.
    PhylomeDBiP63218.
    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.

    P63218-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGSSSVAAM KKVVQQLRLE AGLNRVKVSQ AAADLKQFCL QNAQHDPLLT   50
    GVSSSTNPFR PQKVCSFL 68
    Length:68
    Mass (Da):7,318
    Last modified:January 23, 2007 - v3
    Checksum:i9AF7A16558863602
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF085709, AF085708 Genomic DNA. Translation: AAC72203.1.
    AF038955 mRNA. Translation: AAC39869.1.
    AF493873 mRNA. Translation: AAM12587.1.
    BT006823 mRNA. Translation: AAP35469.1.
    AK312111 mRNA. Translation: BAG35047.1.
    AL359762 Genomic DNA. Translation: CAH70203.1.
    CH471097 Genomic DNA. Translation: EAW73236.1.
    BC003563 mRNA. Translation: AAH03563.1.
    CCDSiCCDS696.1.
    RefSeqiNP_005265.1. NM_005274.2.
    UniGeneiHs.645427.

    Genome annotation databases

    EnsembliENST00000370641; ENSP00000359675; ENSG00000174021.
    ENST00000370645; ENSP00000359679; ENSG00000174021.
    GeneIDi2787.
    KEGGihsa:2787.
    UCSCiuc001djw.4. human.

    Polymorphism databases

    DMDMi52783599.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF085709 , AF085708 Genomic DNA. Translation: AAC72203.1 .
    AF038955 mRNA. Translation: AAC39869.1 .
    AF493873 mRNA. Translation: AAM12587.1 .
    BT006823 mRNA. Translation: AAP35469.1 .
    AK312111 mRNA. Translation: BAG35047.1 .
    AL359762 Genomic DNA. Translation: CAH70203.1 .
    CH471097 Genomic DNA. Translation: EAW73236.1 .
    BC003563 mRNA. Translation: AAH03563.1 .
    CCDSi CCDS696.1.
    RefSeqi NP_005265.1. NM_005274.2.
    UniGenei Hs.645427.

    3D structure databases

    ProteinModelPortali P63218.
    SMRi P63218. Positions 6-59.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109049. 7 interactions.
    STRINGi 9606.ENSP00000359675.

    PTM databases

    PhosphoSitei P63218.

    Polymorphism databases

    DMDMi 52783599.

    Proteomic databases

    MaxQBi P63218.
    PaxDbi P63218.
    PRIDEi P63218.

    Protocols and materials databases

    DNASUi 2787.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370641 ; ENSP00000359675 ; ENSG00000174021 .
    ENST00000370645 ; ENSP00000359679 ; ENSG00000174021 .
    GeneIDi 2787.
    KEGGi hsa:2787.
    UCSCi uc001djw.4. human.

    Organism-specific databases

    CTDi 2787.
    GeneCardsi GC01M084964.
    HGNCi HGNC:4408. GNG5.
    HPAi CAB032623.
    HPA043651.
    MIMi 600874. gene.
    neXtProti NX_P63218.
    PharmGKBi PA28787.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309295.
    HOVERGENi HBG014983.
    InParanoidi P63218.
    KOi K04542.
    OMAi FFNAIET.
    OrthoDBi EOG7H1JP7.
    PhylomeDBi P63218.
    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.

    Miscellaneous databases

    GeneWikii GNG5.
    GenomeRNAii 2787.
    NextBioi 10983.
    PROi P63218.
    SOURCEi Search...

    Gene expression databases

    Bgeei P63218.
    CleanExi HS_GNG5.
    Genevestigatori P63218.

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
      Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
      Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    3. "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].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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.
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18, ACETYLATION AT SER-2.
      Tissue: Platelet.
    10. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGBG5_HUMAN
    AccessioniPrimary (citable) accession number: P63218
    Secondary accession number(s): B2R5A0
    , P30670, Q5VX54, Q61015
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 98 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3