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Protein

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

Gene

GNG5

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

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. signal transduction Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
  6. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiREACT_15457. G-protein activation.
REACT_1665. Glucagon signaling in metabolic regulation.
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. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_263982. Ca2+ pathway.
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 Componenti: 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: UniProtKB
  2. heterotrimeric G-protein complex Source: UniProtKB
  3. membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

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. 22 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.
GeneTreeiENSGT00760000119218.
HOVERGENiHBG014983.
InParanoidiP63218.
KOiK04542.
OMAiADLQQFC.
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

        10         20         30         40         50
MSGSSSVAAM KKVVQQLRLE AGLNRVKVSQ AAADLKQFCL QNAQHDPLLT
60
GVSSSTNPFR PQKVCSFL
Length:68
Mass (Da):7,318
Last modified:January 22, 2007 - v3
Checksum:i9AF7A16558863602
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi109049. 22 interactions.
STRINGi9606.ENSP00000359675.

PTM databases

PhosphoSiteiP63218.

Polymorphism databases

DMDMi52783599.

Proteomic databases

MaxQBiP63218.
PaxDbiP63218.
PRIDEiP63218.

Protocols and materials databases

DNASUi2787.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2787.
GeneCardsiGC01M084964.
HGNCiHGNC:4408. GNG5.
HPAiCAB032623.
HPA043651.
MIMi600874. gene.
neXtProtiNX_P63218.
PharmGKBiPA28787.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG309295.
GeneTreeiENSGT00760000119218.
HOVERGENiHBG014983.
InParanoidiP63218.
KOiK04542.
OMAiADLQQFC.
OrthoDBiEOG7H1JP7.
PhylomeDBiP63218.
TreeFamiTF319909.

Enzyme and pathway databases

ReactomeiREACT_15457. G-protein activation.
REACT_1665. Glucagon signaling in metabolic regulation.
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. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_263982. Ca2+ pathway.
REACT_75831. Activation of G protein gated Potassium channels.

Miscellaneous databases

GeneWikiiGNG5.
GenomeRNAii2787.
NextBioi10983.
PROiP63218.
SOURCEiSearch...

Gene expression databases

BgeeiP63218.
CleanExiHS_GNG5.
GenevestigatoriP63218.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [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 (FEB-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 (APR-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(2003) [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(2005) [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(2003) [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(2002) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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(2010) [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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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 26, 2004
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 104 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.