Full text data of GNG5
GNG5
(GNGT5)
[Confidence: high (present in two of the MS resources)]
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5; Flags: Precursor
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5; Flags: Precursor
hRBCD
IPI00000060
IPI00000060 Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-5 (like) subunit Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-5 (like) subunit membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 n/a 1 n/a n/a n/a n/a n/a n/a inner surface of plasma membrane n/a found at its expected molecular weight found at molecular weight
IPI00000060 Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-5 (like) subunit Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-5 (like) subunit membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 1 n/a 1 n/a n/a n/a n/a n/a n/a inner surface of plasma membrane n/a found at its expected molecular weight found at molecular weight
UniProt
P63218
ID GBG5_HUMAN Reviewed; 68 AA.
AC P63218; B2R5A0; P30670; Q5VX54; Q61015;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;
DE Flags: Precursor;
GN Name=GNG5; Synonyms=GNGT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9790912; DOI=10.1006/bbrc.1998.9439;
RA Liu B., Aronson N.N. Jr.;
RT "Structure of human G protein Ggamma5 gene GNG5.";
RL Biochem. Biophys. Res. Commun. 251:88-94(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-
RT length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-18, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC involved as a modulator or transducer in various transmembrane
CC signaling systems. The beta and gamma chains are required for the
CC GTPase activity, for replacement of GDP by GTP, and for G protein-
CC effector interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC gamma.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential).
CC -!- SIMILARITY: Belongs to the G protein gamma family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF085709; AAC72203.1; -; Genomic_DNA.
DR EMBL; AF085708; AAC72203.1; JOINED; Genomic_DNA.
DR EMBL; AF038955; AAC39869.1; -; mRNA.
DR EMBL; AF493873; AAM12587.1; -; mRNA.
DR EMBL; BT006823; AAP35469.1; -; mRNA.
DR EMBL; AK312111; BAG35047.1; -; mRNA.
DR EMBL; AL359762; CAH70203.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73236.1; -; Genomic_DNA.
DR EMBL; BC003563; AAH03563.1; -; mRNA.
DR RefSeq; NP_005265.1; NM_005274.2.
DR UniGene; Hs.645427; -.
DR ProteinModelPortal; P63218; -.
DR SMR; P63218; 6-59.
DR STRING; 9606.ENSP00000359675; -.
DR PhosphoSite; P63218; -.
DR DMDM; 52783599; -.
DR PaxDb; P63218; -.
DR PRIDE; P63218; -.
DR DNASU; 2787; -.
DR Ensembl; ENST00000370641; ENSP00000359675; ENSG00000174021.
DR Ensembl; ENST00000370645; ENSP00000359679; ENSG00000174021.
DR GeneID; 2787; -.
DR KEGG; hsa:2787; -.
DR UCSC; uc001djw.4; human.
DR CTD; 2787; -.
DR GeneCards; GC01M084964; -.
DR HGNC; HGNC:4408; GNG5.
DR HPA; CAB032623; -.
DR HPA; HPA043651; -.
DR MIM; 600874; gene.
DR neXtProt; NX_P63218; -.
DR PharmGKB; PA28787; -.
DR eggNOG; NOG309295; -.
DR HOVERGEN; HBG014983; -.
DR InParanoid; P63218; -.
DR KO; K04542; -.
DR OMA; ADLQQFC; -.
DR OrthoDB; EOG7H1JP7; -.
DR PhylomeDB; P63218; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_604; Hemostasis.
DR GeneWiki; GNG5; -.
DR GenomeRNAi; 2787; -.
DR NextBio; 10983; -.
DR PRO; PR:P63218; -.
DR Bgee; P63218; -.
DR CleanEx; HS_GNG5; -.
DR Genevestigator; P63218; -.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; NAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; NAS:UniProtKB.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR13809; PTHR13809; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Complete proteome;
KW Direct protein sequencing; Lipoprotein; Membrane; Methylation;
KW Phosphoprotein; Prenylation; Reference proteome; Transducer.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 65 Guanine nucleotide-binding protein
FT G(I)/G(S)/G(O) subunit gamma-5.
FT /FTId=PRO_0000012627.
FT PROPEP 66 68 Removed in mature form (By similarity).
FT /FTId=PRO_0000012628.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 65 65 Cysteine methyl ester (By similarity).
FT LIPID 65 65 S-geranylgeranyl cysteine (By
FT similarity).
SQ SEQUENCE 68 AA; 7318 MW; 9AF7A16558863602 CRC64;
MSGSSSVAAM KKVVQQLRLE AGLNRVKVSQ AAADLKQFCL QNAQHDPLLT GVSSSTNPFR
PQKVCSFL
//
ID GBG5_HUMAN Reviewed; 68 AA.
AC P63218; B2R5A0; P30670; Q5VX54; Q61015;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;
DE Flags: Precursor;
GN Name=GNG5; Synonyms=GNGT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9790912; DOI=10.1006/bbrc.1998.9439;
RA Liu B., Aronson N.N. Jr.;
RT "Structure of human G protein Ggamma5 gene GNG5.";
RL Biochem. Biophys. Res. Commun. 251:88-94(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-
RT length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-18, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC involved as a modulator or transducer in various transmembrane
CC signaling systems. The beta and gamma chains are required for the
CC GTPase activity, for replacement of GDP by GTP, and for G protein-
CC effector interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC gamma.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC side (Potential).
CC -!- SIMILARITY: Belongs to the G protein gamma family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF085709; AAC72203.1; -; Genomic_DNA.
DR EMBL; AF085708; AAC72203.1; JOINED; Genomic_DNA.
DR EMBL; AF038955; AAC39869.1; -; mRNA.
DR EMBL; AF493873; AAM12587.1; -; mRNA.
DR EMBL; BT006823; AAP35469.1; -; mRNA.
DR EMBL; AK312111; BAG35047.1; -; mRNA.
DR EMBL; AL359762; CAH70203.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73236.1; -; Genomic_DNA.
DR EMBL; BC003563; AAH03563.1; -; mRNA.
DR RefSeq; NP_005265.1; NM_005274.2.
DR UniGene; Hs.645427; -.
DR ProteinModelPortal; P63218; -.
DR SMR; P63218; 6-59.
DR STRING; 9606.ENSP00000359675; -.
DR PhosphoSite; P63218; -.
DR DMDM; 52783599; -.
DR PaxDb; P63218; -.
DR PRIDE; P63218; -.
DR DNASU; 2787; -.
DR Ensembl; ENST00000370641; ENSP00000359675; ENSG00000174021.
DR Ensembl; ENST00000370645; ENSP00000359679; ENSG00000174021.
DR GeneID; 2787; -.
DR KEGG; hsa:2787; -.
DR UCSC; uc001djw.4; human.
DR CTD; 2787; -.
DR GeneCards; GC01M084964; -.
DR HGNC; HGNC:4408; GNG5.
DR HPA; CAB032623; -.
DR HPA; HPA043651; -.
DR MIM; 600874; gene.
DR neXtProt; NX_P63218; -.
DR PharmGKB; PA28787; -.
DR eggNOG; NOG309295; -.
DR HOVERGEN; HBG014983; -.
DR InParanoid; P63218; -.
DR KO; K04542; -.
DR OMA; ADLQQFC; -.
DR OrthoDB; EOG7H1JP7; -.
DR PhylomeDB; P63218; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_604; Hemostasis.
DR GeneWiki; GNG5; -.
DR GenomeRNAi; 2787; -.
DR NextBio; 10983; -.
DR PRO; PR:P63218; -.
DR Bgee; P63218; -.
DR CleanEx; HS_GNG5; -.
DR Genevestigator; P63218; -.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; NAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; NAS:UniProtKB.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR001770; Gprotein-gamma.
DR PANTHER; PTHR13809; PTHR13809; 1.
DR Pfam; PF00631; G-gamma; 1.
DR PRINTS; PR00321; GPROTEING.
DR SMART; SM00224; GGL; 1.
DR SUPFAM; SSF48670; SSF48670; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Complete proteome;
KW Direct protein sequencing; Lipoprotein; Membrane; Methylation;
KW Phosphoprotein; Prenylation; Reference proteome; Transducer.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 65 Guanine nucleotide-binding protein
FT G(I)/G(S)/G(O) subunit gamma-5.
FT /FTId=PRO_0000012627.
FT PROPEP 66 68 Removed in mature form (By similarity).
FT /FTId=PRO_0000012628.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 65 65 Cysteine methyl ester (By similarity).
FT LIPID 65 65 S-geranylgeranyl cysteine (By
FT similarity).
SQ SEQUENCE 68 AA; 7318 MW; 9AF7A16558863602 CRC64;
MSGSSSVAAM KKVVQQLRLE AGLNRVKVSQ AAADLKQFCL QNAQHDPLLT GVSSSTNPFR
PQKVCSFL
//
MIM
600874
*RECORD*
*FIELD* NO
600874
*FIELD* TI
*600874 GUANINE NUCLEOTIDE-BINDING PROTEIN, GAMMA-5; GNG5
;;G PROTEIN GAMMA-5 SUBUNIT
read more*FIELD* TX
DESCRIPTION
G proteins are trimeric (alpha-beta-gamma) membrane-associated proteins
that regulate flow of information from cell surface receptors to a
variety of internal metabolic effectors. Interaction of a G protein with
its activated receptor promotes exchange of GTP for GDP that is bound to
the alpha subunit. The alpha-GTP complex dissociates from the beta-gamma
heterodimer so that the subunits, in turn, may interact with and
regulate effector molecules (Gilman, 1987; summary by Ahmad et al.,
1995).
CLONING
Fisher and Aronson (1992) characterized the cDNA and genomic sequence of
the gamma-5 subunit (GNG5). They found, furthermore, a cDNA clone from
human placenta with an altered open reading frame and 3-prime
untranslated region. At base position 957 of the cDNA for native
chitobiase (CTBS; 600873), which would be the 3-prime end of exon 6 of
the chitobiase gene, there was fused in-frame a sequence that
represented exons 2 and 3 from the gamma-5 gene. Exons 2 and 3,
respectively, code for the carboxyl-end of the gamma-5 protein and the
3-prime untranslated portion of its mRNA. This hybrid message was also
identified in human liver and retina by RT-PCR analysis. It was not
known whether a hybrid protein was produced in vivo.
MAPPING
Ahmad et al. (1995) demonstrated that both the CTBS gene and the GNG5
gene map to 1p by PCR analysis of somatic cell hybrids; by fluorescence
in situ hybridization using a YAC clone that contains both chitobiase
and gamma-5 genes, they refined the localization to 1p22.
*FIELD* RF
1. Ahmad, W.; Li, S.; Chen, H.; Tuck-Muller, C. M.; Pittler, S. J.;
Aronson, N. N., Jr.: Lysosomal chitobiase (CTB) and the G-protein
gamma-5 subunit (GNG5) genes co-localize to human chromosome 1p22. Cytogenet.
Cell Genet. 71: 44-46, 1995.
2. Fisher, K. J.; Aronson, N. N.: Characterization of the cDNA and
genomic sequence of a G protein gamma subunit (gamma-5). Molec. Cell
Biol. 12: 1585-1591, 1992.
3. Gilman, A. G.: G proteins: transducers of receptor-generated signals. Annu.
Rev. Biochem. 56: 615-649, 1987.
*FIELD* CD
Victor A. McKusick: 10/16/1995
*FIELD* ED
terry: 11/24/2010
carol: 11/9/2010
carol: 1/5/2000
dkim: 12/16/1998
carol: 7/2/1998
terry: 6/4/1998
mark: 12/13/1995
mark: 10/16/1995
*RECORD*
*FIELD* NO
600874
*FIELD* TI
*600874 GUANINE NUCLEOTIDE-BINDING PROTEIN, GAMMA-5; GNG5
;;G PROTEIN GAMMA-5 SUBUNIT
read more*FIELD* TX
DESCRIPTION
G proteins are trimeric (alpha-beta-gamma) membrane-associated proteins
that regulate flow of information from cell surface receptors to a
variety of internal metabolic effectors. Interaction of a G protein with
its activated receptor promotes exchange of GTP for GDP that is bound to
the alpha subunit. The alpha-GTP complex dissociates from the beta-gamma
heterodimer so that the subunits, in turn, may interact with and
regulate effector molecules (Gilman, 1987; summary by Ahmad et al.,
1995).
CLONING
Fisher and Aronson (1992) characterized the cDNA and genomic sequence of
the gamma-5 subunit (GNG5). They found, furthermore, a cDNA clone from
human placenta with an altered open reading frame and 3-prime
untranslated region. At base position 957 of the cDNA for native
chitobiase (CTBS; 600873), which would be the 3-prime end of exon 6 of
the chitobiase gene, there was fused in-frame a sequence that
represented exons 2 and 3 from the gamma-5 gene. Exons 2 and 3,
respectively, code for the carboxyl-end of the gamma-5 protein and the
3-prime untranslated portion of its mRNA. This hybrid message was also
identified in human liver and retina by RT-PCR analysis. It was not
known whether a hybrid protein was produced in vivo.
MAPPING
Ahmad et al. (1995) demonstrated that both the CTBS gene and the GNG5
gene map to 1p by PCR analysis of somatic cell hybrids; by fluorescence
in situ hybridization using a YAC clone that contains both chitobiase
and gamma-5 genes, they refined the localization to 1p22.
*FIELD* RF
1. Ahmad, W.; Li, S.; Chen, H.; Tuck-Muller, C. M.; Pittler, S. J.;
Aronson, N. N., Jr.: Lysosomal chitobiase (CTB) and the G-protein
gamma-5 subunit (GNG5) genes co-localize to human chromosome 1p22. Cytogenet.
Cell Genet. 71: 44-46, 1995.
2. Fisher, K. J.; Aronson, N. N.: Characterization of the cDNA and
genomic sequence of a G protein gamma subunit (gamma-5). Molec. Cell
Biol. 12: 1585-1591, 1992.
3. Gilman, A. G.: G proteins: transducers of receptor-generated signals. Annu.
Rev. Biochem. 56: 615-649, 1987.
*FIELD* CD
Victor A. McKusick: 10/16/1995
*FIELD* ED
terry: 11/24/2010
carol: 11/9/2010
carol: 1/5/2000
dkim: 12/16/1998
carol: 7/2/1998
terry: 6/4/1998
mark: 12/13/1995
mark: 10/16/1995