GBG11_HUMAN
ID GBG11_HUMAN Reviewed; 73 AA.
AC P61952; P50152;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11;
DE Flags: Precursor;
GN Name=GNG11; Synonyms=GNGT11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ISOPRENYLATION AT CYS-70.
RC TISSUE=Testis;
RX PubMed=7665596; DOI=10.1074/jbc.270.37.21765;
RA Ray K., Kunsch C., Bonner L.M., Robishaw J.D.;
RT "Isolation of cDNA clones encoding eight different human G protein gamma
RT subunits, including three novel forms designated the gamma 4, gamma 10, and
RT gamma 11 subunits.";
RL J. Biol. Chem. 270:21765-21771(1995).
RN [2]
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 sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC Interacts with beta-1 and beta-3, but not with beta-2.
CC -!- INTERACTION:
CC P61952; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-720198, EBI-744115;
CC P61952; Q6BDI9: REP15; NbExp=3; IntAct=EBI-720198, EBI-12048237;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in all tissues tested except
CC for brain.
CC -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR EMBL; U31384; AAC50206.1; -; mRNA.
DR EMBL; AF493878; AAM12592.1; -; mRNA.
DR EMBL; AC002076; AAS02020.1; -; Genomic_DNA.
DR EMBL; BC009709; AAH09709.1; -; mRNA.
DR CCDS; CCDS5634.1; -.
DR PIR; I39159; I39159.
DR RefSeq; NP_004117.1; NM_004126.3.
DR AlphaFoldDB; P61952; -.
DR SMR; P61952; -.
DR BioGRID; 109053; 13.
DR CORUM; P61952; -.
DR IntAct; P61952; 7.
DR STRING; 9606.ENSP00000248564; -.
DR iPTMnet; P61952; -.
DR PhosphoSitePlus; P61952; -.
DR BioMuta; GNG11; -.
DR DMDM; 48428913; -.
DR EPD; P61952; -.
DR jPOST; P61952; -.
DR MassIVE; P61952; -.
DR PaxDb; P61952; -.
DR PeptideAtlas; P61952; -.
DR PRIDE; P61952; -.
DR ProteomicsDB; 57341; -.
DR TopDownProteomics; P61952; -.
DR Antibodypedia; 30078; 98 antibodies from 19 providers.
DR DNASU; 2791; -.
DR Ensembl; ENST00000248564.6; ENSP00000248564.4; ENSG00000127920.6.
DR GeneID; 2791; -.
DR KEGG; hsa:2791; -.
DR MANE-Select; ENST00000248564.6; ENSP00000248564.4; NM_004126.4; NP_004117.1.
DR CTD; 2791; -.
DR DisGeNET; 2791; -.
DR GeneCards; GNG11; -.
DR HGNC; HGNC:4403; GNG11.
DR HPA; ENSG00000127920; Low tissue specificity.
DR MIM; 604390; gene.
DR neXtProt; NX_P61952; -.
DR OpenTargets; ENSG00000127920; -.
DR PharmGKB; PA28782; -.
DR VEuPathDB; HostDB:ENSG00000127920; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT01050000244876; -.
DR HOGENOM; CLU_168377_2_0_1; -.
DR InParanoid; P61952; -.
DR OMA; DCQRDDI; -.
DR OrthoDB; 1573820at2759; -.
DR PhylomeDB; P61952; -.
DR TreeFam; TF319909; -.
DR PathwayCommons; P61952; -.
DR Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
DR Reactome; R-HSA-202040; G-protein activation.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-HSA-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-HSA-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-HSA-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-HSA-9634597; GPER1 signaling.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR SignaLink; P61952; -.
DR BioGRID-ORCS; 2791; 22 hits in 1064 CRISPR screens.
DR ChiTaRS; GNG11; human.
DR GeneWiki; GNG11; -.
DR GenomeRNAi; 2791; -.
DR Pharos; P61952; Tbio.
DR PRO; PR:P61952; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P61952; protein.
DR Bgee; ENSG00000127920; Expressed in pigmented layer of retina and 200 other tissues.
DR ExpressionAtlas; P61952; baseline and differential.
DR Genevisible; P61952; HS.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00068; GGL; 1.
DR Gene3D; 4.10.260.10; -; 1.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
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 Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW Reference proteome; Transducer.
FT CHAIN 1..70
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT subunit gamma-11"
FT /id="PRO_0000012659"
FT PROPEP 71..73
FT /note="Removed in mature form"
FT /id="PRO_0000012660"
FT REGION 51..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 70
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:7665596"
SQ SEQUENCE 73 AA; 8481 MW; 2B13935E3AEFB9E8 CRC64;
MPALHIEDLP EKEKLKMEVE QLRKEVKLQR QQVSKCSEEI KNYIEERSGE DPLVKGIPED
KNPFKEKGSC VIS
