GNA12_HUMAN
ID GNA12_HUMAN Reviewed; 381 AA.
AC Q03113; A4D204; B3KXS2; B7Z3F7; Q2T9L1; Q5PPR5; Q86UM8; Q8TD71; Q9UDU9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-12;
DE Short=G alpha-12;
DE Short=G-protein subunit alpha-12;
GN Name=GNA12;
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] (ISOFORM 1).
RX PubMed=8423800; DOI=10.1128/mcb.13.2.762-768.1993;
RA Chan A.M.-L., Fleming T.P., McGovern E.S., Chedid M., Miki T.,
RA Aaronson S.A.;
RT "Expression cDNA cloning of a transforming gene encoding the wild-type G
RT alpha 12 gene product.";
RL Mol. Cell. Biol. 13:762-768(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Hippocampus, and Placenta;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-68.
RC TISSUE=Brain, and Pancreas;
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).
RN [7]
RP INTERACTION WITH ARHGEF11.
RX PubMed=10026210; DOI=10.1074/jbc.274.9.5868;
RA Fukuhara S., Murga C., Zohar M., Igishi T., Gutkind J.S.;
RT "A novel PDZ domain containing guanine nucleotide exchange factor links
RT heterotrimeric G proteins to Rho.";
RL J. Biol. Chem. 274:5868-5879(1999).
RN [8]
RP INTERACTION WITH ARHGEF12.
RX PubMed=11094164; DOI=10.1016/s0014-5793(00)02224-9;
RA Fukuhara S., Chikumi H., Gutkind J.S.;
RT "Leukemia-associated Rho guanine nucleotide exchange factor (LARG) links
RT heterotrimeric G proteins of the G(12) family to Rho.";
RL FEBS Lett. 485:183-188(2000).
RN [9]
RP FUNCTION.
RX PubMed=11976333; DOI=10.1074/jbc.m201984200;
RA Meigs T.E., Fedor-Chaiken M., Kaplan D.D., Brackenbury R., Casey P.J.;
RT "Galpha12 and Galpha13 negatively regulate the adhesive functions of
RT cadherin.";
RL J. Biol. Chem. 277:24594-24600(2002).
RN [10]
RP FUNCTION.
RX PubMed=12515866; DOI=10.1073/pnas.0234057100;
RA Suzuki N., Nakamura S., Mano H., Kozasa T.;
RT "Galpha 12 activates Rho GTPase through tyrosine-phosphorylated leukemia-
RT associated RhoGEF.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:733-738(2003).
RN [11]
RP FUNCTION, INTERACTION WITH PPP2R1A, AND SUBCELLULAR LOCATION.
RX PubMed=15525651; DOI=10.1074/jbc.c400508200;
RA Zhu D., Kosik K.S., Meigs T.E., Yanamadala V., Denker B.M.;
RT "Galpha12 directly interacts with PP2A: evidence for Galpha12-stimulated
RT PP2A phosphatase activity and dephosphorylation of microtubule-associated
RT protein, tau.";
RL J. Biol. Chem. 279:54983-54986(2004).
RN [12]
RP FUNCTION, INTERACTION WITH CTNND1, AND SUBCELLULAR LOCATION.
RX PubMed=15240885; DOI=10.1073/pnas.0401366101;
RA Krakstad B.F., Ardawatia V.V., Aragay A.M.;
RT "A role for Galpha12/Galpha13 in p120ctn regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10314-10319(2004).
RN [13]
RP FUNCTION, AND INTERACTION WITH UBXD5.
RX PubMed=16202387; DOI=10.1016/j.bbrc.2005.09.097;
RA Tateiwa K., Katoh H., Negishi M.;
RT "Socius, a novel binding partner of Galpha12/13, promotes the Galpha12-
RT induced RhoA activation.";
RL Biochem. Biophys. Res. Commun. 337:615-620(2005).
RN [14]
RP FUNCTION, INTERACTION WITH NAPA, AND SUBCELLULAR LOCATION.
RX PubMed=15980433; DOI=10.1074/jbc.m502844200;
RA Andreeva A.V., Kutuzov M.A., Vaiskunaite R., Profirovic J., Meigs T.E.,
RA Predescu S., Malik A.B., Voyno-Yasenetskaya T.;
RT "G alpha12 interaction with alphaSNAP induces VE-cadherin localization at
RT endothelial junctions and regulates barrier function.";
RL J. Biol. Chem. 280:30376-30383(2005).
RN [15]
RP FUNCTION.
RX PubMed=16787920; DOI=10.1074/jbc.m604376200;
RA Kelly P., Stemmle L.N., Madden J.F., Fields T.A., Daaka Y., Casey P.J.;
RT "A role for the G12 family of heterotrimeric G proteins in prostate cancer
RT invasion.";
RL J. Biol. Chem. 281:26483-26490(2006).
RN [16]
RP FUNCTION.
RX PubMed=16705036; DOI=10.1073/pnas.0510254103;
RA Kelly P., Moeller B.J., Juneja J., Booden M.A., Der C.J., Daaka Y.,
RA Dewhirst M.W., Fields T.A., Casey P.J.;
RT "The G12 family of heterotrimeric G proteins promotes breast cancer
RT invasion and metastasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8173-8178(2006).
RN [17]
RP FUNCTION.
RX PubMed=17565996; DOI=10.1074/jbc.m702804200;
RA Yanamadala V., Negoro H., Gunaratnam L., Kong T., Denker B.M.;
RT "Galpha12 stimulates apoptosis in epithelial cells through JNK1-mediated
RT Bcl-2 degradation and up-regulation of IkappaBalpha.";
RL J. Biol. Chem. 282:24352-24363(2007).
RN [18]
RP INTERACTION WITH RGS22.
RC TISSUE=Testis;
RX PubMed=18703424; DOI=10.1095/biolreprod.107.067504;
RA Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z.,
RA Sha J.;
RT "RGS22, a novel testis-specific regulator of G-protein signaling involved
RT in human and mouse spermiogenesis along with GNA12/13 subunits.";
RL Biol. Reprod. 79:1021-1029(2008).
RN [19]
RP FUNCTION IN TOR SIGNALING.
RX PubMed=22609986; DOI=10.1038/ncb2507;
RA Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D.,
RA Offermanns S., Simon M.I., Wu D.;
RT "PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and
RT cell migration downstream of Galpha12.";
RL Nat. Cell Biol. 14:686-696(2012).
RN [20]
RP FUNCTION.
RX PubMed=23762476; DOI=10.1371/journal.pone.0066133;
RA Jian S.L., Hsieh H.Y., Liao C.T., Yen T.C., Nien S.W., Cheng A.J.,
RA Juang J.L.;
RT "Galpha(1)(2) drives invasion of oral squamous cell carcinoma through up-
RT regulation of proinflammatory cytokines.";
RL PLoS ONE 8:E66133-E66133(2013).
RN [21]
RP FUNCTION.
RX PubMed=27084452; DOI=10.1016/j.bbrc.2016.04.048;
RA Yuan B., Cui J., Wang W., Deng K.;
RT "Galpha12/13 signaling promotes cervical cancer invasion through the
RT RhoA/ROCK-JNK signaling axis.";
RL Biochem. Biophys. Res. Commun. 473:1240-1246(2016).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling systems
CC (PubMed:22609986, PubMed:15525651, PubMed:15240885, PubMed:17565996,
CC PubMed:12515866, PubMed:16787920, PubMed:16705036, PubMed:23762476,
CC PubMed:27084452). Activates effector molecule RhoA by binding and
CC activating RhoGEFs (ARHGEF12/LARG) (PubMed:15240885, PubMed:12515866,
CC PubMed:16202387). GNA12-dependent Rho signaling subsequently regulates
CC transcription factor AP-1 (activating protein-1) (By similarity).
CC GNA12-dependent Rho signaling also regulates protein phosphatese 2A
CC activation causing dephosphorylation of its target proteins
CC (PubMed:15525651, PubMed:17565996). Promotes tumor cell invasion and
CC metastasis by activating RhoA/ROCK signaling pathway and up-regulating
CC pro-inflammatory cytokine production (PubMed:23762476, PubMed:16787920,
CC PubMed:16705036, PubMed:27084452). Inhibits CDH1-mediated cell adhesion
CC in process independent from Rho activation (PubMed:11976333,
CC PubMed:16787920). Together with NAPA promotes CDH5 localization to
CC plasma membrane (PubMed:15980433). May play a role in the control of
CC cell migration through the TOR signaling cascade (PubMed:22609986).
CC {ECO:0000250|UniProtKB:P27600, ECO:0000269|PubMed:11976333,
CC ECO:0000269|PubMed:12515866, ECO:0000269|PubMed:15240885,
CC ECO:0000269|PubMed:15525651, ECO:0000269|PubMed:15980433,
CC ECO:0000269|PubMed:16705036, ECO:0000269|PubMed:16787920,
CC ECO:0000269|PubMed:17565996, ECO:0000269|PubMed:22609986,
CC ECO:0000269|PubMed:23762476, ECO:0000269|PubMed:27084452}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma
CC (PubMed:10026210). The alpha chain contains the guanine nucleotide
CC binding site (By similarity). Interacts with UBXD5 (PubMed:16202387).
CC Interacts (in GTP-bound form) with PPP5C (via TPR repeats); activates
CC PPP5C phosphatase activity and translocates PPP5C to the cell membrane.
CC Interacts with RGS22 (PubMed:18703424). Interacts (via N-terminus) with
CC NAPA; the interaction promotes CDH5 localization to plasma membrane
CC (PubMed:15980433). Interacts with CTNND1 (via N-terminus); the
CC interaction regulates CDH1-mediated cell-cell adhesion
CC (PubMed:15240885). Interacts with PPP2R1A; the interaction promotes
CC protein phosphatase 2A activation causing dephosphorylation of MAPT
CC (PubMed:15525651). Interacts (in GTP-bound form) with ARHGEF1 (By
CC similarity). Interacts (in GTP-bound form) with ARHGEF11 (via RGS
CC domain) (PubMed:10026210). Interacts (in GTP-bound form) with ARHGEF12
CC (via RGS domain) (PubMed:11094164). {ECO:0000250|UniProtKB:P27600,
CC ECO:0000269|PubMed:10026210, ECO:0000269|PubMed:11094164,
CC ECO:0000269|PubMed:15240885, ECO:0000269|PubMed:15525651,
CC ECO:0000269|PubMed:15980433, ECO:0000269|PubMed:16202387,
CC ECO:0000269|PubMed:18703424}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15240885,
CC ECO:0000269|PubMed:15980433}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q63210}. Lateral cell membrane
CC {ECO:0000269|PubMed:15525651}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q63210}. Cytoplasm
CC {ECO:0000269|PubMed:15240885}. Note=CDH1 enhances cell membrane
CC localization. {ECO:0000269|PubMed:15240885}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=Q03113-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03113-2; Sequence=VSP_055171;
CC Name=3;
CC IsoId=Q03113-3; Sequence=VSP_055230, VSP_055231;
CC -!- SIMILARITY: Belongs to the G-alpha family. G(12) subfamily.
CC {ECO:0000305}.
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DR EMBL; L01694; AAA35867.1; -; mRNA.
DR EMBL; AF493901; AAM12615.1; -; mRNA.
DR EMBL; AK127842; BAG54584.1; -; mRNA.
DR EMBL; AK295830; BAH12193.1; -; mRNA.
DR EMBL; AC006028; AAP21870.1; -; Genomic_DNA.
DR EMBL; AC004933; AAD05026.1; -; Genomic_DNA.
DR EMBL; CH236953; EAL23961.1; -; Genomic_DNA.
DR EMBL; BC087537; AAH87537.1; -; mRNA.
DR EMBL; BC111464; AAI11465.1; -; mRNA.
DR CCDS; CCDS5335.1; -. [Q03113-1]
DR CCDS; CCDS64584.1; -. [Q03113-2]
DR PIR; A48071; A48071.
DR RefSeq; NP_001269370.1; NM_001282441.1. [Q03113-2]
DR RefSeq; NP_001280021.1; NM_001293092.1.
DR RefSeq; NP_031379.2; NM_007353.2. [Q03113-1]
DR AlphaFoldDB; Q03113; -.
DR SMR; Q03113; -.
DR BioGRID; 109030; 41.
DR CORUM; Q03113; -.
DR IntAct; Q03113; 10.
DR MINT; Q03113; -.
DR STRING; 9606.ENSP00000275364; -.
DR ChEMBL; CHEMBL3308913; -.
DR iPTMnet; Q03113; -.
DR PhosphoSitePlus; Q03113; -.
DR SwissPalm; Q03113; -.
DR BioMuta; GNA12; -.
DR DMDM; 38258934; -.
DR EPD; Q03113; -.
DR jPOST; Q03113; -.
DR MassIVE; Q03113; -.
DR MaxQB; Q03113; -.
DR PaxDb; Q03113; -.
DR PeptideAtlas; Q03113; -.
DR PRIDE; Q03113; -.
DR ProteomicsDB; 3818; -.
DR ProteomicsDB; 58191; -. [Q03113-1]
DR ProteomicsDB; 6518; -.
DR Antibodypedia; 4103; 233 antibodies from 30 providers.
DR DNASU; 2768; -.
DR Ensembl; ENST00000275364.8; ENSP00000275364.3; ENSG00000146535.14. [Q03113-1]
DR Ensembl; ENST00000407904.7; ENSP00000385935.3; ENSG00000146535.14. [Q03113-2]
DR GeneID; 2768; -.
DR KEGG; hsa:2768; -.
DR MANE-Select; ENST00000275364.8; ENSP00000275364.3; NM_007353.3; NP_031379.2.
DR UCSC; uc003smt.5; human. [Q03113-1]
DR CTD; 2768; -.
DR DisGeNET; 2768; -.
DR GeneCards; GNA12; -.
DR HGNC; HGNC:4380; GNA12.
DR HPA; ENSG00000146535; Low tissue specificity.
DR MIM; 604394; gene.
DR neXtProt; NX_Q03113; -.
DR OpenTargets; ENSG00000146535; -.
DR PharmGKB; PA28765; -.
DR VEuPathDB; HostDB:ENSG00000146535; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000157636; -.
DR HOGENOM; CLU_014184_3_1_1; -.
DR InParanoid; Q03113; -.
DR OMA; MVASNEY; -.
DR PhylomeDB; Q03113; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; Q03113; -.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR SignaLink; Q03113; -.
DR SIGNOR; Q03113; -.
DR BioGRID-ORCS; 2768; 29 hits in 1083 CRISPR screens.
DR ChiTaRS; GNA12; human.
DR GeneWiki; GNA12; -.
DR GenomeRNAi; 2768; -.
DR Pharos; Q03113; Tbio.
DR PRO; PR:Q03113; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q03113; protein.
DR Bgee; ENSG00000146535; Expressed in secondary oocyte and 191 other tissues.
DR ExpressionAtlas; Q03113; baseline and differential.
DR Genevisible; Q03113; HS.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031752; F:D5 dopamine receptor binding; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IPI:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0010762; P:regulation of fibroblast migration; ISS:UniProtKB.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0032006; P:regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000469; Gprotein_alpha_12/13.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00440; GPROTEINA12.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cell membrane; Cytoplasm; GTP-binding; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..381
FT /note="Guanine nucleotide-binding protein subunit alpha-12"
FT /id="PRO_0000203770"
FT DOMAIN 56..381
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 59..72
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 200..208
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 223..232
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 292..299
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 351..356
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 67..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 202..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 296..299
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 353
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14344"
FT LIPID 11
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT VAR_SEQ 1..103
FT /note="MSGVVRTLSRCLLPAEAGGARERRAGSGARDAEREARRRSRDIDALLARERR
FT AVRRLVKILLLGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILK -> MKRR
FT MFPRPCLARMPGSRGSGSTPDGNRKCCRFEHLLIAHPGSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055171"
FT VAR_SEQ 1..76
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055230"
FT VAR_SEQ 174..190
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055231"
FT VARIANT 68
FT /note="S -> G (in dbSNP:rs11552939)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_071044"
FT VARIANT 242
FT /note="F -> L (in dbSNP:rs45606633)"
FT /id="VAR_049359"
FT VARIANT 330
FT /note="Y -> H (in dbSNP:rs45583847)"
FT /id="VAR_049360"
FT CONFLICT 126
FT /note="K -> E (in Ref. 2; AAM12615)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="R -> Q (in Ref. 1; AAA35867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 44279 MW; 04C3F12B29255F89 CRC64;
MSGVVRTLSR CLLPAEAGGA RERRAGSGAR DAEREARRRS RDIDALLARE RRAVRRLVKI
LLLGAGESGK STFLKQMRII HGREFDQKAL LEFRDTIFDN ILKGSRVLVD ARDKLGIPWQ
YSENEKHGMF LMAFENKAGL PVEPATFQLY VPALSALWRD SGIREAFSRR SEFQLGESVK
YFLDNLDRIG QLNYFPSKQD ILLARKATKG IVEHDFVIKK IPFKMVDVGG QRSQRQKWFQ
CFDGITSILF MVSSSEYDQV LMEDRRTNRL VESMNIFETI VNNKLFFNVS IILFLNKMDL
LVEKVKTVSI KKHFPDFRGD PHRLEDVQRY LVQCFDRKRR NRSKPLFHHF TTAIDTENVR
FVFHAVKDTI LQENLKDIML Q
