GNA14_HUMAN
ID GNA14_HUMAN Reviewed; 355 AA.
AC O95837; B1ALW3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-14;
DE Short=G alpha-14;
DE Short=G-protein subunit alpha-14;
GN Name=GNA14;
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].
RX PubMed=10191087; DOI=10.1006/geno.1999.5758;
RA Rubio J.P., Levy E.R., Dobson-Stone C., Monaco A.P.;
RT "Genomic organization of the human G-alpha-14 and G-alpha-Q genes and
RT mutation analysis in chorea-acanthocytosis (CHAC).";
RL Genomics 57:84-93(1999).
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 MRNA].
RC TISSUE=Caudate nucleus;
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].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- INTERACTION:
CC O95837; O96015: DNAL4; NbExp=3; IntAct=EBI-7951023, EBI-742362;
CC O95837; Q92993: KAT5; NbExp=3; IntAct=EBI-7951023, EBI-399080;
CC O95837; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-7951023, EBI-11742507;
CC O95837; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-7951023, EBI-9090795;
CC O95837; P61981: YWHAG; NbExp=3; IntAct=EBI-7951023, EBI-359832;
CC -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; AF105201; AAD17944.1; -; mRNA.
DR EMBL; AF493903; AAM12617.1; -; mRNA.
DR EMBL; AK312460; BAG35367.1; -; mRNA.
DR EMBL; CH471089; EAW62603.1; -; Genomic_DNA.
DR EMBL; BC027886; AAH27886.1; -; mRNA.
DR CCDS; CCDS6657.1; -.
DR RefSeq; NP_004288.1; NM_004297.3.
DR AlphaFoldDB; O95837; -.
DR SMR; O95837; -.
DR BioGRID; 114989; 9.
DR CORUM; O95837; -.
DR IntAct; O95837; 8.
DR MINT; O95837; -.
DR STRING; 9606.ENSP00000365807; -.
DR iPTMnet; O95837; -.
DR PhosphoSitePlus; O95837; -.
DR SwissPalm; O95837; -.
DR BioMuta; GNA14; -.
DR EPD; O95837; -.
DR jPOST; O95837; -.
DR MassIVE; O95837; -.
DR MaxQB; O95837; -.
DR PaxDb; O95837; -.
DR PeptideAtlas; O95837; -.
DR PRIDE; O95837; -.
DR ProteomicsDB; 51083; -.
DR Antibodypedia; 54425; 233 antibodies from 28 providers.
DR DNASU; 9630; -.
DR Ensembl; ENST00000341700.7; ENSP00000365807.4; ENSG00000156049.7.
DR GeneID; 9630; -.
DR KEGG; hsa:9630; -.
DR MANE-Select; ENST00000341700.7; ENSP00000365807.4; NM_004297.4; NP_004288.1.
DR UCSC; uc004aku.4; human.
DR CTD; 9630; -.
DR DisGeNET; 9630; -.
DR GeneCards; GNA14; -.
DR HGNC; HGNC:4382; GNA14.
DR HPA; ENSG00000156049; Low tissue specificity.
DR MalaCards; GNA14; -.
DR MIM; 604397; gene.
DR neXtProt; NX_O95837; -.
DR OpenTargets; ENSG00000156049; -.
DR Orphanet; 2122; Kaposiform hemangioendothelioma.
DR Orphanet; 1063; Tufted angioma.
DR PharmGKB; PA28767; -.
DR VEuPathDB; HostDB:ENSG00000156049; -.
DR eggNOG; KOG0085; Eukaryota.
DR GeneTree; ENSGT00940000158510; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; O95837; -.
DR OMA; CCVSAED; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; O95837; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; O95837; -.
DR Reactome; R-HSA-112043; PLC beta mediated events.
DR Reactome; R-HSA-202040; G-protein activation.
DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; O95837; -.
DR SIGNOR; O95837; -.
DR BioGRID-ORCS; 9630; 18 hits in 1069 CRISPR screens.
DR ChiTaRS; GNA14; human.
DR GenomeRNAi; 9630; -.
DR Pharos; O95837; Tbio.
DR PRO; PR:O95837; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O95837; protein.
DR Bgee; ENSG00000156049; Expressed in secondary oocyte and 130 other tissues.
DR Genevisible; O95837; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; TAS:Reactome.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001508; P:action potential; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
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; PR00442; GPROTEINAQ.
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 ADP-ribosylation; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN 1..355
FT /note="Guanine nucleotide-binding protein subunit alpha-14"
FT /id="PRO_0000203752"
FT DOMAIN 34..355
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 37..50
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 42..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="ADP-ribosylarginine; by cholera toxin"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 41571 MW; EAB73A9876E9C47E CRC64;
MAGCCCLSAE EKESQRISAE IERQLRRDKK DARRELKLLL LGTGESGKST FIKQMRIIHG
SGYSDEDRKG FTKLVYQNIF TAMQAMIRAM DTLRIQYVCE QNKENAQIIR EVEVDKVSML
SREQVEAIKQ LWQDPGIQEC YDRRREYQLS DSAKYYLTDI DRIATPSFVP TQQDVLRVRV
PTTGIIEYPF DLENIIFRMV DVGGQRSERR KWIHCFESVT SIIFLVALSE YDQVLAECDN
ENRMEESKAL FKTIITYPWF LNSSVILFLN KKDLLEEKIM YSHLISYFPE YTGPKQDVRA
ARDFILKLYQ DQNPDKEKVI YSHFTCATDT DNIRFVFAAV KDTILQLNLR EFNLV
