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Protein

Guanine nucleotide-binding protein G(i) subunit alpha-1

Gene

Gnai1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:19703466, PubMed:24596087, PubMed:25037222). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:21158412). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:21158412). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:19703466). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (PubMed:16870394).Curated5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumCombined sources2 Publications
Metal bindingi181 – 1811MagnesiumCombined sources3 Publications
Binding sitei326 – 3261GTP; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 486GTPCombined sources
Nucleotide bindingi150 – 1512GTPCombined sources
Nucleotide bindingi175 – 1784GTPCombined sources
Nucleotide bindingi200 – 2045GTPCombined sources
Nucleotide bindingi269 – 2724GTPCombined sources

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • G-protein coupled receptor binding Source: UniProtKB
  • G-protein coupled serotonin receptor binding Source: RGD
  • GTPase activating protein binding Source: RGD
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: InterPro
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB
  • cellular response to forskolin Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • negative regulation of synaptic transmission Source: RGD
  • regulation of cAMP-mediated signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-112043. PLC beta mediated events.
R-RNO-170670. Adenylate cyclase inhibitory pathway.
R-RNO-202040. G-protein activation.
R-RNO-392170. ADP signalling through P2Y purinoceptor 12.
R-RNO-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-RNO-418594. G alpha (i) signalling events.
SABIO-RKP10824.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-1
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
Gene namesi
Name:Gnai1
Synonyms:Gnai-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2713. Gnai1.

Subcellular locationi

  • Nucleus
  • Cytoplasm 1 Publication
  • Cell membrane 2 Publications; Peripheral membrane protein 2 Publications; Cytoplasmic side Curated
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
  • Membrane By similarity; Lipid-anchor By similarity

  • Note: Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody (By similarity). Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane (PubMed:21158412).By similarity1 Publication

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • heterotrimeric G-protein complex Source: RGD
  • lysosomal membrane Source: Ensembl
  • membrane Source: RGD
  • membrane raft Source: RGD
  • midbody Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431E → A: Mildly impairs receptor binding; mildly decreases basal and receptor-stimulated GDP exchange. 1 Publication
Mutagenesisi149 – 1491N → I: Inhibits interaction with RGS14. Does not inhibit interaction with RIC8A. 1 Publication
Mutagenesisi189 – 1891F → Y: Increases basal GDP exchange rate; no effect on receptor-stimulated GDP exchange. 1 Publication
Mutagenesisi191 – 1911F → Y: No effect on basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication
Mutagenesisi204 – 2041Q → L: Expected to have lost GTPase activity; inhibits the forskolin-mediated increase of cellular cAMP levels. Does not inhibit interaction with RGS14 at centrosomes. 2 Publications
Mutagenesisi329 – 3291T → A: Increases basal GDP exchange rate and inhibits the forskolin-mediated increase of cellular cAMP levels. 1 Publication
Mutagenesisi332 – 3321V → A: Increases basal GDP exchange rate. 1 Publication
Mutagenesisi336 – 3361F → A or C: Increases basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication
Mutagenesisi336 – 3361F → Y: Strongly increases basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication
Mutagenesisi345 – 3451K → L: Mildly impairs receptor binding; mildly decreases basal and receptor-stimulated GDP exchange. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 354353Guanine nucleotide-binding protein G(i) subunit alpha-1PRO_0000203673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi3 – 31S-palmitoyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

PRIDEiP10824.

2D gel databases

World-2DPAGE0004:P10824.

PTM databases

iPTMnetiP10824.
PhosphoSiteiP10824.
SwissPalmiP10824.

Interactioni

Subunit structurei

Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:8521505, PubMed:24596087, PubMed:25037222). Identified in complex with the beta subunit GNB1 and the gamma subunit GNG1 (PubMed:24596087). Identified in complex with the beta subunit GNB1 and the gamma subunit GNG2 (PubMed:8521505). GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins. Interacts (GDP-bound form) with GPSM1; this inhibits guanine nucleotide exchange and GTP binding (PubMed:11121039). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains); this inhibits guanine nucleotide exchange (By similarity). Interacts with RGS10; this strongly enhances GTP hydrolysis. Interacts with RGS1 and RGS16 (By similarity). Interacts with RGS4 (PubMed:9108480). Interacts with RGS12 (PubMed:11387333). Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains) (PubMed:11387333, PubMed:16870394, PubMed:17635935, PubMed:21158412). Interacts with RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro) (By similarity). Interacts (GDP-bound form) with RIC8A (via C-terminus) (PubMed:21158412).By similarity8 Publications

GO - Molecular functioni

  • G-protein coupled receptor binding Source: UniProtKB
  • G-protein coupled serotonin receptor binding Source: RGD
  • GTPase activating protein binding Source: RGD

Protein-protein interaction databases

BioGridi247715. 1 interaction.
DIPiDIP-6073N.
IntActiP10824. 2 interactions.
MINTiMINT-1795581.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 167Combined sources
Helixi20 – 234Combined sources
Helixi27 – 293Combined sources
Beta strandi33 – 397Combined sources
Helixi46 – 5712Combined sources
Helixi63 – 686Combined sources
Helixi70 – 9122Combined sources
Helixi100 – 11011Combined sources
Helixi111 – 1166Combined sources
Helixi121 – 13212Combined sources
Helixi134 – 1407Combined sources
Helixi141 – 1455Combined sources
Helixi152 – 1565Combined sources
Helixi159 – 1624Combined sources
Beta strandi164 – 1663Combined sources
Helixi171 – 1755Combined sources
Beta strandi183 – 1919Combined sources
Beta strandi194 – 2018Combined sources
Helixi205 – 21410Combined sources
Beta strandi219 – 2268Combined sources
Helixi227 – 2315Combined sources
Beta strandi237 – 2415Combined sources
Helixi242 – 25413Combined sources
Helixi257 – 2593Combined sources
Beta strandi262 – 2698Combined sources
Helixi271 – 2788Combined sources
Helixi283 – 2853Combined sources
Helixi296 – 30813Combined sources
Turni314 – 3163Combined sources
Beta strandi319 – 3235Combined sources
Helixi329 – 34618Combined sources
Helixi348 – 3503Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGRX-ray2.80A/D2-354[»]
1AS0X-ray2.00A2-354[»]
1AS2X-ray2.80A2-354[»]
1AS3X-ray2.40A2-354[»]
1BH2X-ray2.10A32-346[»]
1BOFX-ray2.20A2-354[»]
1CIPX-ray1.50A2-354[»]
1GDDX-ray2.20A2-354[»]
1GFIX-ray2.20A2-354[»]
1GG2X-ray2.40A2-354[»]
1GIAX-ray2.00A2-354[»]
1GILX-ray2.30A2-354[»]
1GITX-ray2.60A2-354[»]
1GP2X-ray2.30A2-354[»]
1SHZX-ray2.85A/D22-48[»]
A/D185-353[»]
1SVKX-ray2.00A2-354[»]
1SVSX-ray1.50A2-354[»]
2BCJX-ray3.06Q1-28[»]
2ZJYX-ray2.80A1-354[»]
2ZJZX-ray2.60A/B1-354[»]
3AH8X-ray2.90A2-28[»]
3D7MX-ray2.90A1-354[»]
3FFAX-ray2.30A1-348[»]
3FFBX-ray2.57A1-354[»]
3V00X-ray2.90A/B/C220-298[»]
4N0DX-ray1.55A1-354[»]
4N0EX-ray2.10A1-354[»]
4PAMX-ray2.10A1-354[»]
4PANX-ray2.40A1-354[»]
4PAOX-ray2.00A1-354[»]
4PAQX-ray2.00A1-354[»]
DisProtiDP00035.
ProteinModelPortaliP10824.
SMRiP10824. Positions 5-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10824.

Family & Domainsi

Sequence similaritiesi

Belongs to the G-alpha family. G(i/o/t/z) subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP10824.
KOiK04630.
PhylomeDBiP10824.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10824-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDAAR
110 120 130 140 150
ADDARQLFVL AGAAEEGFMT AELAGVIKRL WKDSGVQACF NRSREYQLND
160 170 180 190 200
SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK TTGIVETHFT FKDLHFKMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF
260 270 280 290 300
DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA
310 320 330 340 350
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD

CGLF
Length:354
Mass (Da):40,345
Last modified:January 23, 2007 - v3
Checksum:i99E9D11B485C2DE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17527 mRNA. Translation: AAA40825.1.
DQ120469 mRNA. Translation: AAZ23808.1.
DQ120470 mRNA. Translation: AAZ23809.1.
PIRiA35377.
C27423. RGRTI1.
RefSeqiNP_037277.1. NM_013145.1.
UniGeneiRn.11391.

Genome annotation databases

EnsembliENSRNOT00000091004; ENSRNOP00000074036; ENSRNOG00000057096.
GeneIDi25686.
KEGGirno:25686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17527 mRNA. Translation: AAA40825.1.
DQ120469 mRNA. Translation: AAZ23808.1.
DQ120470 mRNA. Translation: AAZ23809.1.
PIRiA35377.
C27423. RGRTI1.
RefSeqiNP_037277.1. NM_013145.1.
UniGeneiRn.11391.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGRX-ray2.80A/D2-354[»]
1AS0X-ray2.00A2-354[»]
1AS2X-ray2.80A2-354[»]
1AS3X-ray2.40A2-354[»]
1BH2X-ray2.10A32-346[»]
1BOFX-ray2.20A2-354[»]
1CIPX-ray1.50A2-354[»]
1GDDX-ray2.20A2-354[»]
1GFIX-ray2.20A2-354[»]
1GG2X-ray2.40A2-354[»]
1GIAX-ray2.00A2-354[»]
1GILX-ray2.30A2-354[»]
1GITX-ray2.60A2-354[»]
1GP2X-ray2.30A2-354[»]
1SHZX-ray2.85A/D22-48[»]
A/D185-353[»]
1SVKX-ray2.00A2-354[»]
1SVSX-ray1.50A2-354[»]
2BCJX-ray3.06Q1-28[»]
2ZJYX-ray2.80A1-354[»]
2ZJZX-ray2.60A/B1-354[»]
3AH8X-ray2.90A2-28[»]
3D7MX-ray2.90A1-354[»]
3FFAX-ray2.30A1-348[»]
3FFBX-ray2.57A1-354[»]
3V00X-ray2.90A/B/C220-298[»]
4N0DX-ray1.55A1-354[»]
4N0EX-ray2.10A1-354[»]
4PAMX-ray2.10A1-354[»]
4PANX-ray2.40A1-354[»]
4PAOX-ray2.00A1-354[»]
4PAQX-ray2.00A1-354[»]
DisProtiDP00035.
ProteinModelPortaliP10824.
SMRiP10824. Positions 5-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247715. 1 interaction.
DIPiDIP-6073N.
IntActiP10824. 2 interactions.
MINTiMINT-1795581.

PTM databases

iPTMnetiP10824.
PhosphoSiteiP10824.
SwissPalmiP10824.

2D gel databases

World-2DPAGE0004:P10824.

Proteomic databases

PRIDEiP10824.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000091004; ENSRNOP00000074036; ENSRNOG00000057096.
GeneIDi25686.
KEGGirno:25686.

Organism-specific databases

CTDi2770.
RGDi2713. Gnai1.

Phylogenomic databases

GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP10824.
KOiK04630.
PhylomeDBiP10824.

Enzyme and pathway databases

ReactomeiR-RNO-112043. PLC beta mediated events.
R-RNO-170670. Adenylate cyclase inhibitory pathway.
R-RNO-202040. G-protein activation.
R-RNO-392170. ADP signalling through P2Y purinoceptor 12.
R-RNO-400042. Adrenaline,noradrenaline inhibits insulin secretion.
R-RNO-418594. G alpha (i) signalling events.
SABIO-RKP10824.

Miscellaneous databases

EvolutionaryTraceiP10824.
NextBioi607673.
PROiP10824.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of five GTP-binding protein cDNA species from rat olfactory neuroepithelium."
    Jones D.T., Reed R.R.
    J. Biol. Chem. 262:14241-14249(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genetic similarity between spontaneously hypertensive rats and Wistar-Kyoto rats in the coding regions of signal transduction proteins."
    Jackson E.K., Zhu C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: SHR and Wistar Kyoto.
  3. "Activator of G protein signaling 3 is a guanine dissociation inhibitor for Galpha i subunits."
    de Vries L., Fischer T., Tronchere H., Brothers G.M., Strockbine B., Siderovski D.P., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 97:14364-14369(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPSM1.
  4. "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor activity."
    Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A., Gist Farquhar M., Siderovski D.P.
    J. Biol. Chem. 276:29275-29281(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RGS12 AND RGS14.
  5. "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization."
    Shu F.J., Ramineni S., Amyot W., Hepler J.R.
    Cell. Signal. 19:163-176(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RGS14, SUBCELLULAR LOCATION.
  6. "Localization of Gi alpha proteins in the centrosomes and at the midbody: implication for their role in cell division."
    Cho H., Kehrl J.H.
    J. Cell Biol. 178:245-255(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RGS14, MUTAGENESIS OF GLN-204.
  7. "Activation of the regulator of G protein signaling 14-Galphai1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A."
    Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G., Hepler J.R.
    Biochemistry 50:752-762(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RGS14 AND RIC8A, MUTAGENESIS OF ASN-149, SUBCELLULAR LOCATION.
  8. "Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis."
    Coleman D.E., Berghuis A.M., Lee E., Linder M.E., Gilman A.G., Sprang S.R.
    Science 265:1405-1412(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GDP.
  9. "The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2."
    Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A., Gilman A.G., Sprang S.R.
    Cell 83:1047-1058(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GNB1; GNG2 AND GDP, SUBUNIT.
  10. "Structure of RGS4 bound to AlF4-activated G(i alpha1): stabilization of the transition state for GTP hydrolysis."
    Tesmer J.J.G., Berman D.M., Gilman A.G., Sprang S.R.
    Cell 89:251-261(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RGS4 AND GDP, INTERACTION WITH RGS4.
  11. "Crystal structures of the G protein Gi alpha 1 complexed with GDP and Mg2+: a crystallographic titration experiment."
    Coleman D.E., Sprang S.R.
    Biochemistry 37:14376-14385(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GDP.
  12. "The A326S mutant of Gialpha1 as an approximation of the receptor-bound state."
    Posner B.A., Mixon M.B., Wall M.A., Sprang S.R., Gilman A.G.
    J. Biol. Chem. 273:21752-21758(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-346 IN COMPLEX WITH GDP AND MAGNESIUM.
  13. "Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins."
    Kapoor N., Menon S.T., Chauhan R., Sachdev P., Sakmar T.P.
    J. Mol. Biol. 393:882-897(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-348 OF MUTANT ALA-329 IN COMPLEXES WITH MAGNESIUM; GDP AND GTP ANALOG, FUNCTION, MUTAGENESIS OF GLN-204; THR-329 AND VAL-332.
  14. "A transient interaction between the phosphate binding loop and switch I contributes to the allosteric network between receptor and nucleotide in Galphai1."
    Thaker T.M., Sarwar M., Preininger A.M., Hamm H.E., Iverson T.M.
    J. Biol. Chem. 289:11331-11341(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH GDP AND GTP ANALOG, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH GNB1 AND GNG1, MUTAGENESIS OF GLU-43 AND LYS-345.
  15. "A conserved phenylalanine as a relay between the alpha5 helix and the GDP binding region of heterotrimeric Gi protein alpha subunit."
    Kaya A.I., Lokits A.D., Gilbert J.A., Iverson T.M., Meiler J., Hamm H.E.
    J. Biol. Chem. 289:24475-24487(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF WILD-TYPE AND MUTANTS CYS-336 AND TYR-336 IN COMPLEXES WITH MAGNESIUM; GDP AND GTP ANALOG, FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-189; PHE-191 AND PHE-336.

Entry informationi

Entry nameiGNAI1_RAT
AccessioniPrimary (citable) accession number: P10824
Secondary accession number(s): Q45QN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.