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Protein

Guanine nucleotide-binding protein G(k) subunit alpha

Gene

GNAI3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heterotrimeric 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. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:8774883, PubMed:18434541, PubMed:19478087). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:19478087). Stimulates the activity of receptor-regulated K+ channels (PubMed:2535845). The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division (PubMed:17635935).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumCombined sources1 Publication
Metal bindingi181 – 1811MagnesiumCombined sources1 Publication
Binding sitei326 – 3261GTP; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 486GTPCombined sources
Nucleotide bindingi150 – 1512GTPCombined sources
Nucleotide bindingi175 – 1817GTPCombined sources
Nucleotide bindingi200 – 2045GTPCombined sources1 Publication
Nucleotide bindingi269 – 2724GTPCombined sources

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • G-protein beta/gamma-subunit complex binding Source: GO_Central
  • G-protein coupled receptor binding Source: GO_Central
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • signal transducer activity Source: GO_Central

GO - Biological processi

  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: UniProtKB
  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: GO_Central
  • blood coagulation Source: Reactome
  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB
  • dopamine receptor signaling pathway Source: UniProtKB
  • GTP metabolic process Source: UniProtKB
  • negative regulation of adenylate cyclase activity Source: ProtInc
  • platelet activation Source: Reactome
  • synaptic transmission Source: Reactome
  • transport Source: ProtInc
  • vesicle fusion Source: Ensembl
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-HSA-112043. PLC beta mediated events.
R-HSA-170670. Adenylate cyclase inhibitory pathway.
R-HSA-202040. G-protein activation.
R-HSA-392170. ADP signalling through P2Y purinoceptor 12.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-418597. G alpha (z) signalling events.
SignaLinkiP08754.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(k) subunit alpha1 Publication
Alternative name(s):
G(i) alpha-3
Gene namesi
Name:GNAI3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4387. GNAI3.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell membrane 1 Publication
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
  • Membrane Curated; Lipid-anchor Curated

  • Note: Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody.1 Publication

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • heterotrimeric G-protein complex Source: GO_Central
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • membrane raft Source: Ensembl
  • midbody Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • zymogen granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Auriculocondylar syndrome 1 (ARCND1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant craniofacial malformation syndrome characterized by variable mandibular anomalies, including mild to severe micrognathia, temporomandibular joint ankylosis, cleft palate, and a characteristic ear malformation that consists of separation of the lobule from the external ear, giving the appearance of a question mark (question-mark ear). Other frequently described features include prominent cheeks, cupped and posteriorly rotated ears, preauricular tags, and microstomia.
See also OMIM:602483
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401G → R in ARCND1. 1 Publication
VAR_068558

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiGNAI3.
MIMi602483. phenotype.
Orphaneti137888. Auriculocondylar syndrome.
PharmGKBiPA173.

Chemistry

ChEMBLiCHEMBL4221.

Polymorphism and mutation databases

BioMutaiGNAI3.
DMDMi120996.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 354353Guanine nucleotide-binding protein G(k) subunit alphaPRO_0000203692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Lipidationi3 – 31S-palmitoyl cysteineBy similarity
Modified residuei178 – 1781ADP-ribosylarginine; by cholera toxinBy similarity
Modified residuei204 – 2041Deamidated glutamine; by Photorhabdus PAU_022301 Publication
Modified residuei351 – 3511ADP-ribosylcysteine; by pertussis toxinBy similarity

Post-translational modificationi

(Microbial infection) Deamidated at Gln-204 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA.1 Publication

Keywords - PTMi

ADP-ribosylation, Lipoprotein, Myristate, Palmitate

Proteomic databases

EPDiP08754.
PaxDbiP08754.
PeptideAtlasiP08754.
PRIDEiP08754.

PTM databases

iPTMnetiP08754.
PhosphoSiteiP08754.
SwissPalmiP08754.

Expressioni

Gene expression databases

BgeeiP08754.
CleanExiHS_GNAI3.
GenevisibleiP08754. HS.

Organism-specific databases

HPAiCAB022099.

Interactioni

Subunit structurei

Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha subunit contains the guanine nucleotide binding site. GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins. Interacts with GPSM1 (By similarity). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains) (PubMed:22952234). Does not interact with RGS2 (PubMed:19478087). Interacts with RGS8 and RGS10; this strongly enhances the intrinsic GTPase activity (PubMed:8774883, PubMed:18434541). Interacts with RGS16; this strongly enhances the intrinsic GTPase activity (PubMed:19478087). Interacts with RGS12 (By similarity). Interacts (via active GTP- or inactive GDP-bound form) with RGS14 (By similarity).By similarityCurated3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GPSM3Q9Y4H43EBI-357563,EBI-347538
RGS17Q9UGC63EBI-357563,EBI-3918154

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109035. 93 interactions.
IntActiP08754. 29 interactions.
MINTiMINT-1146232.
STRINGi9606.ENSP00000358867.

Chemistry

BindingDBiP08754.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 396Combined sources
Helixi46 – 5712Combined sources
Helixi63 – 686Combined sources
Helixi70 – 9122Combined sources
Helixi100 – 11011Combined sources
Turni111 – 1166Combined sources
Helixi121 – 13111Combined sources
Helixi134 – 1418Combined sources
Helixi142 – 1454Combined sources
Helixi152 – 1576Combined sources
Helixi159 – 1624Combined 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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IHBX-ray2.71A32-354[»]
2ODEX-ray1.90A/C4-350[»]
2V4ZX-ray2.80A4-350[»]
4G5OX-ray2.90A/B/C/D25-354[»]
4G5RX-ray3.48A/B/C/D25-354[»]
4G5SX-ray3.62A/B/C/D25-354[»]
ProteinModelPortaliP08754.
SMRiP08754. Positions 5-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08754.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP08754.
KOiK04630.
OMAiISQINYI.
OrthoDBiEOG72C50B.
PhylomeDBiP08754.
TreeFamiTF300673.

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.

P08754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEDG YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEAAR
110 120 130 140 150
ADDARQLFVL AGSAEEGVMT PELAGVIKRL WRDGGVQACF SRSREYQLND
160 170 180 190 200
SASYYLNDLD RISQSNYIPT QQDVLRTRVK TTGIVETHFT FKDLYFKMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF
260 270 280 290 300
DSICNNKWFT ETSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA
310 320 330 340 350
AYIQCQFEDL NRRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKE

CGLY
Length:354
Mass (Da):40,532
Last modified:January 23, 2007 - v3
Checksum:iEAB6B4DD3646BC01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211R → C no nucleotide entry (PubMed:2440724).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401G → R in ARCND1. 1 Publication
VAR_068558

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27543 mRNA. Translation: AAA52579.1.
J03005 mRNA. Translation: AAA52557.1.
M20604
, M20597, M20598, M20599, M20600, M20601, M20602, M20603 Genomic DNA. Translation: AAA35895.1.
J03198 mRNA. Translation: AAA35896.1.
J03238 mRNA. Translation: AAA35939.1.
AF493907 mRNA. Translation: AAM12621.1.
BT019973 mRNA. Translation: AAV38776.1.
BT019974 mRNA. Translation: AAV38777.1.
AK312252 mRNA. Translation: BAG35184.1.
CH471122 Genomic DNA. Translation: EAW56393.1.
BC025285 mRNA. Translation: AAH25285.1.
CCDSiCCDS802.1.
PIRiS02348. RGHUI3.
RefSeqiNP_006487.1. NM_006496.3.
UniGeneiHs.73799.
Hs.741171.

Genome annotation databases

EnsembliENST00000369851; ENSP00000358867; ENSG00000065135.
GeneIDi2773.
KEGGihsa:2773.
UCSCiuc001dxz.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27543 mRNA. Translation: AAA52579.1.
J03005 mRNA. Translation: AAA52557.1.
M20604
, M20597, M20598, M20599, M20600, M20601, M20602, M20603 Genomic DNA. Translation: AAA35895.1.
J03198 mRNA. Translation: AAA35896.1.
J03238 mRNA. Translation: AAA35939.1.
AF493907 mRNA. Translation: AAM12621.1.
BT019973 mRNA. Translation: AAV38776.1.
BT019974 mRNA. Translation: AAV38777.1.
AK312252 mRNA. Translation: BAG35184.1.
CH471122 Genomic DNA. Translation: EAW56393.1.
BC025285 mRNA. Translation: AAH25285.1.
CCDSiCCDS802.1.
PIRiS02348. RGHUI3.
RefSeqiNP_006487.1. NM_006496.3.
UniGeneiHs.73799.
Hs.741171.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IHBX-ray2.71A32-354[»]
2ODEX-ray1.90A/C4-350[»]
2V4ZX-ray2.80A4-350[»]
4G5OX-ray2.90A/B/C/D25-354[»]
4G5RX-ray3.48A/B/C/D25-354[»]
4G5SX-ray3.62A/B/C/D25-354[»]
ProteinModelPortaliP08754.
SMRiP08754. Positions 5-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109035. 93 interactions.
IntActiP08754. 29 interactions.
MINTiMINT-1146232.
STRINGi9606.ENSP00000358867.

Chemistry

BindingDBiP08754.
ChEMBLiCHEMBL4221.

PTM databases

iPTMnetiP08754.
PhosphoSiteiP08754.
SwissPalmiP08754.

Polymorphism and mutation databases

BioMutaiGNAI3.
DMDMi120996.

Proteomic databases

EPDiP08754.
PaxDbiP08754.
PeptideAtlasiP08754.
PRIDEiP08754.

Protocols and materials databases

DNASUi2773.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369851; ENSP00000358867; ENSG00000065135.
GeneIDi2773.
KEGGihsa:2773.
UCSCiuc001dxz.4. human.

Organism-specific databases

CTDi2773.
GeneCardsiGNAI3.
HGNCiHGNC:4387. GNAI3.
HPAiCAB022099.
MalaCardsiGNAI3.
MIMi139370. gene.
602483. phenotype.
neXtProtiNX_P08754.
Orphaneti137888. Auriculocondylar syndrome.
PharmGKBiPA173.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0082. Eukaryota.
ENOG410XNVQ. LUCA.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP08754.
KOiK04630.
OMAiISQINYI.
OrthoDBiEOG72C50B.
PhylomeDBiP08754.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiR-HSA-112043. PLC beta mediated events.
R-HSA-170670. Adenylate cyclase inhibitory pathway.
R-HSA-202040. G-protein activation.
R-HSA-392170. ADP signalling through P2Y purinoceptor 12.
R-HSA-418555. G alpha (s) signalling events.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-418597. G alpha (z) signalling events.
SignaLinkiP08754.

Miscellaneous databases

ChiTaRSiGNAI3. human.
EvolutionaryTraceiP08754.
GeneWikiiGNAI3.
GenomeRNAii2773.
NextBioi10906.
PROiP08754.
SOURCEiSearch...

Gene expression databases

BgeeiP08754.
CleanExiHS_GNAI3.
GenevisibleiP08754. HS.

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

« Hide 'large scale' publications
  1. "Molecular cloning of a new human G protein. Evidence for two Gi alpha-like protein families."
    Didsbury J.R., Snyderman R.
    FEBS Lett. 219:259-263(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A small multigene family encodes Gi signal-transduction proteins."
    Beals C.R., Wilson C.B., Perlmutter R.M.
    Proc. Natl. Acad. Sci. U.S.A. 84:7886-7890(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs."
    Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.
    J. Biol. Chem. 263:6656-6664(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Alpha i-3 cDNA encodes the alpha subunit of Gk, the stimulatory G protein of receptor-regulated K+ channels."
    Codina J., Olate J., Abramowitz J., Mattera R., Cook R.G., Birnbaumer L.
    J. Biol. Chem. 263:6746-6750(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Identification of cDNA encoding an additional alpha subunit of a human GTP-binding protein: expression of three alpha i subtypes in human tissues and cell lines."
    Kim S., Ang S.L., Bloch D.B., Bloch K.D., Kawahara Y., Tolman C., Lee R., Seidman J.G., Neer E.J.
    Proc. Natl. Acad. Sci. U.S.A. 85:4153-4157(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  11. "The human genome encodes at least three non-allelic G proteins with alpha i-type subunits."
    Suki W.N., Abramowitz J., Mattera R., Codina J., Birnbaumer L.
    FEBS Lett. 220:187-192(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-354.
  12. "Recombinant alpha i-3 subunit of G protein activates Gk-gated K+ channels."
    Mattera R., Yatani A., Kirsch G.E., Graf R., Okabe K., Olate J., Codina J., Brown A.M., Birnbaumer L.
    J. Biol. Chem. 264:465-471(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "RGS10 is a selective activator of G alpha i GTPase activity."
    Hunt T.W., Fields T.A., Casey P.J., Peralta E.G.
    Nature 383:175-177(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RGS10.
  14. "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.
  15. "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: FUNCTION, SUBCELLULAR LOCATION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins."
    Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E., Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C., Aktories K.
    Nat. Struct. Mol. Biol. 20:1273-1280(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEAMIDATION AT GLN-204 (MICROBIAL INFECTION).
  18. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-350 IN COMPLEX WITH GDP AND RGS10, FUNCTION, INTERACTION WITH RGS8 AND RGS10.
  21. "Structural determinants of G-protein alpha subunit selectivity by regulator of G-protein signaling 2 (RGS2)."
    Kimple A.J., Soundararajan M., Hutsell S.Q., Roos A.K., Urban D.J., Setola V., Temple B.R., Roth B.L., Knapp S., Willard F.S., Siderovski D.P.
    J. Biol. Chem. 284:19402-19411(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 4-350 IN COMPLEX WITH RGS2; MAGNESIUM AND GDP, LACK OF INTERACTION WITH RGS2, INTERACTION WITH RGS16, FUNCTION.
  22. "Crystal structures of the scaffolding protein LGN reveal the general mechanism by which GoLoco binding motifs inhibit the release of GDP from Galphai."
    Jia M., Li J., Zhu J., Wen W., Zhang M., Wang W.
    J. Biol. Chem. 287:36766-36776(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 25-354 IN COMPLEX WITH GPSM2 AND GDP, INTERACTION WITH GPSM2.
  23. Cited for: VARIANT ARCND1 ARG-40.

Entry informationi

Entry nameiGNAI3_HUMAN
AccessioniPrimary (citable) accession number: P08754
Secondary accession number(s): P17539, Q5TZX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 189 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.