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P63096 (GNAI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-1
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
Gene names
Name:GNAI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. 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. May play a role in cell division. Ref.12 Ref.18

Subunit structure

Interacts with GPSM1. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains); the interaction occurs in the centrosomes. Interacts (GDP-bound form) with RIC8A (via C-terminus) By similarity. Interacts with DRD2. G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Ref.18

Subcellular location

Nucleus By similarity. Cytoplasm. Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane By similarity. Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow or the midbody. Ref.12

Sequence similarities

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMADP-ribosylation
Lipoprotein
Myristate
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from mutant phenotype Ref.12. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

response to peptide hormone

Inferred from sequence or structural similarity. Source: BHF-UCL

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcentrosome

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

extrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

midbody

Inferred from direct assay Ref.12. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionG-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

G-protein coupled serotonin receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTP binding

Inferred from sequence or structural similarity. Source: BHF-UCL

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

signal transducer activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GPSM2P812743EBI-618639,EBI-618655
NUMA1Q149804EBI-618639,EBI-521611

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P63096-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P63096-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 354353Guanine nucleotide-binding protein G(i) subunit alpha-1
PRO_0000203671

Regions

Nucleotide binding40 – 478GTP
Nucleotide binding175 – 1817GTP By similarity
Nucleotide binding200 – 2045GTP
Nucleotide binding269 – 2724GTP

Sites

Metal binding471Magnesium By similarity
Metal binding1811Magnesium By similarity
Binding site3261GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue1781ADP-ribosylarginine; by cholera toxin By similarity
Modified residue3511ADP-ribosylcysteine; by pertussis toxin By similarity
Lipidation21N-myristoyl glycine Ref.13
Lipidation31S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence1 – 5252Missing in isoform 2.
VSP_045215

Experimental info

Mutagenesis1161E → L: Enhances interaction (inactive GDP-bound) with RGS14. Ref.17 Ref.20
Mutagenesis1471Q → L: Enhances interaction (inactive GDP-bound) with RGS14. Ref.17 Ref.20
Mutagenesis2451E → L: Enhances interaction (inactive GDP-bound) with RGS14. Ref.20
Sequence conflict1381A → G in CAB43212. Ref.3
Sequence conflict2191T → A in AAH26326. Ref.8
Sequence conflict2441H → Y in AAV38580. Ref.4
Sequence conflict2491L → M in AAV38580. Ref.4
Sequence conflict2881P → Q in AAH26326. Ref.8

Secondary structure

.............................................................. 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9F88311B46E62DE3

FASTA35440,361
        10         20         30         40         50         60 
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG 

        70         80         90        100        110        120 
YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR ADDARQLFVL AGAAEEGFMT 

       130        140        150        160        170        180 
AELAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK 

       190        200        210        220        230        240 
TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM 

       250        260        270        280        290        300 
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA 

       310        320        330        340        350 
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF 

« Hide

Isoform 2 [UniParc].

Checksum: DA5ED62E61B790A9
Show »

FASTA30234,775

References

« Hide 'large scale' references
[1]"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] (ISOFORM 1).
[2]Yu W., Gibbs R.A.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Trachea.
[6]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Brain.
[9]"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] OF 1-101.
[10]"Human cDNA clones for an alpha subunit of Gi signal-transduction protein."
Bray P., Carter A., Guo V., Puckett C., Kamholz J., Spiegel A., Nirenberg M.
Proc. Natl. Acad. Sci. U.S.A. 84:5115-5119(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-354.
[11]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 91-100 AND 162-176.
Tissue: Adipocyte.
[12]"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.
[13]"Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits."
Kimple R.J., Kimple M.E., Betts L., Sondek J., Siderovski D.P.
Nature 416:878-881(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-349 IN COMPLEX WITH RGS14 AND GDP.
[16]"Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange."
Johnston C.A., Willard F.S., Jezyk M.R., Fredericks Z., Bodor E.T., Jones M.B., Blaesius R., Watts V.J., Harden T.K., Sondek J., Ramer J.K., Siderovski D.P.
Structure 13:1069-1080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-354 IN COMPLEX WITH GDP.
[17]"Structure-based protocol for identifying mutations that enhance protein-protein binding affinities."
Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P., Kuhlman B.
J. Mol. Biol. 371:1392-1404(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 31-354, MUTAGENESIS OF GLU-116 AND GLN-147.
[18]"Structural basis for nucleotide exchange on G alpha i subunits and receptor coupling specificity."
Johnston C.A., Siderovski D.P.
Proc. Natl. Acad. Sci. U.S.A. 104:2001-2006(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH DRD2 AND GDP, FUNCTION, INTERACTION WITH DRD2.
[19]Erratum
Johnston C.A., Siderovski D.P.
Proc. Natl. Acad. Sci. U.S.A. 109:1808-1808(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: RETRACTION.
[20]"Structural determinants of affinity enhancement between GoLoco motifs and G-protein alpha subunit mutants."
Bosch D.E., Kimple A.J., Sammond D.W., Muller R.E., Miley M.J., Machius M., Kuhlman B., Willard F.S., Siderovski D.P.
J. Biol. Chem. 286:3351-3358(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 31-354 IN COMPLEX WITH RGS14 AND GDP, MUTAGENESIS OF GLU-116; GLN-147 AND GLU-245.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF493905 mRNA. Translation: AAM12619.1.
AF055013 mRNA. Translation: AAC09361.1.
AL049933 mRNA. Translation: CAB43212.2.
BT019775 mRNA. Translation: AAV38580.1.
AK292953 mRNA. Translation: BAF85642.1.
AK304442 mRNA. Translation: BAG65263.1.
AC004159 Genomic DNA. No translation available.
AC080066 Genomic DNA. No translation available.
CH471091 Genomic DNA. Translation: EAW77011.1.
BC026326 mRNA. Translation: AAH26326.1.
M20596, M20594, M20595 Genomic DNA. Translation: AAA35893.1.
M17219 mRNA. Translation: AAA52581.1.
PIRRGHUI1. A28318.
RefSeqNP_001243343.1. NM_001256414.1.
NP_002060.4. NM_002069.5.
UniGeneHs.134587.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KJYX-ray2.70A/C31-354[»]
1Y3AX-ray2.50A/B/C/D26-354[»]
2G83X-ray2.80A/B33-344[»]
2GTPX-ray2.55A/B32-353[»]
2IK8X-ray2.71A/C31-353[»]
2OM2X-ray2.20A/C31-354[»]
2PZ3X-ray2.42A1-354[»]
2XNSX-ray3.41A/B30-354[»]
3ONWX-ray2.38A/B31-354[»]
3QE0X-ray3.00A/B/C33-354[»]
3QI2X-ray2.80A/B31-354[»]
3UMRX-ray2.24A1-354[»]
3UMSX-ray2.60A1-354[»]
4G5QX-ray2.90A/B/C/D25-354[»]
ProteinModelPortalP63096.
SMRP63096. Positions 5-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109032. 48 interactions.
IntActP63096. 19 interactions.
MINTMINT-2913925.
STRING9606.ENSP00000343027.

Chemistry

BindingDBP63096.
ChEMBLCHEMBL4741.

PTM databases

PhosphoSiteP63096.

Polymorphism databases

DMDM52000964.

Proteomic databases

PaxDbP63096.
PRIDEP63096.

Protocols and materials databases

DNASU2770.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351004; ENSP00000343027; ENSG00000127955. [P63096-1]
ENST00000457358; ENSP00000410572; ENSG00000127955. [P63096-2]
GeneID2770.
KEGGhsa:2770.
UCSCuc003uhb.1. human. [P63096-1]

Organism-specific databases

CTD2770.
GeneCardsGC07P079763.
HGNCHGNC:4384. GNAI1.
HPACAB022449.
MIM139310. gene.
neXtProtNX_P63096.
PharmGKBPA172.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322962.
HOVERGENHBG063184.
InParanoidP63096.
KOK04630.
OMAFFTHASA.
PhylomeDBP63096.
TreeFamTF300673.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13685. Neuronal System.
REACT_604. Hemostasis.
SignaLinkP63096.

Gene expression databases

ArrayExpressP63096.
BgeeP63096.
CleanExHS_GNAI1.
GenevestigatorP63096.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP63096.
GeneWikiGNAI1.
GenomeRNAi2770.
NextBio10896.
PROP63096.
SOURCESearch...

Entry information

Entry nameGNAI1_HUMAN
AccessionPrimary (citable) accession number: P63096
Secondary accession number(s): A8KA88 expand/collapse secondary AC list , B4E2V1, C9J3A4, P04898, P11015, P31871, Q5U074, Q8TAN5, Q9UGA4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM