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P08752 (GNAI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-2
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
Gene names
Name:Gnai2
Synonyms:Gnai-2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length355 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. May play a role in cell division.

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UNC5B. Interacts with GPSM1. Interacts with RGS12 and RGS14 By similarity.

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cell membrane By similarity. Note: Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody By similarity.

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
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMLipoprotein
Myristate
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled acetylcholine receptor signaling pathway

Inferred from mutant phenotype PubMed 11299198. Source: MGI

activation of MAPKK activity

Inferred from electronic annotation. Source: Ensembl

adenosine receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 8622915. Source: MGI

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from sequence or structural similarity. Source: UniProtKB

cell proliferation

Inferred from physical interaction PubMed 14712229. Source: MGI

gamma-aminobutyric acid signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of synaptic transmission

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

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

membrane raft

Inferred from electronic annotation. Source: Ensembl

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionG-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

G-protein coupled receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTP binding

Inferred from sequence alignment Ref.1. Source: MGI

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 8076637. Source: MGI

signal transducer activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 355354Guanine nucleotide-binding protein G(i) subunit alpha-2
PRO_0000203681

Regions

Nucleotide binding40 – 478GTP By similarity
Nucleotide binding176 – 1827GTP By similarity
Nucleotide binding201 – 2055GTP By similarity
Nucleotide binding270 – 2734GTP By similarity

Sites

Metal binding471Magnesium By similarity
Metal binding1821Magnesium By similarity
Binding site3271GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity

Experimental info

Sequence conflict821M → I in AAB30632. Ref.4
Sequence conflict821M → L in AAA37692. Ref.1
Sequence conflict871A → R in AAA37692. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P08752 [UniParc].

Last modified July 27, 2011. Version 5.
Checksum: 90AC64AFA713493E

FASTA35540,489
        10         20         30         40         50         60 
MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG 

        70         80         90        100        110        120 
YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPQR ADDARQLFAL SCAAEEQGML 

       130        140        150        160        170        180 
PEDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV 

       190        200        210        220        230        240 
KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE 

       250        260        270        280        290        300 
MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT QSSLTICFPE YTGANKYDEA 

       310        320        330        340        350 
ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF 

« Hide

References

« Hide 'large scale' references
[1]"Inhibitory and stimulatory G proteins of adenylate cyclase: cDNA and amino acid sequences of the alpha chains."
Sullivan K.A., Liao Y.-C., Alborzi A., Beiderman B., Chang F.-H., Masters S.B., Levinson A.D., Bourne H.R.
Proc. Natl. Acad. Sci. U.S.A. 83:6687-6691(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Inner ear and Placenta.
[3]"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].
Strain: C57BL/6.
Tissue: Brain.
[4]"G protein Gi2 alpha in the cochlea: cloning and selective occurrence in receptor cells."
Tachibana M., Asano T., Wilcox E., Yokotani N., Rivolta M.N., Fex J.
Brain Res. Mol. Brain Res. 21:355-358(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-355.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 36-46; 55-67; 146-162; 182-193; 199-206; 250-258; 279-296 AND 319-331, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13963 mRNA. Translation: AAA37692.1.
AK157998 mRNA. Translation: BAE34308.1.
AK159222 mRNA. Translation: BAE34909.1.
AK167388 mRNA. Translation: BAE39478.1.
BC065159 mRNA. Translation: AAH65159.1.
S71213 mRNA. Translation: AAB30632.2.
CCDSCCDS23502.1.
PIRRGMSI2. B25889.
RefSeqNP_032164.2. NM_008138.4.
XP_006511700.1. XM_006511637.1.
UniGeneMm.196464.

3D structure databases

ProteinModelPortalP08752.
SMRP08752. Positions 5-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199967. 2 interactions.
DIPDIP-605N.
IntActP08752. 6 interactions.
MINTMINT-4096273.
STRING10090.ENSMUSP00000057543.

PTM databases

PhosphoSiteP08752.

Proteomic databases

MaxQBP08752.
PaxDbP08752.
PRIDEP08752.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055704; ENSMUSP00000057543; ENSMUSG00000032562.
GeneID14678.
KEGGmmu:14678.
UCSCuc009rml.1. mouse.

Organism-specific databases

CTD2771.
MGIMGI:95772. Gnai2.

Phylogenomic databases

eggNOGNOG322962.
GeneTreeENSGT00690000101958.
HOGENOMHOG000038730.
HOVERGENHBG063184.
InParanoidQ3TXK7.
KOK04630.
OMAEYAGANK.
OrthoDBEOG72C50B.
TreeFamTF300673.

Gene expression databases

ArrayExpressP08752.
BgeeP08752.
GenevestigatorP08752.

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

ChiTaRSGNAI2. mouse.
NextBio286578.
PROP08752.
SOURCESearch...

Entry information

Entry nameGNAI2_MOUSE
AccessionPrimary (citable) accession number: P08752
Secondary accession number(s): Q3TXK7, Q6P1C0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 141 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot