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P08752

- GNAI2_MOUSE

UniProt

P08752 - GNAI2_MOUSE

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Protein

Guanine nucleotide-binding protein G(i) subunit alpha-2

Gene

Gnai2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471MagnesiumBy similarity
Metal bindingi182 – 1821MagnesiumBy similarity
Binding sitei327 – 3271GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 478GTPBy similarity
Nucleotide bindingi176 – 1827GTPBy similarity
Nucleotide bindingi201 – 2055GTPBy similarity
Nucleotide bindingi270 – 2734GTPBy similarity

GO - Molecular functioni

  1. G-protein beta/gamma-subunit complex binding Source: RefGenome
  2. G-protein coupled receptor binding Source: RefGenome
  3. GTPase activity Source: RefGenome
  4. GTP binding Source: MGI
  5. metal ion binding Source: UniProtKB-KW
  6. signal transducer activity Source: RefGenome

GO - Biological processi

  1. activation of MAPKK activity Source: Ensembl
  2. adenosine receptor signaling pathway Source: RefGenome
  3. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: MGI
  4. cell cycle Source: UniProtKB-KW
  5. cell division Source: UniProtKB
  6. cell proliferation Source: MGI
  7. gamma-aminobutyric acid signaling pathway Source: RefGenome
  8. G-protein coupled acetylcholine receptor signaling pathway Source: MGI
  9. negative regulation of synaptic transmission Source: Ensembl
  10. positive regulation of cell proliferation Source: Ensembl
  11. regulation of calcium ion transport 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

ReactomeiREACT_205726. G-protein activation.
REACT_222824. Adenylate cyclase inhibitory pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-2
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
Gene namesi
Name:Gnai2
Synonyms:Gnai-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:95772. Gnai2.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. heterotrimeric G-protein complex Source: RefGenome
  6. membrane raft Source: Ensembl
  7. midbody Source: UniProtKB
  8. nucleus Source: Ensembl
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 355354Guanine nucleotide-binding protein G(i) subunit alpha-2PRO_0000203681Add
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

MaxQBiP08752.
PaxDbiP08752.
PRIDEiP08752.

PTM databases

PhosphoSiteiP08752.

Expressioni

Gene expression databases

BgeeiP08752.
ExpressionAtlasiP08752. baseline and differential.
GenevestigatoriP08752.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi199967. 2 interactions.
DIPiDIP-605N.
IntActiP08752. 6 interactions.
MINTiMINT-4096273.
STRINGi10090.ENSMUSP00000057543.

Structurei

3D structure databases

ProteinModelPortaliP08752.
SMRiP08752. Positions 5-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322962.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038730.
HOVERGENiHBG063184.
InParanoidiP08752.
KOiK04630.
OMAiEYAGANK.
OrthoDBiEOG72C50B.
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.

P08752 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEDG YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPQR
110 120 130 140 150
ADDARQLFAL SCAAEEQGML PEDLSGVIRR LWADHGVQAC FGRSREYQLN
160 170 180 190 200
DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV KTTGIVETHF TFKDLHFKMF
210 220 230 240 250
DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE MNRMHESMKL
260 270 280 290 300
FDSICNNKWF TDTSIILFLN KKDLFEEKIT QSSLTICFPE YTGANKYDEA
310 320 330 340 350
ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK

DCGLF
Length:355
Mass (Da):40,489
Last modified:July 27, 2011 - v5
Checksum:i90AC64AFA713493E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821M → I in AAB30632. (PubMed:8170357)Curated
Sequence conflicti82 – 821M → L in AAA37692. (PubMed:3092218)Curated
Sequence conflicti87 – 871A → R in AAA37692. (PubMed:3092218)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS23502.1.
PIRiB25889. RGMSI2.
RefSeqiNP_032164.2. NM_008138.4.
XP_006511700.1. XM_006511637.1.
UniGeneiMm.196464.

Genome annotation databases

EnsembliENSMUST00000055704; ENSMUSP00000057543; ENSMUSG00000032562.
GeneIDi14678.
KEGGimmu:14678.
UCSCiuc009rml.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS23502.1.
PIRi B25889. RGMSI2.
RefSeqi NP_032164.2. NM_008138.4.
XP_006511700.1. XM_006511637.1.
UniGenei Mm.196464.

3D structure databases

ProteinModelPortali P08752.
SMRi P08752. Positions 5-354.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199967. 2 interactions.
DIPi DIP-605N.
IntActi P08752. 6 interactions.
MINTi MINT-4096273.
STRINGi 10090.ENSMUSP00000057543.

PTM databases

PhosphoSitei P08752.

Proteomic databases

MaxQBi P08752.
PaxDbi P08752.
PRIDEi P08752.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000055704 ; ENSMUSP00000057543 ; ENSMUSG00000032562 .
GeneIDi 14678.
KEGGi mmu:14678.
UCSCi uc009rml.1. mouse.

Organism-specific databases

CTDi 2771.
MGIi MGI:95772. Gnai2.

Phylogenomic databases

eggNOGi NOG322962.
GeneTreei ENSGT00760000118851.
HOGENOMi HOG000038730.
HOVERGENi HBG063184.
InParanoidi P08752.
KOi K04630.
OMAi EYAGANK.
OrthoDBi EOG72C50B.
TreeFami TF300673.

Enzyme and pathway databases

Reactomei REACT_205726. G-protein activation.
REACT_222824. Adenylate cyclase inhibitory pathway.

Miscellaneous databases

ChiTaRSi GNAI2. mouse.
NextBioi 286578.
PROi P08752.
SOURCEi Search...

Gene expression databases

Bgeei P08752.
ExpressionAtlasi P08752. baseline and differential.
Genevestigatori P08752.

Family and domain databases

Gene3Di 1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10218. PTHR10218. 1 hit.
Pfami PF00503. G-alpha. 1 hit.
[Graphical view ]
PRINTSi PR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTi SM00275. G_alpha. 1 hit.
[Graphical view ]
SUPFAMi SSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGNAI2_MOUSE
AccessioniPrimary (citable) accession number: P08752
Secondary accession number(s): Q3TXK7, Q6P1C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 144 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3