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P21279

- GNAQ_MOUSE

UniProt

P21279 - GNAQ_MOUSE

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Protein
Guanine nucleotide-binding protein G(q) subunit alpha
Gene
Gnaq
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. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Magnesium By similarity
Metal bindingi186 – 1861Magnesium By similarity
Binding sitei331 – 3311GTP; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 538GTP By similarity
Nucleotide bindingi180 – 1867GTP By similarity
Nucleotide bindingi205 – 2095GTP By similarity
Nucleotide bindingi274 – 2774GTP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: MGI
  2. action potential Source: MGI
  3. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
  4. developmental pigmentation Source: MGI
  5. embryonic digit morphogenesis Source: MGI
  6. forebrain neuron development Source: MGI
  7. glutamate receptor signaling pathway Source: MGI
  8. heart development Source: MGI
  9. maternal behavior Source: MGI
  10. negative regulation of protein kinase activity Source: Ensembl
  11. neuron remodeling Source: MGI
  12. phospholipase C-activating dopamine receptor signaling pathway Source: MGI
  13. post-embryonic development Source: MGI
  14. protein stabilization Source: Ensembl
  15. regulation of catenin import into nucleus Source: Ensembl
  16. regulation of melanocyte differentiation Source: MGI
  17. skeletal system development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(q) subunit alpha
Alternative name(s):
Guanine nucleotide-binding protein alpha-q
Gene namesi
Name:Gnaq
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:95776. Gnaq.

Subcellular locationi

Nucleus. Membrane. Nucleus membrane
Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes.1 Publication

GO - Cellular componenti

  1. extrinsic component of cytoplasmic side of plasma membrane Source: RefGenome
  2. heterotrimeric G-protein complex Source: RefGenome
  3. lysosomal membrane Source: Ensembl
  4. membrane Source: MGI
  5. nuclear membrane Source: UniProtKB-SubCell
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91C → S: Abolishes palmitoylation. 1 Publication
Mutagenesisi10 – 101C → S: Abolishes palmitoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Guanine nucleotide-binding protein G(q) subunit alpha
PRO_0000203761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi9 – 91S-palmitoyl cysteine1 Publication
Lipidationi10 – 101S-palmitoyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiP21279.
PaxDbiP21279.
PRIDEiP21279.

PTM databases

PhosphoSiteiP21279.

Expressioni

Gene expression databases

ArrayExpressiP21279.
BgeeiP21279.
GenevestigatoriP21279.

Interactioni

Subunit structurei

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Binds SLC9A3R1. Forms a complex with PECAM1 and BDKRB2. Interacts with PECAM1 By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
AipO089152EBI-771975,EBI-6935014

Protein-protein interaction databases

BioGridi199971. 2 interactions.
DIPiDIP-606N.
IntActiP21279. 5 interactions.
MINTiMINT-4096294.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 457
Beta strandi47 – 515
Helixi52 – 6312
Helixi69 – 735
Helixi76 – 9621
Helixi105 – 11410
Helixi118 – 1203
Helixi128 – 1369
Helixi139 – 1468
Helixi147 – 1504
Helixi157 – 1615
Helixi164 – 1685
Helixi176 – 1794
Beta strandi188 – 1969
Beta strandi199 – 2068
Helixi210 – 2134
Helixi214 – 2196
Beta strandi224 – 2318
Helixi232 – 2365
Beta strandi242 – 2443
Helixi247 – 25913
Helixi262 – 2643
Beta strandi268 – 2747
Helixi276 – 2827
Turni283 – 2853
Helixi288 – 2903
Helixi302 – 31413
Turni318 – 3214
Beta strandi324 – 3285
Helixi334 – 35017

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BCJX-ray3.06Q37-359[»]
2RGNX-ray3.50A/D37-359[»]
3AH8X-ray2.90A37-359[»]
3OHMX-ray2.70A35-359[»]
4EKCX-ray7.40A/C18-359[»]
4EKDX-ray2.71A18-359[»]
4GNKX-ray4.00A/C7-359[»]
ProteinModelPortaliP21279.
SMRiP21279. Positions 18-354.

Miscellaneous databases

EvolutionaryTraceiP21279.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG322962.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP21279.
KOiK04634.
OMAiLKISYGV.
OrthoDBiEOG7ZWD1W.
PhylomeDBiP21279.
TreeFamiTF300673.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000654. Gprotein_alpha_Q.
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.
PR00442. GPROTEINAQ.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

P21279-1 [UniParc]FASTAAdd to Basket

« Hide

MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES    50
GKSTFIKQMR IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP 100
YKYEHNKAHA QLVREVDVEK VSAFENPYVD AIKSLWNDPG IQECYDRRRE 150
YQLSDSTKYY LNDLDRVADP SYLPTQQDVL RVRVPTTGII EYPFDLQSVI 200
FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV ESDNENRMEE 250
SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR 300
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ 350
LNLKEYNLV 359
Length:359
Mass (Da):42,158
Last modified:July 7, 2009 - v4
Checksum:i3BCBA4EE7DADADBF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 292QL → HV in AAA63306. 1 Publication
Sequence conflicti62 – 621Missing in AAH57583. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55412 mRNA. Translation: AAA63306.1.
BC057583 mRNA. Translation: AAH57583.1.
CCDSiCCDS29684.1.
PIRiA38414. RGMSQ.
RefSeqiNP_032165.3. NM_008139.5.
UniGeneiMm.439701.
Mm.441601.

Genome annotation databases

EnsembliENSMUST00000025541; ENSMUSP00000025541; ENSMUSG00000024639.
GeneIDi14682.
KEGGimmu:14682.
UCSCiuc008gwt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55412 mRNA. Translation: AAA63306.1 .
BC057583 mRNA. Translation: AAH57583.1 .
CCDSi CCDS29684.1.
PIRi A38414. RGMSQ.
RefSeqi NP_032165.3. NM_008139.5.
UniGenei Mm.439701.
Mm.441601.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BCJ X-ray 3.06 Q 37-359 [» ]
2RGN X-ray 3.50 A/D 37-359 [» ]
3AH8 X-ray 2.90 A 37-359 [» ]
3OHM X-ray 2.70 A 35-359 [» ]
4EKC X-ray 7.40 A/C 18-359 [» ]
4EKD X-ray 2.71 A 18-359 [» ]
4GNK X-ray 4.00 A/C 7-359 [» ]
ProteinModelPortali P21279.
SMRi P21279. Positions 18-354.
ModBasei Search...

Protein-protein interaction databases

BioGridi 199971. 2 interactions.
DIPi DIP-606N.
IntActi P21279. 5 interactions.
MINTi MINT-4096294.

PTM databases

PhosphoSitei P21279.

Proteomic databases

MaxQBi P21279.
PaxDbi P21279.
PRIDEi P21279.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025541 ; ENSMUSP00000025541 ; ENSMUSG00000024639 .
GeneIDi 14682.
KEGGi mmu:14682.
UCSCi uc008gwt.1. mouse.

Organism-specific databases

CTDi 2776.
MGIi MGI:95776. Gnaq.

Phylogenomic databases

eggNOGi NOG322962.
HOGENOMi HOG000038729.
HOVERGENi HBG063184.
InParanoidi P21279.
KOi K04634.
OMAi LKISYGV.
OrthoDBi EOG7ZWD1W.
PhylomeDBi P21279.
TreeFami TF300673.

Enzyme and pathway databases

Reactomei REACT_207651. G alpha (q) signalling events.
REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).

Miscellaneous databases

EvolutionaryTracei P21279.
NextBioi 286596.
PROi P21279.
SOURCEi Search...

Gene expression databases

ArrayExpressi P21279.
Bgeei P21279.
Genevestigatori P21279.

Family and domain databases

Gene3Di 1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR000654. Gprotein_alpha_Q.
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.
PR00442. GPROTEINAQ.
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. "G protein diversity: a distinct class of alpha subunits is present in vertebrates and invertebrates."
    Strathmann M., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 87:9113-9117(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 20-27; 61-73; 78-92; 121-133; 159-181; 184-210; 283-300; 312-338 AND 346-354, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha."
    Wedegaertner P.B., Chu D.H., Wilson P.T., Levis M.J., Bourne H.R.
    J. Biol. Chem. 268:25001-25008(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-9 AND CYS-10, MUTAGENESIS OF CYS-9 AND CYS-10.
    Tissue: Brain.
  5. "Identification of an alternative G{alpha}q-dependent chemokine receptor signal transduction pathway in dendritic cells and granulocytes."
    Shi G., Partida-Sanchez S., Misra R.S., Tighe M., Borchers M.T., Lee J.J., Simon M.I., Lund F.E.
    J. Exp. Med. 204:2705-2718(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Nuclear alpha1-adrenergic receptors signal activated ERK localization to caveolae in adult cardiac myocytes."
    Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S., O'Connell T.D.
    Circ. Res. 103:992-1000(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. Cited for: FUNCTION.

Entry informationi

Entry nameiGNAQ_MOUSE
AccessioniPrimary (citable) accession number: P21279
Secondary accession number(s): Q6PFF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 7, 2009
Last modified: September 3, 2014
This is version 156 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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