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Entry version 194 (08 May 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Guanine nucleotide-binding protein G(i) subunit alpha-1

Gene

Gnai1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 (PubMed:19703466, PubMed:24596087, PubMed:25037222). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:21158412). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:21158412). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:19703466). 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. Required for normal cytokinesis during mitosis (PubMed:16870394). Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity).By similarityCurated5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi47MagnesiumCombined sources2 Publications1
Metal bindingi181MagnesiumCombined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei326GTP; via amide nitrogenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi43 – 48GTPCombined sources6
Nucleotide bindingi150 – 151GTPCombined sources2
Nucleotide bindingi175 – 178GTPCombined sources4
Nucleotide bindingi200 – 204GTPCombined sources5
Nucleotide bindingi269 – 272GTPCombined sources4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransducer
Biological processCell cycle, Cell division, Mitosis, Transport
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-112043 PLC beta mediated events
R-RNO-170670 Adenylate cyclase inhibitory pathway
R-RNO-202040 G-protein activation
R-RNO-392170 ADP signalling through P2Y purinoceptor 12
R-RNO-400042 Adrenaline,noradrenaline inhibits insulin secretion
R-RNO-418594 G alpha (i) signalling events
R-RNO-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
R-RNO-9009391 Non-genomic estrogen signaling

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P10824

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-1
Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Gnai1
Synonyms:Gnai-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Rat genome database

More...
RGDi
2713 Gnai1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2G → A: Abolishes myristoylation and palmitoylation. 1 Publication1
Mutagenesisi3C → S: Abolishes palmitoylation. 1 Publication1
Mutagenesisi43E → A: Mildly impairs receptor binding; mildly decreases basal and receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi149N → I: Inhibits interaction with RGS14. Does not inhibit interaction with RIC8A. 1 Publication1
Mutagenesisi189F → Y: Increases basal GDP exchange rate; no effect on receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi191F → Y: No effect on basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi204Q → L: Expected to have lost GTPase activity; inhibits the forskolin-mediated increase of cellular cAMP levels. Does not inhibit interaction with RGS14 at centrosomes. 2 Publications1
Mutagenesisi329T → A: Increases basal GDP exchange rate and inhibits the forskolin-mediated increase of cellular cAMP levels. 1 Publication1
Mutagenesisi332V → A: Increases basal GDP exchange rate. 1 Publication1
Mutagenesisi336F → A or C: Increases basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi336F → Y: Strongly increases basal GDP exchange rate; mildly decreases receptor-stimulated GDP exchange. 1 Publication1
Mutagenesisi345K → L: Mildly impairs receptor binding; mildly decreases basal and receptor-stimulated GDP exchange. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002036732 – 354Guanine nucleotide-binding protein G(i) subunit alpha-1Add BLAST353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi3S-palmitoyl cysteine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation.1 Publication
Palmitoylation at Cys-3 varies with membrane lipid composition.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Palmitate

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P10824

PRoteomics IDEntifications database

More...
PRIDEi
P10824

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0004:P10824

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P10824

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P10824

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P10824

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000057096 Expressed in 9 organ(s), highest expression level in brain

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:8521505, PubMed:24596087, PubMed:25037222). Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (By similarity). Identified in complex with the beta subunit GNB1 and the gamma subunit GNG1 (PubMed:24596087). Identified in complex with the beta subunit GNB1 and the gamma subunit GNG2 (PubMed:8521505). GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins. Interacts (GDP-bound form) with GPSM1; this inhibits guanine nucleotide exchange and GTP binding (PubMed:11121039). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains); this inhibits guanine nucleotide exchange (By similarity). Interacts with RGS10; this strongly enhances GTP hydrolysis. Interacts with RGS1 and RGS16 (By similarity). Interacts with RGS4 (PubMed:9108480). Interacts with RGS12 (PubMed:11387333). Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains) (PubMed:11387333, PubMed:16870394, PubMed:17635935, PubMed:21158412). Interacts with RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro) (By similarity). Interacts (GDP-bound form) with RIC8A (via C-terminus) (PubMed:21158412).By similarity8 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
247715, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P10824

Database of interacting proteins

More...
DIPi
DIP-6073N

Protein interaction database and analysis system

More...
IntActi
P10824, 2 interactors

Molecular INTeraction database

More...
MINTi
P10824

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1354
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P10824

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P10824

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini32 – 354G-alphaPROSITE-ProRule annotationAdd BLAST323

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni35 – 48G1 motifPROSITE-ProRule annotationAdd BLAST14
Regioni173 – 181G2 motifPROSITE-ProRule annotation9
Regioni196 – 205G3 motifPROSITE-ProRule annotation10
Regioni265 – 272G4 motifPROSITE-ProRule annotation8
Regioni324 – 329G5 motifPROSITE-ProRule annotation6

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153567

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000038730

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P10824

KEGG Orthology (KO)

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KOi
K04630

Identification of Orthologs from Complete Genome Data

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OMAi
RIAQTSY

Database of Orthologous Groups

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OrthoDBi
754573at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P10824

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00066 G-alpha, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.400.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001408 Gprotein_alpha_I
IPR001019 Gprotein_alpha_su
IPR011025 GproteinA_insert
IPR027417 P-loop_NTPase

The PANTHER Classification System

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PANTHERi
PTHR10218 PTHR10218, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00503 G-alpha, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00318 GPROTEINA
PR00441 GPROTEINAI

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00275 G_alpha, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47895 SSF47895, 1 hit
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51882 G_ALPHA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P10824-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDAAR
110 120 130 140 150
ADDARQLFVL AGAAEEGFMT AELAGVIKRL WKDSGVQACF NRSREYQLND
160 170 180 190 200
SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK TTGIVETHFT FKDLHFKMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF
260 270 280 290 300
DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA
310 320 330 340 350
AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD

CGLF
Length:354
Mass (Da):40,345
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i99E9D11B485C2DE3
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M17527 mRNA Translation: AAA40825.1
DQ120469 mRNA Translation: AAZ23808.1
DQ120470 mRNA Translation: AAZ23809.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A35377
C27423 RGRTI1

NCBI Reference Sequences

More...
RefSeqi
NP_037277.1, NM_013145.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000091004; ENSRNOP00000074036; ENSRNOG00000057096

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25686

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25686

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17527 mRNA Translation: AAA40825.1
DQ120469 mRNA Translation: AAZ23808.1
DQ120470 mRNA Translation: AAZ23809.1
PIRiA35377
C27423 RGRTI1
RefSeqiNP_037277.1, NM_013145.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGRX-ray2.80A/D2-354[»]
1AS0X-ray2.00A2-354[»]
1AS2X-ray2.80A2-354[»]
1AS3X-ray2.40A2-354[»]
1BH2X-ray2.10A32-346[»]
1BOFX-ray2.20A2-354[»]
1CIPX-ray1.50A2-354[»]
1FQJX-ray2.02A/D220-299[»]
1FQKX-ray2.30A/C220-299[»]
1GDDX-ray2.20A2-354[»]
1GFIX-ray2.20A2-354[»]
1GG2X-ray2.40A2-354[»]
1GIAX-ray2.00A2-354[»]
1GILX-ray2.30A2-354[»]
1GITX-ray2.60A2-354[»]
1GP2X-ray2.30A2-354[»]
1SHZX-ray2.85A/D22-48[»]
A/D185-353[»]
1SVKX-ray2.00A2-354[»]
1SVSX-ray1.50A2-354[»]
2BCJX-ray3.06Q1-28[»]
2ZJYX-ray2.80A1-354[»]
2ZJZX-ray2.60A/B1-354[»]
3AH8X-ray2.90A2-28[»]
3D7MX-ray2.90A1-354[»]
3FFAX-ray2.30A1-354[»]
3FFBX-ray2.57A1-354[»]
3V00X-ray2.90A/B/C220-298[»]
4N0DX-ray1.55A1-354[»]
4N0EX-ray2.10A1-354[»]
4PAMX-ray2.10A1-354[»]
4PANX-ray2.40A1-354[»]
4PAOX-ray2.00A1-354[»]
4PAQX-ray2.00A1-354[»]
5KDLX-ray2.67A/B1-354[»]
5KDOX-ray1.90A1-354[»]
SMRiP10824
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247715, 2 interactors
CORUMiP10824
DIPiDIP-6073N
IntActiP10824, 2 interactors
MINTiP10824

PTM databases

iPTMnetiP10824
PhosphoSitePlusiP10824
SwissPalmiP10824

2D gel databases

World-2DPAGEi0004:P10824

Proteomic databases

jPOSTiP10824
PRIDEiP10824

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000091004; ENSRNOP00000074036; ENSRNOG00000057096
GeneIDi25686
KEGGirno:25686

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2770
RGDi2713 Gnai1

Phylogenomic databases

GeneTreeiENSGT00940000153567
HOGENOMiHOG000038730
InParanoidiP10824
KOiK04630
OMAiRIAQTSY
OrthoDBi754573at2759
PhylomeDBiP10824

Enzyme and pathway databases

ReactomeiR-RNO-112043 PLC beta mediated events
R-RNO-170670 Adenylate cyclase inhibitory pathway
R-RNO-202040 G-protein activation
R-RNO-392170 ADP signalling through P2Y purinoceptor 12
R-RNO-400042 Adrenaline,noradrenaline inhibits insulin secretion
R-RNO-418594 G alpha (i) signalling events
R-RNO-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
R-RNO-9009391 Non-genomic estrogen signaling
SABIO-RKiP10824

Miscellaneous databases

EvolutionaryTraceiP10824

Protein Ontology

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PROi
PR:P10824

Gene expression databases

BgeeiENSRNOG00000057096 Expressed in 9 organ(s), highest expression level in brain

Family and domain databases

CDDicd00066 G-alpha, 1 hit
Gene3Di1.10.400.10, 1 hit
InterProiView protein in InterPro
IPR001408 Gprotein_alpha_I
IPR001019 Gprotein_alpha_su
IPR011025 GproteinA_insert
IPR027417 P-loop_NTPase
PANTHERiPTHR10218 PTHR10218, 1 hit
PfamiView protein in Pfam
PF00503 G-alpha, 1 hit
PRINTSiPR00318 GPROTEINA
PR00441 GPROTEINAI
SMARTiView protein in SMART
SM00275 G_alpha, 1 hit
SUPFAMiSSF47895 SSF47895, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51882 G_ALPHA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGNAI1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P10824
Secondary accession number(s): Q45QN2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 194 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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