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Entry version 216 (13 Feb 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Guanine nucleotide-binding protein G(k) subunit alpha

Gene

GNAI3

Organism
Homo sapiens (Human)
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

Heterotrimeric 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. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:8774883, PubMed:18434541, PubMed:19478087). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (PubMed:19478087). Stimulates the activity of receptor-regulated K+ channels (PubMed:2535845). The active GTP-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 (PubMed:17635935).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sources1 Publication1
Metal bindingi181MagnesiumCombined sources1 Publication1
<p>This subsection of the ‘Function’ 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 ‘Function’ 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 – 181GTPCombined sources7
Nucleotide bindingi200 – 204GTPCombined sources1 Publication5
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
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-112043 PLC beta mediated events
R-HSA-170670 Adenylate cyclase inhibitory pathway
R-HSA-202040 G-protein activation
R-HSA-392170 ADP signalling through P2Y purinoceptor 12
R-HSA-418555 G alpha (s) signalling events
R-HSA-418594 G alpha (i) signalling events
R-HSA-418597 G alpha (z) signalling events
R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P08754

SIGNOR Signaling Network Open Resource

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SIGNORi
P08754

<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(k) subunit alpha1 Publication
Alternative name(s):
G(i) alpha-3
<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:GNAI3
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000065135.8

Human Gene Nomenclature Database

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HGNCi
HGNC:4387 GNAI3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
139370 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P08754

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Auriculocondylar syndrome 1 (ARCND1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant craniofacial malformation syndrome characterized by variable mandibular anomalies, including mild to severe micrognathia, temporomandibular joint ankylosis, cleft palate, and a characteristic ear malformation that consists of separation of the lobule from the external ear, giving the appearance of a question mark (question-mark ear). Other frequently described features include prominent cheeks, cupped and posteriorly rotated ears, preauricular tags, and microstomia.
See also OMIM:602483
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06855840G → R in ARCND1. 1 PublicationCorresponds to variant dbSNP:rs387907178EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2773

MalaCards human disease database

More...
MalaCardsi
GNAI3
MIMi602483 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000065135

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
137888 Auriculocondylar syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA173

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4221

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
GNAI3

Domain mapping of disease mutations (DMDM)

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DMDMi
120996

<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_00002036922 – 354Guanine nucleotide-binding protein G(k) subunit alphaAdd 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 cysteineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei178ADP-ribosylarginine; by cholera toxinBy similarity1
Modified residuei204Deamidated glutamine; by Photorhabdus PAU_022301 Publication1
Modified residuei351ADP-ribosylcysteine; by pertussis toxinBy similarity1

<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

(Microbial infection) Deamidated at Gln-204 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA.1 Publication

Keywords - PTMi

ADP-ribosylation, Lipoprotein, Myristate, Palmitate

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P08754

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P08754

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P08754

PeptideAtlas

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PeptideAtlasi
P08754

PRoteomics IDEntifications database

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PRIDEi
P08754

ProteomicsDB human proteome resource

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ProteomicsDBi
52164

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P08754

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

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PhosphoSitePlusi
P08754

SwissPalm database of S-palmitoylation events

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SwissPalmi
P08754

<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

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Bgeei
ENSG00000065135 Expressed in 231 organ(s), highest expression level in esophagus squamous epithelium

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P08754 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB022099
HPA042141

<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 subunit contains the guanine nucleotide binding site. GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins. Interacts with GPSM1 (By similarity). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains) (PubMed:22952234). Does not interact with RGS2 (PubMed:19478087). Interacts with RGS8 and RGS10; this strongly enhances the intrinsic GTPase activity (PubMed:8774883, PubMed:18434541). Interacts with RGS16; this strongly enhances the intrinsic GTPase activity (PubMed:19478087). Interacts with RGS12 (By similarity). Interacts (via active GTP- or inactive GDP-bound form) with RGS14 (By similarity).By similarityCurated3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109035, 109 interactors

Protein interaction database and analysis system

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IntActi
P08754, 42 interactors

Molecular INTeraction database

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MINTi
P08754

STRING: functional protein association networks

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STRINGi
9606.ENSP00000358867

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P08754

<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

Select the link destinations:

Protein Data Bank Europe

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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
2IHBX-ray2.71A32-354[»]
2ODEX-ray1.90A/C4-350[»]
2V4ZX-ray2.80A4-350[»]
4G5OX-ray2.90A/B/C/D25-354[»]
4G5RX-ray3.48A/B/C/D25-354[»]
4G5SX-ray3.62A/B/C/D25-354[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P08754

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

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SMRi
P08754

Database of comparative protein structure models

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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

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EvolutionaryTracei
P08754

<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

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0082 Eukaryota
ENOG410XNVQ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153567

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000038730

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG063184

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P08754

KEGG Orthology (KO)

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KOi
K04630

Identification of Orthologs from Complete Genome Data

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OMAi
MRIIHDV

Database of Orthologous Groups

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OrthoDBi
754573at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P08754

TreeFam database of animal gene trees

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TreeFami
TF300673

Family and domain databases

Conserved Domains Database

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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

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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

<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>.<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.

P08754-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEDG YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEAAR
110 120 130 140 150
ADDARQLFVL AGSAEEGVMT PELAGVIKRL WRDGGVQACF SRSREYQLND
160 170 180 190 200
SASYYLNDLD RISQSNYIPT QQDVLRTRVK TTGIVETHFT FKDLYFKMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF
260 270 280 290 300
DSICNNKWFT ETSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA
310 320 330 340 350
AYIQCQFEDL NRRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKE

CGLY
Length:354
Mass (Da):40,532
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:iEAB6B4DD3646BC01
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti21R → C no nucleotide entry (PubMed:2440724).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06855840G → R in ARCND1. 1 PublicationCorresponds to variant dbSNP:rs387907178EnsemblClinVar.1

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
M27543 mRNA Translation: AAA52579.1
J03005 mRNA Translation: AAA52557.1
M20604
, M20597, M20598, M20599, M20600, M20601, M20602, M20603 Genomic DNA Translation: AAA35895.1
J03198 mRNA Translation: AAA35896.1
J03238 mRNA Translation: AAA35939.1
AF493907 mRNA Translation: AAM12621.1
BT019973 mRNA Translation: AAV38776.1
BT019974 mRNA Translation: AAV38777.1
AK312252 mRNA Translation: BAG35184.1
CH471122 Genomic DNA Translation: EAW56393.1
BC025285 mRNA Translation: AAH25285.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS802.1

Protein sequence database of the Protein Information Resource

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PIRi
S02348 RGHUI3

NCBI Reference Sequences

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RefSeqi
NP_006487.1, NM_006496.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.73799
Hs.741171

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000369851; ENSP00000358867; ENSG00000065135

Database of genes from NCBI RefSeq genomes

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GeneIDi
2773

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2773

UCSC genome browser

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UCSCi
uc001dxz.4 human

<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
M27543 mRNA Translation: AAA52579.1
J03005 mRNA Translation: AAA52557.1
M20604
, M20597, M20598, M20599, M20600, M20601, M20602, M20603 Genomic DNA Translation: AAA35895.1
J03198 mRNA Translation: AAA35896.1
J03238 mRNA Translation: AAA35939.1
AF493907 mRNA Translation: AAM12621.1
BT019973 mRNA Translation: AAV38776.1
BT019974 mRNA Translation: AAV38777.1
AK312252 mRNA Translation: BAG35184.1
CH471122 Genomic DNA Translation: EAW56393.1
BC025285 mRNA Translation: AAH25285.1
CCDSiCCDS802.1
PIRiS02348 RGHUI3
RefSeqiNP_006487.1, NM_006496.3
UniGeneiHs.73799
Hs.741171

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IHBX-ray2.71A32-354[»]
2ODEX-ray1.90A/C4-350[»]
2V4ZX-ray2.80A4-350[»]
4G5OX-ray2.90A/B/C/D25-354[»]
4G5RX-ray3.48A/B/C/D25-354[»]
4G5SX-ray3.62A/B/C/D25-354[»]
ProteinModelPortaliP08754
SMRiP08754
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109035, 109 interactors
IntActiP08754, 42 interactors
MINTiP08754
STRINGi9606.ENSP00000358867

Chemistry databases

BindingDBiP08754
ChEMBLiCHEMBL4221

PTM databases

iPTMnetiP08754
PhosphoSitePlusiP08754
SwissPalmiP08754

Polymorphism and mutation databases

BioMutaiGNAI3
DMDMi120996

Proteomic databases

EPDiP08754
jPOSTiP08754
PaxDbiP08754
PeptideAtlasiP08754
PRIDEiP08754
ProteomicsDBi52164

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2773
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369851; ENSP00000358867; ENSG00000065135
GeneIDi2773
KEGGihsa:2773
UCSCiuc001dxz.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2773
DisGeNETi2773
EuPathDBiHostDB:ENSG00000065135.8

GeneCards: human genes, protein and diseases

More...
GeneCardsi
GNAI3
HGNCiHGNC:4387 GNAI3
HPAiCAB022099
HPA042141
MalaCardsiGNAI3
MIMi139370 gene
602483 phenotype
neXtProtiNX_P08754
OpenTargetsiENSG00000065135
Orphaneti137888 Auriculocondylar syndrome
PharmGKBiPA173

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0082 Eukaryota
ENOG410XNVQ LUCA
GeneTreeiENSGT00940000153567
HOGENOMiHOG000038730
HOVERGENiHBG063184
InParanoidiP08754
KOiK04630
OMAiMRIIHDV
OrthoDBi754573at2759
PhylomeDBiP08754
TreeFamiTF300673

Enzyme and pathway databases

ReactomeiR-HSA-112043 PLC beta mediated events
R-HSA-170670 Adenylate cyclase inhibitory pathway
R-HSA-202040 G-protein activation
R-HSA-392170 ADP signalling through P2Y purinoceptor 12
R-HSA-418555 G alpha (s) signalling events
R-HSA-418594 G alpha (i) signalling events
R-HSA-418597 G alpha (z) signalling events
R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
SignaLinkiP08754
SIGNORiP08754

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
GNAI3 human
EvolutionaryTraceiP08754

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
GNAI3

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
2773

Protein Ontology

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PROi
PR:P08754

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000065135 Expressed in 231 organ(s), highest expression level in esophagus squamous epithelium
GenevisibleiP08754 HS

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<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 nameiGNAI3_HUMAN
<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: P08754
Secondary accession number(s): P17539, Q5TZX1
<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: November 1, 1988
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 216 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
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.

<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
  3. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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