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Entry version 167 (08 May 2019)
Sequence version 2 (23 Jan 2007)
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Protein

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

Gene

GNAI1

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

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). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). 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:17635935). Required for cortical dynein-dynactin complex recruitment during metaphase (PubMed:22327364).By similarity4 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 sources2 Publications1
<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 sitei151GTPCombined sources1
Metal bindingi181MagnesiumCombined sources2 Publications1
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 sources1 Publication6
Nucleotide bindingi175 – 181GTPCombined sources7
Nucleotide bindingi200 – 204GTP1 Publication5
Nucleotide bindingi269 – 272GTPCombined sources1 Publication4

<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-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-400042 Adrenaline,noradrenaline inhibits insulin secretion
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-422356 Regulation of insulin secretion
R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
R-HSA-9009391 Non-genomic estrogen signaling

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

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SignaLinki
P63096

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P63096

<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
<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 7

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:4384 GNAI1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
139310 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P63096

<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>Mutagenesisi42G → R: Abolishes switch to an activated conformation and dissociation from beta and gamma subunits upon GTP binding. Abolishes interaction with RGS family members. 1 Publication1
Mutagenesisi116E → L: Enhances interaction (inactive GDP-bound) with RGS14. 2 Publications1
Mutagenesisi147Q → L: Enhances interaction (inactive GDP-bound) with RGS14. 2 Publications1
Mutagenesisi245E → L: Enhances interaction (inactive GDP-bound) with RGS14. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
2770

Open Targets

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OpenTargetsi
ENSG00000127955

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA172

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4741

Drug and drug target database

More...
DrugBanki
DB04315 Guanosine-5'-Diphosphate
DB04444 Tetrafluoroaluminate Ion

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
GNAI1

Domain mapping of disease mutations (DMDM)

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DMDMi
52000964

<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 methionineiRemoved2 Publications
<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_00002036712 – 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 glycine2 Publications1
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

Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation.By similarity
Palmitoylation at Cys-3 varies with membrane lipid composition.By similarity
(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
P63096

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P63096

MaxQB - The MaxQuant DataBase

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MaxQBi
P63096

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

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PaxDbi
P63096

PeptideAtlas

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PeptideAtlasi
P63096

PRoteomics IDEntifications database

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PRIDEi
P63096

ProteomicsDB human proteome resource

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ProteomicsDBi
57475

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P63096

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

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PhosphoSitePlusi
P63096

SwissPalm database of S-palmitoylation events

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SwissPalmi
P63096

<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
ENSG00000127955 Expressed in 223 organ(s), highest expression level in corpus callosum

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P63096 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P63096 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB022449
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. Part of a spindle orientation complex at least composed of GNAI1, GPSM2 and NUMA1 (PubMed:26766442). The alpha chain contains the guanine nucleotide binding site. Identified in complex with the beta subunit GNB1 and the gamma subunit GNG1 (PubMed:22383884). Identified in complex with the beta subunit GNB1 and the gamma subunit GNG2 (PubMed:18434541). GTP binding causes dissociation of the heterotrimer, liberating the individual subunits so that they can interact with downstream effector proteins (PubMed:22383884). Interacts (GDP-bound form) with GPSM1; this inhibits guanine nucleotide exchange and GTP binding (By similarity). Interacts (GDP-bound form) with GPSM2 (via GoLoco domains); this inhibits guanine nucleotide exchange (PubMed:22952234). Interacts with RGS10; this strongly enhances GTP hydrolysis (PubMed:8774883, PubMed:18434541). Interacts with RGS1 and RGS16; this strongly enhances GTPase activity (PubMed:18434541). Interacts with RGS4 (PubMed:18434541). Interacts with RGS12 (PubMed:18434541). Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains) (PubMed:11976690, PubMed:18434541, PubMed:21115486, PubMed:22383884). Interacts with RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro) (PubMed:18434541). Interacts (GDP-bound form) with RIC8A (via C-terminus) (By similarity).By similarity9 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
109032, 87 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P63096

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P63096

Protein interaction database and analysis system

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IntActi
P63096, 36 interactors

Molecular INTeraction database

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MINTi
P63096

STRING: functional protein association networks

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STRINGi
9606.ENSP00000343027

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P63096

<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
1KJYX-ray2.70A/C30-354[»]
1Y3AX-ray2.50A/B/C/D26-354[»]
2G83X-ray2.80A/B33-345[»]
2GTPX-ray2.55A/B32-354[»]
2IK8X-ray2.71A/C31-354[»]
2OM2X-ray2.20A/C31-354[»]
2XNSX-ray3.41A/B30-354[»]
3ONWX-ray2.38A/B31-354[»]
3QE0X-ray3.00A/B/C33-354[»]
3QI2X-ray2.80A/B31-354[»]
3UMRX-ray2.24A1-354[»]
3UMSX-ray2.60A1-354[»]
4G5QX-ray2.90A/B/C/D25-354[»]
5JS7NMR-A30-354[»]
5JS8NMR-A30-354[»]
5TDHX-ray3.00A/H1-354[»]
6CMOelectron microscopy4.50A1-354[»]
6CRKX-ray2.00A2-354[»]
6DDEelectron microscopy3.50A1-354[»]
6DDFelectron microscopy3.50A1-354[»]
6N4Belectron microscopy3.00A1-354[»]

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

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SMRi
P63096

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
P63096

<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

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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P63096

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
P63096

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

More...
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P63096-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR
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):40,361
Last modified:January 23, 2007 - v2
<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:i9F88311B46E62DE3
GO
Isoform 2 (identifier: P63096-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Show »
Length:302
Mass (Da):34,775
Checksum:iDA5ED62E61B790A9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A3B3ITM0A0A3B3ITM0_HUMAN
Guanine nucleotide-binding protein ...
GNAI1
168Annotation score:

Annotation score:1 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>
A0A3B3IUA8A0A3B3IUA8_HUMAN
Guanine nucleotide-binding protein ...
GNAI1
148Annotation score:

Annotation score:1 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>
A0A3B3IU77A0A3B3IU77_HUMAN
Guanine nucleotide-binding protein ...
GNAI1
43Annotation score:

Annotation score:1 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>
A0A3B3ITX3A0A3B3ITX3_HUMAN
Guanine nucleotide-binding protein ...
GNAI1
60Annotation score:

Annotation score:1 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>
A0A3B3IS42A0A3B3IS42_HUMAN
Guanine nucleotide-binding protein ...
GNAI1
47Annotation score:

Annotation score:1 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>
A0A3B3IRK0A0A3B3IRK0_HUMAN
Guanine nucleotide-binding protein ...
GNAI1
40Annotation score:

Annotation score:1 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>
A0A3B3ITG4A0A3B3ITG4_HUMAN
Guanine nucleotide-binding protein ...
GNAI1
40Annotation score:

Annotation score:1 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>
C9J2Z2C9J2Z2_HUMAN
Guanine nucleotide-binding protein ...
GNAI1
22Annotation score:

Annotation score:1 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 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 conflicti138A → G in CAB43212 (PubMed:11230166).Curated1
Sequence conflicti219T → A in AAH26326 (PubMed:15489334).Curated1
Sequence conflicti244H → Y in AAV38580 (Ref. 4) Curated1
Sequence conflicti249L → M in AAV38580 (Ref. 4) Curated1
Sequence conflicti288P → Q in AAH26326 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0452151 – 52Missing in isoform 2. 1 PublicationAdd BLAST52

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF493905 mRNA Translation: AAM12619.1
AF055013 mRNA Translation: AAC09361.1
AL049933 mRNA Translation: CAB43212.2
BT019775 mRNA Translation: AAV38580.1
AK292953 mRNA Translation: BAF85642.1
AK304442 mRNA Translation: BAG65263.1
AC004159 Genomic DNA No translation available.
AC080066 Genomic DNA No translation available.
CH471091 Genomic DNA Translation: EAW77011.1
BC026326 mRNA Translation: AAH26326.1
M20596, M20594, M20595 Genomic DNA Translation: AAA35893.1
M17219 mRNA Translation: AAA52581.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5595.1 [P63096-1]
CCDS59061.1 [P63096-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A28318 RGHUI1

NCBI Reference Sequences

More...
RefSeqi
NP_001243343.1, NM_001256414.1 [P63096-2]
NP_002060.4, NM_002069.5 [P63096-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000351004; ENSP00000343027; ENSG00000127955 [P63096-1]
ENST00000442586; ENSP00000391439; ENSG00000127955 [P63096-1]
ENST00000457358; ENSP00000410572; ENSG00000127955 [P63096-2]
ENST00000648098; ENSP00000497717; ENSG00000127955 [P63096-1]
ENST00000648306; ENSP00000497773; ENSG00000127955 [P63096-1]
ENST00000648412; ENSP00000497051; ENSG00000127955 [P63096-1]
ENST00000648476; ENSP00000497179; ENSG00000127955 [P63096-1]
ENST00000648663; ENSP00000497379; ENSG00000127955 [P63096-1]
ENST00000648832; ENSP00000497765; ENSG00000127955 [P63096-1]
ENST00000648877; ENSP00000497760; ENSG00000127955 [P63096-1]
ENST00000648953; ENSP00000496800; ENSG00000127955 [P63096-1]
ENST00000649225; ENSP00000496829; ENSG00000127955 [P63096-1]
ENST00000649267; ENSP00000497315; ENSG00000127955 [P63096-1]
ENST00000649487; ENSP00000498091; ENSG00000127955 [P63096-1]
ENST00000649796; ENSP00000497260; ENSG00000127955 [P63096-1]
ENST00000649855; ENSP00000497754; ENSG00000127955 [P63096-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2770

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2770

UCSC genome browser

More...
UCSCi
uc003uhb.2 human [P63096-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF493905 mRNA Translation: AAM12619.1
AF055013 mRNA Translation: AAC09361.1
AL049933 mRNA Translation: CAB43212.2
BT019775 mRNA Translation: AAV38580.1
AK292953 mRNA Translation: BAF85642.1
AK304442 mRNA Translation: BAG65263.1
AC004159 Genomic DNA No translation available.
AC080066 Genomic DNA No translation available.
CH471091 Genomic DNA Translation: EAW77011.1
BC026326 mRNA Translation: AAH26326.1
M20596, M20594, M20595 Genomic DNA Translation: AAA35893.1
M17219 mRNA Translation: AAA52581.1
CCDSiCCDS5595.1 [P63096-1]
CCDS59061.1 [P63096-2]
PIRiA28318 RGHUI1
RefSeqiNP_001243343.1, NM_001256414.1 [P63096-2]
NP_002060.4, NM_002069.5 [P63096-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KJYX-ray2.70A/C30-354[»]
1Y3AX-ray2.50A/B/C/D26-354[»]
2G83X-ray2.80A/B33-345[»]
2GTPX-ray2.55A/B32-354[»]
2IK8X-ray2.71A/C31-354[»]
2OM2X-ray2.20A/C31-354[»]
2XNSX-ray3.41A/B30-354[»]
3ONWX-ray2.38A/B31-354[»]
3QE0X-ray3.00A/B/C33-354[»]
3QI2X-ray2.80A/B31-354[»]
3UMRX-ray2.24A1-354[»]
3UMSX-ray2.60A1-354[»]
4G5QX-ray2.90A/B/C/D25-354[»]
5JS7NMR-A30-354[»]
5JS8NMR-A30-354[»]
5TDHX-ray3.00A/H1-354[»]
6CMOelectron microscopy4.50A1-354[»]
6CRKX-ray2.00A2-354[»]
6DDEelectron microscopy3.50A1-354[»]
6DDFelectron microscopy3.50A1-354[»]
6N4Belectron microscopy3.00A1-354[»]
SMRiP63096
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109032, 87 interactors
CORUMiP63096
ELMiP63096
IntActiP63096, 36 interactors
MINTiP63096
STRINGi9606.ENSP00000343027

Chemistry databases

BindingDBiP63096
ChEMBLiCHEMBL4741
DrugBankiDB04315 Guanosine-5'-Diphosphate
DB04444 Tetrafluoroaluminate Ion

PTM databases

iPTMnetiP63096
PhosphoSitePlusiP63096
SwissPalmiP63096

Polymorphism and mutation databases

BioMutaiGNAI1
DMDMi52000964

Proteomic databases

EPDiP63096
jPOSTiP63096
MaxQBiP63096
PaxDbiP63096
PeptideAtlasiP63096
PRIDEiP63096
ProteomicsDBi57475

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2770
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000351004; ENSP00000343027; ENSG00000127955 [P63096-1]
ENST00000442586; ENSP00000391439; ENSG00000127955 [P63096-1]
ENST00000457358; ENSP00000410572; ENSG00000127955 [P63096-2]
ENST00000648098; ENSP00000497717; ENSG00000127955 [P63096-1]
ENST00000648306; ENSP00000497773; ENSG00000127955 [P63096-1]
ENST00000648412; ENSP00000497051; ENSG00000127955 [P63096-1]
ENST00000648476; ENSP00000497179; ENSG00000127955 [P63096-1]
ENST00000648663; ENSP00000497379; ENSG00000127955 [P63096-1]
ENST00000648832; ENSP00000497765; ENSG00000127955 [P63096-1]
ENST00000648877; ENSP00000497760; ENSG00000127955 [P63096-1]
ENST00000648953; ENSP00000496800; ENSG00000127955 [P63096-1]
ENST00000649225; ENSP00000496829; ENSG00000127955 [P63096-1]
ENST00000649267; ENSP00000497315; ENSG00000127955 [P63096-1]
ENST00000649487; ENSP00000498091; ENSG00000127955 [P63096-1]
ENST00000649796; ENSP00000497260; ENSG00000127955 [P63096-1]
ENST00000649855; ENSP00000497754; ENSG00000127955 [P63096-1]
GeneIDi2770
KEGGihsa:2770
UCSCiuc003uhb.2 human [P63096-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2770
DisGeNETi2770

GeneCards: human genes, protein and diseases

More...
GeneCardsi
GNAI1
HGNCiHGNC:4384 GNAI1
HPAiCAB022449
HPA042141
MIMi139310 gene
neXtProtiNX_P63096
OpenTargetsiENSG00000127955
PharmGKBiPA172

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0082 Eukaryota
ENOG410XNVQ LUCA
GeneTreeiENSGT00940000153567
HOGENOMiHOG000038730
InParanoidiP63096
KOiK04630
OMAiRIAQTSY
OrthoDBi754573at2759
PhylomeDBiP63096
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-400042 Adrenaline,noradrenaline inhibits insulin secretion
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-422356 Regulation of insulin secretion
R-HSA-6814122 Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding
R-HSA-9009391 Non-genomic estrogen signaling
SignaLinkiP63096
SIGNORiP63096

Miscellaneous databases

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

More...
ChiTaRSi
GNAI1 human
EvolutionaryTraceiP63096

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
GNAI1

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

More...
GenomeRNAii
2770

Protein Ontology

More...
PROi
PR:P63096

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000127955 Expressed in 223 organ(s), highest expression level in corpus callosum
ExpressionAtlasiP63096 baseline and differential
GenevisibleiP63096 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
PROSITEiView protein in PROSITE
PS51882 G_ALPHA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiGNAI1_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: P63096
Secondary accession number(s): A8KA88
, B4E2V1, C9J3A4, P04898, P11015, P31871, Q5U074, Q8TAN5, Q9UGA4
<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: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 167 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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