GNAI1

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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	47	MagnesiumCombined sources2 Publications	1
Binding siteⁱ	151	GTPCombined sources	1
Metal bindingⁱ	181	MagnesiumCombined sources2 Publications	1
Binding siteⁱ	326	GTP; via amide nitrogenCombined sources	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	43 – 48	GTPCombined sources1 Publication	6
Nucleotide bindingⁱ	175 – 181	GTPCombined sources	7
Nucleotide bindingⁱ	200 – 204	GTP1 Publication	5
Nucleotide bindingⁱ	269 – 272	GTPCombined sources1 Publication	4

GO - Molecular functionⁱ

GDP binding Source: UniProtKB
G-protein beta/gamma-subunit complex binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
G protein-coupled receptor binding Source: UniProtKB
G protein-coupled serotonin receptor binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
GTPase activity Source: UniProtKB
GTP binding Source: UniProtKB
magnesium ion binding Source: UniProtKB

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway Source: Reactome
adenylate cyclase-modulating G protein-coupled receptor signaling pathway
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cell cycle Source: UniProtKB-KW
cell division
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17635935
cellular response to forskolin Source: UniProtKB
G protein-coupled receptor signaling pathway Source: UniProtKB
positive regulation of protein localization to cell cortex
Source: UniProtKB
Inferred from mutant phenotypeⁱ
protein folding Source: Reactome
regulation of cAMP-mediated signaling Source: UniProtKB
regulation of mitotic spindle organization
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23027904
response to peptide hormone Source: BHF-UCL

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transducer
Biological process	Cell cycle, Cell division, Mitosis, Transport
Ligand	GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

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
SignaLinkⁱ	P63096
SIGNORⁱ	P63096

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Guanine nucleotide-binding protein G(i) subunit alpha-1 Alternative name(s): Adenylate cyclase-inhibiting G alpha protein
Gene namesⁱ	Name:GNAI1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 7

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000127955.15
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4384 GNAI1
MIMⁱ	139310 gene
neXtProtⁱ	NX_P63096

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	42	G → R: Abolishes switch to an activated conformation and dissociation from beta and gamma subunits upon GTP binding. Abolishes interaction with RGS family members. 1 Publication	1
Mutagenesisⁱ	116	E → L: Enhances interaction (inactive GDP-bound) with RGS14. 2 Publications	1
Mutagenesisⁱ	147	Q → L: Enhances interaction (inactive GDP-bound) with RGS14. 2 Publications	1
Mutagenesisⁱ	245	E → L: Enhances interaction (inactive GDP-bound) with RGS14. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2770
Open Targets More...OpenTargetsⁱ	ENSG00000127955
PharmGKBⁱ	PA172

Chemistry databases

ChEMBLⁱ	CHEMBL4741
Drug and drug target database More...DrugBankⁱ	DB04315 Guanosine-5'-Diphosphate DB04444 Tetrafluoroaluminate Ion

Polymorphism and mutation databases

BioMutaⁱ	GNAI1
DMDMⁱ	52000964

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed2 Publications
ChainⁱPRO_0000203671	2 – 354	Guanine nucleotide-binding protein G(i) subunit alpha-1Add BLAST		353

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Lipidationⁱ	2	N-myristoyl glycine2 Publications	1
Lipidationⁱ	3	S-palmitoyl cysteineBy similarity	1
Modified residueⁱ	178	ADP-ribosylarginine; by cholera toxinBy similarity	1
Modified residueⁱ	204	Deamidated glutamine; by Photorhabdus PAU_022301 Publication	1
Modified residueⁱ	351	ADP-ribosylcysteine; by pertussis toxinBy similarity	1

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

EPDⁱ	P63096
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P63096
PaxDbⁱ	P63096
PeptideAtlas More...PeptideAtlasⁱ	P63096
PRIDEⁱ	P63096
ProteomicsDBⁱ	57475

PTM databases

iPTMnetⁱ	P63096
PhosphoSitePlusⁱ	P63096
SwissPalmⁱ	P63096

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000127955 Expressed in 223 organ(s), highest expression level in corpus callosum
CleanExⁱ	HS_GNAI1
ExpressionAtlasⁱ	P63096 baseline and differential
Genevisibleⁱ	P63096 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB022449 HPA042141

HPAⁱ

CAB022449
HPA042141

Interactionⁱ

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

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
GPSM2	P81274	3	EBI-618639,EBI-618655
GPSM3	Q9Y4H4	5	EBI-618639,EBI-347538
NUMA1	Q14980	4	EBI-618639,EBI-521611
RGS17	Q9UGC6	3	EBI-618639,EBI-3918154

GO - Molecular functionⁱ

G protein-coupled receptor binding Source: UniProtKB
G protein-coupled serotonin receptor binding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109032, 78 interactors
CORUMⁱ	P63096
ELMⁱ	P63096
IntActⁱ	P63096, 36 interactors
Molecular INTeraction database More...MINTⁱ	P63096
STRINGⁱ	9606.ENSP00000343027

Chemistry databases

BindingDBⁱ

P63096

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	9 – 16	Combined sources	8
Helixⁱ	20 – 23	Combined sources	4
Helixⁱ	27 – 29	Combined sources	3
Beta strandⁱ	31 – 41	Combined sources	11
Helixⁱ	46 – 57	Combined sources	12
Helixⁱ	63 – 67	Combined sources	5
Helixⁱ	70 – 91	Combined sources	22
Helixⁱ	100 – 113	Combined sources	14
Beta strandⁱ	115 – 117	Combined sources	3
Helixⁱ	121 – 132	Combined sources	12
Helixⁱ	134 – 140	Combined sources	7
Helixⁱ	141 – 145	Combined sources	5
Helixⁱ	152 – 157	Combined sources	6
Helixⁱ	159 – 162	Combined sources	4
Beta strandⁱ	164 – 166	Combined sources	3
Helixⁱ	171 – 175	Combined sources	5
Beta strandⁱ	183 – 191	Combined sources	9
Beta strandⁱ	194 – 201	Combined sources	8
Helixⁱ	208 – 215	Combined sources	8
Beta strandⁱ	220 – 226	Combined sources	7
Helixⁱ	227 – 229	Combined sources	3
Beta strandⁱ	238 – 241	Combined sources	4
Helixⁱ	242 – 254	Combined sources	13
Helixⁱ	257 – 259	Combined sources	3
Beta strandⁱ	260 – 269	Combined sources	10
Helixⁱ	271 – 277	Combined sources	7
Turnⁱ	278 – 280	Combined sources	3
Helixⁱ	283 – 285	Combined sources	3
Helixⁱ	296 – 308	Combined sources	13
Turnⁱ	314 – 316	Combined sources	3
Beta strandⁱ	319 – 323	Combined sources	5
Beta strandⁱ	326 – 328	Combined sources	3
Helixⁱ	329 – 346	Combined sources	18
Helixⁱ	348 – 350	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P63096
SMRⁱ	P63096
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P63096

EvolutionaryTraceⁱ

P63096

Family & Domainsⁱ

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	KOG0082 Eukaryota ENOG410XNVQ LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118851
HOGENOMⁱ	HOG000038730
HOVERGENⁱ	HBG063184
InParanoidⁱ	P63096
KEGG Orthology (KO) More...KOⁱ	K04630
OMAⁱ	RIAQTSY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0VUT
PhylomeDBⁱ	P63096
TreeFamⁱ	TF300673

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00066 G-alpha, 1 hit
Gene3Dⁱ	1.10.400.10, 1 hit
InterProⁱ	View protein in InterPro IPR001408 Gprotein_alpha_I IPR001019 Gprotein_alpha_su IPR011025 GproteinA_insert IPR027417 P-loop_NTPase
PANTHERⁱ	PTHR10218 PTHR10218, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00503 G-alpha, 1 hit
PRINTSⁱ	PR00318 GPROTEINA PR00441 GPROTEINAI
SMARTⁱ	View protein in SMART SM00275 G_alpha, 1 hit
SUPFAMⁱ	SSF47895 SSF47895, 1 hit SSF52540 SSF52540, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P63096-1) [UniParc]FASTA Add 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

Checksum:ⁱ9F88311B46E62DE3

GO

Isoform 2 (identifier: P63096-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MKIIHEAGYS EEECKQYKAV VYSNTIQSII AIIRAMGRLK IDFGDSARAD 
        60         70         80         90        100
DARQLFVLAG AAEEGFMTAE LAGVIKRLWK DSGVQACFNR SREYQLNDSA 
       110        120        130        140        150
AYYLNDLDRI AQPNYIPTQQ DVLRTRVKTT GIVETHFTFK DLHFKMFDVG 
       160        170        180        190        200
GQRSERKKWI HCFEGVTAII FCVALSDYDL VLAEDEEMNR MHESMKLFDS 
       210        220        230        240        250
ICNNKWFTDT SIILFLNKKD LFEEKIKKSP LTICYPEYAG SNTYEEAAAY 
       260        270        280        290        300
IQCQFEDLNK RKDTKEIYTH FTCATDTKNV QFVFDAVTDV IIKNNLKDCG 

LF

Show »

Length:302

Mass (Da):34,775

Checksum:ⁱDA5ED62E61B790A9

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

C9JPP4	C9JPP4_HUMAN	Guanine nucleotide-binding protein ... Guanine nucleotide-binding protein G(i) subunit alpha-1	GNAI1	144	Annotation score:
C9JL77	C9JL77_HUMAN	Guanine nucleotide-binding protein ... Guanine nucleotide-binding protein G(i) subunit alpha-1	GNAI1	41	Annotation score:
C9J2Z2	C9J2Z2_HUMAN	Guanine nucleotide-binding protein ... Guanine nucleotide-binding protein G(i) subunit alpha-1	GNAI1	22	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	138	A → G in CAB43212 (PubMed:11230166).Curated	1
Sequence conflictⁱ	219	T → A in AAH26326 (PubMed:15489334).Curated	1
Sequence conflictⁱ	244	H → Y in AAV38580 (Ref. 4) Curated	1
Sequence conflictⁱ	249	L → M in AAV38580 (Ref. 4) Curated	1
Sequence conflictⁱ	288	P → Q in AAH26326 (PubMed:15489334).Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_045215	1 – 52	Missing in isoform 2. 1 PublicationAdd BLAST		52

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS5595.1 [P63096-1] CCDS59061.1 [P63096-2]
PIRⁱ	A28318 RGHUI1
NCBI Reference Sequences More...RefSeqⁱ	NP_001243343.1, NM_001256414.1 [P63096-2] NP_002060.4, NM_002069.5 [P63096-1]
UniGeneⁱ	Hs.134587

Genome annotation databases

Ensemblⁱ	ENST00000351004; ENSP00000343027; ENSG00000127955 [P63096-1] ENST00000457358; ENSP00000410572; ENSG00000127955 [P63096-2]
GeneIDⁱ	2770
KEGGⁱ	hsa:2770
UCSC genome browser More...UCSCⁱ	uc003uhb.2 human [P63096-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P63096	Guanine nucleotide-binding protein G(i) subunit alpha-1		BOVIN		354	UniRef100_P63096
Guanine nucleotide-binding protein G(i) subunit alpha-1		MOUSE		354
Guanine nucleotide-binding protein G(I) subunit alpha-1 isoform 1		MACMU		354
G protein subunit alpha i1		PANTR		354
guanine nucleotide-binding protein G(I) subunit alpha-1 isoform X1		LIPVE		354
+36
P63096-2	G protein subunit alpha i1		PANTR		302	UniRef100_A0A2J8LG83
GNAI1 isoform 4		PONAB		302
G protein subunit alpha i1		SAIBB		302
Uncharacterized protein		MACMU		302
guanine nucleotide-binding protein G(I) subunit alpha-1 isoform X2		PHYCD		302
+13

Protein	Similar proteins		Species	Score	Length	Source
P63096	Guanine nucleotide-binding protein G(i) subunit alpha-1		BOVIN		354	UniRef90_P63096
Guanine nucleotide-binding protein G(i) subunit alpha-1		MOUSE		354
Guanine nucleotide-binding protein G(I) subunit alpha-1 isoform 1		MACMU		354
G protein subunit alpha i1		PANTR		354
guanine nucleotide-binding protein G(I) subunit alpha-1 isoform X1		LIPVE		354
+43
P63096-2	G protein subunit alpha i1		PANTR		302	UniRef90_A0A2J8LG83
GNAI1 isoform 4		PONAB		302
G protein subunit alpha i1		SAIBB		302
Uncharacterized protein		MACMU		302
guanine nucleotide-binding protein G(I) subunit alpha-1 isoform X2		PHYCD		302
+13

Protein	Similar proteins		Species	Score	Length	Source
P63096	Guanine nucleotide-binding protein G(i) subunit alpha-1		BOVIN		354	UniRef50_P63096
Guanine nucleotide-binding protein G(i) subunit alpha-1		MOUSE		354
Guanine nucleotide-binding protein G(I) subunit alpha-1 isoform 1		MACMU		354
G protein subunit alpha i1		PANTR		354
guanine nucleotide-binding protein G(I) subunit alpha-1 isoform X1		LIPVE		354
+61
P63096-2	G-protein coupled receptor 61		HUMAN		451	UniRef50_Q9BZJ8
Guanine nucleotide-binding protein G(k) subunit alpha (Fragment)		CRIGR		63
G protein-coupled receptor 61		PANTR		451
G protein-coupled receptor 61		PONAB		451
Uncharacterized protein		PANPA		451
+38

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
CCDSⁱ	CCDS5595.1 [P63096-1] CCDS59061.1 [P63096-2]
PIRⁱ	A28318 RGHUI1
RefSeqⁱ	NP_001243343.1, NM_001256414.1 [P63096-2] NP_002060.4, NM_002069.5 [P63096-1]
UniGeneⁱ	Hs.134587

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1KJY	X-ray	2.70	A/C	30-354	[»]
	1Y3A	X-ray	2.50	A/B/C/D	26-354	[»]
	2G83	X-ray	2.80	A/B	33-345	[»]
	2GTP	X-ray	2.55	A/B	32-354	[»]
	2IK8	X-ray	2.71	A/C	31-354	[»]
	2OM2	X-ray	2.20	A/C	31-354	[»]
	2XNS	X-ray	3.41	A/B	30-354	[»]
	3ONW	X-ray	2.38	A/B	31-354	[»]
	3QE0	X-ray	3.00	A/B/C	33-354	[»]
	3QI2	X-ray	2.80	A/B	31-354	[»]
	3UMR	X-ray	2.24	A	1-354	[»]
	3UMS	X-ray	2.60	A	1-354	[»]
	4G5Q	X-ray	2.90	A/B/C/D	25-354	[»]
	5JS7	NMR	-	A	30-354	[»]
	5JS8	NMR	-	A	30-354	[»]
	5TDH	X-ray	3.00	A/H	1-354	[»]
	6CMO	electron microscopy	4.50	A	1-354	[»]
	6DDE	electron microscopy	3.50	A	1-354	[»]
	6DDF	electron microscopy	3.50	A	1-354	[»]
ProteinModelPortalⁱ	P63096
SMRⁱ	P63096
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109032, 78 interactors
CORUMⁱ	P63096
ELMⁱ	P63096
IntActⁱ	P63096, 36 interactors
MINTⁱ	P63096
STRINGⁱ	9606.ENSP00000343027

Chemistry databases

BindingDBⁱ	P63096
ChEMBLⁱ	CHEMBL4741
DrugBankⁱ	DB04315 Guanosine-5'-Diphosphate DB04444 Tetrafluoroaluminate Ion

PTM databases

iPTMnetⁱ	P63096
PhosphoSitePlusⁱ	P63096
SwissPalmⁱ	P63096

Polymorphism and mutation databases

BioMutaⁱ	GNAI1
DMDMⁱ	52000964

Proteomic databases

EPDⁱ	P63096
MaxQBⁱ	P63096
PaxDbⁱ	P63096
PeptideAtlasⁱ	P63096
PRIDEⁱ	P63096
ProteomicsDBⁱ	57475

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	2770
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000351004; ENSP00000343027; ENSG00000127955 [P63096-1] ENST00000457358; ENSP00000410572; ENSG00000127955 [P63096-2]
GeneIDⁱ	2770
KEGGⁱ	hsa:2770
UCSCⁱ	uc003uhb.2 human [P63096-1]

Organism-specific databases

CTDⁱ	2770
DisGeNETⁱ	2770
EuPathDBⁱ	HostDB:ENSG00000127955.15
GeneCardsⁱ	GNAI1
HGNCⁱ	HGNC:4384 GNAI1
HPAⁱ	CAB022449 HPA042141
MIMⁱ	139310 gene
neXtProtⁱ	NX_P63096
OpenTargetsⁱ	ENSG00000127955
PharmGKBⁱ	PA172
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0082 Eukaryota ENOG410XNVQ LUCA
GeneTreeⁱ	ENSGT00760000118851
HOGENOMⁱ	HOG000038730
HOVERGENⁱ	HBG063184
InParanoidⁱ	P63096
KOⁱ	K04630
OMAⁱ	RIAQTSY
OrthoDBⁱ	EOG091G0VUT
PhylomeDBⁱ	P63096
TreeFamⁱ	TF300673

Enzyme and pathway databases

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
SignaLinkⁱ	P63096
SIGNORⁱ	P63096

Miscellaneous databases

ChiTaRSⁱ	GNAI1 human
EvolutionaryTraceⁱ	P63096
GeneWikiⁱ	GNAI1
GenomeRNAiⁱ	2770
Protein Ontology More...PROⁱ	PR:P63096
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000127955 Expressed in 223 organ(s), highest expression level in corpus callosum
CleanExⁱ	HS_GNAI1
ExpressionAtlasⁱ	P63096 baseline and differential
Genevisibleⁱ	P63096 HS

Family and domain databases

CDDⁱ	cd00066 G-alpha, 1 hit
Gene3Dⁱ	1.10.400.10, 1 hit
InterProⁱ	View protein in InterPro IPR001408 Gprotein_alpha_I IPR001019 Gprotein_alpha_su IPR011025 GproteinA_insert IPR027417 P-loop_NTPase
PANTHERⁱ	PTHR10218 PTHR10218, 1 hit
Pfamⁱ	View protein in Pfam PF00503 G-alpha, 1 hit
PRINTSⁱ	PR00318 GPROTEINA PR00441 GPROTEINAI
SMARTⁱ	View protein in SMART SM00275 G_alpha, 1 hit
SUPFAMⁱ	SSF47895 SSF47895, 1 hit SSF52540 SSF52540, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GNAI1_HUMAN
Accessionⁱ	P63096Primary (citable) accession number: P63096 Secondary accession number(s): A8KA88 Q9UGA4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 162 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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.

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P63096 (GNAI1_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

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

Select a section on the left to see content.

<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

Sites

Regions

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Plasma membrane

Cytoskeleton

Nucleus

Other locations

Cytoskeleton

Extracellular region or secreted

Lysosome

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<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

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ