P04899 (GNAI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein G(i) subunit alpha-2

Alternative name(s):
Adenylate cyclase-inhibiting G alpha protein

Gene names

Name:	GNAI2
Synonyms:	GNAI2B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division. Ref.4 Ref.12 Isoform sGi2: Regulates the cell surface density of dopamine receptors DRD2 by sequestrating them as an intracellular pool. Ref.4 Ref.12
Subunit structure	G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with GPSM1. Interacts with RGS12 and RGS14 By similarity. Interacts with UNC5B. Ref.11
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome. Cell membrane. Note: Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. Ref.12
Sequence similarities	Belongs to the G-alpha family. G(i/o/t/z) subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	ADP-ribosylation Lipoprotein Myristate Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled acetylcholine receptor signaling pathway Inferred from electronic annotation. Source: Compara activation of MAPKK activity Inferred from electronic annotation. Source: Compara adenosine receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Traceable author statement. Source: Reactome cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from mutant phenotype Ref.12. Source: UniProtKB cell proliferation Inferred from electronic annotation. Source: Compara gamma-aminobutyric acid signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome intracellular protein kinase cascade Inferred from electronic annotation. Source: Compara negative regulation of adenylate cyclase activity Traceable author statement PubMed 9637720. Source: ProtInc negative regulation of synaptic transmission Inferred from electronic annotation. Source: Compara platelet activation Traceable author statement. Source: Reactome positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of calcium ion transport Inferred from electronic annotation. Source: Compara response to nutrient Traceable author statement PubMed 8587610. Source: ProtInc synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	centrosome Inferred from direct assay Ref.12. Source: UniProtKB cytoplasm Inferred from direct assay Ref.12. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome membrane raft Inferred from electronic annotation. Source: Compara midbody Inferred from direct assay Ref.12. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein coupled receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from Biological aspect of Ancestor. Source: RefGenome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDFI	Q99750	2	EBI-353997,EBI-724076

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P04899-1)

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.

Isoform 2 (identifier: P04899-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLL → MEYAGHLPASSAQGTILACTSCT

Isoform 3 (identifier: P04899-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLL → MR

Note: No experimental confirmation available.

Isoform sGi2 (identifier: P04899-4)

Also known as: sGalphai2;

The sequence of this isoform differs from the canonical sequence as follows:
     332-355: NVQFVFDAVTDVIIKNNLKDCGLF → SRKLFRETYLKLSGPDQHPHPSPAPAPPLSSDSVP

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 355	355	Guanine nucleotide-binding protein G(i) subunit alpha-2		PRO_0000203679
Regions
	Nucleotide binding	40 – 47	8	GTP By similarity
	Nucleotide binding	176 – 182	7	GTP By similarity
	Nucleotide binding	201 – 205	5	GTP By similarity
	Nucleotide binding	270 – 273	4	GTP By similarity
Sites
	Metal binding	47	1	Magnesium By similarity
	Metal binding	182	1	Magnesium By similarity
	Binding site	327	1	GTP; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	179	1	ADP-ribosylarginine; by cholera toxin By similarity
	Modified residue	352	1	ADP-ribosylcysteine; by pertussis toxin By similarity
	Lipidation	2	1	N-myristoyl glycine
	Lipidation	3	1	S-palmitoyl cysteine By similarity
Natural variations
	Alternative sequence	1 – 39	39	MGCTV…KLLLL → MEYAGHLPASSAQGTILACT SCT in isoform 2.		VSP_017497
	Alternative sequence	1 – 39	39	MGCTV…KLLLL → MR in isoform 3.		VSP_043473
	Alternative sequence	332 – 355	24	NVQFV…DCGLF → SRKLFRETYLKLSGPDQHPH PSPAPAPPLSSDSVP in isoform sGi2.		VSP_043903

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BE6D6FF720CF3DCC	FASTA	355	40,451
	10 20 30 40 50 60 MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG 70 80 90 100 110 120 YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPSR ADDARQLFAL SCTAEEQGVL 130 140 150 160 170 180 PDDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV 190 200 210 220 230 240 KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE 250 260 270 280 290 300 MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT HSPLTICFPE YTGANKYDEA 310 320 330 340 350 ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF
	Isoform 2 [UniParc]. Checksum: F14AB734881535C5	FASTA	339	38,473
	10 20 30 40 50 60 MEYAGHLPAS SAQGTILACT SCTGAGESGK STIVKQMKII HEDGYSEEEC RQYRAVVYSN 70 80 90 100 110 120 TIQSIMAIVK AMGNLQIDFA DPSRADDARQ LFALSCTAEE QGVLPDDLSG VIRRLWADHG 130 140 150 160 170 180 VQACFGRSRE YQLNDSAAYY LNDLERIAQS DYIPTQQDVL RTRVKTTGIV ETHFTFKDLH 190 200 210 220 230 240 FKMFDVGGQR SERKKWIHCF EGVTAIIFCV ALSAYDLVLA EDEEMNRMHE SMKLFDSICN 250 260 270 280 290 300 NKWFTDTSII LFLNKKDLFE EKITHSPLTI CFPEYTGANK YDEAASYIQS KFEDLNKRKD 310 320 330 TKEIYTHFTC ATDTKNVQFV FDAVTDVIIK NNLKDCGLF
	Isoform 3 [UniParc]. Checksum: A0131D7E46EC5370	FASTA	318	36,465
	10 20 30 40 50 60 MRGAGESGKS TIVKQMKIIH EDGYSEEECR QYRAVVYSNT IQSIMAIVKA MGNLQIDFAD 70 80 90 100 110 120 PSRADDARQL FALSCTAEEQ GVLPDDLSGV IRRLWADHGV QACFGRSREY QLNDSAAYYL 130 140 150 160 170 180 NDLERIAQSD YIPTQQDVLR TRVKTTGIVE THFTFKDLHF KMFDVGGQRS ERKKWIHCFE 190 200 210 220 230 240 GVTAIIFCVA LSAYDLVLAE DEEMNRMHES MKLFDSICNN KWFTDTSIIL FLNKKDLFEE 250 260 270 280 290 300 KITHSPLTIC FPEYTGANKY DEAASYIQSK FEDLNKRKDT KEIYTHFTCA TDTKNVQFVF 310 DAVTDVIIKN NLKDCGLF
	Isoform sGi2 (sGalphai2) [UniParc]. Checksum: EF7FED14C8A0A8B4	FASTA	366	41,548
	10 20 30 40 50 60 MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG 70 80 90 100 110 120 YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPSR ADDARQLFAL SCTAEEQGVL 130 140 150 160 170 180 PDDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV 190 200 210 220 230 240 KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE 250 260 270 280 290 300 MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT HSPLTICFPE YTGANKYDEA 310 320 330 340 350 360 ASYIQSKFED LNKRKDTKEI YTHFTCATDT KSRKLFRETY LKLSGPDQHP HPSPAPAPPL SSDSVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human Gi protein alpha-subunit: deduction of amino acid structure from a cloned cDNA." Didsbury J.R., Ho Y.-S., Snyderman R. FEBS Lett. 211:160-164(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"A small multigene family encodes Gi signal-transduction proteins." Beals C.R., Wilson C.B., Perlmutter R.M. Proc. Natl. Acad. Sci. U.S.A. 84:7886-7890(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs." Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y. J. Biol. Chem. 263:6656-6664(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Role of a Galphai2 protein splice variant in the formation of an intracellular dopamine D2 receptor pool." Lopez-Aranda M.F., Acevedo M.J., Gutierrez A., Koulen P., Khan Z.U. J. Cell Sci. 120:2171-2178(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SGI2), FUNCTION. Tissue: Brain.
[5]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Testis.
[7]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Kidney and Mammary gland.
[10]	"Cloning and characterization of the human gene for the alpha-subunit of Gi2, a GTP-binding signal transduction protein." Weinstein L.S., Spiegel A.M., Carter A.D. FEBS Lett. 232:333-340(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
[11]	"Modulation of G(ialpha(2)) signaling by the axonal guidance molecule UNC5H2." Komatsuzaki K., Dalvin S., Kinane T.B. Biochem. Biophys. Res. Commun. 297:898-905(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UNC5B.
[12]	"Localization of Gi alpha proteins in the centrosomes and at the midbody: implication for their role in cell division." Cho H., Kehrl J.H. J. Cell Biol. 178:245-255(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04828 mRNA. Translation: CAA28512.1. J03004 mRNA. Translation: AAA52556.1. Sequence problems. M20593 , M20586, M20587, M20588, M20589, M20590, M20591, M20592 Genomic DNA. Translation: AAA35894.1. AY677118 mRNA. Translation: AAT78421.1. AF493906 mRNA. Translation: AAM12620.1. AK302330 mRNA. Translation: BAG63662.1. AC002077 Genomic DNA. No translation available. U73166 Genomic DNA. No translation available. U73169 Genomic DNA. No translation available. CH471055 Genomic DNA. Translation: EAW65056.1. BC012138 mRNA. Translation: AAH12138.1. BC016995 mRNA. Translation: AAH16995.1. X07854 Genomic DNA. Translation: CAA30703.1.
IPI	IPI00217906. IPI00748145. IPI00926935. IPI01015661.
PIR	RGHUI2. S02319.
RefSeq	NP_001159897.1. NM_001166425.1. NP_002061.1. NM_002070.2.
UniGene	Hs.77269.
3D structure databases
ProteinModelPortal	P04899.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-602N.
IntAct	P04899. 18 interactions.
MINT	MINT-139884.
STRING	9606.ENSP00000312999.
PTM databases
PhosphoSite	P04899.
Polymorphism databases
DMDM	121023.
Proteomic databases
PaxDb	P04899.
PRIDE	P04899.
Protocols and materials databases
DNASU	2771.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266027; ENSP00000266027; ENSG00000114353. ENST00000313601; ENSP00000312999; ENSG00000114353. ENST00000451956; ENSP00000406369; ENSG00000114353. ENST00000574925; ENSP00000460235; ENSG00000263156. ENST00000576852; ENSP00000460226; ENSG00000263156.
GeneID	2771.
KEGG	hsa:2771.
UCSC	uc003cyo.1. human. uc003cyq.1. human.
Organism-specific databases
CTD	2771.
GeneCards	GC03P050263.
H-InvDB	HIX0003320.
HGNC	HGNC:4385. GNAI2.
HPA	HPA007704.
MIM	139360. gene.
neXtProt	NX_P04899.
PharmGKB	PA24347.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG322962.
HOGENOM	HOG000038730.
HOVERGEN	HBG063184.
InParanoid	P04899.
KO	K04630.
OrthoDB	EOG4WDDC1.
PhylomeDB	P04899.
Enzyme and pathway databases
Pathway_Interaction_DB	endothelinpathway. Endothelins. hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins. lysophospholipid_pathway. LPA receptor mediated events. er_nongenomic_pathway. Plasma membrane estrogen receptor signaling. s1p_s1p1_pathway. S1P1 pathway. s1p_s1p2_pathway. S1P2 pathway. s1p_s1p3_pathway. S1P3 pathway. s1p_s1p4_pathway. S1P4 pathway. s1p_s1p5_pathway. S1P5 pathway. s1p_meta_pathway. Sphingosine 1-phosphate (S1P) pathway. txa2pathway. Thromboxane A2 receptor signaling.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_13685. Neuronal System. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P04899.
Bgee	P04899.
CleanEx	HS_GNAI2.
Genevestigator	P04899.
GermOnline	ENSG00000114353. Homo sapiens.
Family and domain databases
Gene3D	1.10.400.10. 1 hit.
InterPro	IPR001408. Gprotein_alpha_I. IPR001019. Gprotein_alpha_su. IPR011025. GproteinA_insert. [Graphical view]
PANTHER	PTHR10218. PTHR10218. 1 hit.
Pfam	PF00503. G-alpha. 1 hit. [Graphical view]
PRINTS	PR00318. GPROTEINA. PR00441. GPROTEINAI.
SMART	SM00275. G_alpha. 1 hit. [Graphical view]
SUPFAM	SSF47895. Transducn_insert. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	GNAI2. human.
GenomeRNAi	2771.
NextBio	10900.
SOURCE	Search...

Entry information

Entry name

GNAI2_HUMAN

Accession

Primary (citable) accession number: P04899
Secondary accession number(s): B4DYA0, Q6B6N3, Q8IZ71

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 154 of the entry and version 3 of the sequence. [Complete history]

Entry status

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.