P63096 (GNAI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:

GNAI1

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	354 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. 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. May play a role in cell division. Ref.12 Ref.18
Subunit structure	Interacts with GPSM1. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains); the interaction occurs in the centrosomes. Interacts (GDP-bound form) with RIC8A (via C-terminus) By similarity. Interacts with DRD2. G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Ref.18
Subcellular location	Nucleus By similarity. Cytoplasm. Cell membrane. Cytoplasm › cytoskeleton › centrosome. Note: Localized at the plasma membrane throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma membrane By similarity. Localizes in the centrosomes of interphase and mitotic cells, but not in centrosomes during cytokinesis. Detected at the cleavage furrow 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 Nucleus
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	ADP-ribosylation Lipoprotein Myristate Palmitate
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 platelet activation Traceable author statement. Source: Reactome response to peptide hormone stimulus Inferred from sequence or structural similarity. Source: BHF-UCL 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 heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome midbody Inferred from direct assay Ref.12. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein coupled serotonin receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from sequence or structural similarity. Source: BHF-UCL 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
GPSM2	P81274	3	EBI-618639,EBI-618655
NUMA1	Q14980	4	EBI-618639,EBI-521611

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P63096-1)

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: P63096-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 354

354

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

PRO_0000203671

Regions

Nucleotide binding

40 – 47

8

GTP

Nucleotide binding

175 – 181

7

GTP By similarity

Nucleotide binding

200 – 204

5

GTP

Nucleotide binding

269 – 272

4

GTP

Sites

Metal binding

47

1

Magnesium By similarity

Metal binding

181

1

Magnesium By similarity

Binding site

326

1

GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue

178

1

ADP-ribosylarginine; by cholera toxin By similarity

Modified residue

351

1

ADP-ribosylcysteine; by pertussis toxin By similarity

Lipidation

2

1

N-myristoyl glycine Ref.13

Lipidation

3

1

S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence

1 – 52

52

Missing in isoform 2.

VSP_045215

Experimental info

Mutagenesis

116

1

E → L: Enhances interaction (inactive GDP-bound) with RGS14. Ref.17 Ref.20

Mutagenesis

147

1

Q → L: Enhances interaction (inactive GDP-bound) with RGS14. Ref.17 Ref.20

Mutagenesis

245

1

E → L: Enhances interaction (inactive GDP-bound) with RGS14. Ref.20

Sequence conflict

138

1

A → G in CAB43212. Ref.3

Sequence conflict

219

1

T → A in AAH26326. Ref.8

Sequence conflict

244

1

H → Y in AAV38580. Ref.4

Sequence conflict

249

1

L → M in AAV38580. Ref.4

Sequence conflict

288

1

P → Q in AAH26326. Ref.8

Secondary structure

1

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354

Helix Strand Turn

Details...

Helix

9 – 16

8

Helix

20 – 23

4

Helix

27 – 29

3

Beta strand

31 – 41

11

Helix

46 – 57

12

Helix

63 – 67

5

Helix

70 – 91

22

Helix

100 – 113

14

Beta strand

115 – 117

3

Helix

121 – 132

12

Helix

134 – 140

7

Helix

141 – 145

5

Helix

152 – 157

6

Helix

159 – 162

4

Beta strand

164 – 166

3

Helix

171 – 175

5

Beta strand

183 – 191

9

Beta strand

194 – 201

8

Helix

208 – 215

8

Beta strand

220 – 226

7

Helix

227 – 229

3

Beta strand

238 – 241

4

Helix

242 – 254

13

Helix

257 – 259

3

Beta strand

260 – 269

10

Helix

271 – 277

7

Turn

278 – 280

3

Helix

283 – 285

3

Helix

296 – 308

13

Turn

314 – 316

3

Beta strand

319 – 323

5

Helix

329 – 346

18

Helix

348 – 350

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9F88311B46E62DE3	FASTA	354	40,361
	10 20 30 40 50 60 MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG 70 80 90 100 110 120 YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR ADDARQLFVL AGAAEEGFMT 130 140 150 160 170 180 AELAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK 190 200 210 220 230 240 TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM 250 260 270 280 290 300 NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA 310 320 330 340 350 AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
	Isoform 2 [UniParc]. Checksum: DA5ED62E61B790A9	FASTA	302	34,775
	10 20 30 40 50 60 MKIIHEAGYS EEECKQYKAV VYSNTIQSII AIIRAMGRLK IDFGDSARAD DARQLFVLAG 70 80 90 100 110 120 AAEEGFMTAE LAGVIKRLWK DSGVQACFNR SREYQLNDSA AYYLNDLDRI AQPNYIPTQQ 130 140 150 160 170 180 DVLRTRVKTT GIVETHFTFK DLHFKMFDVG GQRSERKKWI HCFEGVTAII FCVALSDYDL 190 200 210 220 230 240 VLAEDEEMNR MHESMKLFDS ICNNKWFTDT SIILFLNKKD LFEEKIKKSP LTICYPEYAG 250 260 270 280 290 300 SNTYEEAAAY IQCQFEDLNK RKDTKEIYTH FTCATDTKNV QFVFDAVTDV IIKNNLKDCG LF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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).
[2]	Yu W., Gibbs R.A. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"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] (ISOFORMS 1 AND 2). Tissue: Trachea.
[6]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] (ISOFORM 1). Tissue: Brain.
[9]	"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] OF 1-101.
[10]	"Human cDNA clones for an alpha subunit of Gi signal-transduction protein." Bray P., Carter A., Guo V., Puckett C., Kamholz J., Spiegel A., Nirenberg M. Proc. Natl. Acad. Sci. U.S.A. 84:5115-5119(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-354.
[11]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 91-100 AND 162-176. Tissue: Adipocyte.
[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]	"Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system." Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T. Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.
[14]	"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].
[15]	"Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits." Kimple R.J., Kimple M.E., Betts L., Sondek J., Siderovski D.P. Nature 416:878-881(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-349 IN COMPLEX WITH RGS14 AND GDP.
[16]	"Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange." Johnston C.A., Willard F.S., Jezyk M.R., Fredericks Z., Bodor E.T., Jones M.B., Blaesius R., Watts V.J., Harden T.K., Sondek J., Ramer J.K., Siderovski D.P. Structure 13:1069-1080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-354 IN COMPLEX WITH GDP.
[17]	"Structure-based protocol for identifying mutations that enhance protein-protein binding affinities." Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P., Kuhlman B. J. Mol. Biol. 371:1392-1404(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 31-354, MUTAGENESIS OF GLU-116 AND GLN-147.
[18]	"Structural basis for nucleotide exchange on G alpha i subunits and receptor coupling specificity." Johnston C.A., Siderovski D.P. Proc. Natl. Acad. Sci. U.S.A. 104:2001-2006(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH DRD2 AND GDP, FUNCTION, INTERACTION WITH DRD2.
[19]	Erratum Johnston C.A., Siderovski D.P. Proc. Natl. Acad. Sci. U.S.A. 109:1808-1808(2012) [PubMed] [Europe PMC] [Abstract] Cited for: RETRACTION.
[20]	"Structural determinants of affinity enhancement between GoLoco motifs and G-protein alpha subunit mutants." Bosch D.E., Kimple A.J., Sammond D.W., Muller R.E., Miley M.J., Machius M., Kuhlman B., Willard F.S., Siderovski D.P. J. Biol. Chem. 286:3351-3358(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 31-354 IN COMPLEX WITH RGS14 AND GDP, MUTAGENESIS OF GLU-116; GLN-147 AND GLU-245.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00337415.

PIR

RGHUI1. A28318.

RefSeq

NP_001243343.1. NM_001256414.1.
NP_002060.4. NM_002069.5.

UniGene

Hs.134587.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KJY	X-ray	2.70	A/C	31-354	[»]
1Y3A	X-ray	2.50	A/B/C/D	26-354	[»]
2G83	X-ray	2.80	A/B	33-344	[»]
2GTP	X-ray	2.55	A/B	32-353	[»]
2IK8	X-ray	2.71	A/C	31-353	[»]
2OM2	X-ray	2.20	A/C	31-354	[»]
2PZ3	X-ray	2.42	A	1-354	[»]
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	[»]

ProteinModelPortal

P63096.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63096. 16 interactions.

MINT

MINT-2913925.

STRING

9606.ENSP00000343027.

PTM databases

PhosphoSite

P63096.

Polymorphism databases

DMDM

52000964.

Proteomic databases

PaxDb

P63096.

PRIDE

P63096.

Protocols and materials databases

DNASU

2770.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000351004; ENSP00000343027; ENSG00000127955.
ENST00000457358; ENSP00000410572; ENSG00000127955.

GeneID

2770.

KEGG

hsa:2770.

UCSC

uc003uhb.1. human.

Organism-specific databases

CTD

2770.

GeneCards

GC07P079763.

HGNC

HGNC:4384. GNAI1.

HPA

CAB022449.

MIM

139310. gene.

neXtProt

NX_P63096.

PharmGKB

PA172.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG322962.

HOVERGEN

HBG063184.

InParanoid

P63096.

KO

K04630.

OMA

FFTHASA.

PhylomeDB

P63096.

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.

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13685. Neuronal System.
REACT_604. Hemostasis.

SignaLink

P63096.

Gene expression databases

ArrayExpress

P63096.

Bgee

P63096.

CleanEx

HS_GNAI1.

Genevestigator

P63096.

GermOnline

ENSG00000127955. 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.
IPR027417. P-loop_NTPase.
[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

SSF52540. SSF52540. 1 hit.
SSF47895. Transducn_insert. 1 hit.

ProtoNet

Search...

Other

BindingDB

P63096.

ChEMBL

CHEMBL4741.

EvolutionaryTrace

P63096.

GenomeRNAi

2770.

NextBio

10896.

SOURCE

Search...

Entry information

Entry name

GNAI1_HUMAN

Accession

Primary (citable) accession number: P63096
Secondary accession number(s): A8KA88 , B4E2V1, C9J3A4, P04898, P11015, P31871, Q5U074, Q8TAN5, Q9UGA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 108 of the entry and version 2 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.