Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00174
Entry Name
UniProt Accession
Theoretical PI
5.5
Molecular Weight
40532.19
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein G(k) subunit alpha
Protein Synonyms/Alias
G(i) alpha-3;
Gene Name
GNAI3
Gene Synonyms/Alias
Created Date
01-NOV-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
3
Canonical
*****MGCTLSAEDK
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(k) is the stimulatory G protein of receptor- regulated K(+) channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.
Sequence Annotation
Nucleotide-binding: 40 47 GTP.
Nucleotide-binding: 175 181 GTP.
Nucleotide-binding: 200 204 GTP.
Nucleotide-binding: 269 272 GTP.
Metal binding site: 47 47 Magnesium.
Metal binding site: 181 181 Magnesium.
Binding site: 326 326 GTP; via amide nitrogen.
Modified residue: 178 178 ADP-ribosylarginine; by cholera toxin.
Modified residue: 351 351 ADP-ribosylcysteine; by pertussis toxin.
Protein Length
354 AA.
Protein Sequence
(Canonical)
MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV KQMKIIHEDG  60
YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGEAAR ADDARQLFVL AGSAEEGVMT  120
PELAGVIKRL WRDGGVQACF SRSREYQLND SASYYLNDLD RISQSNYIPT QQDVLRTRVK  180
TTGIVETHFT FKDLYFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM  240
NRMHESMKLF DSICNNKWFT ETSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA  300
AYIQCQFEDL NRRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKE CGLY        354
FASTA
(Canonical)
>LipidDB-9606-00174|P08754
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDG
YSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMT
PELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVK
TTGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM
NRMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAA
AYIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKECGLY
Gene Ontology
GO:0005813; C:centrosome; IDA:UniProtKB
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005794; C:Golgi apparatus; IEA:Ensembl
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0045121; C:membrane raft; IEA:Ensembl
GO:0030496; C:midbody; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0042588; C:zymogen granule; IEA:Ensembl
GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome
GO:0031821; F:G-protein coupled serotonin receptor binding; IBA:RefGenome
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IBA:RefGenome
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; IBA:RefGenome
GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:Reactome
GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0007049; P:cell cycle; IEA:UniProtKB-KW
GO:0051301; P:cell division; IDA:UniProtKB
GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc
GO:0030168; P:platelet activation; TAS:Reactome
GO:0007268; P:synaptic transmission; TAS:Reactome
GO:0006810; P:transport; NAS:ProtInc
GO:0006906; P:vesicle fusion; IEA:Ensembl
Interpro
InterPro; IPR001408; Gprotein_alpha_I
InterPro; IPR001019; Gprotein_alpha_su
InterPro; IPR011025; GproteinA_insert
InterPro; IPR027417; P-loop_NTPase
Pfam
Pfam; PF00503; G-alpha;
SMART
SMART; SM00275; G_alpha;
PROSITE
PRINTS
PRINTS; PR00318; GPROTEINA;
PRINTS; PR00441; GPROTEINAI;