Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00120
Entry Name
UniProt Accession
Theoretical PI
8.74
Molecular Weight
43568.03
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein subunit alpha-15
Protein Synonyms/Alias
G alpha-15; G-protein subunit alpha-15; Epididymis tissue protein Li 17E; Guanine nucleotide-binding protein subunit alpha-16; G alpha-16; G-protein subunit alpha-16;
Gene Name
GNA15
Gene Synonyms/Alias
GNA16;
Created Date
01-APR-1993
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
9
Canonical
ARSLTWRCCPWCLTE
[1]
S-Palmitoylation
10
Canonical
RSLTWRCCPWCLTED
[1]
S-Palmitoylation
13
Canonical
TWRCCPWCLTEDEKA
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Pedone KH, Hepler JR. The importance of N-terminal polycysteine and polybasic sequences for G14alpha and G16alpha palmitoylation, plasma membrane localization,and signaling function. J Biol Chem. 2007 Aug 31;282(35):25199-212. Epub 2007 Jul9.[PMID:17620339]
Functional Description
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Sequence Annotation
Nucleotide-binding: 49 56 GTP.
Nucleotide-binding: 183 189 GTP.
Nucleotide-binding: 208 212 GTP.
Nucleotide-binding: 277 280 GTP.
Metal binding site: 56 56 Magnesium.
Metal binding site: 189 189 Magnesium.
Binding site: 346 346 GTP; via amide nitrogen.
Modified residue: 186 186 ADP-ribosylarginine; by cholera toxin.
Protein Length
374 AA.
Protein Sequence
(Canonical)
MARSLTWRCC PWCLTEDEKA AARVDQEINR ILLEQKKQDR GELKLLLLGP GESGKSTFIK  60
QMRIIHGAGY SEEERKGFRP LVYQNIFVSM RAMIEAMERL QIPFSRPESK HHASLVMSQD  120
PYKVTTFEKR YAAAMQWLWR DAGIRAYYER RREFHLLDSA VYYLSHLERI TEEGYVPTAQ  180
DVLRSRMPTT GINEYCFSVQ KTNLRIVDVG GQKSERKKWI HCFENVIALI YLASLSEYDQ  240
CLEENNQENR MKESLALFGT ILELPWFKST SVILFLNKTD ILEEKIPTSH LATYFPSFQG  300
PKQDAEAAKR FILDMYTRMY TGCVDGPEGS KKGARSRRLF SHYTCATDTQ NIRKVFKDVR  360
DSVLARYLDE INLL                                                    374
FASTA
(Canonical)
>LipidDB-9606-00120|P30679
MARSLTWRCCPWCLTEDEKAAARVDQEINRILLEQKKQDRGELKLLLLGPGESGKSTFIK
QMRIIHGAGYSEEERKGFRPLVYQNIFVSMRAMIEAMERLQIPFSRPESKHHASLVMSQD
PYKVTTFEKRYAAAMQWLWRDAGIRAYYERRREFHLLDSAVYYLSHLERITEEGYVPTAQ
DVLRSRMPTTGINEYCFSVQKTNLRIVDVGGQKSERKKWIHCFENVIALIYLASLSEYDQ
CLEENNQENRMKESLALFGTILELPWFKSTSVILFLNKTDILEEKIPTSHLATYFPSFQG
PKQDAEAAKRFILDMYTRMYTGCVDGPEGSKKGARSRRLFSHYTCATDTQNIRKVFKDVR
DSVLARYLDEINLL
Gene Ontology
GO:0005834; C:heterotrimeric G-protein complex; NAS:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome
GO:0001664; F:G-protein coupled 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; IGI:UniProtKB
GO:0007202; P:activation of phospholipase C activity; TAS:ProtInc
GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:RefGenome
GO:0007207; P:phospholipase C-activating G-protein coupled acetylcholine receptor signaling pathway; TAS:ProtInc
GO:0030168; P:platelet activation; TAS:Reactome
GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IGI:UniProtKB
Interpro
InterPro; IPR000654; Gprotein_alpha_Q
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; PR00442; GPROTEINAQ;