Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01307
Entry Name
UniProt Accession
Theoretical PI
5.81
Molecular Weight
41570.64
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein subunit alpha-14
Protein Synonyms/Alias
G alpha-14; G-protein subunit alpha-14;
Gene Name
GNA14
Gene Synonyms/Alias
Created Date
15-JUL-1999
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
4
Canonical
****MAGCCCLSAEE
[1]
S-Palmitoylation
5
Canonical
***MAGCCCLSAEEK
[1]
S-Palmitoylation
6
Canonical
**MAGCCCLSAEEKE
[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: 42 49 GTP.
Nucleotide-binding: 176 182 GTP.
Nucleotide-binding: 201 205 GTP.
Nucleotide-binding: 270 273 GTP.
Metal binding site: 49 49 Magnesium.
Metal binding site: 182 182 Magnesium.
Binding site: 327 327 GTP; via amide nitrogen.
Modified residue: 179 179 ADP-ribosylarginine; by cholera toxin.
Protein Length
355 AA.
Protein Sequence
(Canonical)
MAGCCCLSAE EKESQRISAE IERQLRRDKK DARRELKLLL LGTGESGKST FIKQMRIIHG  60
SGYSDEDRKG FTKLVYQNIF TAMQAMIRAM DTLRIQYVCE QNKENAQIIR EVEVDKVSML  120
SREQVEAIKQ LWQDPGIQEC YDRRREYQLS DSAKYYLTDI DRIATPSFVP TQQDVLRVRV  180
PTTGIIEYPF DLENIIFRMV DVGGQRSERR KWIHCFESVT SIIFLVALSE YDQVLAECDN  240
ENRMEESKAL FKTIITYPWF LNSSVILFLN KKDLLEEKIM YSHLISYFPE YTGPKQDVRA  300
ARDFILKLYQ DQNPDKEKVI YSHFTCATDT DNIRFVFAAV KDTILQLNLR EFNLV       355
FASTA
(Canonical)
>LipidDB-9606-01307|O95837
MAGCCCLSAEEKESQRISAEIERQLRRDKKDARRELKLLLLGTGESGKSTFIKQMRIIHG
SGYSDEDRKGFTKLVYQNIFTAMQAMIRAMDTLRIQYVCEQNKENAQIIREVEVDKVSML
SREQVEAIKQLWQDPGIQECYDRRREYQLSDSAKYYLTDIDRIATPSFVPTQQDVLRVRV
PTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFESVTSIIFLVALSEYDQVLAECDN
ENRMEESKALFKTIITYPWFLNSSVILFLNKKDLLEEKIMYSHLISYFPEYTGPKQDVRA
ARDFILKLYQDQNPDKEKVIYSHFTCATDTDNIRFVFAAVKDTILQLNLREFNLV
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome
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; IBA:RefGenome
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:0030168; P:platelet activation; TAS:Reactome
GO:0007165; P:signal transduction; TAS:ProtInc
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;