Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01273
Entry Name
UniProt Accession
Theoretical PI
7.53
Molecular Weight
40923.75
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein G(z) subunit alpha
Protein Synonyms/Alias
G(x) alpha chain; Gz-alpha;
Gene Name
GNAZ
Gene Synonyms/Alias
Created Date
01-NOV-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGCRQSSEE
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Wilson PT, Bourne HR. Fatty acylation of alpha z. Effects of palmitoylationand myristoylation on alpha z signaling. J Biol Chem. 1995 Apr21;270(16):9667-75.[PMID:7536745]
Functional Description
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Sequence Annotation
Nucleotide-binding: 40 47 GTP.
Nucleotide-binding: 176 182 GTP.
Nucleotide-binding: 201 205 GTP.
Nucleotide-binding: 270 273 GTP.
Metal binding site: 47 47 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)
MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG  60
FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR AYDAVQLFAL TGPAESKGEI  120
TPELLGVMRR LWADPGAQAC FSRSSEYHLE DNAAYYLNDL ERIAAADYIP TVEDILRSRD  180
MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ  240
TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA  300
AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC       355
FASTA
(Canonical)
>LipidDB-9606-01273|P19086
MGCRQSSEEKEAARRSRRIDRHLRSESQRQRREIKLLLLGTSNSGKSTIVKQMKIIHSGG
FNLEACKEYKPLIIYNAIDSLTRIIRALAALRIDFHNPDRAYDAVQLFALTGPAESKGEI
TPELLGVMRRLWADPGAQACFSRSSEYHLEDNAAYYLNDLERIAAADYIPTVEDILRSRD
MTTGIVENKFTFKELTFKMVDVGGQRSERKKWIHCFEGVTAIIFCVELSGYDLKLYEDNQ
TSRMAESLRLFDSICNNNWFINTSLILFLNKKDLLAEKIRRIPLTICFPEYKGQNTYEEA
AVYIQRQFEDLNRNKETKEIYSHFTCATDTSNIQFVFDAVTDVIIQNNLKYIGLC
Gene Ontology
GO:0005829; C:cytosol; IEA:Ensembl
GO:0005783; C:endoplasmic reticulum; TAS:ProtInc
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome
GO:0005635; C:nuclear envelope; TAS:ProtInc
GO:0005886; C:plasma membrane; TAS:Reactome
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:0005057; F:receptor signaling protein activity; TAS:ProtInc
GO:0004871; F:signal transducer activity; IBA:RefGenome
GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IEA:Ensembl
GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome
GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc
GO:0035556; P:intracellular signal transduction; TAS:GOC
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;