Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00774
Entry Name
UniProt Accession
Theoretical PI
5.51
Molecular Weight
42123.33
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein subunit alpha-11
Protein Synonyms/Alias
G alpha-11; G-protein subunit alpha-11; Guanine nucleotide-binding protein G(y) subunit alpha;
Gene Name
GNA11
Gene Synonyms/Alias
GA11;
Created Date
01-APR-1993
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
9
Canonical
TLESMMACCLSDEVK
[1]
S-Palmitoylation
10
Canonical
LESMMACCLSDEVKE
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Forrester MT, Hess DT, Thompson JW, Hultman R, Moseley MA, Stamler JS, CaseyPJ. Site-specific analysis of protein S-acylation by resin-assisted capture. JLipid Res. 2011 Feb;52(2):393-8. doi: 10.1194/jlr.D011106. Epub 2010 Nov 2.[PMID:21044946]
Functional Description
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C.
Sequence Annotation
Nucleotide-binding: 46 53 GTP.
Nucleotide-binding: 180 186 GTP.
Nucleotide-binding: 205 209 GTP.
Nucleotide-binding: 274 277 GTP.
Metal binding site: 53 53 Magnesium.
Metal binding site: 186 186 Magnesium.
Binding site: 331 331 GTP; via amide nitrogen.
Modified residue: 183 183 ADP-ribosylarginine; by cholera toxin.
Protein Length
359 AA.
Protein Sequence
(Canonical)
MTLESMMACC LSDEVKESKR INAEIEKQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR  60
IIHGAGYSEE DKRGFTKLVY QNIFTAMQAM IRAMETLKIL YKYEQNKANA LLIREVDVEK  120
VTTFEHQYVS AIKTLWEDPG IQECYDRRRE YQLSDSAKYY LTDVDRIATL GYLPTQQDVL  180
RVRVPTTGII EYPFDLENII FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV  240
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE DKILYSHLVD YFPEFDGPQR  300
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV   359
FASTA
(Canonical)
>LipidDB-9606-00774|P29992
MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMR
IIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEK
VTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVL
RVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQR
DAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Gene Ontology
GO:0005737; C:cytoplasm; TAS:ProtInc
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0031683; F:G-protein beta/gamma-subunit complex 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:0031826; F:type 2A serotonin receptor binding; IBA:RefGenome
GO:0001508; P:action potential; IBA:RefGenome
GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0071467; P:cellular response to pH; IEA:Ensembl
GO:0048066; P:developmental pigmentation; IEA:Ensembl
GO:0007507; P:heart development; IEA:Ensembl
GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:RefGenome
GO:0030168; P:platelet activation; TAS:Reactome
GO:0045634; P:regulation of melanocyte differentiation; IEA:Ensembl
GO:0007165; P:signal transduction; TAS:ProtInc
GO:0001501; P:skeletal system development; IEA:Ensembl
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;