Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00248
Entry Name
UniProt Accession
Theoretical PI
8.41
Molecular Weight
44054.63
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein subunit alpha-13
Protein Synonyms/Alias
G alpha-13; G-protein subunit alpha-13;
Gene Name
Gna13
Gene Synonyms/Alias
Gna-13;
Created Date
01-AUG-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
14
Canonical
SRSVLSVCFPGCVLT
[1]
S-Palmitoylation
18
Canonical
LSVCFPGCVLTNGEA
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Bhattacharyya R, Wedegaertner PB. Galpha 13 requires palmitoylation for plasmamembrane localization, Rho-dependent signaling, and promotion of p115-RhoGEFmembrane binding. J Biol Chem. 2000 May 19;275(20):14992-9.[PMID:10747909]
Functional Description
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Sequence Annotation
Nucleotide-binding: 55 62 GTP.
Nucleotide-binding: 197 203 GTP.
Nucleotide-binding: 222 226 GTP.
Nucleotide-binding: 291 294 GTP.
Metal binding site: 62 62 Magnesium.
Metal binding site: 203 203 Magnesium.
Binding site: 349 349 GTP; via amide nitrogen.
Modified residue: 203 203 Phosphothreonine.
Protein Length
377 AA.
Protein Sequence
(Canonical)
MADFLPSRSV LSVCFPGCVL TNGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG  60
KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNKNQLHGD  120
KLMAFDTRAP MAAQGMVETR VFLQYLPAIR ALWEDSGIQN AYDRRREFQL GESVKYFLDN  180
LDKLGVPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV  240
TSILFLVSSS EFDQVLMEDR QTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV  300
QVVSIKDYFL EFEGDPHCLR DVQKFLVECF RGKRRDQQQR PLYHHFTTAI NTENIRLVFR  360
DVKDTILHDN LKQLMLQ                                                 377
FASTA
(Canonical)
>LipidDB-10090-00248|P27601
MADFLPSRSVLSVCFPGCVLTNGEAEQQRKSKEIDKCLSREKTYVKRLVKILLLGAGESG
KSTFLKQMRIIHGQDFDQRAREEFRPTIYSNVIKGMRVLVDAREKLHIPWGDNKNQLHGD
KLMAFDTRAPMAAQGMVETRVFLQYLPAIRALWEDSGIQNAYDRRREFQLGESVKYFLDN
LDKLGVPDYIPSQQDILLARRPTKGIHEYDFEIKNVPFKMVDVGGQRSERKRWFECFDSV
TSILFLVSSSEFDQVLMEDRQTNRLTESLNIFETIVNNRVFSNVSIILFLNKTDLLEEKV
QVVSIKDYFLEFEGDPHCLRDVQKFLVECFRGKRRDQQQRPLYHHFTTAINTENIRLVFR
DVKDTILHDNLKQLMLQ
Gene Ontology
GO:0031526; C:brush border membrane; IBA:RefGenome
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005834; C:heterotrimeric G-protein complex; ISA:MGI
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0031752; F:D5 dopamine receptor binding; IBA:RefGenome
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; ISA:MGI
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; IBA:RefGenome
GO:0031702; F:type 1 angiotensin receptor binding; IBA:RefGenome
GO:0031584; P:activation of phospholipase D activity; IBA:RefGenome
GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IGI:MGI
GO:0001525; P:angiogenesis; IMP:MGI
GO:0030154; P:cell differentiation; IDA:MGI
GO:0007186; P:G-protein coupled receptor signaling pathway; ISA:MGI
GO:0001701; P:in utero embryonic development; IGI:MGI
GO:0035556; P:intracellular signal transduction; IDA:MGI
GO:0001569; P:patterning of blood vessels; IMP:MGI
GO:0030168; P:platelet activation; IMP:MGI
GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl
GO:0030334; P:regulation of cell migration; IMP:MGI
GO:0008360; P:regulation of cell shape; IDA:MGI
GO:0007266; P:Rho protein signal transduction; IDA:MGI
Interpro
InterPro; IPR000469; Gprotein_alpha_12
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; PR00440; GPROTEINA12;