Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00249
Entry Name
UniProt Accession
Theoretical PI
9.84
Molecular Weight
44095.08
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein subunit alpha-12
Protein Synonyms/Alias
G alpha-12; G-protein subunit alpha-12;
Gene Name
Gna12
Gene Synonyms/Alias
Gna-12;
Created Date
01-AUG-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
11
Canonical
VVRTLSRCLLPAEAG
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Jones TL, Gutkind JS. Galpha12 requires acylation for its transformingactivity. Biochemistry. 1998 Mar 3;37(9):3196-202.[PMID:9485474]
Functional Description
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. May play a role in the control of cell migration through the TOR signaling cascade.
Sequence Annotation
Nucleotide-binding: 62 69 GTP.
Nucleotide-binding: 200 206 GTP.
Nucleotide-binding: 225 229 GTP.
Nucleotide-binding: 294 297 GTP.
Metal binding site: 69 69 Magnesium.
Metal binding site: 206 206 Magnesium.
Binding site: 351 351 GTP; via amide nitrogen.
Protein Length
379 AA.
Protein Sequence
(Canonical)
MSGVVRTLSR CLLPAEAGAR ERRAGAARDA EREARRRSRD IDALLARERR AVRRLVKILL  60
LGAGESGKST FLKQMRIIHG REFDQKALLE FRDTIFDNIL KGSRVLVDAR DKLGIPWQHS  120
ENEKHGMFLM AFENKAGLPV EPATFQLYVP ALSALWRDSG IREAFSRRSE FQLGESVKYF  180
LDNLDRIGQL NYFPSKQDIL LARKATKGIV EHDFVIKKIP FKMVDVGGQR SQRQKWFQCF  240
DGITSILFMV SSSEYDQVLM EDRRTNRLVE SMNIFETIVN NKLFFNVSII LFLNKMDLLV  300
EKVKSVSIKK HFPDFKGDPH RLEDVQRYLV QCFDRKRRNR SKPLFHHFTT AIDTENIRFV  360
FHAVKDTILQ ENLKDIMLQ                                               379
FASTA
(Canonical)
>LipidDB-10090-00249|P27600
MSGVVRTLSRCLLPAEAGARERRAGAARDAEREARRRSRDIDALLARERRAVRRLVKILL
LGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILKGSRVLVDARDKLGIPWQHS
ENEKHGMFLMAFENKAGLPVEPATFQLYVPALSALWRDSGIREAFSRRSEFQLGESVKYF
LDNLDRIGQLNYFPSKQDILLARKATKGIVEHDFVIKKIPFKMVDVGGQRSQRQKWFQCF
DGITSILFMVSSSEYDQVLMEDRRTNRLVESMNIFETIVNNKLFFNVSIILFLNKMDLLV
EKVKSVSIKKHFPDFKGDPHRLEDVQRYLVQCFDRKRRNRSKPLFHHFTTAIDTENIRFV
FHAVKDTILQENLKDIMLQ
Gene Ontology
GO:0031526; C:brush border membrane; IBA:RefGenome
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome
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:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:RefGenome
GO:0030154; P:cell differentiation; IDA:MGI
GO:0042733; P:embryonic digit morphogenesis; IGI: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:0008360; P:regulation of cell shape; IDA:MGI
GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB
GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB
GO:0032006; P:regulation of TOR signaling; IMP:UniProtKB
GO:0042493; P:response to drug; IEA:Ensembl
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;