Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-44689-00606
Entry Name
UniProt Accession
Theoretical PI
6.63
Molecular Weight
40840.75
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein alpha-2 subunit
Protein Synonyms/Alias
G alpha-2;
Gene Name
gpaB
Gene Synonyms/Alias
DDB_G0276267;
Created Date
01-APR-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGICASSME
[1]
N-Myristoylation
Organism
Dictyostelium discoideum (Slime mold)
NCBI Taxa ID
44689
Reference
[1] Root PA, Prince A, Gundersen RE. Aggregation of Dictyostelium discoideum isdependent on myristoylation and membrane localization of the G proteinalpha-subunit, G alpha 2. J Cell Biochem. 1999 Aug 1;74(2):301-11.[PMID:10404398]
Functional Description
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G alpha-2 is required for the early aggregation process and most of the known cAMP receptor-mediated responses.
Sequence Annotation
Nucleotide-binding: 38 45 GTP.
Nucleotide-binding: 179 185 GTP.
Nucleotide-binding: 204 208 GTP.
Nucleotide-binding: 272 275 GTP.
Metal binding site: 45 45 Magnesium.
Metal binding site: 185 185 Magnesium.
Binding site: 328 328 GTP; via amide nitrogen.
Modified residue: 113 113 Phosphoserine.
Protein Length
357 AA.
Protein Sequence
(Canonical)
MGICASSMEG EKTNTDINLS IEKERKKKHN EVKLLLLGAG ESGKSTISKQ MKIIHQSGYS  60
NEERKEFKPI ITRNILDNMR VLLDGMGRLG MTIDPSNSDA AVMIKELTSL QASIVTDCWG  120
ELNEDQGKKI KALWTDPGVK QAMRRANEFS TLPDSAPYFF DSIDRMTSPV YIPTDQDILH  180
TRVMTRGVHE TNFEIGKIKF RLVDVGGQRS ERKKWLSCFD DVTAVVFCVA LSEYDLLLYE  240
DNSTNRMLES LRVFSDVCNS WFVNTPIILF LNKSDLFREK IKHVDLSETF PEYKGGRDYE  300
RASNYIKERF WQINKTEQKA IYSHITCATD TNNIRVVFEA VKDIIFTQCV MKAGLYS     357
FASTA
(Canonical)
>LipidDB-44689-00606|P16051
MGICASSMEGEKTNTDINLSIEKERKKKHNEVKLLLLGAGESGKSTISKQMKIIHQSGYS
NEERKEFKPIITRNILDNMRVLLDGMGRLGMTIDPSNSDAAVMIKELTSLQASIVTDCWG
ELNEDQGKKIKALWTDPGVKQAMRRANEFSTLPDSAPYFFDSIDRMTSPVYIPTDQDILH
TRVMTRGVHETNFEIGKIKFRLVDVGGQRSERKKWLSCFDDVTAVVFCVALSEYDLLLYE
DNSTNRMLESLRVFSDVCNSWFVNTPIILFLNKSDLFREKIKHVDLSETFPEYKGGRDYE
RASNYIKERFWQINKTEQKAIYSHITCATDTNNIRVVFEAVKDIIFTQCVMKAGLYS
Gene Ontology
GO:0005834; C:heterotrimeric G-protein complex; IDA:dictyBase
GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome
GO:0001664; F:G-protein coupled receptor binding; IDA:dictyBase
GO:0005525; F:GTP binding; IC:dictyBase
GO:0003924; F:GTPase activity; IMP:dictyBase
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; IBA:RefGenome
GO:0032861; P:activation of Rap GTPase activity; IMP:dictyBase
GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IMP:dictyBase
GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IDA:dictyBase
GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase
GO:0006935; P:chemotaxis; IMP:dictyBase
GO:0045762; P:positive regulation of adenylate cyclase activity; IMP:dictyBase
GO:0031284; P:positive regulation of guanylate cyclase activity; IMP:dictyBase
GO:0046578; P:regulation of Ras protein signal transduction; IMP:dictyBase
Interpro
InterPro; IPR002975; Fungi_Gprotein_alpha
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; PR01241; GPROTEINAFNG;