CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013698
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas 
Protein Synonyms/Alias
 Adenylate cyclase-stimulating G alpha protein; Extra large alphas protein; XLalphas 
Gene Name
 GNAS 
Gene Synonyms/Alias
 GNAS1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
696LGAGESGKSTIVKQMubiquitination[1, 2, 3, 4, 5]
701SGKSTIVKQMRILHVubiquitination[2, 3, 5]
731RSNSDGEKATKVQDIubiquitination[3]
734SDGEKATKVQDIKNNubiquitination[2, 3, 5]
739ATKVQDIKNNLKEAIubiquitination[2, 3, 4, 5]
824CAQYFLDKIDVIKQAubiquitination[3]
829LDKIDVIKQADYVPSubiquitination[2, 3, 4, 5, 6]
854TSGIFETKFQVDKVNubiquitination[2, 3, 5]
859ETKFQVDKVNFHMFDubiquitination[2, 3, 4, 5]
917QEALNLFKSIWNNRWubiquitination[2, 3, 4, 5, 6]
936SVILFLNKQDLLAEKubiquitination[1, 3, 5]
943KQDLLAEKVLAGKSKubiquitination[1, 2, 3, 4, 5]
948AEKVLAGKSKIEDYFubiquitination[2, 3, 5]
950KVLAGKSKIEDYFPEubiquitination[2, 3, 4, 5, 6]
981DPRVTRAKYFIRDEFubiquitination[2, 5]
Reference
 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865
Functional Description
 Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. XLas isoforms interact with the same set of receptors as Gnas isoforms (By similarity). 
Sequence Annotation
 NP_BIND 690 697 GTP (By similarity).
 NP_BIND 841 847 GTP (By similarity).
 NP_BIND 866 870 GTP (By similarity).
 NP_BIND 935 938 GTP (By similarity).
 METAL 697 697 Magnesium (By similarity).
 METAL 847 847 Magnesium (By similarity).
 BINDING 1009 1009 GTP; via amide nitrogen (By similarity).
 MOD_RES 844 844 ADP-ribosylarginine; by cholera toxin (By
 MOD_RES 995 995 Phosphoserine.  
Keyword
 ADP-ribosylation; Alternative splicing; Cell membrane; Coiled coil; Complete proteome; Cushing syndrome; Disease mutation; GTP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transducer. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1037 AA 
Protein Sequence
MGVRNCLYGN NMSGQRDIPP EIGEQPEQPP LEAPGAAAPG AGPSPAEEME TEPPHNEPIP 60
VENDGEACGP PEVSRPNFQV LNPAFREAGA HGSYSPPPEE AMPFEAEQPS LGGFWPTLEQ 120
PGFPSGVHAG LEAFGPALME PGAFSGARPG LGGYSPPPEE AMPFEFDQPA QRGCSQLLLQ 180
VPDLAPGGPG AAGVPGAPPE EPQALRPAKA GSRGGYSPPP EETMPFELDG EGFGDDSPPP 240
GLSRVIAQVD GSSQFAAVAA SSAVRLTPAA NAPPLWVPGA IGSPSQEAVR PPSNFTGSSP 300
WMEISGPPFE IGSAPAGVDD TPVNMDSPPI ALDGPPIKVS GAPDKRERAE RPPVEEEAAE 360
MEGAADAAEG GKVPSPGYGS PAAGAASADT AARAAPAAPA DPDSGATPED PDSGTAPADP 420
DSGAFAADPD SGAAPAAPAD PDSGAAPDAP ADPDSGAAPD APADPDAGAA PEAPAAPAAA 480
ETRAAHVAPA APDAGAPTAP AASATRAAQV RRAASAAPAS GARRKIHLRP PSPEIQAADP 540
PTPRPTRASA WRGKSESSRG RRVYYDEGVA SSDDDSSGDE SDDGTSGCLR WFQHRRNRRR 600
RKPQRNLLRN FLVQAFGGCF GRSESPQPKA SRSLKVKKVP LAEKRRQMRK EALEKRAQKR 660
AEKKRSKLID KQLQDEKMGY MCTHRLLLLG AGESGKSTIV KQMRILHVNG FNGEGGEEDP 720
QAARSNSDGE KATKVQDIKN NLKEAIETIV AAMSNLVPPV ELANPENQFR VDYILSVMNV 780
PDFDFPPEFY EHAKALWEDE GVRACYERSN EYQLIDCAQY FLDKIDVIKQ ADYVPSDQDL 840
LRCRVLTSGI FETKFQVDKV NFHMFDVGGQ RDERRKWIQC FNDVTAIIFV VASSSYNMVI 900
REDNQTNRLQ EALNLFKSIW NNRWLRTISV ILFLNKQDLL AEKVLAGKSK IEDYFPEFAR 960
YTTPEDATPE PGEDPRVTRA KYFIRDEFLR ISTASGDGRH YCYPHFTCAV DTENIRRVFN 1020
DCRDIIQRMH LRQYELL 1037 
Gene Ontology
 GO:0005829; C:cytosol; ISS:BHF-UCL.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0005834; C:heterotrimeric G-protein complex; 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; IBA:RefGenome.
 GO:0035255; F:ionotropic glutamate receptor binding; IBA:RefGenome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0031852; F:mu-type opioid receptor binding; IBA:RefGenome.
 GO:0004871; F:signal transducer activity; IBA:RefGenome.
 GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IBA:RefGenome.
 GO:0007610; P:behavior; IEA:Compara.
 GO:0051216; P:cartilage development; IEA:Compara.
 GO:0006306; P:DNA methylation; IEA:Compara.
 GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Compara.
 GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Compara.
 GO:0001958; P:endochondral ossification; IEA:Compara.
 GO:0006112; P:energy reserve metabolic process; IEA:Compara.
 GO:0071514; P:genetic imprinting; IEA:Compara.
 GO:0035264; P:multicellular organism growth; IEA:Compara.
 GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Compara.
 GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Compara.
 GO:0040032; P:post-embryonic body morphogenesis; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0007606; P:sensory perception of chemical stimulus; IBA:RefGenome.
 GO:0043588; P:skin development; IEA:Compara.
 GO:0001894; P:tissue homeostasis; IEA:Compara. 
Interpro
 IPR000367; Gprotein_alpha_S.
 IPR001019; Gprotein_alpha_su.
 IPR011025; GproteinA_insert.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00503; G-alpha 
SMART
 SM00275; G_alpha 
PROSITE
  
PRINTS
 PR00318; GPROTEINA.
 PR00443; GPROTEINAS.