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Protein Page:
GART (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
GART a highly conserved trifunctional enzyme. It has phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase activity which is required for de novo purine biosynthesis. Inhibition of the de novo purine synthesis by folate analogs blocks the p53-dependent G1 checkpoint in human carcinoma cell lines. Two splice variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Nucleotide Metabolism - purine; Cofactor and Vitamin Metabolism - one carbon pool by folate; Mitochondrial; EC 2.1.2.2; Methyltransferase; EC 6.3.3.1; Ligase; Enzyme, cellular metabolism; EC 6.3.4.13
Chromosomal Location of Human Ortholog: 21q22.11
Cellular Component: cytosol
Molecular Function: methyltransferase activity; phosphoribosylamine-glycine ligase activity; metal ion binding; phosphoribosylformylglycinamidine cyclo-ligase activity; phosphoribosylglycinamide formyltransferase activity; ATP binding
Biological Process: response to organic substance; methylation; purine ribonucleoside monophosphate biosynthetic process; glycine metabolic process; tetrahydrofolate biosynthetic process; response to inorganic substance; purine base biosynthetic process; nucleobase, nucleoside and nucleotide metabolic process; cerebellum development; cerebral cortex development; purine base metabolic process; 'de novo' IMP biosynthetic process
Reference #:  P22102 (UniProtKB)
Alt. Names/Synonyms: 5'-phosphoribosylglycinamide transformylase; AIR synthase; AIRS; GAR transformylase; GARS; GART; GARTF; Glycinamide ribonucleotide synthetase; MGC47764; PAIS; PGFT; Phosphoribosyl-aminoimidazole synthetase; Phosphoribosylamine--glycine ligase; Phosphoribosylformylglycinamidine cyclo-ligase; Phosphoribosylglycinamide formyltransferase; phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase; Phosphoribosylglycinamide synthetase; PRGS; PUR2; Trifunctional purine biosynthetic protein adenosine-3
Gene Symbols: GART
Molecular weight: 107,767 Da
Basal Isoelectric point: 6.26  Predict pI for various phosphorylation states
Select Structure to View Below

GART

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 S10-p ARVLIIGsGGREHTL
0 1 K28-ac LAQSHHVkQVLVAPG
0 10 K28-ub LAQSHHVkQVLVAPG
0 1 S42-p GNAGTACsEkISNTA
0 3 K44-ub AGTACsEkISNTAIS
0 10 K63-ub TALAQFCkEkkIEFV
0 1 K65-ub LAQFCkEkkIEFVVV
0 7 K66-ub AQFCkEkkIEFVVVG
0 12 K107-ac AAQLESSkRFAkEFM
0 56 K107-ub AAQLESSkRFAkEFM
0 5 K111-ub ESSkRFAkEFMDRHG
0 1 T121-p MDRHGIPtAQWKAFT
0 1 K148-ub DFPALVVkASGLAAG
0 1 K156 ASGLAAGKGVIVAkS
0 18 K156-ub ASGLAAGkGVIVAkS
0 7 K162-ub GkGVIVAkSKEEACK
0 1 K219-ac MPPAQDHkRLLEGDG
0 2 K219-ub MPPAQDHkRLLEGDG
0 34 K251-ub NDLLLKIkDTVLQRT
0 1 K281-ub YAGIMLTkNGPkVLE
0 10 K285-ub MLTkNGPkVLEFNCR
0 110 Y348-p SKGYPGDytkGVEIT
0 14 T349-p KGYPGDytkGVEITG
0 1 K350-ac GYPGDytkGVEITGF
0 5 K350-ub GYPGDytkGVEITGF
0 3 K375-ub FHAGTALkNGkVVTH
0 11 K378-ub GTALkNGkVVTHGGR
0 2 S398-p AIRENLIsALEEAkk
0 7 K404-ub IsALEEAkkGLAAIk
0 1 K404-sc IsALEEAkkGLAAIk
0 4 K405-ub sALEEAkkGLAAIkF
0 3 K411-ub kkGLAAIkFEGAIyR
0 7 Y417-p IkFEGAIyRKDVGFR
0 10 K438-ub QPRSLTYkEsGVDIA
0 2 S440-p RSLTYkEsGVDIAAG
0 1 K452 AAGNMLVKKIQPLAk
0 5 K459-ub KKIQPLAkATSRSGC
0 2 K467 ATSRSGCKVDLGGFA
0 3 K467-ub ATSRSGCkVDLGGFA
0 2 K480-ub FAGLFDLkAAGFkDP
0 3 K485-ub DLkAAGFkDPLLASG
0 1 T498-p SGTDGVGtkLKIAQL
0 1 K499-ub GTDGVGtkLKIAQLC
0 2 K557-ub AVVAGIAkACGkAGC
0 1 K561-ub GIAkACGkAGCALLG
0 1 S625-p GLHSNGFsLVRKIVA
0 1 S672-p SLLPVLRsGHVKAFA
0 1 T682-p VKAFAHItGGGLLEN
0 3 K697-ub IPRVLPEkLGVDLDA
0 1 K779-ub GSPRVKVkNLIEsMQ
0 1 S784-p KVkNLIEsMQINGSV
0 4 S796-p GSVLKNGsLtNHFsF
0 1 - gap
0 6 T798-p VLKNGsLtNHFsFEK
0 20 S802-p GsLtNHFsFEKKKAR
0 1 K844-ac IDIVISNkAAVAGLD
0 1 T860-p AERAGIPtRVINHkL
0 3 K866-ub PtRVINHkLYKNRVE
0 1 K910-ub FVQKWNGkMLNIHPS
0 15 K982-ac RVKLAEHkIFPAALQ
  mouse

 
S10 ARVLVIGSGGREHTL
K28 LAQSPQVKQVLVAPG
K28 LAQSPQVKQVLVAPG
A42 GNAGTACAGKISNAA
K44 AGTACAGKISNAAVS
K63 SALAQFCKDEKIELV
E65 LAQFCKDEKIELVVV
K66 AQFCKDEKIELVVVG
K107 AAQLESSKKFAKEFM
K107 AAQLESSKKFAKEFM
K111 ESSKKFAKEFMDRHE
T121 MDRHEIPTAQWRAFT
K148 NFPALVVKASGLAAG
K156-ac ASGLAAGkGVIVAKS
K156 ASGLAAGKGVIVAKS
K162 GkGVIVAKSQAEACR
K219 MPPAQDHKRLLDGDE
K219 MPPAQDHKRLLDGDE
K251 KDLLVKIKNTILQRA
K281 YAGIMLTKDGPkVLE
K285-ub MLTKDGPkVLEFNCR
Y348 SKGYPGAYtKGVEIT
T349-p KGYPGAYtKGVEITG
K350 GYPGAYtKGVEITGF
K350 GYPGAYtKGVEITGF
K375 FHAGTALKDGKVVTS
K378 GTALKDGKVVTSGGR
S398-p AVQENLMsALAEARK
R404 MsALAEARKGLAALK
R404 MsALAEARKGLAALK
K405 sALAEARKGLAALKF
K411 RKGLAALKFEGAIYR
Y417 LKFEGAIYRKDIGFR
K438-ub RPRGLTYkDsGVDIA
S440-p RGLTYkDsGVDIAAG
K452-ub AAGNMLVkKIQPLAk
K459-ub kKIQPLAkATSRPGC
S467-p ATSRPGCsVDLGGFA
S467 ATSRPGCSVDLGGFA
K480 FAGLFDLKAAGFkDP
K485-ub DLKAAGFkDPLLASG
T498 SGTDGVGTKLKIAQL
K499 GTDGVGTKLKIAQLC
A557 AVIAGIAAACQQAGC
Q561 GIAAACQQAGCALLG
S625 GLHSNGFSLVRKIVE
S672 SLLPIIRSGRVKAFA
T682 VKAFAHITGGGLLEN
K697-ub IPRVLPQkFGVDLDA
K779 DSPRVRVKNLIETIQ
T784 RVKNLIETIQTNGSL
F796 GSLVANGFLkSNFPV
K798-ub LVANGFLkSNFPVQQ
S799 VANGFLkSNFPVQQK
P802 GFLkSNFPVQQKKAR
K844 IVLVISNKAAVAGLD
T860 AERAGIPTRVINHkL
K866-ub PTRVINHkLYKNRVE
K910 FVRKWDGKMLNIHPS
K982 RVKVAEHKIFPAALQ
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