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GART (human)

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: EC 6.3.3.1; Enzyme, cellular metabolism; Cofactor and Vitamin Metabolism - one carbon pool by folate; EC 6.3.4.13; Mitochondrial; Ligase; Methyltransferase; Nucleotide Metabolism - purine; EC 2.1.2.2 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; purine ribonucleoside monophosphate biosynthetic process; purine base biosynthetic process; response to inorganic substance; nucleobase, nucleoside and nucleotide metabolic process; organ 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 1MEJ - A/B/C=810-1010 (human) 1MEN - A/B/C=810-1010 (human) 1MEO - A=808-1010 (human) 1NJS - A/B=808-1010 (human) 1RBM - A/B=808-1010 (human) 1RBQ - A/B/C/D=808-1010 (human) 1RBY - A/B/C/D=808-1010 (human) 1RBZ - A/B=808-1010 (human) 1RC0 - A/B=808-1010 (human) 1RC1 - A/B=808-1010 (human) 1ZLX - A=808-1010 (human) 1ZLY - A=808-1010 (human) 2QK4 - A/B=1-430 (human) 2V9Y - A/B=467-794 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1MEJ 1MEN 1MEO 1NJS 1RBM 1RBQ 1RBY 1RBZ 1RC0 1RC1 1ZLX 1ZLY 2QK4 2V9Y  |  ENZYME 2.1.2.2 6.3.3.1 6.3.4.13  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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

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	10		K28-u	LAQSHHVkQVLVAPG
0	3		K44-u	AGTACSEkISNTAIS
0	10		K63-u	TALAQFCkEkkIEFV
0	1		K65-u	LAQFCkEkkIEFVVV
0	7		K66-u	AQFCkEkkIEFVVVG
0	12		K107-a	AAQLESSkRFAkEFM
0	56		K107-u	AAQLESSkRFAkEFM
0	5		K111-u	ESSkRFAkEFMDRHG
0	1		T121-p	MDRHGIPtAQWKAFT
0	1		K148-u	DFPALVVkASGLAAG
0	18		K156-u	ASGLAAGkGVIVAkS
0	7		K162-u	GkGVIVAkSKEEACK
0	1		K219-a	MPPAQDHkRLLEGDG
0	2		K219-u	MPPAQDHkRLLEGDG
0	34		K251-u	NDLLLKIkDTVLQRT
0	1		K281-u	YAGIMLTkNGPkVLE
0	10		K285-u	MLTkNGPkVLEFNCR
0	110		Y348-p	SKGYPGDytkGVEIT
0	14		T349-p	KGYPGDytkGVEITG
0	1		K350-a	GYPGDytkGVEITGF
0	5		K350-u	GYPGDytkGVEITGF
0	3		K375-u	FHAGTALkNGkVVTH
0	11		K378-u	GTALkNGkVVTHGGR
0	1		S398	AIRENLISALEEAkk
0	7		K404-u	ISALEEAkkGLAAIk
0	4		K405-u	SALEEAkkGLAAIkF
0	3		K411-u	kkGLAAIkFEGAIyR
0	6		Y417-p	IkFEGAIyRKDVGFR
0	10		K438-u	QPRSLTYkESGVDIA
0	1		S440	RSLTYkESGVDIAAG
0	1		K452	AAGNMLVKKIQPLAk
0	5		K459-u	KKIQPLAkATSRSGC
0	1		K467	ATSRSGCKVDLGGFA
0	3		K467-u	ATSRSGCkVDLGGFA
0	2		K480-u	FAGLFDLkAAGFkDP
0	3		K485-u	DLkAAGFkDPLLASG
0	1		T498-p	SGTDGVGtkLKIAQL
0	1		K499-u	GTDGVGtkLKIAQLC
0	2		K557-u	AVVAGIAkACGkAGC
0	1		K561-u	GIAkACGkAGCALLG
0	1		S625-p	GLHSNGFsLVRKIVA
0	1		S672-p	SLLPVLRsGHVKAFA
0	3		K697-u	IPRVLPEkLGVDLDA
0	1		K779-u	GSPRVKVkNLIESMQ
0	1		-	gap
0	5		T798-p	VLKNGSLtNHFsFEK
0	14		S802-p	GSLtNHFsFEKKKAR
0	1		K844-a	IDIVISNkAAVAGLD
0	1		T860-p	AERAGIPtRVINHkL
0	3		K866-u	PtRVINHkLYKNRVE
0	1		K910-u	FVQKWNGkMLNIHPS
0	15		K982-a	RVKLAEHkIFPAALQ

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

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