PYRG1_HUMAN - dbPTM
PYRG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYRG1_HUMAN
UniProt AC P17812
Protein Name CTP synthase 1 {ECO:0000305}
Gene Name CTPS1 {ECO:0000312|HGNC:HGNC:2519}
Organism Homo sapiens (Human).
Sequence Length 591
Subcellular Localization
Protein Description This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity..
Protein Sequence MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
12PhosphorylationLVTGGVISGIGKGII
EEECCCCCCCCCCHH		23.1921712546
21PhosphorylationIGKGIIASSVGTILK
CCCCHHHHHHHHHHH		18.3623403867
22PhosphorylationGKGIIASSVGTILKS
CCCHHHHHHHHHHHH		18.6223403867
25PhosphorylationIIASSVGTILKSCGL
HHHHHHHHHHHHCCC		22.4527067055
51PhosphorylationNIDAGTFSPYEHGEV
CCCCCCCCCCCCCCE		26.8126074081
53PhosphorylationDAGTFSPYEHGEVFV
CCCCCCCCCCCCEEE		21.2526074081
55UbiquitinationGTFSPYEHGEVFVLD
CCCCCCCCCCEEEEC		31.69-
75UbiquitinationDLDLGNYERFLDIRL
EEECCCCEEEEEEEE		40.74-
78UbiquitinationLGNYERFLDIRLTKD
CCCCEEEEEEEEECC		7.20-
81MethylationYERFLDIRLTKDNNL
CEEEEEEEEECCCCC		35.65-
84UbiquitinationFLDIRLTKDNNLTTG
EEEEEEECCCCCCCC		64.15-
88UbiquitinationRLTKDNNLTTGKIYQ
EEECCCCCCCCEEEE		5.94-
92UbiquitinationDNNLTTGKIYQYVIN
CCCCCCCEEEEEECC		35.8321890473
92AcetylationDNNLTTGKIYQYVIN
CCCCCCCEEEEEECC		35.8325953088
92UbiquitinationDNNLTTGKIYQYVIN
CCCCCCCEEEEEECC		35.8321890473
94PhosphorylationNLTTGKIYQYVINKE
CCCCCEEEEEECCCC		9.4025159151
96PhosphorylationTTGKIYQYVINKERK
CCCEEEEEECCCCCC		6.0720090780
100UbiquitinationIYQYVINKERKGDYL
EEEEECCCCCCCCCC		48.0121890473
100AcetylationIYQYVINKERKGDYL
EEEEECCCCCCCCCC		48.0119608861
100UbiquitinationIYQYVINKERKGDYL
EEEEECCCCCCCCCC		48.0121890473
103UbiquitinationYVINKERKGDYLGKT
EECCCCCCCCCCCCE		58.17-
104UbiquitinationVINKERKGDYLGKTV
ECCCCCCCCCCCCEE		34.71-
106PhosphorylationNKERKGDYLGKTVQV
CCCCCCCCCCCEEEE		26.4820068231
129UbiquitinationQEWVMRQALIPVDED
HHHHHHHCCCCCCCC		9.33-
150UbiquitinationCVIELGGTVGDIESM
EEEECCCEECCHHHC		21.37-
169AcetylationAFRQFQFKVKRENFC
HHHHCCCEECCCCCC		35.7425953088
169MethylationAFRQFQFKVKRENFC
HHHHCCCEECCCCCC		35.74-
169UbiquitinationAFRQFQFKVKRENFC
HHHHCCCEECCCCCC		35.74-
171AcetylationRQFQFKVKRENFCNI
HHCCCEECCCCCCCE		55.3612436271
176GlutathionylationKVKRENFCNIHVSLV
EECCCCCCCEEEEEE		7.6322555962
181PhosphorylationNFCNIHVSLVPQPSS
CCCCEEEEEECCCCC		14.9727080861
187PhosphorylationVSLVPQPSSTGEQKT
EEEECCCCCCCCCCC		34.9727080861
188PhosphorylationSLVPQPSSTGEQKTK
EEECCCCCCCCCCCC		47.3027080861
189PhosphorylationLVPQPSSTGEQKTKP
EECCCCCCCCCCCCC		49.4227080861
193UbiquitinationPSSTGEQKTKPTQNS
CCCCCCCCCCCCCCH		54.97-
195UbiquitinationSTGEQKTKPTQNSVR
CCCCCCCCCCCCHHH		53.77-
200PhosphorylationKTKPTQNSVRELRGL
CCCCCCCHHHHHCCC		16.8524114839
205MethylationQNSVRELRGLGLSPD
CCHHHHHCCCCCCCC		33.27-
210PhosphorylationELRGLGLSPDLVVCR
HHCCCCCCCCEEEEE		17.9930266825
216GlutathionylationLSPDLVVCRCSNPLD
CCCCEEEEECCCCCC		2.5722555962
225PhosphorylationCSNPLDTSVKEKISM
CCCCCCCCHHHHHEE		30.7522985185
227UbiquitinationNPLDTSVKEKISMFC
CCCCCCHHHHHEECC		53.72-
229AcetylationLDTSVKEKISMFCHV
CCCCHHHHHEECCCC		34.07-
229UbiquitinationLDTSVKEKISMFCHV
CCCCHHHHHEECCCC		34.07-
229UbiquitinationLDTSVKEKISMFCHV
CCCCHHHHHEECCCC		34.07-
231PhosphorylationTSVKEKISMFCHVEP
CCHHHHHEECCCCCH		19.51-
235UbiquitinationEKISMFCHVEPEQVI
HHHEECCCCCHHHEE		18.73-
259UbiquitinationRVPLLLEEQGVVDYF
ECHHHHHHCCHHHHH		53.24-
265PhosphorylationEEQGVVDYFLRRLDL
HHCCHHHHHHHHCCC		7.91-
267UbiquitinationQGVVDYFLRRLDLPI
CCHHHHHHHHCCCCC		2.25-
286AcetylationRKMLMKWKEMADRYD
HHHHHHHHHHHHHHH		31.9028304403
286UbiquitinationRKMLMKWKEMADRYD
HHHHHHHHHHHHHHH		31.90-
299GlutathionylationYDRLLETCSIALVGK
HHHHHHHHHHHHHCC		1.7022555962
304UbiquitinationETCSIALVGKYTKFS
HHHHHHHHCCCEECC		4.61-
306AcetylationCSIALVGKYTKFSDS
HHHHHHCCCEECCHH		42.1225438201
306UbiquitinationCSIALVGKYTKFSDS
HHHHHHCCCEECCHH		42.12-
307PhosphorylationSIALVGKYTKFSDSY
HHHHHCCCEECCHHH		14.83-
309UbiquitinationALVGKYTKFSDSYAS
HHHCCCEECCHHHHH		39.5221890473
309AcetylationALVGKYTKFSDSYAS
HHHCCCEECCHHHHH		39.5225953088
309UbiquitinationALVGKYTKFSDSYAS
HHHCCCEECCHHHHH		39.5221890473
311PhosphorylationVGKYTKFSDSYASVI
HCCCEECCHHHHHHH		27.4829523821
313PhosphorylationKYTKFSDSYASVIKA
CCEECCHHHHHHHHH		22.7729523821
314PhosphorylationYTKFSDSYASVIKAL
CEECCHHHHHHHHHH		14.1129523821
316PhosphorylationKFSDSYASVIKALEH
ECCHHHHHHHHHHHH		19.0129523821
319UbiquitinationDSYASVIKALEHSAL
HHHHHHHHHHHHHHH		44.7721890473
319UbiquitinationDSYASVIKALEHSAL
HHHHHHHHHHHHHHH		44.7721890473
326UbiquitinationKALEHSALAINHKLE
HHHHHHHHHHCCCEE		5.72-
331UbiquitinationSALAINHKLEIKYID
HHHHHCCCEEEEEEE		43.24-
335UbiquitinationINHKLEIKYIDSADL
HCCCEEEEEEECCCC		27.1221890473
336PhosphorylationNHKLEIKYIDSADLE
CCCEEEEEEECCCCC		18.6728851738
346PhosphorylationSADLEPITSQEEPVR
CCCCCCCCCCCCCCC		34.7628851738
347PhosphorylationADLEPITSQEEPVRY
CCCCCCCCCCCCCCH		35.9920044836
360AcetylationRYHEAWQKLCSAHGV
CHHHHHHHHHHHCCC		40.5426051181
360UbiquitinationRYHEAWQKLCSAHGV
CHHHHHHHHHHHCCC		40.54-
362S-nitrosocysteineHEAWQKLCSAHGVLV
HHHHHHHHHHCCCEE		4.32-
362S-nitrosylationHEAWQKLCSAHGVLV
HHHHHHHHHHCCCEE		4.3219483679
381UbiquitinationGVRGTEGKIQAIAWA
CCCCCCCHHHHHHHH		25.97-
389MethylationIQAIAWARNQKKPFL
HHHHHHHCCCCCCCH		35.10-
428PhosphorylationSTEFDPTTSHPVVVD
CCCCCCCCCCCEEEC		30.35-
447PhosphorylationNPGQMGGTMRLGKRR
CCCCCCCCCCCCCCC		8.0627080861
455PhosphorylationMRLGKRRTLFQTKNS
CCCCCCCCHHHHHHH		35.6417463002
459PhosphorylationKRRTLFQTKNSVMRK
CCCCHHHHHHHHHHH		25.5128509920
460UbiquitinationRRTLFQTKNSVMRKL
CCCHHHHHHHHHHHH		36.1221890473
460AcetylationRRTLFQTKNSVMRKL
CCCHHHHHHHHHHHH		36.1223236377
460UbiquitinationRRTLFQTKNSVMRKL
CCCHHHHHHHHHHHH		36.1221890473
462PhosphorylationTLFQTKNSVMRKLYG
CHHHHHHHHHHHHHC		20.8817463002
466UbiquitinationTKNSVMRKLYGDADY
HHHHHHHHHHCCHHH		28.15-
468PhosphorylationNSVMRKLYGDADYLE
HHHHHHHHCCHHHHH		18.9228152594
473PhosphorylationKLYGDADYLEERHRH
HHHCCHHHHHHHHHH		20.1025884760
477MethylationDADYLEERHRHRFEV
CHHHHHHHHHHCCCC		23.82-
4892-HydroxyisobutyrylationFEVNPVWKKCLEEQG
CCCCHHHHHHHHHCC		33.57-
489AcetylationFEVNPVWKKCLEEQG
CCCCHHHHHHHHHCC		33.5725953088
489MethylationFEVNPVWKKCLEEQG
CCCCHHHHHHHHHCC		33.57-
489UbiquitinationFEVNPVWKKCLEEQG
CCCCHHHHHHHHHCC		33.57-
490MethylationEVNPVWKKCLEEQGL
CCCHHHHHHHHHCCC		28.48-
490UbiquitinationEVNPVWKKCLEEQGL
CCCHHHHHHHHHCCC		28.48-
498AcetylationCLEEQGLKFVGQDVE
HHHHCCCEEEEECCC		44.8425953088
498UbiquitinationCLEEQGLKFVGQDVE
HHHHCCCEEEEECCC		44.84-
535UbiquitinationEFLSRPIKPSPPYFG
HHHCCCCCCCCCCHH		41.9721890473
535UbiquitinationEFLSRPIKPSPPYFG
HHHCCCCCCCCCCHH		41.9721890473
537PhosphorylationLSRPIKPSPPYFGLL
HCCCCCCCCCCHHHH		33.2420068231
540PhosphorylationPIKPSPPYFGLLLAS
CCCCCCCCHHHHHHH		17.4220068231
547PhosphorylationYFGLLLASVGRLSHY
CHHHHHHHHHHHHHH		25.6920068231
552PhosphorylationLASVGRLSHYLQKGC
HHHHHHHHHHHHCCC		14.5521406692
554PhosphorylationSVGRLSHYLQKGCRL
HHHHHHHHHHCCCCC		13.8827251275
557AcetylationRLSHYLQKGCRLSPR
HHHHHHHCCCCCCCC		58.3326051181
557UbiquitinationRLSHYLQKGCRLSPR
HHHHHHHCCCCCCCC		58.33-
562PhosphorylationLQKGCRLSPRDTYSD
HHCCCCCCCCCCCCC		9.8730266825
566PhosphorylationCRLSPRDTYSDRSGS
CCCCCCCCCCCCCCC		26.6322167270
567PhosphorylationRLSPRDTYSDRSGSS
CCCCCCCCCCCCCCC		16.9222167270
568PhosphorylationLSPRDTYSDRSGSSS
CCCCCCCCCCCCCCC		28.7422167270
570MethylationPRDTYSDRSGSSSPD
CCCCCCCCCCCCCCC		36.66-
571PhosphorylationRDTYSDRSGSSSPDS
CCCCCCCCCCCCCCC		48.2829255136
573PhosphorylationTYSDRSGSSSPDSEI
CCCCCCCCCCCCCCC		28.9629255136
574PhosphorylationYSDRSGSSSPDSEIT
CCCCCCCCCCCCCCE		49.7929255136
575PhosphorylationSDRSGSSSPDSEITE
CCCCCCCCCCCCCEE		34.1319664994
578PhosphorylationSGSSSPDSEITELKF
CCCCCCCCCCEECCC		33.9922167270
581PhosphorylationSSPDSEITELKFPSI
CCCCCCCEECCCCCC		31.0822167270
584SumoylationDSEITELKFPSINHD
CCCCEECCCCCCCCC		49.34-
584UbiquitinationDSEITELKFPSINHD
CCCCEECCCCCCCCC		49.34-
587PhosphorylationITELKFPSINHD---
CEECCCCCCCCC---		38.8723927012
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
455TPhosphorylationKinasePRKACAP17612
GPS
455TPhosphorylationKinasePRKCAP17252
GPS
455TPhosphorylationKinasePKA-FAMILY-GPS
455TPhosphorylationKinasePKA_GROUP-PhosphoELM
462SPhosphorylationKinasePRKCAP17252
GPS
571SPhosphorylationKinaseGSK3AP49840
GPS
571SPhosphorylationKinaseGSK3BP49841
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PYRG1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PYRG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM28_HUMANRBM28physical
22939629
RPAC1_HUMANPOLR1Cphysical
22939629
DCTP1_HUMANDCTPP1physical
22863883
DFFA_HUMANDFFAphysical
22863883
PSF3_HUMANGINS3physical
22863883
PAPS1_HUMANPAPSS1physical
22863883
KPYM_HUMANPKMphysical
22863883
PPP5_HUMANPPP5Cphysical
22863883
PYRG1_HUMANCTPS1physical
25416956
CTBP2_HUMANCTBP2physical
26344197
IMDH2_HUMANIMPDH2physical
26344197
NH2L1_HUMANNHP2L1physical
26344197
NMD3_HUMANNMD3physical
26344197
ANM1_HUMANPRMT1physical
26344197
PUS7_HUMANPUS7physical
26344197
SK2L2_HUMANSKIV2L2physical
26344197
TSN_HUMANTSNphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615897Immunodeficiency 24 (IMD24)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00130L-Glutamine
Regulatory Network of PYRG1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-100, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571; SER-574 ANDSER-575, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571; SER-573;SER-574 AND SER-575, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571; SER-573;SER-574; SER-575; THR-581 AND SER-587, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571; SER-573 ANDSER-575, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571; SER-573;SER-574 AND SER-575, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND MASSSPECTROMETRY.
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571; SER-573 ANDSER-574, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASSSPECTROMETRY.

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