PYRG1_MOUSE - dbPTM
PYRG1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYRG1_MOUSE
UniProt AC P70698
Protein Name CTP synthase 1 {ECO:0000305}
Gene Name Ctps1
Organism Mus musculus (Mouse).
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 MKYILVTGGVISGIGKGVIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQSRKMLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSTDLEPSTLQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARKQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPKTSHPVVIDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDTDYLEERHRHRFEVNPVLKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLPHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSISQD
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
30S-nitrosocysteineVGTILKSCGLHVTSI
HHHHHHHCCCEEEEE
6.85-
30S-nitrosylationVGTILKSCGLHVTSI
HHHHHHHCCCEEEEE
6.8520925432
53PhosphorylationDAGTFSPYEHGEVFV
CCCCCCCCCCCCEEE
21.2518563927
100AcetylationIYQYVINKERKGDYL
EEEEECCCCCCCCCC
48.0123236377
100UbiquitinationIYQYVINKERKGDYL
EEEEECCCCCCCCCC
48.01-
210PhosphorylationELRGLGLSPDLVVCR
HHCCCCCCCCEEEEE
17.9923984901
216S-nitrosocysteineLSPDLVVCRCSNPLD
CCCCEEEEECCCCCC
2.57-
216GlutathionylationLSPDLVVCRCSNPLD
CCCCEEEEECCCCCC
2.5724333276
216S-nitrosylationLSPDLVVCRCSNPLD
CCCCEEEEECCCCCC
2.5720925432
218GlutathionylationPDLVVCRCSNPLDTS
CCEEEEECCCCCCCC
3.7924333276
306AcetylationCSIALVGKYTKFSDS
HHHHHHCCCEECCHH
42.1222826441
309AcetylationALVGKYTKFSDSYAS
HHHCCCEECCHHHHH
39.5223806337
319UbiquitinationDSYASVIKALEHSAL
HHHHHHHHHHHHHHH
44.77-
362GlutathionylationHEAWQKLCSAHGVLV
HHHHHHHHHHCCCEE
4.3224333276
447PhosphorylationNPGQMGGTMRLGKRR
CCCCCCCCCCCCCCC
8.0629109428
460AcetylationRRTLFQTKNSVMRKL
CCEEHCCCHHHHHHH
36.1223806337
466AcetylationTKNSVMRKLYGDTDY
CCHHHHHHHHCCCHH
28.1523806337
473PhosphorylationKLYGDTDYLEERHRH
HHHCCCHHHHHHHHH
20.3625177544
562PhosphorylationLQKGCRLSPRDTYSD
HHCCCCCCCCCCCCC
9.8726824392
566PhosphorylationCRLSPRDTYSDRSGS
CCCCCCCCCCCCCCC
26.6321082442
567PhosphorylationRLSPRDTYSDRSGSS
CCCCCCCCCCCCCCC
16.9225168779
568PhosphorylationLSPRDTYSDRSGSSS
CCCCCCCCCCCCCCC
28.7427087446
571PhosphorylationRDTYSDRSGSSSPDS
CCCCCCCCCCCCCCC
48.2825521595
573PhosphorylationTYSDRSGSSSPDSEI
CCCCCCCCCCCCCCC
28.9625521595
574PhosphorylationYSDRSGSSSPDSEIT
CCCCCCCCCCCCCCE
49.7927087446
575PhosphorylationSDRSGSSSPDSEITE
CCCCCCCCCCCCCEE
34.1324925903
578PhosphorylationSGSSSPDSEITELKF
CCCCCCCCCCEECCC
33.9925521595
581PhosphorylationSSPDSEITELKFPSI
CCCCCCCEECCCCCC
31.0824925903
587PhosphorylationITELKFPSISQD---
CEECCCCCCCCC---
37.7025619855
589PhosphorylationELKFPSISQD-----
ECCCCCCCCC-----
32.4125619855

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

Oops, there are no upstream regulatory protein records of PYRG1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PYRG1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PYRG1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PYRG1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-566; TYR-567; SER-568;SER-571; SER-573 AND SER-574, AND MASS SPECTROMETRY.

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