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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
30 | S-nitrosocysteine | VGTILKSCGLHVTSI HHHHHHHCCCEEEEE | 6.85 | - | |
30 | S-nitrosylation | VGTILKSCGLHVTSI HHHHHHHCCCEEEEE | 6.85 | 20925432 | |
53 | Phosphorylation | DAGTFSPYEHGEVFV CCCCCCCCCCCCEEE | 21.25 | 18563927 | |
100 | Acetylation | IYQYVINKERKGDYL EEEEECCCCCCCCCC | 48.01 | 23236377 | |
100 | Ubiquitination | IYQYVINKERKGDYL EEEEECCCCCCCCCC | 48.01 | - | |
210 | Phosphorylation | ELRGLGLSPDLVVCR HHCCCCCCCCEEEEE | 17.99 | 23984901 | |
216 | S-nitrosocysteine | LSPDLVVCRCSNPLD CCCCEEEEECCCCCC | 2.57 | - | |
216 | Glutathionylation | LSPDLVVCRCSNPLD CCCCEEEEECCCCCC | 2.57 | 24333276 | |
216 | S-nitrosylation | LSPDLVVCRCSNPLD CCCCEEEEECCCCCC | 2.57 | 20925432 | |
218 | Glutathionylation | PDLVVCRCSNPLDTS CCEEEEECCCCCCCC | 3.79 | 24333276 | |
306 | Acetylation | CSIALVGKYTKFSDS HHHHHHCCCEECCHH | 42.12 | 22826441 | |
309 | Acetylation | ALVGKYTKFSDSYAS HHHCCCEECCHHHHH | 39.52 | 23806337 | |
319 | Ubiquitination | DSYASVIKALEHSAL HHHHHHHHHHHHHHH | 44.77 | - | |
362 | Glutathionylation | HEAWQKLCSAHGVLV HHHHHHHHHHCCCEE | 4.32 | 24333276 | |
447 | Phosphorylation | NPGQMGGTMRLGKRR CCCCCCCCCCCCCCC | 8.06 | 29109428 | |
460 | Acetylation | RRTLFQTKNSVMRKL CCEEHCCCHHHHHHH | 36.12 | 23806337 | |
466 | Acetylation | TKNSVMRKLYGDTDY CCHHHHHHHHCCCHH | 28.15 | 23806337 | |
473 | Phosphorylation | KLYGDTDYLEERHRH HHHCCCHHHHHHHHH | 20.36 | 25177544 | |
562 | Phosphorylation | LQKGCRLSPRDTYSD HHCCCCCCCCCCCCC | 9.87 | 26824392 | |
566 | Phosphorylation | CRLSPRDTYSDRSGS CCCCCCCCCCCCCCC | 26.63 | 21082442 | |
567 | Phosphorylation | RLSPRDTYSDRSGSS CCCCCCCCCCCCCCC | 16.92 | 25168779 | |
568 | Phosphorylation | LSPRDTYSDRSGSSS CCCCCCCCCCCCCCC | 28.74 | 27087446 | |
571 | Phosphorylation | RDTYSDRSGSSSPDS CCCCCCCCCCCCCCC | 48.28 | 25521595 | |
573 | Phosphorylation | TYSDRSGSSSPDSEI CCCCCCCCCCCCCCC | 28.96 | 25521595 | |
574 | Phosphorylation | YSDRSGSSSPDSEIT CCCCCCCCCCCCCCE | 49.79 | 27087446 | |
575 | Phosphorylation | SDRSGSSSPDSEITE CCCCCCCCCCCCCEE | 34.13 | 24925903 | |
578 | Phosphorylation | SGSSSPDSEITELKF CCCCCCCCCCEECCC | 33.99 | 25521595 | |
581 | Phosphorylation | SSPDSEITELKFPSI CCCCCCCEECCCCCC | 31.08 | 24925903 | |
587 | Phosphorylation | ITELKFPSISQD--- CEECCCCCCCCC--- | 37.70 | 25619855 | |
589 | Phosphorylation | ELKFPSISQD----- ECCCCCCCCC----- | 32.41 | 25619855 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PYRG1_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PYRG1_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |