| UniProt ID | URA7_YEAST | |
|---|---|---|
| UniProt AC | P28274 | |
| Protein Name | CTP synthase 1 | |
| Gene Name | URA7 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 579 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.. | |
| Protein Sequence | MKYVVVSGGVISGIGKGVLASSTGMLMKTLGLKVTSIKIDPYMNIDAGTMSPLEHGECFVLDDGGETDLDLGNYERYLGVTLTKDHNITTGKIYSHVIAKERKGDYLGKTVQIVPHLTNAIQDWIERVAKIPVDDTGMEPDVCIIELGGTVGDIESAPFVEALRQFQFKVGKENFALIHVSLVPVIHGEQKTKPTQAAIKGLRSLGLVPDMIACRCSETLDKPTIDKIAMFCHVGPEQVVNVHDVNSTYHVPLLLLEQKMIDYLHARLKLDEISLTEEEKQRGLELLSKWKATTGNFDESMETVKIALVGKYTNLKDSYLSVIKALEHSSMKCRRKLDIKWVEATDLEPEAQESNKTKFHEAWNMVSTADGILIPGGFGVRGTEGMVLAARWARENHIPFLGVCLGLQIATIEFTRSVLGRKDSHSAEFYPDIDEKNHVVVFMPEIDKETMGGSMRLGLRPTFFQNETEWSQIKKLYGDVSEVHERHRHRYEINPKMVDELENNGLIFVGKDDTGKRCEILELKNHPYYIATQYHPEYTSKVLDPSKPFLGLVAASAGILQDVIEGKYDLEAGENKFNF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MKYVVVSGGV -----CCEEEEECCE | 9.36 | 21126336 | |
| 7 | Phosphorylation | -MKYVVVSGGVISGI -CCEEEEECCEECCC | 20.44 | 21126336 | |
| 28 | Methylation | SSTGMLMKTLGLKVT HHHHHHHHHHCCEEE | 36.31 | 20137074 | |
| 33 | Ubiquitination | LMKTLGLKVTSIKID HHHHHCCEEEEEEEC | 41.49 | 23749301 | |
| 36 | Phosphorylation | TLGLKVTSIKIDPYM HHCCEEEEEEECCCC | 25.52 | 28889911 | |
| 84 | Acetylation | YLGVTLTKDHNITTG EEEEEEECCCCCCCC | 61.17 | 24489116 | |
| 84 | Ubiquitination | YLGVTLTKDHNITTG EEEEEEECCCCCCCC | 61.17 | 23749301 | |
| 100 | Acetylation | IYSHVIAKERKGDYL EEEEEEECCCCCCCC | 47.10 | 22865919 | |
| 109 | Acetylation | RKGDYLGKTVQIVPH CCCCCCCCEEEHHHH | 42.82 | 24489116 | |
| 109 | Ubiquitination | RKGDYLGKTVQIVPH CCCCCCCCEEEHHHH | 42.82 | 17644757 | |
| 193 | Ubiquitination | IHGEQKTKPTQAAIK ECCCCCCCHHHHHHH | 53.77 | 23749301 | |
| 227 | Ubiquitination | LDKPTIDKIAMFCHV CCCCCCCEEEEECCC | 28.63 | 17644757 | |
| 259 | Ubiquitination | PLLLLEQKMIDYLHA HHHHHHHHHHHHHHH | 28.57 | 17644757 | |
| 269 | Acetylation | DYLHARLKLDEISLT HHHHHHHCCCCCCCC | 48.62 | 24489116 | |
| 269 | Succinylation | DYLHARLKLDEISLT HHHHHHHCCCCCCCC | 48.62 | 23954790 | |
| 280 | Acetylation | ISLTEEEKQRGLELL CCCCHHHHHHHHHHH | 48.88 | 24489116 | |
| 289 | Ubiquitination | RGLELLSKWKATTGN HHHHHHHHHHCCCCC | 53.32 | 23749301 | |
| 289 | Acetylation | RGLELLSKWKATTGN HHHHHHHHHHCCCCC | 53.32 | 24489116 | |
| 293 | Phosphorylation | LLSKWKATTGNFDES HHHHHHCCCCCCCCC | 31.35 | 21126336 | |
| 294 | Phosphorylation | LSKWKATTGNFDESM HHHHHCCCCCCCCCH | 34.68 | 27214570 | |
| 311 | Acetylation | VKIALVGKYTNLKDS EEEEEEEECCCCHHH | 41.23 | 24489116 | |
| 311 | Ubiquitination | VKIALVGKYTNLKDS EEEEEEEECCCCHHH | 41.23 | 24961812 | |
| 312 | Phosphorylation | KIALVGKYTNLKDSY EEEEEEECCCCHHHH | 8.57 | 28889911 | |
| 313 | Phosphorylation | IALVGKYTNLKDSYL EEEEEECCCCHHHHH | 37.25 | 28889911 | |
| 316 | Acetylation | VGKYTNLKDSYLSVI EEECCCCHHHHHHHH | 46.85 | 24489116 | |
| 316 | Ubiquitination | VGKYTNLKDSYLSVI EEECCCCHHHHHHHH | 46.85 | 24961812 | |
| 316 | Succinylation | VGKYTNLKDSYLSVI EEECCCCHHHHHHHH | 46.85 | 23954790 | |
| 324 | Ubiquitination | DSYLSVIKALEHSSM HHHHHHHHHHHHCCC | 44.77 | 24961812 | |
| 324 | Acetylation | DSYLSVIKALEHSSM HHHHHHHHHHHHCCC | 44.77 | 24489116 | |
| 330 | Phosphorylation | IKALEHSSMKCRRKL HHHHHHCCCHHHHCC | 24.94 | 28889911 | |
| 340 | Ubiquitination | CRRKLDIKWVEATDL HHHCCCCEEEECCCC | 44.87 | 15699485 | |
| 354 | Phosphorylation | LEPEAQESNKTKFHE CCHHHHHHCCCHHHH | 31.39 | 28889911 | |
| 356 | Acetylation | PEAQESNKTKFHEAW HHHHHHCCCHHHHHH | 63.47 | 24489116 | |
| 356 | Ubiquitination | PEAQESNKTKFHEAW HHHHHHCCCHHHHHH | 63.47 | 15699485 | |
| 358 | Ubiquitination | AQESNKTKFHEAWNM HHHHCCCHHHHHHHH | 46.46 | 15699485 | |
| 422 | Ubiquitination | TRSVLGRKDSHSAEF HHHHHCCCCCCCCCC | 62.88 | 12872131 | |
| 424 | Phosphorylation | SVLGRKDSHSAEFYP HHHCCCCCCCCCCCC | 23.52 | 12709422 | |
| 426 | Phosphorylation | LGRKDSHSAEFYPDI HCCCCCCCCCCCCCC | 33.18 | 19779198 | |
| 448 | Acetylation | VFMPEIDKETMGGSM EECCCCCCCCCCCCC | 61.82 | 24489116 | |
| 454 | Phosphorylation | DKETMGGSMRLGLRP CCCCCCCCCCCCCCC | 8.59 | 28889911 | |
| 474 | Acetylation | ETEWSQIKKLYGDVS HHHHHHHHHHHCCHH | 29.14 | 24489116 | |
| 474 | Ubiquitination | ETEWSQIKKLYGDVS HHHHHHHHHHHCCHH | 29.14 | 17644757 | |
| 475 | Ubiquitination | TEWSQIKKLYGDVSE HHHHHHHHHHCCHHH | 48.87 | 17644757 | |
| 511 | Ubiquitination | NGLIFVGKDDTGKRC CCEEEEEECCCCCEE | 47.32 | 24961812 | |
| 511 | Acetylation | NGLIFVGKDDTGKRC CCEEEEEECCCCCEE | 47.32 | 24489116 | |
| 524 | Ubiquitination | RCEILELKNHPYYIA EEEEEEECCCCEEEE | 43.78 | 15699485 | |
| 541 | Ubiquitination | YHPEYTSKVLDPSKP CCHHHHCCCCCCCCC | 38.73 | 15699485 | |
| 576 | Ubiquitination | DLEAGENKFNF---- CCCCCCCCCCC---- | 37.06 | 23749301 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of URA7_YEAST !! | ||||||
* 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 URA7_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Ubiquitylation | |
| Reference | PubMed |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422, AND MASSSPECTROMETRY. | |
