| UniProt ID | GUAA_YEAST | |
|---|---|---|
| UniProt AC | P38625 | |
| Protein Name | GMP synthase [glutamine-hydrolyzing] | |
| Gene Name | GUA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 525 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | ||
| Protein Sequence | MAAGEQVSNMFDTILVLDFGSQYSHLITRRLREFNIYAEMLPCTQKISELGWTPKGVILSGGPYSVYAEDAPHVDHAIFDLNVPILGICYGMQELAWINGKQVGRGDKREYGPATLKVIDDSNSLFKGMNDSTVWMSHGDKLHGLPTGYKTIATSDNSPYCGIVHETKPIYGIQFHPEVTHSTQGKTLLKNFAVDLCHAKQNWTMENFIDTEINRIRKLVGPTAEVIGAVSGGVDSTVASKLMTEAIGDRFHAILVDNGVLRLNEAANVKKTLVEGLGINLMVVDASEEFLSKLKGVTDPEKKRKIIGNTFIHVFEREAEKIKPKDGKEIQFLLQGTLYPDVIESISFKGPSQTIKTHHNVGGLLENMKLKLIEPLRELFKDEVRHLGELLGIPHDLVWRHPFPGPGIAIRVLGEVTKEQVEIARKADNIYIEEIKKAGLYNQISQAFACLLPVKSVGVMGDQRTYDQVIALRAIETTDFMTADWFPFEHSFLKKVASRIVNEVDGVARVTYDITSKPPATVEWE | |
| 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 |
|---|---|---|---|---|---|
| 117 | Acetylation | EYGPATLKVIDDSNS CCCCCEEEEEECCCC | 32.56 | 24489116 | |
| 122 | Phosphorylation | TLKVIDDSNSLFKGM EEEEEECCCCCCCCC | 25.27 | 28152593 | |
| 124 | Phosphorylation | KVIDDSNSLFKGMND EEEECCCCCCCCCCC | 38.85 | 22369663 | |
| 132 | Phosphorylation | LFKGMNDSTVWMSHG CCCCCCCCEEEECCC | 21.61 | 25521595 | |
| 133 | Phosphorylation | FKGMNDSTVWMSHGD CCCCCCCEEEECCCC | 22.50 | 25521595 | |
| 141 | Acetylation | VWMSHGDKLHGLPTG EEECCCCEECCCCCC | 47.15 | 24489116 | |
| 147 | Phosphorylation | DKLHGLPTGYKTIAT CEECCCCCCCCEEEC | 59.18 | 21440633 | |
| 155 | Phosphorylation | GYKTIATSDNSPYCG CCCEEECCCCCCCCC | 26.27 | 21440633 | |
| 160 | Phosphorylation | ATSDNSPYCGIVHET ECCCCCCCCCEEECC | 11.79 | 21440633 | |
| 168 | Acetylation | CGIVHETKPIYGIQF CCEEECCCCEEEEEC | 26.83 | 24489116 | |
| 190 | Acetylation | TQGKTLLKNFAVDLC CCCCHHHHHHHHHHH | 53.80 | 24489116 | |
| 200 | Acetylation | AVDLCHAKQNWTMEN HHHHHCCCCCCCHHH | 22.09 | 25381059 | |
| 223 | Phosphorylation | IRKLVGPTAEVIGAV HHHHHCCHHHHHHHH | 29.53 | 22369663 | |
| 231 | Phosphorylation | AEVIGAVSGGVDSTV HHHHHHHCCCCCHHH | 29.33 | 22369663 | |
| 236 | Phosphorylation | AVSGGVDSTVASKLM HHCCCCCHHHHHHHH | 23.52 | 22369663 | |
| 237 | Phosphorylation | VSGGVDSTVASKLMT HCCCCCHHHHHHHHH | 18.67 | 22369663 | |
| 240 | Phosphorylation | GVDSTVASKLMTEAI CCCHHHHHHHHHHHH | 23.22 | 22369663 | |
| 241 | Ubiquitination | VDSTVASKLMTEAIG CCHHHHHHHHHHHHH | 32.32 | 24961812 | |
| 270 | Succinylation | LNEAANVKKTLVEGL HHHHHCHHHHHHHCC | 39.59 | 23954790 | |
| 272 | Phosphorylation | EAANVKKTLVEGLGI HHHCHHHHHHHCCCC | 30.25 | 27017623 | |
| 292 | Phosphorylation | DASEEFLSKLKGVTD CCCHHHHHHCCCCCC | 41.06 | 27017623 | |
| 302 | Acetylation | KGVTDPEKKRKIIGN CCCCCHHHHHHEECC | 64.37 | 24489116 | |
| 352 | Phosphorylation | SISFKGPSQTIKTHH HCEEECCCCCCCCCC | 48.93 | 30377154 | |
| 371 | Acetylation | LLENMKLKLIEPLRE HHHHHHHHHHHHHHH | 41.73 | 24489116 | |
| 381 | Acetylation | EPLRELFKDEVRHLG HHHHHHHHHHHHHHH | 66.65 | 24489116 | |
| 418 | Acetylation | RVLGEVTKEQVEIAR EEEEECCHHHHHHHH | 51.85 | 24489116 | |
| 426 | Ubiquitination | EQVEIARKADNIYIE HHHHHHHHCCCEEHH | 51.58 | 22106047 | |
| 436 | Acetylation | NIYIEEIKKAGLYNQ CEEHHHHHHCCCHHH | 39.59 | 24489116 | |
| 436 | Succinylation | NIYIEEIKKAGLYNQ CEEHHHHHHCCCHHH | 39.59 | 23954790 | |
| 441 | Phosphorylation | EIKKAGLYNQISQAF HHHHCCCHHHHHHHH | 12.24 | 22369663 | |
| 445 | Phosphorylation | AGLYNQISQAFACLL CCCHHHHHHHHHHHC | 12.99 | 22369663 | |
| 456 | Phosphorylation | ACLLPVKSVGVMGDQ HHHCCCCEEEEECCC | 25.08 | 22369663 | |
| 498 | Phosphorylation | SFLKKVASRIVNEVD HHHHHHHHHHHHHCC | 26.06 | 21440633 | |
| 517 | Ubiquitination | VTYDITSKPPATVEW EEEECCCCCCCEEEC | 46.50 | 23749301 |
| 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 GUAA_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GUAA_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 GUAA_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GUAA_YEAST !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY. | |