UniProt ID | GSH1_YEAST | |
---|---|---|
UniProt AC | P32477 | |
Protein Name | Glutamate--cysteine ligase | |
Gene Name | GSH1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 678 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MGLLALGTPLQWFESRTYNEHIRDEGIEQLLYIFQAAGKRDNDPLFWGDELEYMVVDFDDKERNSMLDVCHDKILTELNMEDSSLCEANDVSFHPEYGRYMLEATPASPYLNYVGSYVEVNMQKRRAIAEYKLSEYARQDSKNNLHVGSRSVPLTLTVFPRMGCPDFINIKDPWNHKNAASRSLFLPDEVINRHVRFPNLTASIRTRRGEKVCMNVPMYKDIATPETDDSIYDRDWFLPEDKEAKLASKPGFIYMDSMGFGMGCSCLQVTFQAPNINKARYLYDALVNFAPIMLAFSAAAPAFKGWLADQDVRWNVISGAVDDRTPKERGVAPLLPKYNKNGFGGIAKDVQDKVLEIPKSRYSSVDLFLGGSKFFNRTYNDTNVPINEKVLGRLLENDKAPLDYDLAKHFAHLYIRDPVSTFEELLNQDNKTSSNHFENIQSTNWQTLRFKPPTQQATPDKKDSPGWRVEFRPFEVQLLDFENAAYSVLIYLIVDSILTFSDNINAYIHMSKVWENMKIAHHRDAILFEKFHWKKSFRNDTDVETEDYSISEIFHNPENGIFPQFVTPILCQKGFVTKDWKELKHSSKHERLYYYLKLISDRASGELPTTAKFFRNFVLQHPDYKHDSKISKSINYDLLSTCDRLTHLDDSKGELTSFLGAEIAEYVKKNKPSIESKC | |
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 |
---|---|---|---|---|---|
116 | Phosphorylation | PYLNYVGSYVEVNMQ CCHHHCCEEEEEECH | 18.89 | 28889911 | |
224 | Phosphorylation | PMYKDIATPETDDSI CCCCCCCCCCCCCCC | 23.22 | 27017623 | |
227 | Phosphorylation | KDIATPETDDSIYDR CCCCCCCCCCCCCCC | 46.43 | 27017623 | |
230 | Phosphorylation | ATPETDDSIYDRDWF CCCCCCCCCCCCCCC | 26.34 | 27017623 | |
242 | Acetylation | DWFLPEDKEAKLASK CCCCCCCHHHHHHCC | 58.89 | 24489116 | |
337 | Acetylation | GVAPLLPKYNKNGFG CCCCCCCCCCCCCCC | 62.52 | 24489116 | |
360 | Phosphorylation | KVLEIPKSRYSSVDL HHHHCCHHHCCCEEE | 30.97 | 22369663 | |
362 | Phosphorylation | LEIPKSRYSSVDLFL HHCCHHHCCCEEEEE | 16.64 | 22369663 | |
363 | Phosphorylation | EIPKSRYSSVDLFLG HCCHHHCCCEEEEEC | 23.83 | 29734811 | |
364 | Phosphorylation | IPKSRYSSVDLFLGG CCHHHCCCEEEEECC | 15.66 | 22369663 | |
389 | Acetylation | TNVPINEKVLGRLLE CCCCCCHHHHHHHHC | 37.97 | 24489116 | |
399 | Acetylation | GRLLENDKAPLDYDL HHHHCCCCCCCCHHH | 64.58 | 24489116 | |
578 | Acetylation | CQKGFVTKDWKELKH CCCCCCCCCHHHHCC | 57.18 | 24489116 | |
612 | Acetylation | GELPTTAKFFRNFVL CCCCCHHHHHHHHHH | 42.83 | 24489116 | |
612 | Ubiquitination | GELPTTAKFFRNFVL CCCCCHHHHHHHHHH | 42.83 | 24961812 | |
646 | Phosphorylation | LSTCDRLTHLDDSKG HHHCCCCCCCCCCCC | 22.68 | 27017623 | |
677 | Ubiquitination | NKPSIESKC------ HCCCCCCCC------ | 31.04 | 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 GSH1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GSH1_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 GSH1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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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-116, AND MASSSPECTROMETRY. |