UniProt ID | METX_YEAST | |
---|---|---|
UniProt AC | Q04533 | |
Protein Name | Putative cystathionine gamma-synthase YML082W | |
Gene Name | YML082W | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 649 | |
Subcellular Localization | ||
Protein Description | Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia (By similarity).. | |
Protein Sequence | MVSAQVATELGQPIPLDTQHAVSVCFPTWKSVISYVEKDPKVLGCLKSGYPRFWIHPSIQKLRDILIEKYAKENETCFCFPSYRVAKRCREYVRRKCAHRNGKVRILQLATAKPINEEQKTWKRECKIAVVFVDGAYENILKQYWQYTGEIISSRLAEYVLHELFMVEKKSSPAEEKEYIEMRYGRNLNFAFADRAKELIKKRIATKVIDKDEHDEEENYHFLAGNQDEQDFQDTFLDSSLNEANHGEDHDGGISGEVDSQEEPHNGLVSTIPPEPIEMSTIEEEQSVEEDAGRCALRVCPERDVFLFPSGMASIFTAHRLLLQWDSLRLNRSRNGSDVTSSPPNKKTVIFGFPYADTLHVLQEFNETYFLGEGDESSMKELTKILHSGEQILAVFIETPSNPLLKMGNLLELKRLSELFGFFIIIDETVGGIVNIDGLPFADIVCSSLTKTFSGDSNVIGGSMVLNPQSRVYEFASRFMQLEDEYEDLLWCEDAIYLERNSRDFIARTIRINYSTEYLLDKILKPHVGENKLFKKIYYPNLTSKETLTNYDMVRCKKEGGYGGLFSLTFHDEDHAAAFYDNLKLNKGPSLGTNFTLAFPYTLMTYYHELDMAEKFGVERNLLRISVGLESQSILGKIFQEAIDKTVEI | |
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 |
---|---|---|---|---|---|
31 | Phosphorylation | VCFPTWKSVISYVEK EECCCHHHHHHHHHC | 19.08 | 28889911 | |
38 | Acetylation | SVISYVEKDPKVLGC HHHHHHHCCCCHHCH | 70.10 | 24489116 | |
171 | Phosphorylation | LFMVEKKSSPAEEKE HHHHCCCCCCHHHHH | 53.26 | 19779198 | |
287 | Phosphorylation | STIEEEQSVEEDAGR CCCCCHHCHHHHHCC | 34.47 | 28889911 | |
340 | Phosphorylation | SRNGSDVTSSPPNKK CCCCCCCCCCCCCCC | 28.60 | 28889911 | |
341 | Phosphorylation | RNGSDVTSSPPNKKT CCCCCCCCCCCCCCE | 40.47 | 25315811 | |
342 | Phosphorylation | NGSDVTSSPPNKKTV CCCCCCCCCCCCCEE | 34.70 | 28889911 | |
451 | N6-(pyridoxal phosphate)lysine | IVCSSLTKTFSGDSN HHHHCCCEECCCCCC | 53.52 | - | |
451 | Other | IVCSSLTKTFSGDSN HHHHCCCEECCCCCC | 53.52 | - | |
562 | Phosphorylation | RCKKEGGYGGLFSLT EEEECCCCCCEEEEE | 20.91 | 24930733 | |
567 | Phosphorylation | GGYGGLFSLTFHDED CCCCCEEEEEECCCC | 31.38 | 24930733 | |
569 | Phosphorylation | YGGLFSLTFHDEDHA CCCEEEEEECCCCCH | 20.09 | 24930733 | |
631 | Phosphorylation | RISVGLESQSILGKI EEEECCCHHHHHHHH | 33.98 | 27017623 | |
633 | Phosphorylation | SVGLESQSILGKIFQ EECCCHHHHHHHHHH | 29.12 | 27017623 |
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 METX_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of METX_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 METX_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MET30_YEAST | MET30 | physical | 18719252 | |
MED6_YEAST | MED6 | genetic | 27708008 | |
FIP1_YEAST | FIP1 | genetic | 27708008 | |
NEP1_YEAST | EMG1 | genetic | 27708008 | |
SEC22_YEAST | SEC22 | genetic | 27708008 | |
NOP2_YEAST | NOP2 | genetic | 27708008 | |
DCP2_YEAST | DCP2 | genetic | 27708008 | |
TYSY_YEAST | CDC21 | genetic | 27708008 | |
CHK1_YEAST | CHK1 | genetic | 27708008 | |
RLA1_YEAST | RPP1A | genetic | 27708008 | |
YP089_YEAST | YPR089W | genetic | 27708008 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
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-287, AND MASSSPECTROMETRY. |