METX_YEAST - dbPTM
METX_YEAST - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
31PhosphorylationVCFPTWKSVISYVEK
EECCCHHHHHHHHHC
19.0828889911
38AcetylationSVISYVEKDPKVLGC
HHHHHHHCCCCHHCH
70.1024489116
171PhosphorylationLFMVEKKSSPAEEKE
HHHHCCCCCCHHHHH
53.2619779198
287PhosphorylationSTIEEEQSVEEDAGR
CCCCCHHCHHHHHCC
34.4728889911
340PhosphorylationSRNGSDVTSSPPNKK
CCCCCCCCCCCCCCC
28.6028889911
341PhosphorylationRNGSDVTSSPPNKKT
CCCCCCCCCCCCCCE
40.4725315811
342PhosphorylationNGSDVTSSPPNKKTV
CCCCCCCCCCCCCEE
34.7028889911
451N6-(pyridoxal phosphate)lysineIVCSSLTKTFSGDSN
HHHHCCCEECCCCCC
53.52-
451OtherIVCSSLTKTFSGDSN
HHHHCCCEECCCCCC
53.52-
562PhosphorylationRCKKEGGYGGLFSLT
EEEECCCCCCEEEEE
20.9124930733
567PhosphorylationGGYGGLFSLTFHDED
CCCCCEEEEEECCCC
31.3824930733
569PhosphorylationYGGLFSLTFHDEDHA
CCCEEEEEECCCCCH
20.0924930733
631PhosphorylationRISVGLESQSILGKI
EEEECCCHHHHHHHH
33.9827017623
633PhosphorylationSVGLESQSILGKIFQ
EECCCHHHHHHHHHH
29.1227017623

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of METX_YEAST !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MET30_YEASTMET30physical
18719252
MED6_YEASTMED6genetic
27708008
FIP1_YEASTFIP1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
NOP2_YEASTNOP2genetic
27708008
DCP2_YEASTDCP2genetic
27708008
TYSY_YEASTCDC21genetic
27708008
CHK1_YEASTCHK1genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
YP089_YEASTYPR089Wgenetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of METX_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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