DUG2_YEAST - dbPTM
DUG2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUG2_YEAST
UniProt AC P38149
Protein Name Probable di- and tripeptidase DUG2
Gene Name DUG2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 878
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond..
Protein Sequence MYDSRGVALHSELIHRWNHAFSILSIVAFPKKRLLFAGSQDSKILVFDLPTYNLIHTIRLGESQEETHTRSSVLCLTGSEDENFLFSGGADSLVRIWSIGEKTIRDDFLPVTEIATVYSVTDIGDIFSLAYLDSLETIVFGCQNASLLYVENLIQKIEKKSSDGVENINKLPHRRYDKFFDSLGPTGYSSNSLSQTSLTSLQENCGAAIIEVPSENIIKYAHYGFIYSINKLCPRFNQLLEKSSRTSGAEHIISSAGDGISKLWEFSKDKGQNTVKISLINDKIDNEDSVISQTIEFPFLYCGLTDGIIKIWDLNTQQIISTLKTKHESDVISISVYMDHVFAIDESGITHFYQNQVNHWNPQQGKILSSEIFSKSNAGSVSLLTGGSDGSLTLWDITSLLSAVPLSSNSPINASSTLQTTNLWAAYQSASLNNEEMLNTLRELISFQTVSQSKDTTNTLSLRRCAIYLQQLFLKFGATNSQLFPLPDGGNPVVFAYFQGNGKVSQVKGAKKKRILWYGHYDVISSGNTFNWNTDPFTLTCENGYLKGRGVSDNKGPLVSAIHSVAYLFQQGELVNDVVFLVEGSEEIGSASLKQVCEKYHDIIGKDIDWILLSNSTWVDQEHPCLNYGLRGVINAQIKVWSDKPDGHSGLNGGVYDEPMVNLVKIVSKLQNEQNEIMIPNFYSPLKDLTEEEYQRFQKITELANIDENTTVQDLITNWTKPSLSMTTVKFSGPGNITVIPKSVTMGISIRLVPEQSVEQVKRDLKAYLEESFKQLKSQNHLEIKVLNEAEGWLGDPTNHAYQILKDEITTAWDVEPLLVREGGSISCLRMLERIFDAPAVQIPCGQSTDNGHLANENLRIKNWSNLTEILSKVFNRL
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
194PhosphorylationGYSSNSLSQTSLTSL
CCCCCCCCHHHCHHH		31.1021551504
199PhosphorylationSLSQTSLTSLQENCG
CCCHHHCHHHHHHCC		27.4521551504
200PhosphorylationLSQTSLTSLQENCGA
CCHHHCHHHHHHCCC		33.0928889911
762UbiquitinationEQSVEQVKRDLKAYL
HHHHHHHHHHHHHHH		39.6319722269
862AcetylationANENLRIKNWSNLTE
CCCCCCCCCHHHHHH		46.0224489116
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 DUG2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUG2_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 DUG2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VTH1_YEASTVTH1physical
16554755
DUG3_YEASTDUG3physical
17179087
DUG2_YEASTDUG2physical
22277648
DUG3_YEASTDUG3physical
22277648
SSB1_YEASTSSB1physical
22940862
MCM1_YEASTMCM1genetic
27708008
DED1_YEASTDED1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
CDC10_YEASTCDC10genetic
27708008
CDC11_YEASTCDC11genetic
27708008
ORC1_YEASTORC1genetic
27708008
NAB3_YEASTNAB3genetic
27708008
DEP1_YEASTDEP1genetic
27708008
RXT2_YEASTRXT2genetic
27708008
MTU1_YEASTSLM3genetic
27708008
RXT3_YEASTRXT3genetic
27708008
VMA21_YEASTVMA21genetic
27708008
YHY2_YEASTYHR182Wgenetic
27708008
SDS3_YEASTSDS3genetic
27708008
PBS2_YEASTPBS2genetic
27708008
PTK2_YEASTPTK2genetic
27708008
SAP30_YEASTSAP30genetic
27708008
PHO23_YEASTPHO23genetic
27708008
SIN3_YEASTSIN3genetic
27708008
UME1_YEASTUME1genetic
27708008
KAR3_YEASTKAR3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DUG2_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-200, AND MASSSPECTROMETRY.

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