DUG1_YEAST - dbPTM
DUG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUG1_YEAST
UniProt AC P43616
Protein Name Cys-Gly metallodipeptidase DUG1
Gene Name DUG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 481
Subcellular Localization Cytoplasm .
Protein Description Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2-DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides..
Protein Sequence MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFHDIKMVDLGIQPPPISTPNLSLPPVILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEAKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTSLYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPAKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFNAQFTAAKKATKLVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQYYSESPEN
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
2Phosphorylation------MSHSLTSVF
------CCCCHHHHH		23.0622369663
4Phosphorylation----MSHSLTSVFQK
----CCCCHHHHHHH		26.4922369663
11UbiquitinationSLTSVFQKIDSLKPQ
CHHHHHHHHHHCCHH		36.7022817900
14PhosphorylationSVFQKIDSLKPQFFS
HHHHHHHHCCHHHHH		41.5922369663
16AcetylationFQKIDSLKPQFFSRL
HHHHHHCCHHHHHHH		40.5024489116
16SuccinylationFQKIDSLKPQFFSRL
HHHHHHCCHHHHHHH		40.5023954790
16UbiquitinationFQKIDSLKPQFFSRL
HHHHHHCCHHHHHHH		40.5023749301
21PhosphorylationSLKPQFFSRLTKAIQ
HCCHHHHHHHHHHHC		27.8921440633
25AcetylationQFFSRLTKAIQIPAV
HHHHHHHHHHCCCCC		48.3524489116
34PhosphorylationIQIPAVSSDESLRSK
HCCCCCCCCHHHHHH		38.5128889911
37PhosphorylationPAVSSDESLRSKVFD
CCCCCCHHHHHHHHH		33.7921440633
452-HydroxyisobutyrylationLRSKVFDKAKFISEQ
HHHHHHHHHHHHHHH		41.85-
47AcetylationSKVFDKAKFISEQLS
HHHHHHHHHHHHHHH		49.3124489116
50PhosphorylationFDKAKFISEQLSQSG
HHHHHHHHHHHHHCC		23.5622369663
54PhosphorylationKFISEQLSQSGFHDI
HHHHHHHHHCCCCCE		23.2222369663
56PhosphorylationISEQLSQSGFHDIKM
HHHHHHHCCCCCEEE		39.8022369663
94SuccinylationRFGSDPSKKTVLVYG
HCCCCCCCCEEEEEE		58.8323954790
127AcetylationKLVIDEAKGIMKGRG
EEEEECCCCHHCCCC		47.0924489116
1832-HydroxyisobutyrylationLKLDELIKKEANGYF
CCHHHHHHHHHCCCC		58.13-
212PhosphorylationGTKKPVLTYGLRGCN
CCCCCEEEEECCCCC		18.7722369663
213PhosphorylationTKKPVLTYGLRGCNY
CCCCEEEEECCCCCC		15.2522369663
277UbiquitinationMVAPLTEKEKALYKD
HCCCCCHHHHHHHHC		60.3222817900
277AcetylationMVAPLTEKEKALYKD
HCCCCCHHHHHHHHC		60.3224489116
279UbiquitinationAPLTEKEKALYKDIE
CCCCHHHHHHHHCCE		55.5522817900
283UbiquitinationEKEKALYKDIEFSVE
HHHHHHHHCCEEEHH		53.7522817900
288PhosphorylationLYKDIEFSVEELNAA
HHHCCEEEHHHHHHH		18.8122369663
305AcetylationSKTSLYDKKEDILMH
CCCCCCCCHHHEEEE		44.5024489116
306AcetylationKTSLYDKKEDILMHR
CCCCCCCHHHEEEEC		58.6924489116
340AcetylationAKTVIPAKVFGKFSI
CCEEEEEEEECEEEE		32.5124489116
340UbiquitinationAKTVIPAKVFGKFSI
CCEEEEEEEECEEEE		32.5123749301
357AcetylationVPDMDSEKLTSLVQK
CCCCCHHHHHHHHHH		62.1024489116
359PhosphorylationDMDSEKLTSLVQKHC
CCCHHHHHHHHHHHH		30.9627017623
360PhosphorylationMDSEKLTSLVQKHCD
CCHHHHHHHHHHHHH		36.6627017623
364AcetylationKLTSLVQKHCDAKFK
HHHHHHHHHHHHHHH		38.4325381059
364UbiquitinationKLTSLVQKHCDAKFK
HHHHHHHHHHHHHHH		38.4322817900
369AcetylationVQKHCDAKFKSLNSP
HHHHHHHHHHCCCCC		39.8225381059
369UbiquitinationVQKHCDAKFKSLNSP
HHHHHHHHHHCCCCC		39.8222817900
371AcetylationKHCDAKFKSLNSPNK
HHHHHHHHCCCCCCC		54.0125381059
371UbiquitinationKHCDAKFKSLNSPNK
HHHHHHHHCCCCCCC		54.0122817900
375PhosphorylationAKFKSLNSPNKCRTE
HHHHCCCCCCCCCCE		34.8323749301
378UbiquitinationKSLNSPNKCRTELIH
HCCCCCCCCCCEEEE		28.6023749301
403UbiquitinationNAQFTAAKKATKLVY
CCHHHHHHHHHHEEE		40.2422817900
404UbiquitinationAQFTAAKKATKLVYG
CHHHHHHHHHHEEEE		57.4722817900
407UbiquitinationTAAKKATKLVYGVDP
HHHHHHHHEEEECCC		40.5922817900
407AcetylationTAAKKATKLVYGVDP
HHHHHHHHEEEECCC		40.5924489116
451PhosphorylationRGDDGAHSINEKLDI
CCCCCCCCHHHCCCC		26.9528889911
455AcetylationGAHSINEKLDISNFV
CCCCHHHCCCCHHHH		47.1524489116
467PhosphorylationNFVGGMKTMAAYLQY
HHHHHHHHHHHHHHH		11.8021126336
478PhosphorylationYLQYYSESPEN----
HHHHHHHCCCC----		31.4119779198
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 DUG1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUG1_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 DUG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DUG1_YEASTDUG1physical
17179087
DUG2_YEASTDUG2physical
17179087
DUG3_YEASTDUG3physical
17179087
DUG1_YEASTDUG1physical
19346245
DUG1_YEASTDUG1physical
20868722
DUG1_YEASTDUG1physical
22277648
DUG1_YEASTDUG1physical
25427234
STE50_YEASTSTE50genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
VPS41_YEASTVPS41genetic
27708008
IMG2_YEASTIMG2genetic
27708008
BRE1_YEASTBRE1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
MED20_YEASTSRB2genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
ERG3_YEASTERG3genetic
27708008
SIC1_YEASTSIC1genetic
27708008
ELO3_YEASTELO3genetic
27708008
SST2_YEASTSST2genetic
27708008
CYB5_YEASTCYB5genetic
27708008
PALA_YEASTRIM20genetic
27708008
ROX1_YEASTROX1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DUG1_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-451, AND MASSSPECTROMETRY.

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