GLO2_YEAST - dbPTM
GLO2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLO2_YEAST
UniProt AC Q05584
Protein Name Hydroxyacylglutathione hydrolase, cytoplasmic isozyme
Gene Name GLO2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 274
Subcellular Localization Cytoplasm.
Protein Description Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid..
Protein Sequence MQVKSIKMRWESGGVNYCYLLSDSKNKKSWLIDPAEPPEVLPELTEDEKISVEAIVNTHHHYDHADGNADILKYLKEKNPTSKVEVIGGSKDCPKVTIIPENLKKLHLGDLEITCIRTPCHTRDSICYYVKDPTTDERCIFTGDTLFTAGCGRFFEGTGEEMDIALNNSILETVGRQNWSKTRVYPGHEYTSDNVKFVRKIYPQVGENKALDELEQFCSKHEVTAGRFTLKDEVEFNPFMRLEDPKVQKAAGDTNNSWDRAQIMDKLRAMKNRM
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
5Phosphorylation---MQVKSIKMRWES
---CCCEEEEEEEEC
28.6921126336
12PhosphorylationSIKMRWESGGVNYCY
EEEEEEECCCCCEEE
33.6123749301
17PhosphorylationWESGGVNYCYLLSDS
EECCCCCEEEEEECC
4.6923749301
22PhosphorylationVNYCYLLSDSKNKKS
CCEEEEEECCCCCCE
36.9223749301
24PhosphorylationYCYLLSDSKNKKSWL
EEEEEECCCCCCEEE
34.4523749301
104AcetylationTIIPENLKKLHLGDL
EECCCCCCCCCCCCC
65.9424489116
131AcetylationDSICYYVKDPTTDER
CCEEEEEECCCCCCC
41.7024489116
131UbiquitinationDSICYYVKDPTTDER
CCEEEEEECCCCCCC
41.7023749301
148PhosphorylationFTGDTLFTAGCGRFF
EECCEEEECCCCCCC
25.8319779198
158PhosphorylationCGRFFEGTGEEMDIA
CCCCCCCCCCHHHHH
33.9319779198
169PhosphorylationMDIALNNSILETVGR
HHHHHHCCHHHHHCC
27.7227017623
173PhosphorylationLNNSILETVGRQNWS
HHCCHHHHHCCCCCC
25.4719779198
196AcetylationEYTSDNVKFVRKIYP
CCCCCCHHHHHHHHH
44.3824489116
220AcetylationELEQFCSKHEVTAGR
HHHHHHHHCCCCCCC
44.9924489116
249UbiquitinationLEDPKVQKAAGDTNN
CCCHHHHHHCCCCCC
43.1023749301
254PhosphorylationVQKAAGDTNNSWDRA
HHHHCCCCCCCCHHH
35.0722369663
257PhosphorylationAAGDTNNSWDRAQIM
HCCCCCCCCHHHHHH
32.2122369663
266AcetylationDRAQIMDKLRAMKNR
HHHHHHHHHHHHHHC
23.6124489116

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 GLO2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLO2_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 GLO2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRX1_YEASTTRX1physical
16554755
HSV2_YEASTHSV2physical
18467557
THDH_YEASTILV1genetic
21623372

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLO2_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-257, AND MASSSPECTROMETRY.

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