GSTM5_HUMAN - dbPTM
GSTM5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSTM5_HUMAN
UniProt AC P46439
Protein Name Glutathione S-transferase Mu 5
Gene Name GSTM5
Organism Homo sapiens (Human).
Sequence Length 218
Subcellular Localization Cytoplasm.
Protein Description Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles..
Protein Sequence MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLNLKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK
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
23PhosphorylationAIRLLLEYTDSSYVE
HHHHHHHHCCHHHHC
18.8025907765
24PhosphorylationIRLLLEYTDSSYVEK
HHHHHHHCCHHHHCC
21.7425907765
26PhosphorylationLLLEYTDSSYVEKKY
HHHHHCCHHHHCCEE
18.7728509920
27PhosphorylationLLEYTDSSYVEKKYT
HHHHCCHHHHCCEEE
35.6928509920
28PhosphorylationLEYTDSSYVEKKYTL
HHHCCHHHHCCEEEC
19.3128509920
41PhosphorylationTLGDAPDYDRSQWLN
ECCCCCCCCHHHHHH
16.5225884760
50UbiquitinationRSQWLNEKFKLGLDF
HHHHHHHHCCCCCCC
46.8821906983
52UbiquitinationQWLNEKFKLGLDFPN
HHHHHHCCCCCCCCC
53.352190698
61UbiquitinationGLDFPNLPYLIDGAH
CCCCCCCCEEECCCH
28.6421906983
62PhosphorylationLDFPNLPYLIDGAHK
CCCCCCCEEECCCHH
21.32-
63UbiquitinationDFPNLPYLIDGAHKI
CCCCCCEEECCCHHH
2.4421906983
71PhosphorylationIDGAHKITQSNAILR
ECCCHHHHCHHHHHH
30.6520068231
73PhosphorylationGAHKITQSNAILRYI
CCHHHHCHHHHHHHH
21.4128857561
78MethylationTQSNAILRYIARKHN
HCHHHHHHHHHHHCC
18.07-
83UbiquitinationILRYIARKHNLCGET
HHHHHHHHCCCCCCC
28.02-
94UbiquitinationCGETEEEKIRVDILE
CCCCCCHHHHHHHHH
38.81-
126UbiquitinationDFEKLKPKYLEELPE
CHHHHCHHHHHHHHH
61.96-
126AcetylationDFEKLKPKYLEELPE
CHHHHCHHHHHHHHH
61.96-
134UbiquitinationYLEELPEKLKLYSEF
HHHHHHHHHHHHHHH
49.32-
136UbiquitinationEELPEKLKLYSEFLG
HHHHHHHHHHHHHHC
57.35-
144UbiquitinationLYSEFLGKRPWFAGD
HHHHHHCCCCCCCCC
58.39-
199UbiquitinationKKISAYMKSSQFLRG
HHHHHHHHHHHHHHH
33.99-

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 GSTM5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSTM5_HUMAN !!

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 GSTM5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSTM5_HUMANGSTM5physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
GSTM3_HUMANGSTM3physical
26186194
GSTM4_HUMANGSTM4physical
26186194
ARFG1_HUMANARFGAP1physical
26186194
GSTM5_HUMANGSTM5physical
21516116
GSTM4_HUMANGSTM4physical
28514442
GSTM3_HUMANGSTM3physical
28514442
ARFG1_HUMANARFGAP1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00143Glutathione
Regulatory Network of GSTM5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126, AND MASS SPECTROMETRY.

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