GSTM2_MOUSE - dbPTM
GSTM2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSTM2_MOUSE
UniProt AC P15626
Protein Name Glutathione S-transferase Mu 2
Gene Name Gstm2
Organism Mus musculus (Mouse).
Sequence Length 218
Subcellular Localization Cytoplasm.
Protein Description Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles..
Protein Sequence MPMTLGYWDIRGLAHAIRLLLEYTDTSYEDKKYTMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLARKHNLCGETEEERIRVDILENQAMDTRIQLAMVCYSPDFEKKKPEYLEGLPEKMKLYSEFLGKQPWFAGNKVTYVDFLVYDVLDQHRIFEPKCLDAFPNLKDFMGRFEGLKKISDYMKSSRFLSKPIFAKMAFWNPK
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
27PhosphorylationLLEYTDTSYEDKKYT
HHHCCCCCHHCCCCC
29.36-
31AcetylationTDTSYEDKKYTMGDA
CCCCHHCCCCCCCCC
35.4219864859
31UbiquitinationTDTSYEDKKYTMGDA
CCCCHHCCCCCCCCC
35.4222790023
32AcetylationDTSYEDKKYTMGDAP
CCCHHCCCCCCCCCC
59.2722826441
34PhosphorylationSYEDKKYTMGDAPDY
CHHCCCCCCCCCCCC
24.4520139300
44PhosphorylationDAPDYDRSQWLSEKF
CCCCCCHHHHHHHHH
23.86-
50UbiquitinationRSQWLSEKFKLGLDF
HHHHHHHHHCCCCCC
44.4122790023
52AcetylationQWLSEKFKLGLDFPN
HHHHHHHCCCCCCCC
53.357872623
52UbiquitinationQWLSEKFKLGLDFPN
HHHHHHHCCCCCCCC
53.3522790023
62PhosphorylationLDFPNLPYLIDGSHK
CCCCCCCEEECCCCC
21.3223984901
67PhosphorylationLPYLIDGSHKITQSN
CCEEECCCCCCCCHH
20.1921082442
69AcetylationYLIDGSHKITQSNAI
EEECCCCCCCCHHHH
49.507872633
69UbiquitinationYLIDGSHKITQSNAI
EEECCCCCCCCHHHH
49.50-
71PhosphorylationIDGSHKITQSNAILR
ECCCCCCCCHHHHHH
30.6523984901
73PhosphorylationGSHKITQSNAILRYL
CCCCCCCHHHHHHHH
21.4123984901
83UbiquitinationILRYLARKHNLCGET
HHHHHHHHCCCCCCC
31.1022790023
87S-nitrosylationLARKHNLCGETEEER
HHHHCCCCCCCHHHH
5.8521278135
87S-nitrosocysteineLARKHNLCGETEEER
HHHHCCCCCCCHHHH
5.85-
115S-nitrosylationRIQLAMVCYSPDFEK
HHHHHHHHHCCCHHH
1.4621278135
115S-nitrosocysteineRIQLAMVCYSPDFEK
HHHHHHHHHCCCHHH
1.46-
117PhosphorylationQLAMVCYSPDFEKKK
HHHHHHHCCCHHHCC
16.9326643407
136MalonylationEGLPEKMKLYSEFLG
CCCCHHHHHHHHHHC
56.1726320211
136AcetylationEGLPEKMKLYSEFLG
CCCCHHHHHHHHHHC
56.1722733758
136UbiquitinationEGLPEKMKLYSEFLG
CCCCHHHHHHHHHHC
56.17-
139PhosphorylationPEKMKLYSEFLGKQP
CHHHHHHHHHHCCCC
32.1026643407
144AcetylationLYSEFLGKQPWFAGN
HHHHHHCCCCCCCCC
56.1623954790
144UbiquitinationLYSEFLGKQPWFAGN
HHHHHHCCCCCCCCC
56.1622790023
173AcetylationQHRIFEPKCLDAFPN
HCCCCCHHHHHHCCC
39.9922733758
174S-nitrosylationHRIFEPKCLDAFPNL
CCCCCHHHHHHCCCH
6.4321278135
174S-nitrosocysteineHRIFEPKCLDAFPNL
CCCCCHHHHHHCCCH
6.43-
192AcetylationMGRFEGLKKISDYMK
HHHHHHHHHHHHHHH
59.942372787
199MalonylationKKISDYMKSSRFLSK
HHHHHHHHHHCCCCC
38.7626320211
199AcetylationKKISDYMKSSRFLSK
HHHHHHHHHHCCCCC
38.7623954790
205PhosphorylationMKSSRFLSKPIFAKM
HHHHCCCCCCHHHHH
33.40-
206UbiquitinationKSSRFLSKPIFAKMA
HHHCCCCCCHHHHHH
44.2622790023

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 GSTM2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSTM2_MOUSE !!

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 GSTM2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GSTM2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GSTM2_MOUSE

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Related Literatures of Post-Translational Modification

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