GSTM3_HUMAN - dbPTM
GSTM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSTM3_HUMAN
UniProt AC P21266
Protein Name Glutathione S-transferase Mu 3
Gene Name GSTM3
Organism Homo sapiens (Human).
Sequence Length 225
Subcellular Localization Cytoplasm.
Protein Description Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers..
Protein Sequence MSCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLDFPNLPYLLDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCYSSDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVDFLTYDILDQNRIFDPKCLDEFPNLKAFMCRFEALEKIAAYLQSDQFCKMPINNKMAQWGNKPVC
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------MSCESSMVL
------CCCCCCCCC
26.9628857561
5Phosphorylation---MSCESSMVLGYW
---CCCCCCCCCCHH
28.2328857561
6Phosphorylation--MSCESSMVLGYWD
--CCCCCCCCCCHHH
7.2128857561
28PhosphorylationIRLLLEFTDTSYEEK
HHHHHHCCCCCHHHH
29.06-
30PhosphorylationLLLEFTDTSYEEKRY
HHHHCCCCCHHHHCC
30.10-
31PhosphorylationLLEFTDTSYEEKRYT
HHHCCCCCHHHHCCC
33.1021712546
35UbiquitinationTDTSYEEKRYTCGEA
CCCCHHHHCCCCCCC
38.47-
37PhosphorylationTSYEEKRYTCGEAPD
CCHHHHCCCCCCCCC
19.9030622161
38PhosphorylationSYEEKRYTCGEAPDY
CHHHHCCCCCCCCCC
20.3330622161
39S-nitrosocysteineYEEKRYTCGEAPDYD
HHHHCCCCCCCCCCC
3.25-
39S-nitrosylationYEEKRYTCGEAPDYD
HHHHCCCCCCCCCCC
3.2519483679
45PhosphorylationTCGEAPDYDRSQWLD
CCCCCCCCCHHHCCE
16.5230622161
47MethylationGEAPDYDRSQWLDVK
CCCCCCCHHHCCEEE
25.23-
48PhosphorylationEAPDYDRSQWLDVKF
CCCCCCHHHCCEEEE
23.8630622161
54SumoylationRSQWLDVKFKLDLDF
HHHCCEEEEEEECCC
36.1328112733
54UbiquitinationRSQWLDVKFKLDLDF
HHHCCEEEEEEECCC
36.1321890473
56UbiquitinationQWLDVKFKLDLDFPN
HCCEEEEEEECCCCC
35.06-
66PhosphorylationLDFPNLPYLLDGKNK
CCCCCCCEEECCCCC
24.06-
71AcetylationLPYLLDGKNKITQSN
CCEEECCCCCCCCHH
55.5225038526
71UbiquitinationLPYLLDGKNKITQSN
CCEEECCCCCCCCHH
55.52-
73SumoylationYLLDGKNKITQSNAI
EEECCCCCCCCHHHH
51.0928112733
73UbiquitinationYLLDGKNKITQSNAI
EEECCCCCCCCHHHH
51.09-
732-HydroxyisobutyrylationYLLDGKNKITQSNAI
EEECCCCCCCCHHHH
51.09-
75PhosphorylationLDGKNKITQSNAILR
ECCCCCCCCHHHHHH
27.7920068231
77PhosphorylationGKNKITQSNAILRYI
CCCCCCCHHHHHHHH
21.4128857561
82MethylationTQSNAILRYIARKHN
CCHHHHHHHHHHHCC
18.07-
87AcetylationILRYIARKHNMCGET
HHHHHHHHCCCCCCC
30.2426210075
87UbiquitinationILRYIARKHNMCGET
HHHHHHHHCCCCCCC
30.24-
90SulfoxidationYIARKHNMCGETEEE
HHHHHCCCCCCCCCH
2.8830846556
109SulfoxidationDIIENQVMDFRTQLI
HHHHHHHHHHHHHHH
2.6528183972
121PhosphorylationQLIRLCYSSDHEKLK
HHHHHHHCCCHHHHC
28.4427732954
122PhosphorylationLIRLCYSSDHEKLKP
HHHHHHCCCHHHHCH
19.2627732954
128UbiquitinationSSDHEKLKPQYLEEL
CCCHHHHCHHHHHHC
40.9421890473
128SumoylationSSDHEKLKPQYLEEL
CCCHHHHCHHHHHHC
40.94-
128SumoylationSSDHEKLKPQYLEEL
CCCHHHHCHHHHHHC
40.94-
131PhosphorylationHEKLKPQYLEELPGQ
HHHHCHHHHHHCCCH
25.3030622161
140UbiquitinationEELPGQLKQFSMFLG
HHCCCHHHHHHHHHH
41.22-
143PhosphorylationPGQLKQFSMFLGKFS
CCHHHHHHHHHHHCC
13.2121712546
158PhosphorylationWFAGEKLTFVDFLTY
CCCCCCCEEEEECCH
32.4525693802
164PhosphorylationLTFVDFLTYDILDQN
CEEEEECCHHCCCCC
21.1030622161
165PhosphorylationTFVDFLTYDILDQNR
EEEEECCHHCCCCCC
11.7930622161
177UbiquitinationQNRIFDPKCLDEFPN
CCCCCCHHHHHCCCC
49.64-
177AcetylationQNRIFDPKCLDEFPN
CCCCCCHHHHHCCCC
49.6427452117
186AcetylationLDEFPNLKAFMCRFE
HHCCCCHHHHHHHHH
46.3326051181
186UbiquitinationLDEFPNLKAFMCRFE
HHCCCCHHHHHHHHH
46.33-
197UbiquitinationCRFEALEKIAAYLQS
HHHHHHHHHHHHHHC
38.20-
201PhosphorylationALEKIAAYLQSDQFC
HHHHHHHHHHCCCCC
9.0330622161
204PhosphorylationKIAAYLQSDQFCKMP
HHHHHHHCCCCCCCC
30.6821712546
208S-nitrosocysteineYLQSDQFCKMPINNK
HHHCCCCCCCCCCCC
2.83-
208S-nitrosylationYLQSDQFCKMPINNK
HHHCCCCCCCCCCCC
2.8319483679
208GlutathionylationYLQSDQFCKMPINNK
HHHCCCCCCCCCCCC
2.8322555962
209UbiquitinationLQSDQFCKMPINNKM
HHCCCCCCCCCCCCC
49.34-
215UbiquitinationCKMPINNKMAQWGNK
CCCCCCCCCCCCCCC
30.99-
222UbiquitinationKMAQWGNKPVC----
CCCCCCCCCCC----
34.58-

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 GSTM3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSTM3_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 GSTM3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSTM3_HUMANGSTM3physical
16189514
GSTM3_HUMANGSTM3physical
19060904
GSTM3_HUMANGSTM3physical
25416956
GSTM4_HUMANGSTM4physical
25416956
GSTM5_HUMANGSTM5physical
25416956
GSTM4_HUMANGSTM4physical
26186194
PLSI_HUMANPLS1physical
26186194
LANC2_HUMANLANCL2physical
26186194
GNB1L_HUMANGNB1Lphysical
26186194
TPX2_HUMANTPX2physical
26186194
HNRLL_HUMANHNRNPLLphysical
26186194
KLH42_HUMANKLHL42physical
26186194
ASPP1_HUMANPPP1R13Bphysical
26186194
ECT2L_HUMANECT2Lphysical
26186194
F120B_HUMANFAM120Bphysical
26186194
SLBP_HUMANSLBPphysical
26186194
GSTM3_HUMANGSTM3physical
21516116
GSTM4_HUMANGSTM4physical
28514442
ASPP1_HUMANPPP1R13Bphysical
28514442
HNRLL_HUMANHNRNPLLphysical
28514442
SLBP_HUMANSLBPphysical
28514442
TPX2_HUMANTPX2physical
28514442
PLSI_HUMANPLS1physical
28514442
F120B_HUMANFAM120Bphysical
28514442
LANC2_HUMANLANCL2physical
28514442
GNB1L_HUMANGNB1Lphysical
28514442
ECT2L_HUMANECT2Lphysical
28514442
SPB5_HUMANSERPINB5physical
16049007

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
DB00163Vitamin E
Regulatory Network of GSTM3_HUMAN

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Related Literatures of Post-Translational Modification

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