Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Glutathione S-transferase omega-1  

UniProtKB / Swiss-Prot ID :  GSTO1_HUMAN

Gene Name (Synonyms) : 
GSTO1, GSTTLP28  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytosol. 

Protein Function :  Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. 

Protein Sequence MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFG...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCEEEEEECCCCCHHHHHHHHHHHCCCCEEEEECCHHCCCHHHHHHCCCC...
Protein Variant
LocationDescription
32C -> Y (in dbSNP:rs45529437). VAR_061231
86S -> C (in dbSNP:rs11509436). VAR_029269
140A -> D (in allele GSTO1*C; no effect onprotein stability; dbSNP:rs4925).
155Missing (in allele GSTO1*B; decreasedprotein stability).
208E -> K (in dbSNP:rs11509438). VAR_024484
236A -> V (in dbSNP:rs11509439). VAR_026583
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylserine---MSGESA
---CCCCCC
51.79HPRD
Link-
11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RSLGKGSAP
CCCCCCCCC
55.79Phosphositeplus
Link
13O-linked (GlcNAc)LGKGSAPPG
CCCCCCCCC
40.88Phosphositeplus
Link
57N6-acetyllysineNINLKNKPE
ECCHHCCCH
59.44HPRD
Link
57N6-acetyllysineNINLKNKPE
ECCHHCCCH
59.44Phosphositeplus
Link
57N6-acetyllysine.NINLKNKPE
ECCHHCCCH
59.44UniProtKB
Link
65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EWFFKKNPF
HHHHHHCCC
42.01Phosphositeplus
Link
65N6-acetyllysineEWFFKKNPF
HHHHHHCCC
42.01HPRD
Link
122N6-acetyllysineELFSKVPSL
HHHHHHHHH
51.32HPRD
Link
122N6-acetyllysineELFSKVPSL
HHHHHHHHH
51.32Phosphositeplus
Link
122N6-acetyllysine.ELFSKVPSL
HHHHHHHHH
51.32UniProtKB
Link
125PhosphoserineSKVPSLVGS
HHHHHHHHH
38.38HPRD
Link
125PhosphoserineSKVPSLVGS
HHHHHHHHH
38.38Phosphositeplus
Link
129PhosphoserineSLVGSFIRS
HHHHHHHCC
15.26HPRD
Link
136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RSQNKEDYA
CCCCHHHHH
44.30Phosphositeplus
Link
143N6-acetyllysineYAGLKEEFR
HHHHHHHHH
55.04HPRD
Link
143N6-acetyllysineYAGLKEEFR
HHHHHHHHH
55.04Phosphositeplus
Link
143N6-acetyllysine.YAGLKEEFR
HHHHHHHHH
55.04UniProtKB
Link
148N6-acetyllysineEEFRKEFTK
HHHHHHHHH
63.60HPRD
Link
148N6-acetyllysineEEFRKEFTK
HHHHHHHHH
63.60Phosphositeplus
Link
148N6-acetyllysine.EEFRKEFTK
HHHHHHHHH
63.60UniProtKB
Link
152N6-acetyllysineKEFTKLEEV
HHHHHHHHH
60.26HPRD
Link
152N6-acetyllysineKEFTKLEEV
HHHHHHHHH
60.26Phosphositeplus
Link
152N6-acetyllysine.KEFTKLEEV
HHHHHHHHH
60.26UniProtKB
Link
160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VLTNKKTTF
HHHCCCCCE
46.38Phosphositeplus
Link
188Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEAMKLNEC
HHHCCCHHH
56.03Phosphositeplus
Link
207Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MAAMKEDPT
HHHHHCCHH
54.99Phosphositeplus
Link
213PhosphoserineDPTVSALLT
CHHHHHHCC
18.71HPRD
Link
218PhosphoserineALLTSEKDW
HHCCCHHHH
42.49HPRD
Link
229PhosphotyrosineFLELYLQNS
HHHHHHCCC
9.25Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
EF1G_HUMANphysical interactionMINT-64765MINT16169070
SETB1_HUMANphysical interactionMINT-64766MINT16169070
TIP60_HUMANphysical interactionMINT-64767MINT16169070
K1377_HUMANphysical interactionMINT-64769MINT16169070
YG012_HUMANphysical interactionEBI-728952
intact16169070
Q5RL73_HUMANphysical interactionEBI-728952
intact16169070
EF1G_HUMANphysical interactionEBI-728955
intact16169070
K1377_HUMANphysical interactionEBI-728958
intact16169070
TIP60_HUMANphysical interactionEBI-730090
intact16169070
SETB1_HUMANphysical interactionEBI-730093
intact16169070
EF1G_HUMANyeast 2-hybridHPRD:10401HPRD16169070
K1377_HUMANyeast 2-hybridHPRD:10401HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00143Glutathione
DB00163Vitamin E
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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-57; LYS-122; LYS-143;LYS-148 AND LYS-152, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures