mutLBSgeneDB

mutLBSgeneDB
mutated Ligand Binding Site gene DataBase

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Gene Summary

Ligand Binding Site Mutation Information

Protein Structure Related Information

Gene Expression and Gene-Gene Network

Phenotype Information

Pharmacological Information

Conservation Information for LBS

Gene summary for GSTO1
Gene summary
Basic gene Info.Gene symbolGSTO1
Gene nameglutathione S-transferase omega 1
SynonymsGSTO 1-1|GSTTLp28|HEL-S-21|P28|SPG-R
CytomapUCSC genome browser: 10q25.1
Type of geneprotein-coding
RefGenesNM_001191002.1,
NM_001191003.1,NM_004832.2,
DescriptionGSTO-1MMA(V) reductaseS-(Phenacyl)glutathione reductaseepididymis secretory protein Li 21glutathione S-transferase omega 1-1glutathione S-transferase omega-1glutathione-S-transferase likeglutathione-dependent dehydroascorbate reductasemonomethylar
Modification date20141207
dbXrefs MIM : 605482
HGNC : HGNC
Ensembl : ENSG00000148834
HPRD : 10401
Vega : OTTHUMG00000019001
ProteinUniProt: P78417
go to UniProt's Cross Reference DB Table
ExpressionCleanEX: HS_GSTO1
BioGPS: 9446
PathwayNCI Pathway Interaction Database: GSTO1
KEGG: GSTO1
REACTOME: GSTO1
Pathway Commons: GSTO1
ContextiHOP: GSTO1
ligand binding site mutation search in PubMed: GSTO1
UCL Cancer Institute: GSTO1
Assigned class in mutLBSgeneDBC: This gene just belongs to mutLBSgenes.

Gene ontology having evidence of Inferred from Direct Assay (IDA) from Entrez
GO IDGO TermPubMed ID
GO:0010880regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum11035031
GO:0019852L-ascorbic acid metabolic process11511179
GO:0042178xenobiotic catabolic process12928150
GO:0060315negative regulation of ryanodine-sensitive calcium-release channel activity11035031
GO:0060316positive regulation of ryanodine-sensitive calcium-release channel activity11035031
GO:0071243cellular response to arsenic-containing substance11511179


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Ligand binding site mutations for GSTO1
Lollipop-style diagram of mutations at LBS in amino-acid sequence.
We represented ligand binding site mutations only. (You can see big image via clicking.)
 
: non-synonymous mutation on LBS, Circle size denotes number of samples.

Cancer type specific mutLBS sorted by frequency
LBSAAchange of nsSNVCancer type# samples
V127L126FLUSC1
P33P33LSKCM1
E85E85KUCEC1
K57K57TUCEC1
cf) Cancer type abbreviation. BLCA: Bladder urothelial carcinoma, BRCA: Breast invasive carcinoma, CESC: Cervical squamous cell carcinoma and endocervical adenocarcinoma, COAD: Colon adenocarcinoma, GBM: Glioblastoma multiforme, LGG: Brain lower grade glioma, HNSC: Head and neck squamous cell carcinoma, KICH: Kidney chromophobe, KIRC: Kidney renal clear cell carcinoma, KIRP: Kidney renal papillary cell carcinoma, LAML: Acute myeloid leukemia, LUAD: Lung adenocarcinoma, LUSC: Lung squamous cell carcinoma, OV: Ovarian serous cystadenocarcinoma, PAAD: Pancreatic adenocarcinoma, PRAD: Prostate adenocarcinoma, SKCM: Skin cutaneous melanoma, STAD: Stomach adenocarcinoma, THCA: Thyroid carcinoma, UCEC: Uterine corpus endometrial carcinoma.


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Protein structure related information for GSTO1
Relative protein structure stability change (ΔΔE) using Mupro 1.1
Mupro score denotes assessment of the effect of mutations on thermodynamic stability.
  (ΔΔE<0: mutation decreases stability, ΔΔE>0: mutation increases stability)
: nsSNV at non-LBS: nsSNV at LBS

nsSNVs sorted by the relative stability change of protein structure by each mutation
Blue: mutations of positive stability change. and red : the most recurrent mutation for this gene.
LBSAAchange of nsSNVRelative stability change
V127L126F-1.3709066
E85E85K-1.3520468
K57K57T-1.0477333
P33P33L-0.23463063
(MuPro1.1: Jianlin Cheng et al., Prediction of Protein Stability Changes for Single-Site Mutations Using Support Vector Machines, PROTEINS: Structure, Function, and Bioinformatics. 2006, 62:1125-1132)

Structure image for GSTO1 from PDB

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Differential gene expression and gene-gene network for GSTO1
Differential gene expression between mutated and non-mutated LBS samples in all 16 major cancer types

Differential co-expressed gene network based on protein-protein interaction data (CePIN)
* Left PPI network was created from samples with mutations in the LBS of GSTO1 and the right PPI network was created from samples without mutations in the LBS of GSTO1. Only genes with p-value < 0.05 are shown.
Red circle: input gene. Orange circle: LBSgene. Blue circle: other gene.


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Phenotype information for GSTO1
Gene level disease information (DisGeNet)
Disease IDDisease name# PubMedAssociation type
umls:C0027651Neoplasms2Biomarker, GeneticVariation
umls:C0037274Skin Diseases2Biomarker, GeneticVariation
umls:C0524851Neurodegenerative Diseases2Biomarker
umls:C0024115Lung Diseases1Biomarker, GeneticVariation
umls:C0279626Esophageal Squamous Cell Carcinoma1Biomarker
umls:C0023418Leukemia1Biomarker
umls:C0032927Precancerous Conditions1Biomarker
umls:C0033578Prostatic Neoplasms1Biomarker

Mutation level pathogenic information (ClinVar annotation)
Allele IDAA changeClinical significanceOriginPhenotype IDs

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Pharmacological information for GSTO1
Gene expression profile of anticancer drug treated cell-lines (CCLE)
Heatmap showing the correlation between gene expression and drug response across all the cell-lines. We chose the top 20 among 138 drugs.We used Pearson's correlation coefficient.

Gene-centered drug-gene interaction network
Drug information targeting mutLBSgene (Approved drugs only)
Drug statusDrugBank IDNameTypeDrug structure
Approved|nutraceuticalDB00143GlutathioneSmall molecule

Gene-centered ligand-gene interaction network

Ligands binding to mutated ligand binding site of GSTO1 go to BioLip
Ligand IDLigand short nameLigand long namePDB IDPDB namemutLBS
ASCASCORBIC ACID3vlnAE85
GSHGLUTATHIONATE(1-)1eemAP33 E85
GSHGLUTATHIONATE(1-)3lflAP33 E85
GSHGLUTATHIONATE(1-)3lflBP33 E85
GSHGLUTATHIONATE(1-)3lflCP33 E85
GDSGLUTATHIONE DISULFIDE4is0AP33 K57 E85 V127


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Conservation information for LBS of GSTO1
Multiple alignments for P78417 in multiple species
LBSAA sequence# speciesSpecies
A87LIYESAITCEY1Homo sapiens
A87VVIESGFIPEY1Caenorhabditis elegans
A87IVIESAVIPEY1Caenorhabditis elegans
A87VLTESLLICEY1Drosophila melanogaster
A87LVTESVITCEY1Mus musculus
C32YSMRFCPFAQR2Drosophila melanogaster, Mus musculus
C32YSMRFCPFAER1Homo sapiens
C32YNMRFCPWAER1Caenorhabditis elegans
C32YNMRYCPWAQR1Caenorhabditis elegans
E85-QLIYESAITC1Homo sapiens
E85-KVVIESGFIP1Caenorhabditis elegans
E85KKIVIESAVIP1Caenorhabditis elegans
E85PPVLTESLLIC1Drosophila melanogaster
E85-HLVTESVITC1Mus musculus
E91SAITCEYLDEA1Homo sapiens
E91SGFIPEYLDDA1Caenorhabditis elegans
E91SAVIPEYLDDI1Caenorhabditis elegans
E91SLLICEYLDEQ1Drosophila melanogaster
E91SVITCEYLDEA1Mus musculus
F34MRFCPFAERTR1Homo sapiens
F34MRFCPWAERAM1Caenorhabditis elegans
F34MRYCPWAQRAL1Caenorhabditis elegans
F34MRFCPFAQRVH1Drosophila melanogaster
F34MRFCPFAQRTL1Mus musculus
G70KKNPFGLVPVL1Homo sapiens
G70TKHYQGKAPAV1Caenorhabditis elegans
G70TKHYKGQVPAL1Caenorhabditis elegans
G70EKNPQGKVPAL1Drosophila melanogaster
G70EKNPLGLVPVL1Mus musculus
K114EKACQKMILEL1Homo sapiens
K114EKVQQKLLADR1Caenorhabditis elegans
K114EKVQQKLLLDR1Caenorhabditis elegans
K114KKVQDKLLIER1Drosophila melanogaster
K114KKARQKMTLES1Mus musculus
K57ININLKNKPEW2Homo sapiens, Mus musculus
K57VNLNVTDKLEW1Caenorhabditis elegans
K57INIHLDQKPDW1Caenorhabditis elegans
K57IYINLTDKPEW1Drosophila melanogaster
K59INLKNKPEWFF2Homo sapiens, Mus musculus
K59LNVTDKLEWYW1Caenorhabditis elegans
K59IHLDQKPDWFF1Caenorhabditis elegans
K59INLTDKPEWLL1Drosophila melanogaster
L117CQKMILELFSK1Homo sapiens
L117QQKLLADRLTA1Caenorhabditis elegans
L117QQKLLLDRISG1Caenorhabditis elegans
L117QDKLLIERFRA1Drosophila melanogaster
L117RQKMTLESFSK1Mus musculus
L176SMIDYLIWPWF1Homo sapiens
L176GYPDYLSFPFF1Caenorhabditis elegans
L176GFVDYLIYPNI1Caenorhabditis elegans
L176GILDYMIWPWC1Drosophila melanogaster
L176SMVDYLTWPWF1Mus musculus
L228QGFLELYLQNS1Homo sapiens
L228AAFMNAYATHQ1Caenorhabditis elegans
L228VEFFKSWIIGA1Caenorhabditis elegans
L228AEFLRTRSLGR1Drosophila melanogaster
L228REYLNLYLQDS1Mus musculus
L56VININLKNKPE2Homo sapiens, Mus musculus
L56VVNLNVTDKLE1Caenorhabditis elegans
L56VINIHLDQKPD1Caenorhabditis elegans
L56SIYINLTDKPE1Drosophila melanogaster
L71KNPFGLVPVLE1Homo sapiens
L71KHYQGKAPAVE1Caenorhabditis elegans
L71KHYKGQVPALE1Caenorhabditis elegans
L71KNPQGKVPALE1Drosophila melanogaster
L71KNPLGLVPVLE1Mus musculus
M172-NSISMIDYLI1Homo sapiens
M172-SQPGYPDYLS1Caenorhabditis elegans
M172TSKPGFVDYLI1Caenorhabditis elegans
M172-EQTGILDYMI1Drosophila melanogaster
M172-DSPSMVDYLT1Mus musculus
P33SMRFCPFAERT1Homo sapiens
P33NMRFCPWAERA1Caenorhabditis elegans
P33NMRYCPWAQRA1Caenorhabditis elegans
P33SMRFCPFAQRV1Drosophila melanogaster
P33SMRFCPFAQRT1Mus musculus
P73PFGLVPVLE--1Homo sapiens
P73YQGKAPAVE--1Caenorhabditis elegans
P73YKGQVPALE--1Caenorhabditis elegans
P73PQGKVPALEIV1Drosophila melanogaster
P73PLGLVPVLE--1Mus musculus
R37CPFAERTRLVL1Homo sapiens
R37CPWAERAMLYV1Caenorhabditis elegans
R37CPWAQRALIFA1Caenorhabditis elegans
R37CPFAQRVHLVL1Drosophila melanogaster
R37CPFAQRTLMVL1Mus musculus
S121ILELFSKVPSL1Homo sapiens
S121LADRLTAVAHA1Caenorhabditis elegans
S121LLDRISG--QL1Caenorhabditis elegans
S121LIERFRA---V1Drosophila melanogaster
S121TLESFSKVPPL1Mus musculus
S86QLIYESAITCE1Homo sapiens
S86KVVIESGFIPE1Caenorhabditis elegans
S86KIVIESAVIPE1Caenorhabditis elegans
S86PVLTESLLICE1Drosophila melanogaster
S86HLVTESVITCE1Mus musculus
V127KVPSLVGSFIR1Homo sapiens
V127AVAHAVPLLFA1Caenorhabditis elegans
V127G--QLSSAFYG1Caenorhabditis elegans
V127A---VLGAFFK1Drosophila melanogaster
V127KVPPLIASFVR1Mus musculus
V72NPFGLVPVLE-1Homo sapiens
V72HYQGKAPAVE-1Caenorhabditis elegans
V72HYKGQVPALE-1Caenorhabditis elegans
V72NPQGKVPALEI1Drosophila melanogaster
V72NPLGLVPVLE-1Mus musculus
W222TSEKDWQGFLE1Homo sapiens
W222QSLEHGAAFMN1Caenorhabditis elegans
W222QPTETAVEFFK1Caenorhabditis elegans
W222MEAEVQAEFLR1Drosophila melanogaster
W222IDAKTYREYLN1Mus musculus
Y229GFLELYLQNSP1Homo sapiens
Y229AFMNAYATHQE1Caenorhabditis elegans
Y229EFFKSWIIGAP1Caenorhabditis elegans
Y229EFLRTRSLGRP1Drosophila melanogaster
Y229EYLNLYLQDSP1Mus musculus


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