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 SULT1A1
Gene summary
Basic gene Info.Gene symbolSULT1A1
Gene namesulfotransferase family, cytosolic, 1A, phenol-preferring, member 1
SynonymsHAST1/HAST2|P-PST|PST|ST1A1|ST1A3|STP|STP1|TSPST1
CytomapUCSC genome browser: 16p12.1
Type of geneprotein-coding
RefGenesNM_001055.3,
NM_177529.2,NM_177530.2,NM_177534.2,NM_177536.3,
DescriptionP-PST 1aryl sulfotransferase 1phenol-sulfating phenol sulfotransferase 1sulfotransferase 1A1thermostable phenol sulfotransferase1ts-PST
Modification date20141207
dbXrefs MIM : 171150
HGNC : HGNC
Ensembl : ENSG00000196502
HPRD : 01372
Vega : OTTHUMG00000131765
ProteinUniProt: P50225
go to UniProt's Cross Reference DB Table
ExpressionCleanEX: HS_SULT1A1
BioGPS: 6817
PathwayNCI Pathway Interaction Database: SULT1A1
KEGG: SULT1A1
REACTOME: SULT1A1
Pathway Commons: SULT1A1
ContextiHOP: SULT1A1
ligand binding site mutation search in PubMed: SULT1A1
UCL Cancer Institute: SULT1A1
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:0006805xenobiotic metabolic process12471039
GO:0008210estrogen metabolic process16221673
GO:0009812flavonoid metabolic process20056724
GO:0051923sulfation20056724


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Ligand binding site mutations for SULT1A1

Cancer type specific mutLBS sorted by frequency
LBSAAchange of nsSNVCancer type# samples
I21P19LKIRC2
M77R78WCOAD1
T51T51SCOAD1
H108,K106T107AOV1
K197E198KSKCM1
M232M232ISKCM1
P90P90SSKCM1
F255P254HSKCM1
M77M77IUCEC1
P244V243IUCEC1
H149P150HUCEC1
T227T227MUCEC1
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 SULT1A1
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
I21P19L0.21192881
M232M232I-1.4898216
T51T51S-1.2384974
K106T107A-1.2016868
H108T107A-1.2016868
F255P254H-1.0100322
M77M77I-0.96341859
P90P90S-0.86716596
P244V243I-0.83765769
K197E198K-0.80113954
H149P150H-0.62033247
M77R78W-0.54830287
T227T227M-0.30068789
(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 SULT1A1 from PDB
PDB IDPDB titlePDB structure
4GRACrystal structure of SULT1A1 bound with PAP

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Differential gene expression and gene-gene network for SULT1A1
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 SULT1A1 and the right PPI network was created from samples without mutations in the LBS of SULT1A1. 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 SULT1A1
Gene level disease information (DisGeNet)
Disease IDDisease name# PubMedAssociation type
umls:C0033578Prostatic Neoplasms3Biomarker, GeneticVariation
umls:C0042076Urologic Neoplasms2Biomarker, GeneticVariation
umls:C0008625Chromosome Aberrations1Biomarker
umls:C0009375Colonic Neoplasms1Biomarker
umls:C0151744Myocardial Ischemia1Biomarker

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

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Pharmacological information for SULT1A1
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
ExperimentalDB01812Adenosine-3'-5'-DiphosphateSmall molecule
ExperimentalDB04417P-NitrophenolSmall molecule

Gene-centered ligand-gene interaction network

Ligands binding to mutated ligand binding site of SULT1A1 go to BioLip
Ligand IDLigand short nameLigand long namePDB IDPDB namemutLBS
NPO4-NITROPHENOL1ls6AI21 K106 H108 H149
03V2-NAPHTHOL3u3kAI21 K106 H108 H149
03V2-NAPHTHOL3u3kBI21 K106 H108 H149
NPO4-NITROPHENOL3u3rAI21 K106 H108 H149
ESTESTRADIOL2d06AK106 H108
ESTESTRADIOL2d06BK106 H108
3QV7-HYDROXY-2-OXO-2H-CHROMENE-3-CARBONITRILE3qvvAK106 H108
3QV7-HYDROXY-2-OXO-2H-CHROMENE-3-CARBONITRILE3qvvBK106 H108
3QV7-HYDROXY-2-OXO-2H-CHROMENE-3-CARBONITRILE3u3oAK106 H108
NPO4-NITROPHENOL3qvuAK106 H108 H149
NPO4-NITROPHENOL3qvuBK106 H108 H149
3QV7-HYDROXY-2-OXO-2H-CHROMENE-3-CARBONITRILE3u3mAK106 H108 H149
3QV7-HYDROXY-2-OXO-2H-CHROMENE-3-CARBONITRILE3u3oAM77 P90 P244
A3PADENOSINE 3',5'-BISPHOSPHATE1ls6AT51 K197 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3qvvBT51 K197 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3u3jBT51 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3qvuBT51 T227 M232
A3PADENOSINE 3',5'-BISPHOSPHATE1z28AT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE2d06AT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE2d06BT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3qvuAT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3qvvAT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3u3jAT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3u3kAT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3u3kBT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3u3mAT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3u3oAT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE3u3rAT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE4graAT51 T227 M232 F255
A3PADENOSINE 3',5'-BISPHOSPHATE4graBT51 T227 M232 F255


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Conservation information for LBS of SULT1A1
Multiple alignments for P50225 in multiple species
LBSAA sequence# speciesSpecies
A146HFYHMAKVHPE1Homo sapiens
A146HFDRMNIVEPD1Danio rerio
A146HFDRMNMGQPE1Danio rerio
F142VSYYHFYHMAK1Homo sapiens
F142VSYFHFDRMNI1Danio rerio
F142VSYFHFDRMNM1Danio rerio
F229VQHTSFKEMKK1Homo sapiens
F229TKDVQFDAMKQ1Danio rerio
F229TKGVQFDVMKQ1Danio rerio
F24PLIKYFAEALG1Homo sapiens
F24SMINHFTENWE1Danio rerio
F24SMTRYFTDNWE1Danio rerio
F247TLP--VMDFKI2Danio rerio, Danio rerio
F247TVPQEFMDHSI1Homo sapiens
F255FKISPFMRKGK2Danio rerio, Danio rerio
F255HSISPFMRKGM1Homo sapiens
F76TSQPIYMRVPF2Danio rerio, Danio rerio
F76RA-PIFMRVPF1Homo sapiens
F81FMRVPFLEFKA1Homo sapiens
F81YMRVPFLESCF1Danio rerio
F81YMRVPFLEMCF1Danio rerio
F84VPFLEFKAPGI1Homo sapiens
F84VPFLESCFKVI1Danio rerio
F84VPFLEMCFQGL1Danio rerio
G259PFMRKGKVGDW2Danio rerio, Danio rerio
G259PFMRKGMAGDW1Homo sapiens
G50TYPKAGTTWVS2Danio rerio, Danio rerio
G50TYPKSGTTWVS1Homo sapiens
H108RLLKTHLPLAL1Homo sapiens
H108RLIKTHLPVQL1Danio rerio
H108RPIKTHLPVQL1Danio rerio
H149HMAKVHPEPGT1Homo sapiens
H149RMNIVEPDPGD1Danio rerio
H149RMNMGQPEPGD1Danio rerio
I21KGVPLIKYFAE1Homo sapiens
I21EGISMINHFTE1Danio rerio
I21EGVSMTRYFTD1Danio rerio
I89FKAPGIPSGME1Homo sapiens
I89SCFKVIASGTE1Danio rerio
I89MCFQGLPLGTE1Danio rerio
K106APRLLKTHLPL1Homo sapiens
K106SPRLIKTHLPV1Danio rerio
K106SPRPIKTHLPV1Danio rerio
K197FYEDMKENPKR1Homo sapiens
K197FYEDLVEDTGR1Danio rerio
K197FYEDMVEDTGR1Danio rerio
K258SPFMRKGKVGD2Danio rerio, Danio rerio
K258SPFMRKGMAGD1Homo sapiens
K48IATYPKAGTTW2Danio rerio, Danio rerio
K48ISTYPKSGTTW1Homo sapiens
M232TSFKEMKKNPM1Homo sapiens
M232VQFDAMKQNKM1Danio rerio
M232VQFDVMKQNKM1Danio rerio
M248LP--VMDFKIS2Danio rerio, Danio rerio
M248VPQEFMDHSIS1Homo sapiens
M256KISPFMRKGKV2Danio rerio, Danio rerio
M256SISPFMRKGMA1Homo sapiens
M77SQPIYMRVPFL2Danio rerio, Danio rerio
M77A-PIFMRVPFL1Homo sapiens
P244NYSTLP--VMD2Danio rerio, Danio rerio
P244NYTTVPQEFMD1Homo sapiens
P47LIATYPKAGTT2Danio rerio, Danio rerio
P47LISTYPKSGTT1Homo sapiens
P90KAPGIPSGMET1Homo sapiens
P90CFKVIASGTEL1Danio rerio
P90CFQGLPLGTEL1Danio rerio
R130VVYVARNAKDN2Danio rerio, Danio rerio
R130VVYVARNAKDV1Homo sapiens
R257ISPFMRKGKVG2Danio rerio, Danio rerio
R257ISPFMRKGMAG1Homo sapiens
S138KDVAVSYYHFY1Homo sapiens
S138KDNVVSYFHFD1Danio rerio
S138KDNAVSYFHFD1Danio rerio
S228VVQHTSFKEMK1Homo sapiens
S228ITKDVQFDAMK1Danio rerio
S228ITKGVQFDVMK1Danio rerio
S49ATYPKAGTTWV2Danio rerio, Danio rerio
S49STYPKSGTTWV1Homo sapiens
T227FVVQHTSFKEM1Homo sapiens
T227KITKDVQFDAM1Danio rerio
T227RITKGVQFDVM1Danio rerio
T51YPKAGTTWVSY2Danio rerio, Danio rerio
T51YPKSGTTWVSQ1Homo sapiens
T52PKAGTTWVSYI2Danio rerio, Danio rerio
T52PKSGTTWVSQI1Homo sapiens
V148YHMAKVHPEPG1Homo sapiens
V148DRMNIVEPDPG1Danio rerio
V148DRMNMGQPEPG1Danio rerio
W53KAGTTWVSYIL2Danio rerio, Danio rerio
W53KSGTTWVSQIL1Homo sapiens
Y193VLYLFYEDMKE1Homo sapiens
Y193LLYLFYEDLVE1Danio rerio
Y193ILYMFYEDMVE1Danio rerio
Y240NKMTNYSTLP-2Danio rerio, Danio rerio
Y240NPMTNYTTVPQ1Homo sapiens


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