mutated Ligand Binding Site gene DataBase





About Us

Bioinformatics and Systems Medicine Laboratory Bioinformatics and Systems Medicine Laboratory

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 FSHR
Gene summary
Basic gene Info.Gene symbolFSHR
Gene namefollicle stimulating hormone receptor
CytomapUCSC genome browser: 2p21-p16
Type of geneprotein-coding
DescriptionFSH receptorfollicle-stimulating hormone receptorfollitropin receptor
Modification date20141222
dbXrefs MIM : 136435
Ensembl : ENSG00000170820
HPRD : 00639
Vega : OTTHUMG00000129259
ProteinUniProt: P23945
go to UniProt's Cross Reference DB Table
ExpressionCleanEX: HS_FSHR
BioGPS: 2492
PathwayNCI Pathway Interaction Database: FSHR
Pathway Commons: FSHR
ContextiHOP: FSHR
ligand binding site mutation search in PubMed: FSHR
UCL Cancer Institute: FSHR
Assigned class in mutLBSgeneDBA: This gene has a literature evidence and it belongs to targetable_mutLBSgenes.
References showing study about ligand binding site mutation for FSHR.1. "De Leener A, Caltabiano G, Erkan S, Idil M, Vassart G, Pardo L, Costagliola S. Identification of the first germline mutation in the extracellular domain of the follitropin receptor responsible for spontaneous ovarian hyperstimulation syndrome. Hum Mutat. 2008 Jan;29(1):91-8. PubMed PMID: 17721928. " 17721928
2. "Peltoketo H, Strauss L, Karjalainen R, Zhang M, Stamp GW, Segaloff DL, Poutanen M, Huhtaniemi IT. Female mice expressing constitutively active mutants of FSH receptor present with a phenotype of premature follicle depletion and estrogen excess. Endocrinology. 2010 Apr;151(4):1872-83. doi: 10.1210/en.2009-0966. Epub 2010 Feb 19. PubMed PMID: 20172968; PubMed CentralPMCID: PMC2851188. " 20172968
3. "Tapanainen JS, Aittomäki K, Min J, Vaskivuo T, Huhtaniemi IT. Men homozygous for an inactivating mutation of the follicle-stimulating hormone (FSH) receptor gene present variable suppression of spermatogenesis and fertility. Nat Genet. 1997 Feb;15(2):205-6. PubMed PMID: 9020851. " 9020851

Gene ontology having evidence of Inferred from Direct Assay (IDA) from Entrez

Ligand binding site mutations for FSHR
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
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.

Protein structure related information for FSHR
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
(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 FSHR from PDB
PDB IDPDB titlePDB structure
1XWDCrystal Structure of Human Follicle Stimulating Hormone Complexed with its Receptor

Differential gene expression and gene-gene network for FSHR
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 FSHR and the right PPI network was created from samples without mutations in the LBS of FSHR. Only genes with p-value < 0.05 are shown.
Red circle: input gene. Orange circle: LBSgene. Blue circle: other gene.


Phenotype information for FSHR
Gene level disease information (DisGeNet)
Disease IDDisease name# PubMedAssociation type
umls:C0085083Ovarian Hyperstimulation Syndrome20Biomarker, GeneticVariation
umls:C0032460Polycystic Ovary Syndrome20AlteredExpression, Biomarker, GeneticVariation
umls:C0949595Gonadal Dysgenesis, 46,XX3Biomarker, GeneticVariation

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

Pharmacological information for FSHR
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
ApprovedDB00066Follitropin betaBiotech
ApprovedDB00097Chorionic Gonadotropin (Recombinant)Biotech
ApprovedDB04786SuraminSmall molecule

Gene-centered ligand-gene interaction network

Ligands binding to mutated ligand binding site of FSHR go to BioLip
Ligand IDLigand short nameLigand long namePDB IDPDB namemutLBS
JEFJEFFAMINE4mqwZH139 R162 N163 V166

Conservation information for LBS of FSHR
Multiple alignments for P23945 in multiple species
LBSAA sequence# speciesSpecies
H139HLPAVHKIQSL2Rattus norvegicus, Bos taurus
H139HLPDVHKIHSL1Homo sapiens
H139FLPVVHKVHSF1Gallus gallus
H139HLPAFHKIQSL1Mus musculus
N163HTIERNSFVGL1Homo sapiens
N163RTIERNTFMGL1Gallus gallus
N163HIIARNSFMGL1Mus musculus
N163HIVARNSFMGL1Rattus norvegicus
N163HTVERNSFMGL1Bos taurus
R162IHTIERNSFVG1Homo sapiens
R162IRTIERNTFMG1Gallus gallus
R162IHIIARNSFMG1Mus musculus
R162IHIVARNSFMG1Rattus norvegicus
R162IHTVERNSFMG1Bos taurus
V166ARNSFMGLSFE2Mus musculus, Rattus norvegicus
V166ERNSFVGLSFE1Homo sapiens
V166ERNTFMGLSSE1Gallus gallus
V166ERNSFMGLSFE1Bos taurus

Copyright © 2016-Present - The University of Texas Health Science Center at Houston
Site Policies | State of Texas