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 BMPR1B
Gene summary
Basic gene Info.Gene symbolBMPR1B
Gene namebone morphogenetic protein receptor, type IB
CytomapUCSC genome browser: 4q22-q24
Type of geneprotein-coding
DescriptionBMP type-1B receptorBMPR-1Bactivin receptor-like kinase 6bone morphogenetic protein receptor type-1Bserine/threonine receptor kinase
Modification date20141207
dbXrefs MIM : 603248
Ensembl : ENSG00000138696
HPRD : 04457
Vega : OTTHUMG00000130991
ProteinUniProt: O00238
go to UniProt's Cross Reference DB Table
ExpressionCleanEX: HS_BMPR1B
BioGPS: 658
PathwayNCI Pathway Interaction Database: BMPR1B
Pathway Commons: BMPR1B
ContextiHOP: BMPR1B
ligand binding site mutation search in PubMed: BMPR1B
UCL Cancer Institute: BMPR1B
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 BMPR1B.1. "Demirhan O, Türkmen S, Schwabe GC, Soyupak S, Akgül E, Tastemir D, Karahan D, Mundlos S, Lehmann K. A homozygous BMPR1B mutation causes a new subtype of acromesomelic chondrodysplasia with genital anomalies. J Med Genet. 2005 Apr;42(4):314-7. PubMed PMID: 15805157; PubMed Central PMCID: PMC1736042. " 15805157
2. "Graul-Neumann LM, Deichsel A, Wille U, Kakar N, Koll R, Bassir C, Ahmad J, Cormier-Daire V, Mundlos S, Kubisch C, Borck G, Klopocki E, Mueller TD, Doelken SC, Seemann P. Homozygous missense and nonsense mutations in BMPR1B cause acromesomelic chondrodysplasia-type Grebe. Eur J Hum Genet. 2014 Jun;22(6):726-33. doi: 10.1038/ejhg.2013.222. Epub 2013 Oct 16. PubMed PMID:24129431; PubMed Central PMCID: PMC4023204." 24129431
3. "Stange K, Désir J, Kakar N, Mueller TD, Budde BS, Gordon CT, Horn D, Seemann P, Borck G. A hypomorphic BMPR1B mutation causes du Pan acromesomelic dysplasia. Orphanet J Rare Dis. 2015 Jun 24;10:84. doi: 10.1186/s13023-015-0299-5. PubMed PMID: 26105076; PubMed Central PMCID: PMC4482310. " 26105076

Gene ontology having evidence of Inferred from Direct Assay (IDA) from Entrez
GO:0006468protein phosphorylation12065756
GO:0030509BMP signaling pathway18436533

Ligand binding site mutations for BMPR1B

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 BMPR1B
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 BMPR1B from PDB

Differential gene expression and gene-gene network for BMPR1B
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 BMPR1B and the right PPI network was created from samples without mutations in the LBS of BMPR1B. Only genes with p-value < 0.05 are shown.
Red circle: input gene. Orange circle: LBSgene. Blue circle: other gene.


Phenotype information for BMPR1B
Gene level disease information (DisGeNet)
Disease IDDisease name# PubMedAssociation type
umls:C1832702Brachydactyly type A26Biomarker, GeneticVariation
umls:C0033578Prostatic Neoplasms2AlteredExpression, Biomarker
umls:C1836182Chondrodysplasia, acromesomelic, with genital anomalies1Biomarker, GeneticVariation
umls:C0005941Bone Diseases, Developmental1Biomarker
umls:C0376634Craniofacial Abnormalities1Biomarker
umls:C0015393Eye Abnormalities1Biomarker
umls:C0031117Peripheral Nervous System Diseases1Biomarker

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

Pharmacological information for BMPR1B
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

Gene-centered ligand-gene interaction network

Ligands binding to mutated ligand binding site of BMPR1B go to BioLip
Ligand IDLigand short nameLigand long namePDB IDPDB namemutLBS

Conservation information for LBS of BMPR1B
Multiple alignments for O00238 in multiple species
LBSAA sequence# speciesSpecies
A229RGEKVAVKVFF3Homo sapiens, Gallus gallus, Mus musculus
A229RGSYVAVKTFY1Caenorhabditis elegans
A349GTCCIADLGLA3Homo sapiens, Gallus gallus, Mus musculus
A349NVCCIADLGLA1Caenorhabditis elegans
D280LYLITDYHENG3Homo sapiens, Gallus gallus, Mus musculus
D280MLLITDYHELG1Caenorhabditis elegans
D289NGSLYDYL-KS3Homo sapiens, Gallus gallus, Mus musculus
D289LGSLSDYLCRE1Caenorhabditis elegans
D350TCCIADLGLAV3Homo sapiens, Gallus gallus, Mus musculus
D350VCCIADLGLAL1Caenorhabditis elegans
E283ITDYHENGSLY3Homo sapiens, Gallus gallus, Mus musculus
E283ITDYHELGSLS1Caenorhabditis elegans
G285DYHENGSLYDY3Homo sapiens, Gallus gallus, Mus musculus
G285DYHELGSLSDY1Caenorhabditis elegans
H282LITDYHENGSL3Homo sapiens, Gallus gallus, Mus musculus
H282LITDYHELGSL1Caenorhabditis elegans
I210QMVKQIGKGRY3Homo sapiens, Gallus gallus, Mus musculus
I210TIIKTIGQGRY1Caenorhabditis elegans
K336RDLKSKNILVK3Homo sapiens, Gallus gallus, Mus musculus
K336RDIKSKNIIVK1Caenorhabditis elegans
L259RHENILGFIAA3Homo sapiens, Gallus gallus, Mus musculus
L259NHENILQFVAA1Caenorhabditis elegans
L339KSKNILVKKNG3Homo sapiens, Gallus gallus, Mus musculus
L339KSKNIIVKRPN1Caenorhabditis elegans
N337DLKSKNILVKK3Homo sapiens, Gallus gallus, Mus musculus
N337DIKSKNIIVKR1Caenorhabditis elegans
T279QLYLITDYHEN3Homo sapiens, Gallus gallus, Mus musculus
T279KMLLITDYHEL1Caenorhabditis elegans
V218GRYGEVWMGKW3Homo sapiens, Gallus gallus, Mus musculus
V218GRYGEVRKALY1Caenorhabditis elegans
Y281YLITDYHENGS3Homo sapiens, Gallus gallus, Mus musculus
Y281LLITDYHELGS1Caenorhabditis elegans

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