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 DDR2
Gene summary
Basic gene Info.Gene symbolDDR2
Gene namediscoidin domain receptor tyrosine kinase 2
SynonymsMIG20a|NTRKR3|TKT|TYRO10
CytomapUCSC genome browser: 1q23.3
Type of geneprotein-coding
RefGenesNM_001014796.1,
NM_006182.2,
DescriptionCD167 antigen-like family member Bcell migration-inducing protein 20discoidin domain receptor 2discoidin domain receptor family, member 2discoidin domain-containing receptor 2discoidin domain-containing receptor tyrosine kinase 2hydroxyaryl-protein
Modification date20141207
dbXrefs MIM : 191311
HGNC : HGNC
Ensembl : ENSG00000162733
HPRD : 01868
Vega : OTTHUMG00000034423
ProteinUniProt: Q16832
go to UniProt's Cross Reference DB Table
ExpressionCleanEX: HS_DDR2
BioGPS: 4921
PathwayNCI Pathway Interaction Database: DDR2
KEGG: DDR2
REACTOME: DDR2
Pathway Commons: DDR2
ContextiHOP: DDR2
ligand binding site mutation search in PubMed: DDR2
UCL Cancer Institute: DDR2
Assigned class in mutLBSgeneDBB: This gene belongs to targetable_mutLBSgenes.

Gene ontology having evidence of Inferred from Direct Assay (IDA) from Entrez
GO IDGO TermPubMed ID
GO:0018108peptidyl-tyrosine phosphorylation20004161
GO:0038063collagen-activated tyrosine kinase receptor signaling pathway16186108
GO:0046777protein autophosphorylation16186108


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Ligand binding site mutations for DDR2
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
R105R105CCOAD2
W52S50NCOAD1
R105R105CKICH1
C73W72LLUAD1
R105G104VLUAD1
H172D171YLUSC1
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.

Clinical information for DDR2 from My Cancer Genome.
DDR2 (discoidin death receptor 2) is a member of the DDR family of receptor tyrosine kinases that are stimulated by collagen rather than peptide growth factors. Downstream signaling in cancer cells is poorly understood but may be via SRC and STAT signaling pathways. Similar to integrin receptors, DDR2 may play a role in modulating cellular interactions with the extracellular matrix. DDR2 mutations have been found at low frequency in a number of cancers, including renal cell carcinoma, glioblastoma multiforme, endometrial cancer, colorectal cancer (COSMIC). The highest reported frequency is in squamous cell carcinoma of the lung (Hammerman et al. 2011). Related Pathways: Receptor tyrosine kinase/growth factor signaling. Paik, P.K. . 2015. DDR2. My Cancer Genomehttps://www.mycancergenome.org/content/gene/ddr2/ (Updated December 2015)

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Protein structure related information for DDR2
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
R105R105C-1.058482
R105G104V-0.29828989
W52S50N-0.27840686
C73W72L-0.16969475
H172D171Y-0.13842535
(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 DDR2 from PDB
PDB IDPDB titlePDB structure
2Z4FSolution structure of the Discoidin Domain of DDR2

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Differential gene expression and gene-gene network for DDR2
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 DDR2 and the right PPI network was created from samples without mutations in the LBS of DDR2. 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 DDR2
Gene level disease information (DisGeNet)
Disease IDDisease name# PubMedAssociation type
umls:C1849011Spondylometaepiphyseal Dysplasia, Short Limb-Hand Type1Biomarker, GeneticVariation

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

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Pharmacological information for DDR2
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
ApprovedDB08896RegorafenibSmall molecule

Gene-centered ligand-gene interaction network

Ligands binding to mutated ligand binding site of DDR2 go to BioLip
Ligand IDLigand short nameLigand long namePDB IDPDB namemutLBS
IIIPeptide ligand (ACE,GLY,PRO,PRO,GLY,PRO,PRO,GLY,PRO,PRO,GLY,PRO,ARG,GLY,GLN,PRO,GLY,VAL,LEU,GLY,PHE,PRO,GLY,PRO,PRO,GLY,PRO,PRO,GLY)2wuhAW52 C73 R105 H172
IIIPeptide ligand (GLY,PRO,PRO,GLY,PRO,PRO,GLY,PRO,PRO,GLY,PRO,ARG,GLY,GLN,PRO,GLY,VAL,LEU,GLY,PHE,PRO,GLY,PRO,PRO,GLY,PRO,PRO,GLY)2wuhAW52 R105


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Conservation information for LBS of DDR2
Multiple alignments for Q16832 in multiple species
LBSAA sequence# speciesSpecies
C177HSMNVCMRVEL2Homo sapiens, Mus musculus
C177STRTVCMRVEV1Caenorhabditis elegans
C73GDGAWCPEIPV2Homo sapiens, Mus musculus
C73GSGAWCPKNQI1Caenorhabditis elegans
D69DSEEGDGAWCP2Homo sapiens, Mus musculus
D69HQESGSGAWCP1Caenorhabditis elegans
E113GGHGIEFAPMY2Homo sapiens, Mus musculus
E113DGRGMEYATAF1Caenorhabditis elegans
H110RHAGGHGIEFA2Homo sapiens, Mus musculus
H110RFDDGRGMEYA1Caenorhabditis elegans
H172IPVTDHSMNVC2Homo sapiens, Mus musculus
H172VPVSNSTRTVC1Caenorhabditis elegans
I112AGGHGIEFAPM2Homo sapiens, Mus musculus
I112DDGRGMEYATA1Caenorhabditis elegans
N175TDHSMNVCMRV2Homo sapiens, Mus musculus
N175SNSTRTVCMRV1Caenorhabditis elegans
R105VGTQGRHAGGH2Homo sapiens, Mus musculus
R105VETQGRFDDGR1Caenorhabditis elegans
S173PVTDHSMNVCM2Homo sapiens, Mus musculus
S173PVSNSTRTVCM1Caenorhabditis elegans
T56WS-ESTAAKYG2Homo sapiens, Mus musculus
T56FDLQSTGPQHA1Caenorhabditis elegans
W52TASSQWS-EST2Homo sapiens, Mus musculus
W52SASSSFDLQST1Caenorhabditis elegans


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