mutLBSgeneDB

mutLBSgeneDB
mutated Ligand Binding Site gene DataBase

Home

Download

 Statistics

Help

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 PGLYRP3
Gene summary
Basic gene Info.Gene symbolPGLYRP3
Gene namepeptidoglycan recognition protein 3
SynonymsPGRP-Ialpha|PGRPIA
CytomapUCSC genome browser: 1q21
Type of geneprotein-coding
RefGenesNM_052891.1,
DescriptionPGLYRPIalphaPGRP-I-alphapeptidoglycan recognition protein I alphapeptidoglycan recognition protein I-alphapeptidoglycan recognition protein intermediate alphapeptidoglycan recognition protein-I-alpha
Modification date20141207
dbXrefs MIM : 608197
HGNC : HGNC
Ensembl : ENSG00000159527
HPRD : 16297
Vega : OTTHUMG00000014044
ProteinUniProt: Q96LB9
go to UniProt's Cross Reference DB Table
ExpressionCleanEX: HS_PGLYRP3
BioGPS: 114771
PathwayNCI Pathway Interaction Database: PGLYRP3
KEGG: PGLYRP3
REACTOME: PGLYRP3
Pathway Commons: PGLYRP3
ContextiHOP: PGLYRP3
ligand binding site mutation search in PubMed: PGLYRP3
UCL Cancer Institute: PGLYRP3
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:0002221pattern recognition receptor signaling pathway11461926
GO:0016045detection of bacterium11461926
GO:0050830defense response to Gram-positive bacterium11461926


Top
Ligand binding site mutations for PGLYRP3

Cancer type specific mutLBS sorted by frequency
LBSAAchange of nsSNVCancer type# samples
A210A210TBRCA1
Q327G326VBRCA1
F230S229PCOAD1
I207I207TKIRC1
R235R235LLUAD1
V320,I322N321KLUAD1
F230S229YOV1
F237C238FPRAD1
S324P325SSKCM1
H264H264YSKCM1
H316G315SSKCM1
A210A210DSKCM1
R235R235WSTAD1
H316G315DSTAD1
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.


Top
Protein structure related information for PGLYRP3
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
H264H264Y0.13487347
V320N321K0.050583949
I322N321K0.050583949
I207I207T-1.7458347
H316G315S-1.1809845
H316G315D-1.1391297
F237C238F-0.9864054
R235R235W-0.89685866
F230S229P-0.75182845
F230S229Y-0.64074435
R235R235L-0.60568161
A210A210D-0.52372537
S324P325S-0.40832214
A210A210T-0.36248791
Q327G326V-0.18652722
(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 PGLYRP3 from PDB

Top
Differential gene expression and gene-gene network for PGLYRP3
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 PGLYRP3 and the right PPI network was created from samples without mutations in the LBS of PGLYRP3. Only genes with p-value < 0.05 are shown.
Red circle: input gene. Orange circle: LBSgene. Blue circle: other gene.


Top

Top
Phenotype information for PGLYRP3
Gene level disease information (DisGeNet)
Disease IDDisease name# PubMedAssociation type

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

Top
Pharmacological information for PGLYRP3

Gene-centered drug-gene interaction network
Drug information targeting mutLBSgene (Approved drugs only)
Drug statusDrugBank IDNameTypeDrug structure
ExperimentalDB047362-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE(BETA1-4)-2-ACETAMIDO-1,6-ANHYDRO-3-O-[(R)-1-CARBOXYETHYL]-2-DEOXY-BETA-D-GLUCOPYRANOSE-L-ALANYL-GAMMA-D-GLUTAMYL-MESO-DIAMINOPIMELYL-D-ALANINESmall molecule

Gene-centered ligand-gene interaction network

Ligands binding to mutated ligand binding site of PGLYRP3 go to BioLip
Ligand IDLigand short nameLigand long namePDB IDPDB namemutLBS
IIIPeptide ligand (AMU,ALA,GLU,LYS,ALA,ALA,NH2)2aphBI207 A210 F230 R235 F237 H264 V320 I322 S324
IIIPeptide ligand (AMU,ALA,GLU,LYS,ALA,ALA,NH2)2aphAI207 A210 R235 F237 H264 H316 V320 S324
IIIPeptide ligand (AMU,ALA,GLU,LYS,NH2)1twqAI207 R235 F237 H264 H316 I322 S324
NASODIUM(1+)1sk4AV320 I322 S324 Q327


Top
Conservation information for LBS of PGLYRP3
Multiple alignments for Q96LB9 in multiple species
LBSAA sequence# speciesSpecies
A210IIIHTAGTSCT1Homo sapiens
A210RFVATNTPSCF1Drosophila melanogaster
A210IIIHTAGKSCN1Mus musculus
D318LMGHSDVVNIL1Homo sapiens
D318LIDDLEKS---1Drosophila melanogaster
D318LMGHSDVSNIL1Mus musculus
F230RNIQSFHMDTR1Homo sapiens
F230RLLQNWHIESN1Drosophila melanogaster
F230RDTQSFHIDNQ1Mus musculus
F237MDTRNFCDIGY1Homo sapiens
F237IESNGYKDINY1Drosophila melanogaster
F237IDNQDFCDIAY1Mus musculus
G267GSHTYGFNDIA1Homo sapiens
G267CEPPKDADELV1Drosophila melanogaster
G267GSHTYGYNDIA1Mus musculus
H208YVIIIHTAGTS1Homo sapiens
H208SVRFVATNTPS1Drosophila melanogaster
H208FVIIIHTAGKS1Mus musculus
H231NIQSFHMDTRN1Homo sapiens
H231LLQNWHIESNG1Drosophila melanogaster
H231DTQSFHIDNQD1Mus musculus
H264HIQGSHTYGFN1Homo sapiens
H264DHSCEPPKDAD1Drosophila melanogaster
H264NIEGSHTYGYN1Mus musculus
H316YLLMGHSDVVN1Homo sapiens
H316YSLIDDLEKS-1Drosophila melanogaster
H316YLLMGHSDVSN1Mus musculus
I207KYVIIIHTAGT1Homo sapiens
I207ESVRFVATNTP1Drosophila melanogaster
I207KFVIIIHTAGK1Mus musculus
I322SDVVNILSPGQ1Homo sapiens
I322LEKS-------1Drosophila melanogaster
I322SDVSNILSPGQ1Mus musculus
L323DVVNILSPGQA1Homo sapiens
L323EKS--------1Drosophila melanogaster
L323DVSNILSPGQA1Mus musculus
N236HMDTRNFCDIG1Homo sapiens
N236HIESNGYKDIN1Drosophila melanogaster
N236HIDNQDFCDIA1Mus musculus
N269HTYGFNDIALG1Homo sapiens
N269PPKDADELV--1Drosophila melanogaster
N269HTYGYNDIALG1Mus musculus
Q327ILSPGQALYNI2Homo sapiens, Mus musculus
Q327-----------1Drosophila melanogaster
R235FHMDTRNFCDI1Homo sapiens
R235WHIESNGYKDI1Drosophila melanogaster
R235FHIDNQDFCDI1Mus musculus
S263WHIQGSHTYGF1Homo sapiens
S263WDHSCEPPKDA1Drosophila melanogaster
S263WNIEGSHTYGY1Mus musculus
S317LLMGHSDVVNI1Homo sapiens
S317SLIDDLEKS--1Drosophila melanogaster
S317LLMGHSDVSNI1Mus musculus
S324VVNILSPGQAL1Homo sapiens
S324KS---------1Drosophila melanogaster
S324VSNILSPGQAL1Mus musculus
T209VIIIHTAGTSC1Homo sapiens
T209VRFVATNTPSC1Drosophila melanogaster
T209VIIIHTAGKSC1Mus musculus
T265IQGSHTYGFND1Homo sapiens
T265HSCEPPKDADE1Drosophila melanogaster
T265IEGSHTYGYND1Mus musculus
V319MGHSDVVNILS1Homo sapiens
V319IDDLEKS----1Drosophila melanogaster
V319MGHSDVSNILS1Mus musculus
V320GHSDVVNILSP1Homo sapiens
V320DDLEKS-----1Drosophila melanogaster
V320GHSDVSNILSP1Mus musculus
Y242FCDIGYHFLVG1Homo sapiens
Y242YKDINYNFVAA1Drosophila melanogaster
Y242FCDIAYHFLVG1Mus musculus
Y266QGSHTYGFNDI1Homo sapiens
Y266SCEPPKDADEL1Drosophila melanogaster
Y266EGSHTYGYNDI1Mus musculus


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