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 MMP7
Gene summary
Basic gene Info.Gene symbolMMP7
Gene namematrix metallopeptidase 7 (matrilysin, uterine)
SynonymsMMP-7|MPSL1|PUMP-1
CytomapUCSC genome browser: 11q21-q22
Type of geneprotein-coding
RefGenesNM_002423.3,
Descriptionmatrilysinmatrinmatrix metalloproteinase 7 (matrilysin, uterine)matrix metalloproteinase-7pump-1 proteaseuterine matrilysinuterine metalloproteinase
Modification date20141222
dbXrefs MIM : 178990
HGNC : HGNC
Ensembl : ENSG00000137673
HPRD : 01525
Vega : OTTHUMG00000048193
ProteinUniProt: P09237
go to UniProt's Cross Reference DB Table
ExpressionCleanEX: HS_MMP7
BioGPS: 4316
PathwayNCI Pathway Interaction Database: MMP7
KEGG: MMP7
REACTOME: MMP7
Pathway Commons: MMP7
ContextiHOP: MMP7
ligand binding site mutation search in PubMed: MMP7
UCL Cancer Institute: MMP7
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 MMP7.1. Yoshioka, S., King, M. L., Ran, S., Okuda, H., MacLean, J. A., McAsey, M. E., ... & Hayashi, K. (2012). WNT7A regulates tumor growth and progression in ovarian cancer through the WNT/β-catenin pathway. Molecular Cancer Research, 10(3), 469-482. 25084196

Gene ontology having evidence of Inferred from Direct Assay (IDA) from Entrez
GO IDGO TermPubMed ID


Top
Ligand binding site mutations for MMP7
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
G171G171EGBM1
T175T175MGBM1
Y210Y210CLUAD1
Y167P168SSKCM1
D165D165NSKCM1
G187G187ESKCM1
W198,E196R197LSTAD1
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 MMP7
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
G187G187E0.20122621
T175T175M0.002958772
E196R197L-1.5445244
W198R197L-1.5445244
Y167P168S-1.0768526
G171G171E-0.81689822
D165D165N-0.73246761
Y210Y210C-0.65172307
(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 MMP7 from PDB

Top
Differential gene expression and gene-gene network for MMP7
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 MMP7 and the right PPI network was created from samples without mutations in the LBS of MMP7. 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 MMP7
Gene level disease information (DisGeNet)
Disease IDDisease name# PubMedAssociation type
umls:C0009375Colonic Neoplasms4AlteredExpression, Biomarker
umls:C0000786Abortion, Spontaneous1Biomarker

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

Top
Pharmacological information for MMP7
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
Approved|investigationalDB00786MarimastatSmall molecule
ExperimentalDB08170(1R)-N,6-DIHYDROXY-7-METHOXY-2-[(4-METHOXYPHENYL)SULFONYL]-1,2,3,4-TETRAHYDROISOQUINOLINE-1-CARBOXAMIDESmall molecule
ExperimentalDB08489N4-HYDROXY-2-ISOBUTYL-N1-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.013,18]NONADECA-12(19),13,15,17-TETRAEN-10-YL)-SUCCINAMIDESmall molecule
ExperimentalDB084935-METHYL-3-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.013,18]NONADECA-12(19),13,15,17-TETRAEN-10-YLCARBAMOYL)-HEXANOIC ACIDSmall molecule

Gene-centered ligand-gene interaction network

Ligands binding to mutated ligand binding site of MMP7 go to BioLip
Ligand IDLigand short nameLigand long namePDB IDPDB namemutLBS


Top
Conservation information for LBS of MMP7
Multiple alignments for P09237 in multiple species
LBSAA sequence# speciesSpecies
A152-VWGTADIMIG1Homo sapiens
A152-SWGTADIIIG1Rattus norvegicus
A152DDFTTADLKIG1Arabidopsis thaliana
A177PGNTLAHAFAP1Homo sapiens
A177PGNTLGHAFAP1Rattus norvegicus
A177VLGTLAHAFAP1Arabidopsis thaliana
A179NTLAHAFAPGT1Homo sapiens
A179NTLGHAFAPGP1Rattus norvegicus
A179GTLAHAFAPE-1Arabidopsis thaliana
A211INFLYAATHEL1Homo sapiens
A211VNFLFVATHEL1Rattus norvegicus
A211VDLESVATHEI1Arabidopsis thaliana
C87MQKPRCGVPD-2Homo sapiens, Rattus norvegicus
C87MSLPRCGVSDT1Arabidopsis thaliana
D153VWGTADIMIGF1Homo sapiens
D153SWGTADIIIGF1Rattus norvegicus
D153DFTTADLKIGF1Arabidopsis thaliana
D165RGAHGDSYPFD1Homo sapiens
D165RGDHGDNFPFD1Rattus norvegicus
D165AGDHGDGLPFD1Arabidopsis thaliana
D170DSYPFDGPGNT1Homo sapiens
D170DNFPFDGPGNT1Rattus norvegicus
D170DGLPFDGVLGT1Arabidopsis thaliana
D189TGLGGDAHFDE1Homo sapiens
D189PGLGGDAHFDK1Rattus norvegicus
D189---NGRLHLDA1Arabidopsis thaliana
D193GDAHFDEDERW1Homo sapiens
D193GDAHFDKDEYW1Rattus norvegicus
D193GRLHLDAAETW1Arabidopsis thaliana
E196HFDEDERWTDG1Homo sapiens
E196HFDKDEYWTDG1Rattus norvegicus
E196HLDAAETWIVD1Arabidopsis thaliana
E215YAATHELGHSL1Homo sapiens
E215FVATHELGHSL1Rattus norvegicus
E215SVATHEIGHLL1Arabidopsis thaliana
F180TLAHAFAPGTG1Homo sapiens
F180TLGHAFAPGPG1Rattus norvegicus
F180TLAHAFAPE--1Arabidopsis thaliana
F244GDPQNFKLSQD1Homo sapiens
F244DHSEDFSLTKD1Rattus norvegicus
F244PRTKKVDLTVD1Arabidopsis thaliana
F98AEYSLFPNSPK1Homo sapiens
F98AEFSLMPNSPK1Rattus norvegicus
F98AHYTYFNGKPK1Arabidopsis thaliana
G171SYPFDGPGNTL1Homo sapiens
G171NFPFDGPGNTL1Rattus norvegicus
G171GLPFDGVLGTL1Arabidopsis thaliana
G173PFDGPGNTLAH1Homo sapiens
G173PFDGPGNTLGH1Rattus norvegicus
G173PFDGVLGTLAH1Arabidopsis thaliana
G185FAPGTGLGGDA1Homo sapiens
G185FAPGPGLGGDA1Rattus norvegicus
G185FAPE---NGRL1Arabidopsis thaliana
G187PGTGLGGDAHF1Homo sapiens
G187PGPGLGGDAHF1Rattus norvegicus
G187PE---NGRLHL1Arabidopsis thaliana
G188GTGLGGDAHFD1Homo sapiens
G188GPGLGGDAHFD1Rattus norvegicus
G188E---NGRLHLD1Arabidopsis thaliana
H163FARGAHGDSYP1Homo sapiens
H163FARGDHGDNFP1Rattus norvegicus
H163FYAGDHGDGLP1Arabidopsis thaliana
H178GNTLAHAFAPG1Homo sapiens
H178GNTLGHAFAPG1Rattus norvegicus
H178LGTLAHAFAPE1Arabidopsis thaliana
H191LGGDAHFDEDE1Homo sapiens
H191LGGDAHFDKDE1Rattus norvegicus
H191-NGRLHLDAAE1Arabidopsis thaliana
H214LYAATHELGHS1Homo sapiens
H214LFVATHELGHS1Rattus norvegicus
H214ESVATHEIGHL1Arabidopsis thaliana
H218THELGHSLGMG1Homo sapiens
H218THELGHSLGLG1Rattus norvegicus
H218THEIGHLLGLG1Arabidopsis thaliana
H224SLGMGHSSDPN1Homo sapiens
H224SLGLGHSSVPS1Rattus norvegicus
H224LLGLGHSSQES1Arabidopsis thaliana
I206----GINFLYA1Homo sapiens
I206----GVNFLFV1Rattus norvegicus
I206SSEVAVDLESV1Arabidopsis thaliana
L176GPGNTLAHAFA1Homo sapiens
L176GPGNTLGHAFA1Rattus norvegicus
L176GVLGTLAHAFA1Arabidopsis thaliana
L186APGTGLGGDAH1Homo sapiens
L186APGPGLGGDAH1Rattus norvegicus
L186APE---NGRLH1Arabidopsis thaliana
N174FDGPGNTLAHA1Homo sapiens
N174FDGPGNTLGHA1Rattus norvegicus
N174FDGVLGTLAHA1Arabidopsis thaliana
N207---GINFLYAA1Homo sapiens
N207---GVNFLFVA1Rattus norvegicus
N207SEVAVDLESVA1Arabidopsis thaliana
P172YPFDGPGNTLA1Homo sapiens
P172FPFDGPGNTLG1Rattus norvegicus
P172LPFDGVLGTLA1Arabidopsis thaliana
P234NAVMYPTYGNG1Homo sapiens
P234SSVMYPTYQGD1Rattus norvegicus
P234SAVMYPSLR-P1Arabidopsis thaliana
T175DGPGNTLAHAF1Homo sapiens
T175DGPGNTLGHAF1Rattus norvegicus
T175DGVLGTLAHAF1Arabidopsis thaliana
T235AVMYPTYGNGD1Homo sapiens
T235SVMYPTYQGDH1Rattus norvegicus
T235AVMYPSLR-PR1Arabidopsis thaliana
V231SDPNAVMYPTY1Homo sapiens
V231SVPSSVMYPTY1Rattus norvegicus
V231SQESAVMYPSL1Arabidopsis thaliana
W198DEDERWTDGSS1Homo sapiens
W198DKDEYWTDGED1Rattus norvegicus
W198DAAETWIVDDD1Arabidopsis thaliana
Y167AHGDSYPFDGP1Homo sapiens
Y167DHGDNFPFDGP1Rattus norvegicus
Y167DHGDGLPFDGV1Arabidopsis thaliana
Y210GINFLYAATHE1Homo sapiens
Y210GVNFLFVATHE1Rattus norvegicus
Y210AVDLESVATHE1Arabidopsis thaliana
Y236VMYPTYGNGDP1Homo sapiens
Y236VMYPTYQGDHS1Rattus norvegicus
Y236VMYPSLR-PRT1Arabidopsis thaliana


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