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 FGF1
Gene summary
Basic gene Info.Gene symbolFGF1
Gene namefibroblast growth factor 1 (acidic)
SynonymsAFGF|ECGF|ECGF-beta|ECGFA|ECGFB|FGF-1|FGF-alpha|FGFA|GLIO703|HBGF-1|HBGF1
CytomapUCSC genome browser: 5q31
Type of geneprotein-coding
RefGenesNM_000800.4,
NM_001144892.2,NM_001144934.1,NM_001144935.1,NM_001257205.1,
NM_001257206.1,NM_001257207.1,NM_001257208.1,NM_001257209.1,
NM_001257210.1,NM_001257211.1,NM_001257212.1,NM_033136.3,
NM_033137.2,
Descriptionbeta-endothelial cell growth factorendothelial cell growth factor, alphaendothelial cell growth factor, betafibroblast growth factor 1heparin-binding growth factor 1
Modification date20141207
dbXrefs MIM : 131220
HGNC : HGNC
Ensembl : ENSG00000113578
HPRD : 00567
Vega : OTTHUMG00000059703
ProteinUniProt: P05230
go to UniProt's Cross Reference DB Table
ExpressionCleanEX: HS_FGF1
BioGPS: 2246
PathwayNCI Pathway Interaction Database: FGF1
KEGG: FGF1
REACTOME: FGF1
Pathway Commons: FGF1
ContextiHOP: FGF1
ligand binding site mutation search in PubMed: FGF1
UCL Cancer Institute: FGF1
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:0008543fibroblast growth factor receptor signaling pathway20145243
GO:0030335positive regulation of cell migration20145243
GO:0034605cellular response to heat12746488
GO:0045542positive regulation of cholesterol biosynthetic process19229075
GO:0045766positive regulation of angiogenesis20145243
GO:0045944positive regulation of transcription from RNA polymerase II promoter19229075
GO:0051781positive regulation of cell division20145243
GO:0060681branch elongation involved in ureteric bud branching11731227
GO:0072163mesonephric epithelium development11731227
GO:1902533positive regulation of intracellular signal transduction19229075


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Ligand binding site mutations for FGF1
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
P149L148FBLCA1
L101F100LCOAD1
G34G35DCOAD1
Y109N110TCOAD1
R137R137WHNSC1
Y109T111PSTAD1
K27L29ISTAD1
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.


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Protein structure related information for FGF1
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
K27L29I-1.619585
Y109T111P-1.0755595
P149L148F-1.0239865
G34G35D-0.96350033
Y109N110T-0.86940262
L101F100L-0.62161943
R137R137W-0.072217329
(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 FGF1 from PDB

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Differential gene expression and gene-gene network for FGF1
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 FGF1 and the right PPI network was created from samples without mutations in the LBS of FGF1. 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 FGF1
Gene level disease information (DisGeNet)
Disease IDDisease name# PubMedAssociation type
umls:C0023418Leukemia2Biomarker
umls:C0025500Mesothelioma2Biomarker
umls:C0151744Myocardial Ischemia2Biomarker
umls:C0034069Pulmonary Fibrosis2Biomarker
umls:C0020649Hypotension1Biomarker
umls:C0043094Weight Gain1Biomarker

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

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Pharmacological information for FGF1
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
ApprovedDB00686Pentosan PolysulfateSmall molecule
Approved|investigationalDB01025AmlexanoxSmall molecule
ExperimentalDB01901SucrosofateSmall molecule
ExperimentalDB01942Formic AcidSmall molecule
ExperimentalDB02264O2-Sulfo-Glucuronic AcidSmall molecule
ExperimentalDB03959N,O6-Disulfo-GlucosamineSmall molecule
ExperimentalDB04409Naphthalene TrisulfonateSmall molecule
ApprovedDB06589PazopanibSmall molecule
ExperimentalDB082385-AMINO-NAPHTALENE-2-MONOSULFONATESmall molecule

Gene-centered ligand-gene interaction network

Ligands binding to mutated ligand binding site of FGF1 go to BioLip
Ligand IDLigand short nameLigand long namePDB IDPDB namemutLBS


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Conservation information for LBS of FGF1
Multiple alignments for P05230 in multiple species
LBSAA sequence# speciesSpecies
A118TSKKHAEKNWF2Mus musculus, Rattus norvegicus
A118ISKKHAEKNWF1Homo sapiens
A118ISKKHADKNWF1Gallus gallus
A118ISKKHAEKHWF1Bos taurus
A144HYGQKAILFLP4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
A144HFGQKAILFLP1Bos taurus
G125KNWFVGLKKNG4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
G125KHWFVGLKKNG1Bos taurus
G141PRTHYGQKAIL4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
G141PRTHFGQKAIL1Bos taurus
G21FNLPLGNYKKP3Bos taurus, Mus musculus, Rattus norvegicus
G21FNLPPGNYKKP1Homo sapiens
G21FGLPLGNYKKP1Gallus gallus
G34LYCSNGGHFLR4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
G34LYCSNGGYFLR1Bos taurus
H139RGPRTHYGQKA3Homo sapiens, Mus musculus, Rattus norvegicus
H139LGPRTHYGQKA1Gallus gallus
H139LGPRTHFGQKA1Bos taurus
I145YGQKAILFLPL4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
I145FGQKAILFLPL1Bos taurus
K120KKHAEKNWFVG3Homo sapiens, Mus musculus, Rattus norvegicus
K120KKHADKNWFVG1Gallus gallus
K120KKHAEKHWFVG1Bos taurus
K127WFVGLKKNGSC3Homo sapiens, Mus musculus, Rattus norvegicus
K127WFVGLKKNGNS1Gallus gallus
K127WFVGLKKNGRS1Bos taurus
K128FVGLKKNGSCK3Homo sapiens, Mus musculus, Rattus norvegicus
K128FVGLKKNGNSK1Gallus gallus
K128FVGLKKNGRSK1Bos taurus
K133KNGSCKRGPRT3Homo sapiens, Mus musculus, Rattus norvegicus
K133KNGNSKLGPRT1Gallus gallus
K133KNGRSKLGPRT1Bos taurus
K143THYGQKAILFL4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
K143THFGQKAILFL1Bos taurus
K27NYKKPKLLYCS5Homo sapiens, Gallus gallus, Bos taurus, Mus musculus, Rattus norvegicus
L101EECLFLERLEE5Homo sapiens, Gallus gallus, Bos taurus, Mus musculus, Rattus norvegicus
L146GQKAILFLPLP5Homo sapiens, Gallus gallus, Bos taurus, Mus musculus, Rattus norvegicus
L150ILFLPLPVSSD4Homo sapiens, Bos taurus, Mus musculus, Rattus norvegicus
L150ILFLPLPVSAD1Gallus gallus
N107ERLEENHYNTY5Homo sapiens, Gallus gallus, Bos taurus, Mus musculus, Rattus norvegicus
N129VGLKKNGSCKR3Homo sapiens, Mus musculus, Rattus norvegicus
N129VGLKKNGNSKL1Gallus gallus
N129VGLKKNGRSKL1Bos taurus
N33LLYCSNGGHFL4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
N33LLYCSNGGYFL1Bos taurus
P136SCKRGPRTHYG3Homo sapiens, Mus musculus, Rattus norvegicus
P136NSKLGPRTHYG1Gallus gallus
P136RSKLGPRTHFG1Bos taurus
P149AILFLPLPVSS4Homo sapiens, Bos taurus, Mus musculus, Rattus norvegicus
P149AILFLPLPVSA1Gallus gallus
P151LFLPLPVSSD4Homo sapiens, Bos taurus, Mus musculus, Rattus norvegicus
P151LFLPLPVSAD1Gallus gallus
Q142RTHYGQKAILF4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
Q142RTHFGQKAILF1Bos taurus
R134NGSCKRGPRTH3Homo sapiens, Mus musculus, Rattus norvegicus
R134NGNSKLGPRTH1Gallus gallus
R134NGRSKLGPRTH1Bos taurus
R137CKRGPRTHYGQ3Homo sapiens, Mus musculus, Rattus norvegicus
R137SKLGPRTHYGQ1Gallus gallus
R137SKLGPRTHFGQ1Bos taurus
S32KLLYCSNGGHF4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
S32KLLYCSNGGYF1Bos taurus
T138KRGPRTHYGQK3Homo sapiens, Mus musculus, Rattus norvegicus
T138KLGPRTHYGQK1Gallus gallus
T138KLGPRTHFGQK1Bos taurus
W122HAEKNWFVGLK3Homo sapiens, Mus musculus, Rattus norvegicus
W122HADKNWFVGLK1Gallus gallus
W122HAEKHWFVGLK1Bos taurus
Y109LEENHYNTYIS3Homo sapiens, Gallus gallus, Bos taurus
Y109LEENHYNTYTS2Mus musculus, Rattus norvegicus
Y140GPRTHYGQKAI4Homo sapiens, Gallus gallus, Mus musculus, Rattus norvegicus
Y140GPRTHFGQKAI1Bos taurus


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