mutLBSgeneDB |
Gene summary for LYN |
Gene summary |
Basic gene Info. | Gene symbol | LYN |
Gene name | LYN proto-oncogene, Src family tyrosine kinase | |
Synonyms | JTK8|p53Lyn|p56Lyn | |
Cytomap | UCSC genome browser: 8q13 | |
Type of gene | protein-coding | |
RefGenes | NM_001111097.2, NM_002350.3, | |
Description | lck/Yes-related novel protein tyrosine kinasetyrosine-protein kinase Lynv-yes-1 Yamaguchi sarcoma viral related oncogene homolog | |
Modification date | 20141207 | |
dbXrefs | MIM : 165120 | |
HGNC : HGNC | ||
Ensembl : ENSG00000254087 | ||
HPRD : 01301 | ||
Vega : OTTHUMG00000044345 | ||
Protein | UniProt: P07948 go to UniProt's Cross Reference DB Table | |
Expression | CleanEX: HS_LYN | |
BioGPS: 4067 | ||
Pathway | NCI Pathway Interaction Database: LYN | |
KEGG: LYN | ||
REACTOME: LYN | ||
Pathway Commons: LYN | ||
Context | iHOP: LYN | |
ligand binding site mutation search in PubMed: LYN | ||
UCL Cancer Institute: LYN | ||
Assigned class in mutLBSgeneDB | B: This gene belongs to targetable_mutLBSgenes. |
Gene ontology having evidence of Inferred from Direct Assay (IDA) from Entrez |
GO ID | GO Term | PubMed ID | GO:0006468 | protein phosphorylation | 11517336 | GO:0006974 | cellular response to DNA damage stimulus | 10891478 | GO:0018108 | peptidyl-tyrosine phosphorylation | 7682714 | GO:0046777 | protein autophosphorylation | 7682714 | GO:0051272 | positive regulation of cellular component movement | 16467205 | GO:0070304 | positive regulation of stress-activated protein kinase signaling cascade | 10891478 |
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Ligand binding site mutations for LYN |
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 |
LBS | AAchange of nsSNV | Cancer type | # samples | Y117 | A119V | COAD | 1 | Y117 | A119S | COAD | 1 | Y117 | A119V | GBM | 1 | K275 | L277P | LUAD | 1 | H96 | E95D | SKCM | 1 | A371 | R369G | STAD | 1 |
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 LYN |
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. |
LBS | AAchange of nsSNV | Relative stability change | H96 | E95D | -1.7647652 | K275 | L277P | -1.5354246 | A371 | R369G | -1.285713 | Y117 | A119S | -0.78755894 | Y117 | A119V | -0.39947273 |
(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 LYN from PDB |
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Differential gene expression and gene-gene network for LYN |
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) |
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Phenotype information for LYN |
Gene level disease information (DisGeNet) |
Disease ID | Disease name | # PubMed | Association type |
umls:C0019693 | HIV Infections | 2 | Biomarker, GeneticVariation |
Mutation level pathogenic information (ClinVar annotation) |
Allele ID | AA change | Clinical significance | Origin | Phenotype IDs |
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Pharmacological information for LYN |
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 status | DrugBank ID | Name | Type | Drug structure |
Experimental | DB03023 | 1-Tert-Butyl-3-(4-Chloro-Phenyl)-1h-Pyrazolo[3,4-D]Pyrimidin-4-Ylamine | Small molecule | |
Approved | DB06616 | Bosutinib | Small molecule | |
Approved | DB08901 | Ponatinib | Small molecule | |
Approved | DB09079 | Nintedanib | Small molecule |
Gene-centered ligand-gene interaction network |
Ligands binding to mutated ligand binding site of LYN go to BioLip |
Ligand ID | Ligand short name | Ligand long name | PDB ID | PDB name | mutLBS |
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Conservation information for LBS of LYN |
Multiple alignments for P07948 in multiple species |
LBS | AA sequence | # species | Species | A273 | NSTKVAVKTLK | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | A371 | RDLRAANVLVS | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | D75 | ALYPYDGIHPD | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | D80 | DGIHPDDLSFK | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | D81 | GIHPDDLSFKK | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | E320 | IYIITEFMAKG | 2 | Mus musculus, Rattus norvegicus | E320 | IYIITEYMAKG | 1 | Homo sapiens | E98 | LEEHGEWWKAK | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | F112 | SKREGFIPSNY | 2 | Mus musculus, Rattus norvegicus | F112 | TKKEGFIPSNY | 1 | Homo sapiens | G325 | EFMAKGSLLDF | 2 | Mus musculus, Rattus norvegicus | G325 | EYMAKGSLLDF | 1 | Homo sapiens | G97 | VLEEHGEWWKA | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | H78 | PYDGIHPDDLS | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | H96 | KVLEEHGEWWK | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | I77 | YPYDGIHPDDL | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | K275 | TKVAVKTLKPG | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | L253 | KLVKKLGAGQF | 2 | Mus musculus, Rattus norvegicus | L253 | KLVKRLGAGQF | 1 | Homo sapiens | L374 | RAANVLVSESL | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | M322 | IITEFMAKGSL | 2 | Mus musculus, Rattus norvegicus | M322 | IITEYMAKGSL | 1 | Homo sapiens | N116 | GFIPSNYVAKV | 2 | Mus musculus, Rattus norvegicus | N116 | GFIPSNYVAKL | 1 | Homo sapiens | P114 | REGFIPSNYVA | 2 | Mus musculus, Rattus norvegicus | P114 | KEGFIPSNYVA | 1 | Homo sapiens | P73 | VVALYPYDGIH | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | S115 | EGFIPSNYVAK | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | S326 | FMAKGSLLDFL | 2 | Mus musculus, Rattus norvegicus | S326 | YMAKGSLLDFL | 1 | Homo sapiens | T319 | PIYIITEFMAK | 2 | Mus musculus, Rattus norvegicus | T319 | PIYIITEYMAK | 1 | Homo sapiens | V261 | GQFGEVWMGYY | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | W100 | EHGEWWKAKSL | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | W99 | EEHGEWWKAKS | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | Y117 | FIPSNYVAKVN | 2 | Mus musculus, Rattus norvegicus | Y117 | FIPSNYVAKLN | 1 | Homo sapiens | Y321 | YIITEFMAKGS | 2 | Mus musculus, Rattus norvegicus | Y321 | YIITEYMAKGS | 1 | Homo sapiens | Y72 | IVVALYPYDGI | 3 | Homo sapiens, Mus musculus, Rattus norvegicus | Y74 | VALYPYDGIHP | 3 | Homo sapiens, Mus musculus, Rattus norvegicus |
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