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LPAR1 (lysophosphatidic acid receptor 1)

Written2009-04Mandi M Murph, Harish Radhakrishna
University of Georgia College of Pharmacy, Department of Pharmaceutical, Biomedical Sciences, 250 W Green Street, Rm 376 Athens, Georgia 30602 USA (MMM); Global Research & Technology, The Coca-Cola Company, 1 Coca-Cola Plaza Atlanta, GA 30313 USA (HR)

(Note : for Links provided by Atlas : click)

Identity

Alias_namesEDG2
endothelial differentiation
Alias_symbol (synonym)edg-2
rec.1.3
vzg-1
Gpcr26
Mrec1.3
LPA1
GPR26
Other aliasLPA-1
VZG1
HGNC (Hugo) LPAR1
LocusID (NCBI) 1902
Atlas_Id 40405
Location 9q31.3  [Link to chromosome band 9q31]
Location_base_pair Starts at 110873774 and ends at 111038085 bp from pter ( according to hg19-Feb_2009)  [Mapping LPAR1.png]
Fusion genes
(updated 2016)
ADAMTS17 (15q26.3) / LPAR1 (9q31.3)NAA15 (4q31.1) / LPAR1 (9q31.3)NDRG1 (8q24.22) / LPAR1 (9q31.3)
SNX30 (9q32) / LPAR1 (9q31.3)

DNA/RNA

Note mRNA length 3104 or 3182 bp, depending on alternative splicing.
 

Protein

 
  Figure of the LPAR1, a G protein-coupled receptor, spanning the plasma membrane seven times. The receptor has three numbered extracellular and intracellular loops that are involved in signal transduction. Also shown are the amino terminus and carboxyl terminal tail.
Three regions of the carboxyl terminal tail have been shown to be important for the LPAR1 signaling and receptor regulation. LPAR1 contains a canonical Type 1 PDZ binding domain (a.a. 362-364) at the extreme C-terminus. This domain has been shown to be required for LPA-induced cell proliferation and activation of Rho family GTPases via PDZ-Rho guanine nucleotide exchange factors. Further upstream in the carboxyl terminal tail, LPAR1 contains a di-leucine sequence (a.a. 351 and 352), which is required for phorbol ester-induced internalization. Still further upstream lies a serine-rich cluster (a.a. 341-347) that is required for beta-arrestin association, which is critical for signal attenuation and receptor endocytosis.
Description LPAR1 is an abbreviation for the LPA1 receptor, the first receptor cloned and identified from a growing number of LPA receptors that includes the Edg-family and the purinergic receptors.
Expression LPAR1 is ubiquitously expressed throughout cells and tissues in the body.
High level of expression is found in amygdale, prefrontal cortex, caudate nucleus, hypothalamus, medulla oblongata, olfactory bulb, parietal lobe, spinal cord and thalamus.
Moderately high level of expression is found in adipocytes, cingulated cortex, occipital lobe, pons, whole brain, globus pallidus, subthalamic nucleus, temporal lobe, appendix, monocytes and smooth muscle.
Slightly above median level of expression is found in bronchial epithelial cells, cerebellum peduncies, dorsal root ganglia, ciliary ganglion, uterus, uterus corpus, atrioventricular node, fetal lung, fetal thyroid, skeletal muscle, cardiac myocytes, salivary gland, tongue and lymph node.
It is also expressed in tissues during neuronal development.
The expression of LPAR1 is increased in blister skin compared to normal skin.
The mRNA of LPAR1 is significantly increased 8 days after unilateral uretheral obstruction in mice kidneys where expression is higher in the medulla than the cortex.
The expression of LPAR1 is variable in cancer.
Localisation It is a requirement of G protein-coupled receptor functioning that receptors are embedded into membranes for proper structure. The LPAR1 spans the plasma membrane seven times in a barrel conformation with three extracellular and three intracellular loops. At steady state, LPAR1 is located on the plasma membrane at the cell surface until it binds LPA, which triggers dynamin2-dependent, clathrin-mediated endocytosis into the cell. LPAR1 requires membrane cholesterol for association with beta-arrestin, which targets the receptor to clathrin-coated pits for internalization. In addition to LPA, phorbol ester stimulation of protein kinase C also induces internalization of LPAR1, but this does not require beta-arrestin. Rather, phorbol ester-dependent internalization of LPAR1 requires AP-2 clathrin adaptors. The LPAR1 is subsequently sorted through Rab-5 dependent early and recycling endosomes before it is recycled back to the cell surface or degraded in lysosomes.
The receptor may also be localized to the nuclear membrane in the cell. Some evidence indicates that a portion of the total cellular LPAR1 localizes to the nuclear membrane in PC12 cells, micro-vascular endothelial cells, and human bronchial epithelial cells. The exact function of this nuclear LPAR1 pool is not known.
Function The LPAR1 binds LPA and initiates G protein-dependent signal transduction cascades throughout the cell that result in a number of functional outcomes, depending on the specific cell or tissue type. The G alpha proteins involved are Gi, Gq and G 12/13.
The receptor has critical functions that have been elucidated through gene knock-out studies in mice. LPAR1-null mice have deficiencies in olfactory development that impairs their ability to locate maternal nipples and initiate suckling required for survival. The lack of olfactant detection leads to 50% lethality among pups. Other LPAR1-null mice demonstrate alterations in neurotransmitters that mimic models of schizophrenia. LPAR1-null mice are 10-15% shorter than wild-type mice and have gross anatomical defects due to bone development, including incisor overgrowth that affects ability to feed.
The LPAR1 functions in normal cortical development and commits cortical neuroblasts to differentiate through the neural lineage. It may also play a role in the formation of dendritic spine synapses.
Through autotoxin-generated LPA, LPAR1 mediates neuropathic pain induced by nerve injury.
Activation of the LPAR1 functions in the inflammatory response; receptor activation stimulates the recruitment of macrophages.
The LPAR1 positively regulates motility in a variety of cell types, exerting a dominant signal in the absence of LPAR4.
Homology The LPAR1 has significant homology with LPAR2 (57%) and LPAR3 (51%), members of the original or classical endothelial differentiation gene (Edg) family. It has approximately 33-38% homology with individual sphingosine 1-phosphate receptors and no significant homology with the purinergic family of receptors that also bind LPA.

Mutations

Note There are several single nucleotide polymorphisms (SNPs) reported within the LPAR1 gene and several of these are associated with altered phenotype and disease states.
A functional SNP located in the promoter region of the gene (-2,820G/A; rs10980705) is associated with increased susceptibility to knee osteoarthritis in Japanese by showing an increase in binding and activity.
A change in amino acid sequence at position 125 from glutamine to glutamate in the LPAR1 will result in the ability of the receptor to recognize both S1P and LPA.
A change in amino acid sequence at position 236 from threonine to lysine in the LPAR1 will result in the enhanced activation of serum response factor.
Mutations in the LPAR1 were detected in a small percentage of adenomas and adenocarcinomas of rats given BHP in their drinking water. Missense mutations in the LPAR1 were detected in rat hepatocellular carcinomas induced by N-nitrosodiethylamine and choline-deficient l-amino acid-defined diets.
Deletion of the PDZ domain of the receptor prevents signal attenuation that controls LPA-mediated receptor activation and cell proliferation.

Implicated in

Note
  
Entity Various cancers
Note Overexpression of the LPAR1 in mice contributes to the tumorigenicity and aggressiveness of ovarian cancer.
Prognosis Upregulation of the LPAR1 appears to enhance tumor progression in the previous examples.
Oncogenesis The LPAR1 is a proto-oncogene contributing to the metastatic potential of breast cancers and may require signals from ErbB2/HER2 dimerization. In a study designed to assess the functional consequences of overexpression as it relates to breast carcinogenesis, 1000 selected/suspected cDNAs were inserted into immortalized MCF-10A cells and a derivative cell line, MCF-10A.B2 expressing an inducibly active variant of ErbB2. The study examined three assays (cell proliferation, migration and 3-D matrigel acinar morphogenesis) and the LPAR1 scored positive in all three; thus, it was determined to be a proto-oncogene in this disease. Several observations are of interest: first, the LPAR1 induced migration in the absence of ErbB2 activation but not in the absence of dimerization which suggests that the LPAR1 may require weak signals from ligand-independent dimerization of ErbB2 to induce migration; second, in the acinar morphogenesis assay, phenotypical changes of cells with the LPAR1 included the formation of features of invasive tumor cells, such as disorganized acinar structure, large structures and protrusive behavior; third, the LPAR1 was capable of establishing abnormal 3-D morphogenesis in the absence of conditions to dimerize ErbB2.
  
  
Entity Lung injury
Note The LPAR1 mediates fibroblast migration and recruitment in the injured lung. The chemotactic activity of fibroblasts is dependent on LPAR1 expression.
Disease Pulmonary fibrosis
The concentration of LPA is elevated in bronchoalveolar lavage samples from patients with idiopathic pulmonary fibrosis. The fibroblasts of these patients require expression of LPAR1 for the chemotactic activity present in this pathology. Data suggests that LPAR1-null mice are substantially protected from fibroblast accumulation. This corresponds to lung injury where aberrant wound-healing responses exacerbate pulmonary fibrosis pathogenesis.
Prognosis LPAR1 links lung injury with pulmonary fibrosis development.
  

Bibliography

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Requirement for the lpA1 lysophosphatidic acid receptor gene in normal suckling behavior.
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Absence of LPA1 signaling results in defective cortical development.
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Lysophosphatidic acid stimulates neuronal differentiation of cortical neuroblasts through the LPA1-G(i/o) pathway.
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LPA1 receptor-deficient mice have phenotypic changes observed in psychiatric disease.
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PMID 14697676
 
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Mol Biol Cell. 2008 Dec;19(12):5435-45. Epub 2008 Oct 8.
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A functional SNP in EDG2 increases susceptibility to knee osteoarthritis in Japanese.
Mototani H, Iida A, Nakajima M, Furuichi T, Miyamoto Y, Tsunoda T, Sudo A, Kotani A, Uchida A, Ozaki K, Tanaka Y, Nakamura Y, Tanaka T, Notoya K, Ikegawa S.
Hum Mol Genet. 2008 Jun 15;17(12):1790-7. Epub 2008 Mar 6.
PMID 18325907
 
Identification of the orphan GPCR, P2Y(10) receptor as the sphingosine-1-phosphate and lysophosphatidic acid receptor.
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Biochem Biophys Res Commun. 2008 Jul 11;371(4):707-12. Epub 2008 May 6.
PMID 18466763
 
Lysophosphatidic acid decreases the nuclear localization and cellular abundance of the p53 tumor suppressor in A549 lung carcinoma cells. Murph MM, Hurst-Kennedy J, Newton V, Brindley DN, Radhakrishna H.
Mol Cancer Res. 2007 Nov;5(11):1201-11.
PMID 18025263
 
Sharpening the edges of understanding the structure/function of the LPA1 receptor: expression in cancer and mechanisms of regulation.
Murph MM, Nguyen GH, Radhakrishna H, Mills GB.
Biochim Biophys Acta. 2008 Sep;1781(9):547-57. Epub 2008 Apr 29. (REVIEW)
PMID 18501205
 
Agonist-induced endocytosis of lysophosphatidic acid-coupled LPA1/EDG-2 receptors via a dynamin2- and Rab5-dependent pathway.
Murph MM, Scaccia LA, Volpicelli LA, Radhakrishna H.
J Cell Sci. 2003 May 15;116(Pt 10):1969-80. Epub 2003 Mar 26.
PMID 12668728
 
Frequent mutations of lysophosphatidic acid receptor-1 gene in rat liver tumors.
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Mutat Res. 2009 Jan 15;660(1-2):47-50. Epub 2008 Oct 21.
PMID 19000703
 
The role of LPA1 in formation of synapses among cultured hippocampal neurons.
Pilpel Y, Segal M.
J Neurochem. 2006 Jun;97(5):1379-92. Epub 2006 Apr 21.
PMID 16638019
 
Lysophosphatidic acid and renal fibrosis.
Pradere JP, Gonzalez J, Klein J, Valet P, Gres S, Salant D, Bascands JL, Saulnier-Blache JS, Schanstra JP.
Biochim Biophys Acta. 2008 Sep;1781(9):582-7. Epub 2008 Apr 11. (REVIEW)
PMID 18455518
 
Neurochemical changes in LPA1 receptor deficient mice--a putative model of schizophrenia.
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Neurochem Res. 2005 Mar;30(3):371-7.
PMID 16018581
 
Different mechanisms regulate lysophosphatidic acid (LPA)-dependent versus phorbol ester-dependent internalization of the LPA1 receptor.
Urs NM, Kowalczyk AP, Radhakrishna H.
J Biol Chem. 2008 Feb 29;283(9):5249-57. Epub 2007 Dec 18.
PMID 18089565
 
A single amino acid determines lysophospholipid specificity of the S1P1 (EDG1) and LPA1 (EDG2) phospholipid growth factor receptors.
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PMID 11604399
 
Integrin signalling regulates the nuclear localization and function of the lysophosphatidic acid receptor-1 (LPA1) in mammalian cells.
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Functional proteomics approach to investigate the biological activities of cDNAs implicated in breast cancer.
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Mutations of lysophosphatidic acid receptor-1 gene during progression of lung tumors in rats.
Yamada T, Obo Y, Furukawa M, Hotta M, Yamasaki A, Honoki K, Fukushima N, Tsujiuchi T.
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PMID 19026987
 
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PMID 15755723
 
Lysophosphatidic acid receptors determine tumorigenicity and aggressiveness of ovarian cancer cells.
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Citation

This paper should be referenced as such :
Murph, MM ; Radhakrishna, H
LPAR1 (lysophosphatidic acid receptor 1)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(3):289-292.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/LPAR1ID40405ch9q31.html


External links

Nomenclature
HGNC (Hugo)LPAR1   3166
Cards
AtlasLPAR1ID40405ch9q31
Entrez_Gene (NCBI)LPAR1  1902  lysophosphatidic acid receptor 1
AliasesEDG2; GPR26; Gpcr26; LPA1; 
Mrec1.3; VZG1; edg-2; rec.1.3; vzg-1
GeneCards (Weizmann)LPAR1
Ensembl hg19 (Hinxton)ENSG00000198121 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000198121 [Gene_View]  chr9:110873774-111038085 [Contig_View]  LPAR1 [Vega]
ICGC DataPortalENSG00000198121
TCGA cBioPortalLPAR1
AceView (NCBI)LPAR1
Genatlas (Paris)LPAR1
WikiGenes1902
SOURCE (Princeton)LPAR1
Genetics Home Reference (NIH)LPAR1
Genomic and cartography
GoldenPath hg38 (UCSC)LPAR1  -     chr9:110873774-111038085 -  9q31.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)LPAR1  -     9q31.3   [Description]    (hg19-Feb_2009)
EnsemblLPAR1 - 9q31.3 [CytoView hg19]  LPAR1 - 9q31.3 [CytoView hg38]
Mapping of homologs : NCBILPAR1 [Mapview hg19]  LPAR1 [Mapview hg38]
OMIM602282   
Gene and transcription
Genbank (Entrez)AK022808 AK290287 AK296374 AK298590 AK299279
RefSeq transcript (Entrez)NM_001401 NM_057159
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)LPAR1
Cluster EST : UnigeneHs.126667 [ NCBI ]
CGAP (NCI)Hs.126667
Alternative Splicing GalleryENSG00000198121
Gene ExpressionLPAR1 [ NCBI-GEO ]   LPAR1 [ EBI - ARRAY_EXPRESS ]   LPAR1 [ SEEK ]   LPAR1 [ MEM ]
Gene Expression Viewer (FireBrowse)LPAR1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1902
GTEX Portal (Tissue expression)LPAR1
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ92633   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ92633  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ92633
Splice isoforms : SwissVarQ92633
PhosPhoSitePlusQ92633
Domaine pattern : Prosite (Expaxy)G_PROTEIN_RECEP_F1_1 (PS00237)    G_PROTEIN_RECEP_F1_2 (PS50262)   
Domains : Interpro (EBI)GPCR_Rhodpsn    GPCR_Rhodpsn_7TM    LPA_rcpt    LPA_rcpt_EDG2   
Domain families : Pfam (Sanger)7tm_1 (PF00001)   
Domain families : Pfam (NCBI)pfam00001   
Domain families : Smart (EMBL)7TM_GPCR_Srsx (SM01381)  
Conserved Domain (NCBI)LPAR1
DMDM Disease mutations1902
Blocks (Seattle)LPAR1
PDB (SRS)4Z34    4Z35    4Z36   
PDB (PDBSum)4Z34    4Z35    4Z36   
PDB (IMB)4Z34    4Z35    4Z36   
PDB (RSDB)4Z34    4Z35    4Z36   
Structural Biology KnowledgeBase4Z34    4Z35    4Z36   
SCOP (Structural Classification of Proteins)4Z34    4Z35    4Z36   
CATH (Classification of proteins structures)4Z34    4Z35    4Z36   
SuperfamilyQ92633
Human Protein AtlasENSG00000198121
Peptide AtlasQ92633
HPRD03790
IPIIPI01010769   IPI00022525   IPI01013061   IPI01009783   IPI00646631   
Protein Interaction databases
DIP (DOE-UCLA)Q92633
IntAct (EBI)Q92633
FunCoupENSG00000198121
BioGRIDLPAR1
STRING (EMBL)LPAR1
ZODIACLPAR1
Ontologies - Pathways
QuickGOQ92633
Ontology : AmiGOactivation of MAPK activity  G-protein alpha-subunit binding  G-protein coupled receptor activity  protein binding  endosome  plasma membrane  plasma membrane  integral component of plasma membrane  G-protein coupled receptor signaling pathway  adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway  activation of phospholipase C activity  positive regulation of cytosolic calcium ion concentration  regulation of cell shape  cell surface  negative regulation of neuron projection development  oligodendrocyte development  cerebellum development  optic nerve development  corpus callosum development  endocytic vesicle  PDZ domain binding  negative regulation of cAMP biosynthetic process  bleb assembly  positive regulation of Rho protein signal transduction  lysophosphatidic acid binding  myelination  neuronal cell body  positive regulation of apoptotic process  positive regulation of I-kappaB kinase/NF-kappaB signaling  dendritic spine  dendritic shaft  positive regulation of MAPK cascade  positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway  positive regulation of stress fiber assembly  cell chemotaxis  positive regulation of dendritic spine development  lysophosphatidic acid receptor activity  lysophosphatidic acid receptor activity  cellular response to oxygen levels  positive regulation of smooth muscle cell chemotaxis  cellular response to 1-oleoyl-sn-glycerol 3-phosphate  
Ontology : EGO-EBIactivation of MAPK activity  G-protein alpha-subunit binding  G-protein coupled receptor activity  protein binding  endosome  plasma membrane  plasma membrane  integral component of plasma membrane  G-protein coupled receptor signaling pathway  adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway  activation of phospholipase C activity  positive regulation of cytosolic calcium ion concentration  regulation of cell shape  cell surface  negative regulation of neuron projection development  oligodendrocyte development  cerebellum development  optic nerve development  corpus callosum development  endocytic vesicle  PDZ domain binding  negative regulation of cAMP biosynthetic process  bleb assembly  positive regulation of Rho protein signal transduction  lysophosphatidic acid binding  myelination  neuronal cell body  positive regulation of apoptotic process  positive regulation of I-kappaB kinase/NF-kappaB signaling  dendritic spine  dendritic shaft  positive regulation of MAPK cascade  positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway  positive regulation of stress fiber assembly  cell chemotaxis  positive regulation of dendritic spine development  lysophosphatidic acid receptor activity  lysophosphatidic acid receptor activity  cellular response to oxygen levels  positive regulation of smooth muscle cell chemotaxis  cellular response to 1-oleoyl-sn-glycerol 3-phosphate  
Pathways : BIOCARTARho-Selective Guanine Exchange Factor AKAP13 Mediates Stress Fiber Formation [Genes]   
Pathways : KEGGRap1 signaling pathway    Neuroactive ligand-receptor interaction    PI3K-Akt signaling pathway    Gap junction   
REACTOMEQ92633 [protein]
REACTOME PathwaysR-HSA-419408 [pathway]   
NDEx NetworkLPAR1
Atlas of Cancer Signalling NetworkLPAR1
Wikipedia pathwaysLPAR1
Orthology - Evolution
OrthoDB1902
GeneTree (enSembl)ENSG00000198121
Phylogenetic Trees/Animal Genes : TreeFamLPAR1
HOVERGENQ92633
HOGENOMQ92633
Homologs : HomoloGeneLPAR1
Homology/Alignments : Family Browser (UCSC)LPAR1
Gene fusions - Rearrangements
Fusion : MitelmanADAMTS17/LPAR1 [15q26.3/9q31.3]  [t(9;15)(q31;q26)]  
Fusion : MitelmanNAA15/LPAR1 [4q31.1/9q31.3]  [t(4;9)(q31;q31)]  
Fusion : MitelmanSNX30/LPAR1 [9q32/9q31.3]  [t(9;9)(q31;q32)]  
Fusion: TCGANAA15 4q31.1 LPAR1 9q31.3 GBM
Fusion: TCGASNX30 9q32 LPAR1 9q31.3 LGG
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerLPAR1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)LPAR1
dbVarLPAR1
ClinVarLPAR1
1000_GenomesLPAR1 
Exome Variant ServerLPAR1
ExAC (Exome Aggregation Consortium)LPAR1 (select the gene name)
Genetic variants : HAPMAP1902
Genomic Variants (DGV)LPAR1 [DGVbeta]
DECIPHERLPAR1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisLPAR1 
Mutations
ICGC Data PortalLPAR1 
TCGA Data PortalLPAR1 
Broad Tumor PortalLPAR1
OASIS PortalLPAR1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICLPAR1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDLPAR1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch LPAR1
DgiDB (Drug Gene Interaction Database)LPAR1
DoCM (Curated mutations)LPAR1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)LPAR1 (select a term)
intoGenLPAR1
NCG5 (London)LPAR1
Cancer3DLPAR1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602282   
Orphanet
MedgenLPAR1
Genetic Testing Registry LPAR1
NextProtQ92633 [Medical]
TSGene1902
GENETestsLPAR1
Target ValidationLPAR1
Huge Navigator LPAR1 [HugePedia]
snp3D : Map Gene to Disease1902
BioCentury BCIQLPAR1
ClinGenLPAR1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD1902
Chemical/Pharm GKB GenePA162394187
Clinical trialLPAR1
Miscellaneous
canSAR (ICR)LPAR1 (select the gene name)
Probes
Litterature
PubMed79 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineLPAR1
EVEXLPAR1
GoPubMedLPAR1
iHOPLPAR1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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