Human Gene LYPLA2 (ENST00000374514.8_4) from GENCODE V47lift37
  Description: lysophospholipase 2 (from RefSeq NM_007260.3)
Gencode Transcript: ENST00000374514.8_4
Gencode Gene: ENSG00000011009.12_9
Transcript (Including UTRs)
   Position: hg19 chr1:24,117,635-24,122,029 Size: 4,395 Total Exon Count: 10 Strand: +
Coding Region
   Position: hg19 chr1:24,119,173-24,121,222 Size: 2,050 Coding Exon Count: 9 

Page IndexSequence and LinksUniProtKB CommentsPrimersCTDGene Alleles
RNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther SpeciesGO Annotations
mRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr1:24,117,635-24,122,029)mRNA (may differ from genome)Protein (231 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
AlphaFoldBioGPSEnsemblEntrez GeneExonPrimerGeneCards
HGNCMGIOMIMPubMedReactomeUniProtKB
BioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: LYPA2_HUMAN
DESCRIPTION: RecName: Full=Acyl-protein thioesterase 2; Short=APT-2; EC=3.1.2.-; AltName: Full=Lysophospholipase II; Short=LPL-II; Short=LysoPLA II;
FUNCTION: May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity (By similarity). Deacylates GAP43.
CATALYTIC ACTIVITY: Palmitoyl-protein + H(2)O = palmitate + protein.
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the AB hydrolase 2 family.
SEQUENCE CAUTION: Sequence=AAP97210.1; Type=Frameshift; Positions=5, 164, 179;

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 42.37 RPKM in Kidney - Cortex
Total median expression: 1039.21 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -54.20132-0.411 Picture PostScript Text
3' UTR -353.00807-0.437 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR003140 - PLipase/COase/thioEstase

Pfam Domains:
PF01738 - Dienelactone hydrolase family
PF02230 - Phospholipase/Carboxylesterase
PF12697 - Alpha/beta hydrolase family

SCOP Domains:
53474 - alpha/beta-Hydrolases

ModBase Predicted Comparative 3D Structure on O95372
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The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologNo orthologGenome Browser
Gene DetailsGene Details Gene Details Gene Details
Gene SorterGene Sorter Gene Sorter Gene Sorter
 RGDEnsembl  SGD
     Protein Sequence
     Alignment

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0008474 palmitoyl-(protein) hydrolase activity
GO:0016787 hydrolase activity
GO:0045296 cadherin binding
GO:0052689 carboxylic ester hydrolase activity

Biological Process:
GO:0002084 protein depalmitoylation
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0007411 axon guidance

Cellular Component:
GO:0005737 cytoplasm
GO:0005795 Golgi stack
GO:0005829 cytosol
GO:0070062 extracellular exosome


-  Descriptions from all associated GenBank mRNAs
  AF098668 - Homo sapiens acyl-protein thioesterase mRNA, complete cds.
HM005316 - Homo sapiens clone HTL-T-3 testicular tissue protein Li 3 mRNA, complete cds.
BC017034 - Homo sapiens lysophospholipase II, mRNA (cDNA clone MGC:9106 IMAGE:3845764), complete cds.
JD493963 - Sequence 474987 from Patent EP1572962.
BC017193 - Homo sapiens lysophospholipase II, mRNA (cDNA clone MGC:1904 IMAGE:3138786), complete cds.
AF090423 - Homo sapiens lysophospholipase LPL-I mRNA, complete cds.
JD191057 - Sequence 172081 from Patent EP1572962.
DQ896824 - Synthetic construct Homo sapiens clone IMAGE:100011284; FLH177210.01L; RZPDo839E08123D lysophospholipase II (LYPLA2) gene, encodes complete protein.
EU176281 - Synthetic construct Homo sapiens clone IMAGE:100006389; FLH177216.01X; RZPDo839F12250D lysophospholipase II (LYPLA2) gene, encodes complete protein.
AK024724 - Homo sapiens cDNA: FLJ21071 fis, clone CAS01789, highly similar to AF098668 Homo sapiens acyl-protein thioesterase mRNA.
JD258525 - Sequence 239549 from Patent EP1572962.
JD535997 - Sequence 517021 from Patent EP1572962.
JD335963 - Sequence 316987 from Patent EP1572962.
JD252960 - Sequence 233984 from Patent EP1572962.
JD400619 - Sequence 381643 from Patent EP1572962.
JD217858 - Sequence 198882 from Patent EP1572962.
JD191275 - Sequence 172299 from Patent EP1572962.
JD216607 - Sequence 197631 from Patent EP1572962.
JD397430 - Sequence 378454 from Patent EP1572962.
JD191583 - Sequence 172607 from Patent EP1572962.
JD144863 - Sequence 125887 from Patent EP1572962.
JD283784 - Sequence 264808 from Patent EP1572962.
JD460059 - Sequence 441083 from Patent EP1572962.
JD460060 - Sequence 441084 from Patent EP1572962.
JD071661 - Sequence 52685 from Patent EP1572962.
JD249382 - Sequence 230406 from Patent EP1572962.
JD219600 - Sequence 200624 from Patent EP1572962.
JD467378 - Sequence 448402 from Patent EP1572962.
JD416826 - Sequence 397850 from Patent EP1572962.
JD226748 - Sequence 207772 from Patent EP1572962.
JD425531 - Sequence 406555 from Patent EP1572962.
JD297625 - Sequence 278649 from Patent EP1572962.
JD466430 - Sequence 447454 from Patent EP1572962.
JD216764 - Sequence 197788 from Patent EP1572962.
JD181527 - Sequence 162551 from Patent EP1572962.
JD348743 - Sequence 329767 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein O95372 (Reactome details) participates in the following event(s):

R-HSA-8933328 LYPLA2 hydrolyses PALM-C3,4-GAP43
R-HSA-373760 L1CAM interactions
R-HSA-422475 Axon guidance
R-HSA-1266738 Developmental Biology

-  Other Names for This Gene
  Alternate Gene Symbols: APT2, ENST00000374514.1, ENST00000374514.2, ENST00000374514.3, ENST00000374514.4, ENST00000374514.5, ENST00000374514.6, ENST00000374514.7, LYPA2_HUMAN, NM_007260, O95372, Q7Z4Z2, uc318lql.1, uc318lql.2
UCSC ID: ENST00000374514.8_4
RefSeq Accession: NM_007260.3
Protein: O95372 (aka LYPA2_HUMAN or LYA2_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.