Human Gene ERAP2 (ENST00000437043.8_8) from GENCODE V47lift37
  Description: endoplasmic reticulum aminopeptidase 2, transcript variant 1 (from RefSeq NM_022350.5)
Gencode Transcript: ENST00000437043.8_8
Gencode Gene: ENSG00000164308.18_15
Transcript (Including UTRs)
   Position: hg19 chr5:96,212,204-96,255,407 Size: 43,204 Total Exon Count: 19 Strand: +
Coding Region
   Position: hg19 chr5:96,215,390-96,253,309 Size: 37,920 Coding Exon Count: 18 

Page IndexSequence and LinksUniProtKB CommentsPrimersMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr5:96,212,204-96,255,407)mRNA (may differ from genome)Protein (960 aa)
Gene SorterGenome BrowserOther Species FASTAGene interactionsTable SchemaAlphaFold
BioGPSEnsemblEntrez GeneExonPrimerGeneCardsHGNC
MalacardsMGIOMIMPubMedReactomeUniProtKB
WikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: ERAP2_HUMAN
DESCRIPTION: RecName: Full=Endoplasmic reticulum aminopeptidase 2; EC=3.4.11.-; AltName: Full=Leukocyte-derived arginine aminopeptidase; Short=L-RAP;
FUNCTION: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Heterodimer with ERAP1.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein.
TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in spleen and leukocytes.
INDUCTION: By IFNG/IFN-gamma.
PTM: N-glycosylated.
MISCELLANEOUS: Defects in the expression of this gene may cause improper antigen processing, possibly leading to favor tumor escape from the immune surveillance.
SIMILARITY: Belongs to the peptidase M1 family.

-  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


-  MalaCards Disease Associations
  MalaCards Gene Search: ERAP2
Diseases sorted by gene-association score: spondylitis (16), birdshot chorioretinopathy (6)

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene

+  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: 15.45 RPKM in Cells - EBV-transformed lymphocytes
Total median expression: 162.82 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 -24.70150-0.165 Picture PostScript Text
3' UTR -532.102098-0.254 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
IPR024571 - DUF3358
IPR001930 - Peptidase_M1
IPR014782 - Peptidase_M1_N

Pfam Domains:
PF01433 - Peptidase family M1 domain
PF11838 - ERAP1-like C-terminal domain
PF17900 - Peptidase M1 N-terminal domain

SCOP Domains:
63737 - Leukotriene A4 hydrolase N-terminal domain
55486 - Metalloproteases ("zincins"), catalytic domain

Protein Data Bank (PDB) 3-D Structure
MuPIT help
3SE6 - X-ray MuPIT 4E36 - X-ray MuPIT


ModBase Predicted Comparative 3D Structure on Q6P179
FrontTopSide
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 orthologNo ortholog
Gene DetailsGene Details    
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-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0004175 endopeptidase activity
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0042277 peptide binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity

Biological Process:
GO:0002250 adaptive immune response
GO:0002376 immune system process
GO:0002474 antigen processing and presentation of peptide antigen via MHC class I
GO:0006508 proteolysis
GO:0007165 signal transduction
GO:0007267 cell-cell signaling
GO:0008217 regulation of blood pressure
GO:0019885 antigen processing and presentation of endogenous peptide antigen via MHC class I
GO:0043171 peptide catabolic process

Cellular Component:
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005789 endoplasmic reticulum membrane
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0016021 integral component of membrane


-  Descriptions from all associated GenBank mRNAs
  AK074281 - Homo sapiens cDNA FLJ23701 fis, clone HEP10760, highly similar to Homo sapiens aminopeptidase mRNA.
AK312864 - Homo sapiens cDNA, FLJ93308, highly similar to Homo sapiens leukocyte-derived arginine aminopeptidase (LRAP), mRNA.
AB109031 - Homo sapiens l-rap mRNA for leukocyte-derived arginine aminopeptidase long form variant, complete cds.
AB163917 - Homo sapiens l-rap mRNA for leukocyte-derived arginine aminopeptidase short form variant 2, complete cds.
BC065240 - Homo sapiens endoplasmic reticulum aminopeptidase 2, mRNA (cDNA clone MGC:74931 IMAGE:6166289), complete cds.
BC017927 - Homo sapiens endoplasmic reticulum aminopeptidase 2, mRNA (cDNA clone IMAGE:4337700), complete cds.
AF191545 - Homo sapiens aminopeptidase mRNA, complete cds.
AY028805 - Homo sapiens leukocyte-derived arginine aminopeptidase short form mRNA, complete cds, alternatively spliced.
JD411732 - Sequence 392756 from Patent EP1572962.
AB385154 - Synthetic construct DNA, clone: pF1KB5679, Homo sapiens ERAP2 gene for leukocyte-derived arginine aminopeptidase, complete cds, without stop codon, in Flexi system.
AK074387 - Homo sapiens cDNA FLJ23807 fis, clone HRC03762, highly similar to Homo sapiens aminopeptidase mRNA.
JD022941 - Sequence 3965 from Patent EP1572962.
JD029517 - Sequence 10541 from Patent EP1572962.
AK074213 - Homo sapiens cDNA FLJ23633 fis, clone CAS05313, highly similar to Homo sapiens aminopeptidase mRNA.
JD313585 - Sequence 294609 from Patent EP1572962.
JD433684 - Sequence 414708 from Patent EP1572962.
JD432469 - Sequence 413493 from Patent EP1572962.
JD056832 - Sequence 37856 from Patent EP1572962.
JD088410 - Sequence 69434 from Patent EP1572962.
JD320275 - Sequence 301299 from Patent EP1572962.
JD410446 - Sequence 391470 from Patent EP1572962.
JD136165 - Sequence 117189 from Patent EP1572962.
JD079533 - Sequence 60557 from Patent EP1572962.
JD405288 - Sequence 386312 from Patent EP1572962.
JD156659 - Sequence 137683 from Patent EP1572962.
JD113377 - Sequence 94401 from Patent EP1572962.
JD149476 - Sequence 130500 from Patent EP1572962.
JD518046 - Sequence 499070 from Patent EP1572962.
JD518048 - Sequence 499072 from Patent EP1572962.
JD117309 - Sequence 98333 from Patent EP1572962.
JD106067 - Sequence 87091 from Patent EP1572962.
JD220083 - Sequence 201107 from Patent EP1572962.

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

Protein Q6P179 (Reactome details) participates in the following event(s):

R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC
R-HSA-983169 Class I MHC mediated antigen processing & presentation
R-HSA-1280218 Adaptive Immune System
R-HSA-168256 Immune System

-  Other Names for This Gene
  Alternate Gene Symbols: ENST00000437043.1, ENST00000437043.2, ENST00000437043.3, ENST00000437043.4, ENST00000437043.5, ENST00000437043.6, ENST00000437043.7, ERAP2_HUMAN, LRAP, NM_022350, Q6P179, Q7Z5K1, Q8TD32, Q8WVJ4, Q9HBX2, uc320fjw.1, uc320fjw.2
UCSC ID: ENST00000437043.8_8
RefSeq Accession: NM_022350.5
Protein: Q6P179 (aka ERAP2_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.