Human Gene CTSE (ENST00000358184.7_7) from GENCODE V47lift37
  Description: cathepsin E, transcript variant 1 (from RefSeq NM_001910.4)
Gencode Transcript: ENST00000358184.7_7
Gencode Gene: ENSG00000196188.12_14
Transcript (Including UTRs)
   Position: hg19 chr1:206,317,473-206,332,104 Size: 14,632 Total Exon Count: 9 Strand: +
Coding Region
   Position: hg19 chr1:206,317,577-206,331,185 Size: 13,609 Coding Exon Count: 9 

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 (chr1:206,317,473-206,332,104)mRNA (may differ from genome)Protein (396 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
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HGNCMalacardsMGIOMIMPubMedReactome
UniProtKBWikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: CATE_HUMAN
DESCRIPTION: RecName: Full=Cathepsin E; EC=3.4.23.34; Contains: RecName: Full=Cathepsin E form I; Contains: RecName: Full=Cathepsin E form II; Flags: Precursor;
FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain.
CATALYTIC ACTIVITY: Similar to cathepsin D, but slightly broader specificity.
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 mM for hemoglobin; KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu; KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu;
SUBUNIT: Homodimer; disulfide-linked.
SUBCELLULAR LOCATION: Endosome. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome.
TISSUE SPECIFICITY: Expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. Not expressed in resting B- lymphocytes.
PTM: Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In erythrocyte membranes, both the proenzyme and mature enzyme contain a complex-type oligosaccharide.
PTM: Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57.
SIMILARITY: Belongs to the peptidase A1 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: CTSE
Diseases sorted by gene-association score: gastric adenocarcinoma (3), rosai-dorfman disease (3), pancreatic ductal adenocarcinoma (2)

-  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: 144.76 RPKM in Stomach
Total median expression: 175.59 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 -31.00104-0.298 Picture PostScript Text
3' UTR -204.80919-0.223 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
IPR001461 - Peptidase_A1
IPR021109 - Peptidase_aspartic
IPR001969 - Peptidase_aspartic_AS
IPR009007 - Peptidase_aspartic_catalytic
IPR012848 - Propep_A1

Pfam Domains:
PF00026 - Eukaryotic aspartyl protease
PF07966 - A1 Propeptide
PF14543 - Xylanase inhibitor N-terminal

SCOP Domains:
50630 - Acid proteases

Protein Data Bank (PDB) 3-D Structure
MuPIT help
1LCG - Model 1TZS - X-ray


ModBase Predicted Comparative 3D Structure on P14091
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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 orthologNo ortholog
Gene DetailsGene Details    
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-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0004190 aspartic-type endopeptidase activity
GO:0008233 peptidase activity
GO:0016787 hydrolase activity
GO:0042803 protein homodimerization activity

Biological Process:
GO:0006508 proteolysis
GO:0016540 protein autoprocessing
GO:0019886 antigen processing and presentation of exogenous peptide antigen via MHC class II
GO:0030163 protein catabolic process

Cellular Component:
GO:0005768 endosome


-  Descriptions from all associated GenBank mRNAs
  AJ250716 - Homo sapiens mRNA for cathepsin E (CatE gene), alternative splicing, isolated from adenocarcinoma cell lines.
AJ250717 - Homo sapiens mRNA for procathepsin E (CatE gene).
BC042537 - Homo sapiens cathepsin E, mRNA (cDNA clone MGC:34609 IMAGE:5174814), complete cds.
JD157480 - Sequence 138504 from Patent EP1572962.
JD399384 - Sequence 380408 from Patent EP1572962.
JD152490 - Sequence 133514 from Patent EP1572962.
JD483942 - Sequence 464966 from Patent EP1572962.
J05036 - Human cathepsin E mRNA, complete cds.
AK292057 - Homo sapiens cDNA FLJ75771 complete cds, highly similar to Homo sapiens cathepsin E (CTSE), transcript variant 1, mRNA.
JD435909 - Sequence 416933 from Patent EP1572962.
CU692090 - Synthetic construct Homo sapiens gateway clone IMAGE:100021144 5' read CTSE mRNA.
JF432419 - Synthetic construct Homo sapiens clone IMAGE:100073625 cathepsin E (CTSE) gene, encodes complete protein.
KJ891001 - Synthetic construct Homo sapiens clone ccsbBroadEn_00395 CTSE gene, encodes complete protein.
AK298069 - Homo sapiens cDNA FLJ60742 complete cds, highly similar to Homo sapiens cathepsin E (CTSE), transcript variant 2, mRNA.
JD276185 - Sequence 257209 from Patent EP1572962.
JD445941 - Sequence 426965 from Patent EP1572962.
JD077352 - Sequence 58376 from Patent EP1572962.
JD077353 - Sequence 58377 from Patent EP1572962.
JD484845 - Sequence 465869 from Patent EP1572962.
JD241993 - Sequence 223017 from Patent EP1572962.
JD241994 - Sequence 223018 from Patent EP1572962.
JD241357 - Sequence 222381 from Patent EP1572962.
JD267999 - Sequence 249023 from Patent EP1572962.
JD359619 - Sequence 340643 from Patent EP1572962.
JD263343 - Sequence 244367 from Patent EP1572962.
JD392413 - Sequence 373437 from Patent EP1572962.
JD142185 - Sequence 123209 from Patent EP1572962.
JD352196 - Sequence 333220 from Patent EP1572962.
JD411194 - Sequence 392218 from Patent EP1572962.
JD256115 - Sequence 237139 from Patent EP1572962.
JD466681 - Sequence 447705 from Patent EP1572962.
JD206438 - Sequence 187462 from Patent EP1572962.

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

Protein P14091 (Reactome details) participates in the following event(s):

R-HSA-2130504 Cleavage of lip22 to lip10
R-HSA-2130349 Generation of CLIP from lip10
R-HSA-2130706 MHC class II antigen processing
R-HSA-2132295 MHC class II antigen presentation
R-HSA-1280218 Adaptive Immune System
R-HSA-168256 Immune System

-  Other Names for This Gene
  Alternate Gene Symbols: CATE_HUMAN, ENST00000358184.1, ENST00000358184.2, ENST00000358184.3, ENST00000358184.4, ENST00000358184.5, ENST00000358184.6, NM_001910, P14091, Q5TZ01, Q5TZ02, Q9NY58, Q9UCE3, Q9UCE4, uc318akw.1, uc318akw.2
UCSC ID: ENST00000358184.7_7
RefSeq Accession: NM_001910.4
Protein: P14091 (aka CATE_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.