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Protein

Cathepsin E

Gene

CTSE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Similar to cathepsin D, but slightly broader specificity.2 Publications

Kineticsi

  1. KM=0.06 mM for hemoglobin1 Publication
  2. KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu1 Publication
  3. KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei96 – 961PROSITE-ProRule annotation
Active sitei286 – 2861PROSITE-ProRule annotation

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: UniProtKB
  2. digestion Source: ProtInc
  3. protein autoprocessing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
SABIO-RKP14091.

Protein family/group databases

MEROPSiA01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin E (EC:3.4.23.34)
Cleaved into the following 2 chains:
Gene namesi
Name:CTSE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2530. CTSE.

Subcellular locationi

Endosome 1 Publication
Note: The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome.

GO - Cellular componenti

  1. endosome Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601C → A: Abolishes homodimerization. 1 Publication

Organism-specific databases

PharmGKBiPA27030.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Propeptidei20 – 5334Activation peptide2 PublicationsPRO_0000025974Add
BLAST
Chaini54 – 401348Cathepsin E form IPRO_0000025975Add
BLAST
Chaini57 – 401345Cathepsin E form IIPRO_0000354668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 – 60Interchain1 Publication
Glycosylationi90 – 901N-linked (GlcNAc...)
Disulfide bondi109 ↔ 114By similarity
Disulfide bondi277 ↔ 281By similarity
Disulfide bondi319 ↔ 356By similarity

Post-translational modificationi

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.3 Publications
Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57.

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP14091.
PRIDEiP14091.

PTM databases

PhosphoSiteiP14091.

Miscellaneous databases

PMAP-CutDBP14091.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiP14091.
CleanExiHS_CTSE.
ExpressionAtlasiP14091. baseline and differential.
GenevestigatoriP14091.

Organism-specific databases

HPAiCAB032687.
HPA012940.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi107890. 1 interaction.
IntActiP14091. 2 interactions.
MINTiMINT-1388890.
STRINGi9606.ENSP00000350911.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCGmodel-A1-401[»]
1TZSX-ray2.35A54-401[»]
P19-53[»]
ProteinModelPortaliP14091.
SMRiP14091. Positions 21-400.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14091.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG248684.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP14091.
KOiK01382.
PhylomeDBiP14091.
TreeFamiTF314990.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 3 (identifier: P14091-3) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN
60 70 80 90 100
LDMIQFTESC SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS
110 120 130 140 150
NLWVPSVYCT SPACKTHSRF QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA
160 170 180 190 200
DQVSAFATQV EGLTVVGQQF GESVTEPGQT FVDAEFDGIL GLGYPSLAVG
210 220 230 240 250
GVTPVFDNMM AQNLVDLPMF SVYMSSNPEG GAGSELIFGG YDHSHFSGSL
260 270 280 290 300
NWVPVTKQAY WQIALDNIQV GGTVMFCSEG CQAIVDTGTS LITGPSDKIK
310 320 330 340 350
QLQNAIGAAP VDGEYAVECA NLNVMPDVTF TINGVPYTLS PTAYTLLDFV
360 370 380 390 400
DGMQFCSSGF QGLDIHPPAG PLWILGDVFI RQFYSVFDRG NNRVGLAPAV

P
Length:401
Mass (Da):43,312
Last modified:March 29, 2004 - v2
Checksum:i46A2BA35266032CB
GO
Isoform 1 (identifier: P14091-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.

Show »
Length:396
Mass (Da):42,794
Checksum:i40B643C5FB01521E
GO
Isoform 2 (identifier: P14091-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.
     268-368: IQVGGTVMFC...GFQGLDIHPP → MLWSVPTLTS...CVCACLSDRP
     369-401: Missing.

Show »
Length:363
Mass (Da):39,553
Checksum:i4443819D6393C1FC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821I → V.
Corresponds to variant rs57621203 [ dbSNP | Ensembl ].
VAR_061731
Natural varianti329 – 3291T → I.
Corresponds to variant rs6503 [ dbSNP | Ensembl ].
VAR_014572

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei155 – 1595Missing in isoform 1 and isoform 2. 5 PublicationsVSP_009729
Alternative sequencei268 – 368101IQVGG…DIHPP → MLWSVPTLTSCRMSPSPLTE SPIPSAQLPTPYWTSWMECS SAAVAFKDLTSTLQLGPSGS WGMSSFDSFTQSLTVGITVW DWPQQSPKEGPCVCACLSDR P in isoform 2. 2 PublicationsVSP_009730Add
BLAST
Alternative sequencei369 – 40133Missing in isoform 2. 2 PublicationsVSP_009731Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05036 mRNA. Translation: AAA52130.1.
M84424
, M84413, M84417, M84418, M84419, M84420, M84421, M84422 Genomic DNA. Translation: AAA52300.1.
AJ250716 mRNA. Translation: CAB82849.1.
AJ250717 mRNA. Translation: CAB82850.1.
AK292057 mRNA. Translation: BAF84746.1.
BX571818 Genomic DNA. Translation: CAH73264.1.
BX571818 Genomic DNA. Translation: CAH73265.1.
CH471067 Genomic DNA. Translation: EAW91592.1.
CH471067 Genomic DNA. Translation: EAW91593.1.
BC042537 mRNA. Translation: AAH42537.1.
CCDSiCCDS73012.1. [P14091-2]
CCDS73013.1. [P14091-1]
PIRiA42038. A34401.
RefSeqiNP_001901.1. NM_001910.3. [P14091-1]
NP_683865.1. NM_148964.2. [P14091-2]
UniGeneiHs.644082.

Genome annotation databases

EnsembliENST00000358184; ENSP00000350911; ENSG00000196188. [P14091-1]
ENST00000360218; ENSP00000353350; ENSG00000196188. [P14091-2]
GeneIDi1510.
KEGGihsa:1510.
UCSCiuc001hdu.3. human. [P14091-1]
uc001hdv.3. human. [P14091-2]

Polymorphism databases

DMDMi46397366.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05036 mRNA. Translation: AAA52130.1.
M84424
, M84413, M84417, M84418, M84419, M84420, M84421, M84422 Genomic DNA. Translation: AAA52300.1.
AJ250716 mRNA. Translation: CAB82849.1.
AJ250717 mRNA. Translation: CAB82850.1.
AK292057 mRNA. Translation: BAF84746.1.
BX571818 Genomic DNA. Translation: CAH73264.1.
BX571818 Genomic DNA. Translation: CAH73265.1.
CH471067 Genomic DNA. Translation: EAW91592.1.
CH471067 Genomic DNA. Translation: EAW91593.1.
BC042537 mRNA. Translation: AAH42537.1.
CCDSiCCDS73012.1. [P14091-2]
CCDS73013.1. [P14091-1]
PIRiA42038. A34401.
RefSeqiNP_001901.1. NM_001910.3. [P14091-1]
NP_683865.1. NM_148964.2. [P14091-2]
UniGeneiHs.644082.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCGmodel-A1-401[»]
1TZSX-ray2.35A54-401[»]
P19-53[»]
ProteinModelPortaliP14091.
SMRiP14091. Positions 21-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107890. 1 interaction.
IntActiP14091. 2 interactions.
MINTiMINT-1388890.
STRINGi9606.ENSP00000350911.

Chemistry

BindingDBiP14091.
ChEMBLiCHEMBL3092.
GuidetoPHARMACOLOGYi2346.

Protein family/group databases

MEROPSiA01.010.

PTM databases

PhosphoSiteiP14091.

Polymorphism databases

DMDMi46397366.

Proteomic databases

PaxDbiP14091.
PRIDEiP14091.

Protocols and materials databases

DNASUi1510.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358184; ENSP00000350911; ENSG00000196188. [P14091-1]
ENST00000360218; ENSP00000353350; ENSG00000196188. [P14091-2]
GeneIDi1510.
KEGGihsa:1510.
UCSCiuc001hdu.3. human. [P14091-1]
uc001hdv.3. human. [P14091-2]

Organism-specific databases

CTDi1510.
GeneCardsiGC01P206319.
HGNCiHGNC:2530. CTSE.
HPAiCAB032687.
HPA012940.
MIMi116890. gene.
neXtProtiNX_P14091.
PharmGKBiPA27030.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG248684.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP14091.
KOiK01382.
PhylomeDBiP14091.
TreeFamiTF314990.

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
SABIO-RKP14091.

Miscellaneous databases

EvolutionaryTraceiP14091.
GeneWikiiCathepsin_E.
GenomeRNAii1510.
NextBioi6251.
PMAP-CutDBP14091.
PROiP14091.
SOURCEiSearch...

Gene expression databases

BgeeiP14091.
CleanExiHS_CTSE.
ExpressionAtlasiP14091. baseline and differential.
GenevestigatoriP14091.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases."
    Azuma T., Pals G., Mohandas T.K., Couvreur J.M., Taggart R.T.
    J. Biol. Chem. 264:16748-16753(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Gastric mucosa.
  2. "Human gastric cathepsin E gene. Multiple transcripts result from alternative polyadenylation of the primary transcripts of a single gene locus at 1q31-q32."
    Azuma T., Liu W.G., Vander Laan D.J., Bowcock A.M., Taggart R.T.
    J. Biol. Chem. 267:1609-1614(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY.
  3. "Subcellular localization and targeting of cathepsin E."
    Finley E.M., Kornfeld S.
    J. Biol. Chem. 269:31259-31266(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, GLYCOSYLATION.
    Tissue: Intestine.
  4. "An alternatively spliced variant of cathepsin E in human gastric adenocarcinoma cells."
    Tatnell P.J., Cook M., Kay J.
    Biochim. Biophys. Acta 1625:203-206(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Gastric adenocarcinoma.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Stomach.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  9. "Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes."
    Takeda-Ezaki M., Yamamoto K.
    Arch. Biochem. Biophys. 304:352-358(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-38 AND 54-76, BIOPHYSICOCHEMICAL PROPERTIES, AUTOCATALYTIC CLEAVAGE, GLYCOSYLATION.
    Tissue: Erythrocyte.
  10. "Structural evidence for two isozymic forms and the carbohydrate attachment site of human gastric cathepsin E."
    Athauda S.B.P., Matsuzaki O., Kgeyama T., Takahashi K.
    Biochem. Biophys. Res. Commun. 168:878-885(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 54-68; 77-95; 141-154; 280-290 AND 394-401, GLYCOSYLATION.
    Tissue: Gastric mucosa.
  11. Cited for: CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-60.
  12. "Regulation of cathepsin E expression during human B cell differentiation in vitro."
    Sealy L., Mota F., Rayment N., Tatnell P.J., Kay J., Chain B.
    Eur. J. Immunol. 26:1838-1843(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  13. "Regulation of human and mouse procathepsin E gene expression."
    Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.
    Eur. J. Biochem. 268:2658-2668(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiCATE_HUMAN
AccessioniPrimary (citable) accession number: P14091
Secondary accession number(s): Q5TZ01
, Q5TZ02, Q9NY58, Q9UCE3, Q9UCE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: March 29, 2004
Last modified: February 4, 2015
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.