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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

    • aspartic-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    • antigen processing and presentation of exogenous peptide antigen via MHC class II Source: UniProtKB
    • digestion Source: ProtInc
    • protein autoprocessing Source: Ensembl
    • protein catabolic process Source: GO_Central
    • proteolysis Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    BRENDAi3.4.23.34. 2681.
    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 Componenti: 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

    • endosome Source: UniProtKB
    • extracellular 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.

    Polymorphism and mutation databases

    BioMutaiCTSE.
    DMDMi46397366.

    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.
    GenevisibleiP14091. HS.

    Organism-specific databases

    HPAiCAB032687.
    HPA012940.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.1 Publication

    Protein-protein interaction databases

    BioGridi107890. 7 interactions.
    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
    Helixi71 – 733Combined sources
    Beta strandi74 – 763Combined sources
    Beta strandi79 – 846Combined sources
    Turni85 – 884Combined sources
    Beta strandi89 – 968Combined sources
    Beta strandi102 – 1065Combined sources
    Helixi112 – 1143Combined sources
    Helixi122 – 1243Combined sources
    Beta strandi134 – 1418Combined sources
    Beta strandi143 – 15412Combined sources
    Beta strandi163 – 17311Combined sources
    Helixi179 – 1835Combined sources
    Beta strandi187 – 1915Combined sources
    Helixi195 – 1973Combined sources
    Helixi199 – 2013Combined sources
    Helixi205 – 2117Combined sources
    Beta strandi216 – 2238Combined sources
    Beta strandi235 – 2384Combined sources
    Helixi243 – 2453Combined sources
    Beta strandi251 – 2544Combined sources
    Turni258 – 2614Combined sources
    Beta strandi262 – 2709Combined sources
    Beta strandi273 – 2764Combined sources
    Beta strandi281 – 2855Combined sources
    Beta strandi290 – 2945Combined sources
    Helixi296 – 30611Combined sources
    Beta strandi312 – 3176Combined sources
    Helixi319 – 3246Combined sources
    Beta strandi328 – 3325Combined sources
    Beta strandi335 – 3395Combined sources
    Turni341 – 3433Combined sources
    Beta strandi344 – 3463Combined sources
    Beta strandi356 – 3627Combined sources
    Turni367 – 3693Combined sources
    Beta strandi373 – 3753Combined sources
    Helixi377 – 3826Combined sources
    Beta strandi383 – 3886Combined sources
    Turni389 – 3924Combined sources
    Beta strandi393 – 3997Combined 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.
    OMAiGEYAMEC.
    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. AlignAdd to basket

    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]

    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. 7 interactions.
    IntActiP14091. 2 interactions.
    MINTiMINT-1388890.
    STRINGi9606.ENSP00000350911.

    Chemistry

    BindingDBiP14091.
    ChEMBLiCHEMBL3092.
    GuidetoPHARMACOLOGYi2346.

    Protein family/group databases

    MEROPSiA01.010.

    PTM databases

    PhosphoSiteiP14091.

    Polymorphism and mutation databases

    BioMutaiCTSE.
    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.
    OMAiGEYAMEC.
    PhylomeDBiP14091.
    TreeFamiTF314990.

    Enzyme and pathway databases

    BRENDAi3.4.23.34. 2681.
    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.
    GenevisibleiP14091. HS.

    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: July 22, 2015
    This is version 172 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.