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P14091

- CATE_HUMAN

UniProt

P14091 - CATE_HUMAN

Protein

Cathepsin E

Gene

CTSE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (29 Mar 2004)
      Previous versions | rss
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    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

    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: UniProt

    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

    ArrayExpressiP14091.
    BgeeiP14091.
    CleanExiHS_CTSE.
    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 – 254
    Helixi71 – 733
    Beta strandi74 – 763
    Beta strandi79 – 846
    Turni85 – 884
    Beta strandi89 – 968
    Beta strandi102 – 1065
    Helixi112 – 1143
    Helixi122 – 1243
    Beta strandi134 – 1418
    Beta strandi143 – 15412
    Beta strandi163 – 17311
    Helixi179 – 1835
    Beta strandi187 – 1915
    Helixi195 – 1973
    Helixi199 – 2013
    Helixi205 – 2117
    Beta strandi216 – 2238
    Beta strandi235 – 2384
    Helixi243 – 2453
    Beta strandi251 – 2544
    Turni258 – 2614
    Beta strandi262 – 2709
    Beta strandi273 – 2764
    Beta strandi281 – 2855
    Beta strandi290 – 2945
    Helixi296 – 30611
    Beta strandi312 – 3176
    Helixi319 – 3246
    Beta strandi328 – 3325
    Beta strandi335 – 3395
    Turni341 – 3433
    Beta strandi344 – 3463
    Beta strandi356 – 3627
    Turni367 – 3693
    Beta strandi373 – 3753
    Helixi377 – 3826
    Beta strandi383 – 3886
    Turni389 – 3924
    Beta strandi393 – 3997

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN    50
    LDMIQFTESC SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS 100
    NLWVPSVYCT SPACKTHSRF QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA 150
    DQVSAFATQV EGLTVVGQQF GESVTEPGQT FVDAEFDGIL GLGYPSLAVG 200
    GVTPVFDNMM AQNLVDLPMF SVYMSSNPEG GAGSELIFGG YDHSHFSGSL 250
    NWVPVTKQAY WQIALDNIQV GGTVMFCSEG CQAIVDTGTS LITGPSDKIK 300
    QLQNAIGAAP VDGEYAVECA NLNVMPDVTF TINGVPYTLS PTAYTLLDFV 350
    DGMQFCSSGF QGLDIHPPAG PLWILGDVFI RQFYSVFDRG NNRVGLAPAV 400
    P 401
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSiCCDS1461.1. [P14091-2]
    CCDS1462.1. [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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1461.1. [P14091-2 ]
    CCDS1462.1. [P14091-1 ]
    PIRi A42038. A34401.
    RefSeqi NP_001901.1. NM_001910.3. [P14091-1 ]
    NP_683865.1. NM_148964.2. [P14091-2 ]
    UniGenei Hs.644082.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LCG model - A 1-401 [» ]
    1TZS X-ray 2.35 A 54-401 [» ]
    P 19-53 [» ]
    ProteinModelPortali P14091.
    SMRi P14091. Positions 21-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107890. 1 interaction.
    IntActi P14091. 2 interactions.
    MINTi MINT-1388890.
    STRINGi 9606.ENSP00000350911.

    Chemistry

    BindingDBi P14091.
    ChEMBLi CHEMBL3092.
    GuidetoPHARMACOLOGYi 2346.

    Protein family/group databases

    MEROPSi A01.010.

    PTM databases

    PhosphoSitei P14091.

    Polymorphism databases

    DMDMi 46397366.

    Proteomic databases

    PaxDbi P14091.
    PRIDEi P14091.

    Protocols and materials databases

    DNASUi 1510.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358184 ; ENSP00000350911 ; ENSG00000196188 . [P14091-1 ]
    ENST00000360218 ; ENSP00000353350 ; ENSG00000196188 . [P14091-2 ]
    GeneIDi 1510.
    KEGGi hsa:1510.
    UCSCi uc001hdu.3. human. [P14091-1 ]
    uc001hdv.3. human. [P14091-2 ]

    Organism-specific databases

    CTDi 1510.
    GeneCardsi GC01P206319.
    HGNCi HGNC:2530. CTSE.
    HPAi CAB032687.
    HPA012940.
    MIMi 116890. gene.
    neXtProti NX_P14091.
    PharmGKBi PA27030.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248684.
    HOGENOMi HOG000197681.
    HOVERGENi HBG000482.
    InParanoidi P14091.
    KOi K01382.
    PhylomeDBi P14091.
    TreeFami TF314990.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    SABIO-RK P14091.

    Miscellaneous databases

    EvolutionaryTracei P14091.
    GeneWikii Cathepsin_E.
    GenomeRNAii 1510.
    NextBioi 6251.
    PMAP-CutDB P14091.
    PROi P14091.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14091.
    Bgeei P14091.
    CleanExi HS_CTSE.
    Genevestigatori P14091.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 162 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