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P07711

- CATL1_HUMAN

UniProt

P07711 - CATL1_HUMAN

Protein

Cathepsin L1

Gene

CTSL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 2 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    Important for the overall degradation of proteins in lysosomes.

    Catalytic activityi

    Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei138 – 1381
    Active sitei276 – 2761
    Active sitei300 – 3001

    GO - Molecular functioni

    1. collagen binding Source: BHF-UCL
    2. cysteine-type endopeptidase activity Source: UniProtKB
    3. cysteine-type peptidase activity Source: UniProtKB
    4. fibronectin binding Source: BHF-UCL
    5. histone binding Source: BHF-UCL
    6. protein binding Source: IntAct
    7. proteoglycan binding Source: BHF-UCL

    GO - Biological processi

    1. adaptive immune response Source: UniProtKB
    2. antigen processing and presentation Source: UniProtKB
    3. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    4. cellular response to thyroid hormone stimulus Source: UniProtKB
    5. collagen catabolic process Source: BHF-UCL
    6. extracellular matrix disassembly Source: Reactome
    7. extracellular matrix organization Source: Reactome
    8. innate immune response Source: Reactome
    9. macrophage apoptotic process Source: BHF-UCL
    10. proteolysis Source: UniProtKB
    11. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
    12. toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.15. 2681.
    ReactomeiREACT_111168. Endosomal/Vacuolar pathway.
    REACT_118572. Degradation of the extracellular matrix.
    REACT_118632. Trafficking and processing of endosomal TLR.
    REACT_121399. MHC class II antigen presentation.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiC01.032.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin L1 (EC:3.4.22.15)
    Alternative name(s):
    Cathepsin L
    Major excreted protein
    Short name:
    MEP
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CTSL
    Synonyms:CTSL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:2537. CTSL.

    Subcellular locationi

    GO - Cellular componenti

    1. endolysosome lumen Source: Reactome
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. lysosomal lumen Source: Reactome
    6. lysosome Source: UniProtKB
    7. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162382890.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 11396Activation peptidePRO_0000026244Add
    BLAST
    Chaini114 – 288175Cathepsin L1 heavy chainPRO_0000026245Add
    BLAST
    Propeptidei289 – 2913PRO_0000026246
    Chaini292 – 33342Cathepsin L1 light chainPRO_0000026247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi135 ↔ 178
    Disulfide bondi169 ↔ 211
    Glycosylationi221 – 2211N-linked (GlcNAc...)3 Publications
    Disulfide bondi269 ↔ 322Interchain (between heavy and light chains)

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP07711.
    PaxDbiP07711.
    PeptideAtlasiP07711.
    PRIDEiP07711.

    PTM databases

    PhosphoSiteiP07711.

    Miscellaneous databases

    PMAP-CutDBP07711.

    Expressioni

    Gene expression databases

    ArrayExpressiP07711.
    BgeeiP07711.
    CleanExiHS_CTSL1.
    GenevestigatoriP07711.

    Organism-specific databases

    HPAiCAB000459.

    Interactioni

    Subunit structurei

    Dimer of a heavy and a light chain linked by disulfide bonds.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    srp-6G5EFH42EBI-1220160,EBI-1549936From a different organism.

    Protein-protein interaction databases

    BioGridi107894. 12 interactions.
    IntActiP07711. 13 interactions.
    MINTiMINT-3005764.
    STRINGi9606.ENSP00000345344.

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 253
    Helixi26 – 3510
    Helixi44 – 6724
    Beta strandi72 – 754
    Turni79 – 824
    Helixi85 – 928
    Beta strandi103 – 1053
    Helixi120 – 1234
    Beta strandi134 – 1363
    Helixi138 – 15518
    Helixi163 – 1697
    Turni171 – 1744
    Helixi177 – 1793
    Helixi183 – 19311
    Beta strandi196 – 1983
    Turni199 – 2013
    Helixi215 – 2173
    Beta strandi218 – 2203
    Beta strandi223 – 2275
    Helixi232 – 24110
    Beta strandi245 – 2495
    Helixi254 – 2574
    Beta strandi261 – 2644
    Beta strandi271 – 2733
    Beta strandi276 – 28510
    Beta strandi289 – 2913
    Beta strandi294 – 2996
    Beta strandi304 – 3063
    Beta strandi311 – 3155
    Beta strandi317 – 3204
    Helixi321 – 3233
    Turni324 – 3263
    Beta strandi329 – 3324

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CJLX-ray2.20A22-333[»]
    1CS8X-ray1.80A19-333[»]
    1ICFX-ray2.00A/C114-288[»]
    B/D292-333[»]
    1MHWX-ray1.90A/B114-288[»]
    C/D292-333[»]
    2NQDX-ray1.75B113-333[»]
    2VHSX-ray1.50A/B/C/D114-285[»]
    A/B/C/D294-333[»]
    2XU1X-ray1.45A/B/C/D114-333[»]
    2XU3X-ray0.90A114-333[»]
    2XU4X-ray1.12A114-333[»]
    2XU5X-ray1.60A114-333[»]
    2YJ2X-ray1.15A114-333[»]
    2YJ8X-ray1.30A114-333[»]
    2YJ9X-ray1.35A114-333[»]
    2YJBX-ray1.40A114-333[»]
    2YJCX-ray1.14A114-333[»]
    3BC3X-ray2.20A/B114-333[»]
    3H89X-ray2.50A/B/C/D/E/F114-333[»]
    3H8BX-ray1.80A/B/C/D/E/F114-333[»]
    3H8CX-ray2.50A/B114-333[»]
    3HHAX-ray1.27A/B/C/D114-333[»]
    3HWNX-ray2.33A/B/C/D76-333[»]
    3IV2X-ray2.20A/B114-333[»]
    3K24X-ray2.50A/B114-333[»]
    3KSEX-ray1.71A/B/C114-333[»]
    3OF8X-ray2.20A113-333[»]
    3OF9X-ray1.76A113-333[»]
    4AXLX-ray1.92A114-333[»]
    4AXMX-ray2.80A/B/F/I/L/O114-333[»]
    ProteinModelPortaliP07711.
    SMRiP07711. Positions 18-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07711.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000230774.
    HOVERGENiHBG011513.
    InParanoidiP07711.
    KOiK01365.
    OMAiNPEYSVA.
    OrthoDBiEOG786H3P.
    PhylomeDBiP07711.
    TreeFamiTF313739.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PfamiPF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view]
    PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07711-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA    50
    VWEKNMKMIE LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP 100
    RKGKVFQEPL FYEAPRSVDW REKGYVTPVK NQGQCGSCWA FSATGALEGQ 150
    MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG GLMDYAFQYV QDNGGLDSEE 200
    SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA TVGPISVAID 250
    AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN 300
    SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV 333
    Length:333
    Mass (Da):37,564
    Last modified:October 1, 1989 - v2
    Checksum:i8CD17D00EF859D85
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561M → V in AAH12612. (PubMed:15489334)Curated
    Sequence conflicti268 – 2681D → N AA sequence (PubMed:3342889)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12451 mRNA. Translation: CAA30981.1.
    M20496 mRNA. Translation: AAA66974.1.
    CR457053 mRNA. Translation: CAG33334.1.
    BX537395 mRNA. Translation: CAD97637.1.
    AL160279 Genomic DNA. Translation: CAI16308.1.
    BC012612 mRNA. Translation: AAH12612.1.
    X05256 mRNA. Translation: CAA28877.1.
    CCDSiCCDS6675.1.
    PIRiS01002. KHHUL.
    RefSeqiNP_001244900.1. NM_001257971.1.
    NP_001244901.1. NM_001257972.1.
    NP_001903.1. NM_001912.4.
    NP_666023.1. NM_145918.2.
    XP_005251773.1. XM_005251716.1.
    UniGeneiHs.731507.

    Genome annotation databases

    EnsembliENST00000340342; ENSP00000365061; ENSG00000135047.
    ENST00000343150; ENSP00000345344; ENSG00000135047.
    GeneIDi1514.
    KEGGihsa:1514.
    UCSCiuc004aph.3. human.

    Polymorphism databases

    DMDMi115741.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12451 mRNA. Translation: CAA30981.1 .
    M20496 mRNA. Translation: AAA66974.1 .
    CR457053 mRNA. Translation: CAG33334.1 .
    BX537395 mRNA. Translation: CAD97637.1 .
    AL160279 Genomic DNA. Translation: CAI16308.1 .
    BC012612 mRNA. Translation: AAH12612.1 .
    X05256 mRNA. Translation: CAA28877.1 .
    CCDSi CCDS6675.1.
    PIRi S01002. KHHUL.
    RefSeqi NP_001244900.1. NM_001257971.1.
    NP_001244901.1. NM_001257972.1.
    NP_001903.1. NM_001912.4.
    NP_666023.1. NM_145918.2.
    XP_005251773.1. XM_005251716.1.
    UniGenei Hs.731507.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CJL X-ray 2.20 A 22-333 [» ]
    1CS8 X-ray 1.80 A 19-333 [» ]
    1ICF X-ray 2.00 A/C 114-288 [» ]
    B/D 292-333 [» ]
    1MHW X-ray 1.90 A/B 114-288 [» ]
    C/D 292-333 [» ]
    2NQD X-ray 1.75 B 113-333 [» ]
    2VHS X-ray 1.50 A/B/C/D 114-285 [» ]
    A/B/C/D 294-333 [» ]
    2XU1 X-ray 1.45 A/B/C/D 114-333 [» ]
    2XU3 X-ray 0.90 A 114-333 [» ]
    2XU4 X-ray 1.12 A 114-333 [» ]
    2XU5 X-ray 1.60 A 114-333 [» ]
    2YJ2 X-ray 1.15 A 114-333 [» ]
    2YJ8 X-ray 1.30 A 114-333 [» ]
    2YJ9 X-ray 1.35 A 114-333 [» ]
    2YJB X-ray 1.40 A 114-333 [» ]
    2YJC X-ray 1.14 A 114-333 [» ]
    3BC3 X-ray 2.20 A/B 114-333 [» ]
    3H89 X-ray 2.50 A/B/C/D/E/F 114-333 [» ]
    3H8B X-ray 1.80 A/B/C/D/E/F 114-333 [» ]
    3H8C X-ray 2.50 A/B 114-333 [» ]
    3HHA X-ray 1.27 A/B/C/D 114-333 [» ]
    3HWN X-ray 2.33 A/B/C/D 76-333 [» ]
    3IV2 X-ray 2.20 A/B 114-333 [» ]
    3K24 X-ray 2.50 A/B 114-333 [» ]
    3KSE X-ray 1.71 A/B/C 114-333 [» ]
    3OF8 X-ray 2.20 A 113-333 [» ]
    3OF9 X-ray 1.76 A 113-333 [» ]
    4AXL X-ray 1.92 A 114-333 [» ]
    4AXM X-ray 2.80 A/B/F/I/L/O 114-333 [» ]
    ProteinModelPortali P07711.
    SMRi P07711. Positions 18-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107894. 12 interactions.
    IntActi P07711. 13 interactions.
    MINTi MINT-3005764.
    STRINGi 9606.ENSP00000345344.

    Chemistry

    BindingDBi P07711.
    ChEMBLi CHEMBL3837.
    DrugBanki DB00040. Glucagon recombinant.
    GuidetoPHARMACOLOGYi 2351.

    Protein family/group databases

    MEROPSi C01.032.

    PTM databases

    PhosphoSitei P07711.

    Polymorphism databases

    DMDMi 115741.

    Proteomic databases

    MaxQBi P07711.
    PaxDbi P07711.
    PeptideAtlasi P07711.
    PRIDEi P07711.

    Protocols and materials databases

    DNASUi 1514.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340342 ; ENSP00000365061 ; ENSG00000135047 .
    ENST00000343150 ; ENSP00000345344 ; ENSG00000135047 .
    GeneIDi 1514.
    KEGGi hsa:1514.
    UCSCi uc004aph.3. human.

    Organism-specific databases

    CTDi 1514.
    GeneCardsi GC09P090352.
    H-InvDB HIX0058839.
    HIX0170314.
    HGNCi HGNC:2537. CTSL.
    HPAi CAB000459.
    MIMi 116880. gene.
    neXtProti NX_P07711.
    PharmGKBi PA162382890.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000230774.
    HOVERGENi HBG011513.
    InParanoidi P07711.
    KOi K01365.
    OMAi NPEYSVA.
    OrthoDBi EOG786H3P.
    PhylomeDBi P07711.
    TreeFami TF313739.

    Enzyme and pathway databases

    BRENDAi 3.4.22.15. 2681.
    Reactomei REACT_111168. Endosomal/Vacuolar pathway.
    REACT_118572. Degradation of the extracellular matrix.
    REACT_118632. Trafficking and processing of endosomal TLR.
    REACT_121399. MHC class II antigen presentation.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    ChiTaRSi CTSL1. human.
    EvolutionaryTracei P07711.
    GeneWikii Cathepsin_L1.
    GenomeRNAii 1514.
    NextBioi 6271.
    PMAP-CutDB P07711.
    PROi P07711.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07711.
    Bgeei P07711.
    CleanExi HS_CTSL1.
    Genevestigatori P07711.

    Family and domain databases

    InterProi IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR013201. Prot_inhib_I29.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    Pfami PF08246. Inhibitor_I29. 1 hit.
    PF00112. Peptidase_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi SM00848. Inhibitor_I29. 1 hit.
    SM00645. Pept_C1. 1 hit.
    [Graphical view ]
    PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    PS00639. THIOL_PROTEASE_HIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence of a cDNA for human pro-(cathepsin L)."
      Gal S., Gottesman M.M.
      Biochem. J. 253:303-306(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts."
      Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P.
      J. Clin. Invest. 81:1621-1629(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon endothelium.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Prostate.
    7. "Amino acid sequences of the human kidney cathepsins H and L."
      Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.
      FEBS Lett. 228:341-345(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 114-288 AND 292-333.
    8. "The major ras induced protein in NIH3T3 cells is cathepsin L."
      Joseph L.J., Lapid S., Sukhatme V.P.
      Nucleic Acids Res. 15:3186-3186(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 113-154.
    9. "The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line."
      Mason R.W., Walker J.E., Northrop F.D.
      Biochem. J. 240:373-377(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 114-154 AND 292-333.
    10. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-221.
    11. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
      Tissue: Plasma.
    12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
      Tissue: Liver.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment."
      Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., Cygler M.
      EMBO J. 15:5492-5503(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-333.
    15. "The crystal structure of human cathepsin L complexed with E-64."
      Fujishima A., Imai Y., Nomura T., Fujisawa Y., Yamamoto Y., Sugarawa T.
      FEBS Lett. 407:47-50(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-333.
    16. Cygler M., Coulombe R.
      Submitted (AUG-1999) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-333.

    Entry informationi

    Entry nameiCATL1_HUMAN
    AccessioniPrimary (citable) accession number: P07711
    Secondary accession number(s): Q6IAV1, Q96QJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 170 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 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3