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P25774

- CATS_HUMAN

UniProt

P25774 - CATS_HUMAN

Protein

Cathepsin S

Gene

CTSS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (21 Feb 2006)
      Previous versions | rss
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    Functioni

    Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.

    Catalytic activityi

    Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei139 – 1391By similarity
    Active sitei278 – 2781By similarity
    Active sitei298 – 2981By similarity

    GO - Molecular functioni

    1. collagen binding Source: BHF-UCL
    2. cysteine-type endopeptidase activity Source: BHF-UCL
    3. fibronectin binding Source: BHF-UCL
    4. laminin binding Source: BHF-UCL
    5. 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 I Source: Reactome
    4. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
    5. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    6. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    7. basement membrane disassembly Source: BHF-UCL
    8. cellular response to thyroid hormone stimulus Source: UniProtKB
    9. collagen catabolic process Source: BHF-UCL
    10. extracellular matrix disassembly Source: Reactome
    11. extracellular matrix organization Source: Reactome
    12. immune response Source: ProtInc
    13. innate immune response Source: Reactome
    14. proteolysis Source: ProtInc
    15. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
    16. toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.27. 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.

    Protein family/group databases

    MEROPSiC01.034.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin S (EC:3.4.22.27)
    Gene namesi
    Name:CTSS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2545. CTSS.

    Subcellular locationi

    GO - Cellular componenti

    1. endolysosome lumen Source: Reactome
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: BHF-UCL
    4. intracellular membrane-bounded organelle Source: HPA
    5. lysosomal lumen Source: Reactome
    6. lysosome Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27041.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Propeptidei17 – 11498Activation peptidePRO_0000026313Add
    BLAST
    Chaini115 – 331217Cathepsin SPRO_0000026314Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi126 ↔ 2241 Publication
    Disulfide bondi136 ↔ 1801 Publication
    Disulfide bondi170 ↔ 2131 Publication
    Disulfide bondi272 ↔ 3201 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP25774.
    PaxDbiP25774.
    PeptideAtlasiP25774.
    PRIDEiP25774.

    PTM databases

    PhosphoSiteiP25774.

    Miscellaneous databases

    PMAP-CutDBP25774.

    Expressioni

    Gene expression databases

    BgeeiP25774.
    CleanExiHS_CTSS.
    GenevestigatoriP25774.

    Organism-specific databases

    HPAiCAB000460.
    HPA002988.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi107900. 2 interactions.
    IntActiP25774. 2 interactions.
    STRINGi9606.ENSP00000357981.

    Structurei

    Secondary structure

    1
    331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 243
    Helixi25 – 3511
    Helixi44 – 6724
    Beta strandi72 – 754
    Helixi79 – 824
    Helixi85 – 917
    Helixi100 – 1023
    Helixi121 – 1244
    Beta strandi135 – 1373
    Helixi139 – 15618
    Helixi164 – 1707
    Helixi173 – 1753
    Helixi179 – 1813
    Helixi185 – 19511
    Beta strandi198 – 2003
    Turni201 – 2033
    Helixi217 – 2193
    Beta strandi220 – 2223
    Beta strandi226 – 2294
    Helixi235 – 24410
    Beta strandi248 – 2525
    Helixi257 – 2615
    Beta strandi264 – 2674
    Beta strandi278 – 28811
    Beta strandi291 – 2977
    Turni301 – 3033
    Beta strandi309 – 3135
    Beta strandi315 – 3184
    Helixi319 – 3213
    Turni322 – 3243
    Beta strandi327 – 3304

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BXFmodel-A115-331[»]
    1GLOX-ray2.20A115-331[»]
    1MS6X-ray1.90A115-331[»]
    1NPZX-ray2.00A/B115-331[»]
    1NQCX-ray1.80A115-331[»]
    2C0YX-ray2.10A17-331[»]
    2F1GX-ray1.90A/B112-331[»]
    2FQ9X-ray1.65A/B114-331[»]
    2FRAX-ray1.90A/B114-330[»]
    2FRQX-ray1.60A/B114-331[»]
    2FT2X-ray1.70A/B114-331[»]
    2FUDX-ray1.95A/B114-331[»]
    2FYEX-ray2.20A115-331[»]
    2G6DX-ray2.50A115-331[»]
    2G7YX-ray2.00A/B114-330[»]
    2H7JX-ray1.50A/B112-331[»]
    2HH5X-ray1.80A/B112-331[»]
    2HHNX-ray1.55A/B112-331[»]
    2HXZX-ray1.90A/B/C112-331[»]
    2OP3X-ray1.60A/B112-331[»]
    2R9MX-ray1.97A/B115-331[»]
    2R9NX-ray2.00A/B115-331[»]
    2R9OX-ray2.00A/B115-331[»]
    3IEJX-ray2.18A/B115-331[»]
    3KWNX-ray2.10A/B115-331[»]
    3MPEX-ray2.25A/B114-331[»]
    3MPFX-ray1.80A/B115-331[»]
    3N3GX-ray1.60A/B115-331[»]
    3N4CX-ray1.90A/B115-331[»]
    3OVXX-ray1.49A/B114-331[»]
    ProteinModelPortaliP25774.
    SMRiP25774. Positions 18-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25774.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000230774.
    HOVERGENiHBG011513.
    InParanoidiP25774.
    KOiK01368.
    OMAiMERTRVP.
    OrthoDBiEOG786H3P.
    PhylomeDBiP25774.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P25774-1) [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

    MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL    50
    IWEKNLKFVM LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LMSSLRVPSQ 100
    WQRNITYKSN PNRILPDSVD WREKGCVTEV KYQGSCGACW AFSAVGALEA 150
    QLKLKTGKLV SLSAQNLVDC STEKYGNKGC NGGFMTTAFQ YIIDNKGIDS 200
    DASYPYKAMD QKCQYDSKYR AATCSKYTEL PYGREDVLKE AVANKGPVSV 250
    GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG KEYWLVKNSW 300
    GHNFGEEGYI RMARNKGNHC GIASFPSYPE I 331
    Length:331
    Mass (Da):37,496
    Last modified:February 21, 2006 - v3
    Checksum:i86093619DB6F0269
    GO
    Isoform 2 (identifier: P25774-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         84-133: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:281
    Mass (Da):31,626
    Checksum:iC0445894FAD89713
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921M → T(PubMed:1373132)Curated
    Sequence conflicti92 – 921M → T(PubMed:8157683)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti113 – 1131R → W.3 Publications
    Corresponds to variant rs2230061 [ dbSNP | Ensembl ].
    VAR_025385
    Natural varianti161 – 1611S → T.2 Publications
    Corresponds to variant rs1059604 [ dbSNP | Ensembl ].
    VAR_025386

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei84 – 13350Missing in isoform 2. 1 PublicationVSP_042712Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S93414 mRNA. Translation: AAB22005.1.
    M86553 mRNA. Translation: AAA35655.1.
    M90696 mRNA. Translation: AAC37592.1.
    U07374
    , U07370, U07371, U07372, U07373 Genomic DNA. Translation: AAB60643.2.
    CR541676 mRNA. Translation: CAG46477.1.
    AK301472 mRNA. Translation: BAG62991.1.
    AK314482 mRNA. Translation: BAG37086.1.
    AL356292 Genomic DNA. Translation: CAI13657.1.
    CH471121 Genomic DNA. Translation: EAW53518.1.
    CH471121 Genomic DNA. Translation: EAW53519.1.
    BC002642 mRNA. Translation: AAH02642.1.
    CCDSiCCDS55634.1. [P25774-2]
    CCDS968.1. [P25774-1]
    PIRiA42482.
    RefSeqiNP_001186668.1. NM_001199739.1. [P25774-2]
    NP_004070.3. NM_004079.4. [P25774-1]
    UniGeneiHs.181301.

    Genome annotation databases

    EnsembliENST00000368985; ENSP00000357981; ENSG00000163131. [P25774-1]
    ENST00000448301; ENSP00000408414; ENSG00000163131. [P25774-2]
    GeneIDi1520.
    KEGGihsa:1520.
    UCSCiuc001evn.3. human. [P25774-1]
    uc010pcj.2. human. [P25774-2]

    Polymorphism databases

    DMDMi88984046.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S93414 mRNA. Translation: AAB22005.1 .
    M86553 mRNA. Translation: AAA35655.1 .
    M90696 mRNA. Translation: AAC37592.1 .
    U07374
    , U07370 , U07371 , U07372 , U07373 Genomic DNA. Translation: AAB60643.2 .
    CR541676 mRNA. Translation: CAG46477.1 .
    AK301472 mRNA. Translation: BAG62991.1 .
    AK314482 mRNA. Translation: BAG37086.1 .
    AL356292 Genomic DNA. Translation: CAI13657.1 .
    CH471121 Genomic DNA. Translation: EAW53518.1 .
    CH471121 Genomic DNA. Translation: EAW53519.1 .
    BC002642 mRNA. Translation: AAH02642.1 .
    CCDSi CCDS55634.1. [P25774-2 ]
    CCDS968.1. [P25774-1 ]
    PIRi A42482.
    RefSeqi NP_001186668.1. NM_001199739.1. [P25774-2 ]
    NP_004070.3. NM_004079.4. [P25774-1 ]
    UniGenei Hs.181301.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BXF model - A 115-331 [» ]
    1GLO X-ray 2.20 A 115-331 [» ]
    1MS6 X-ray 1.90 A 115-331 [» ]
    1NPZ X-ray 2.00 A/B 115-331 [» ]
    1NQC X-ray 1.80 A 115-331 [» ]
    2C0Y X-ray 2.10 A 17-331 [» ]
    2F1G X-ray 1.90 A/B 112-331 [» ]
    2FQ9 X-ray 1.65 A/B 114-331 [» ]
    2FRA X-ray 1.90 A/B 114-330 [» ]
    2FRQ X-ray 1.60 A/B 114-331 [» ]
    2FT2 X-ray 1.70 A/B 114-331 [» ]
    2FUD X-ray 1.95 A/B 114-331 [» ]
    2FYE X-ray 2.20 A 115-331 [» ]
    2G6D X-ray 2.50 A 115-331 [» ]
    2G7Y X-ray 2.00 A/B 114-330 [» ]
    2H7J X-ray 1.50 A/B 112-331 [» ]
    2HH5 X-ray 1.80 A/B 112-331 [» ]
    2HHN X-ray 1.55 A/B 112-331 [» ]
    2HXZ X-ray 1.90 A/B/C 112-331 [» ]
    2OP3 X-ray 1.60 A/B 112-331 [» ]
    2R9M X-ray 1.97 A/B 115-331 [» ]
    2R9N X-ray 2.00 A/B 115-331 [» ]
    2R9O X-ray 2.00 A/B 115-331 [» ]
    3IEJ X-ray 2.18 A/B 115-331 [» ]
    3KWN X-ray 2.10 A/B 115-331 [» ]
    3MPE X-ray 2.25 A/B 114-331 [» ]
    3MPF X-ray 1.80 A/B 115-331 [» ]
    3N3G X-ray 1.60 A/B 115-331 [» ]
    3N4C X-ray 1.90 A/B 115-331 [» ]
    3OVX X-ray 1.49 A/B 114-331 [» ]
    ProteinModelPortali P25774.
    SMRi P25774. Positions 18-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107900. 2 interactions.
    IntActi P25774. 2 interactions.
    STRINGi 9606.ENSP00000357981.

    Chemistry

    BindingDBi P25774.
    ChEMBLi CHEMBL2954.
    GuidetoPHARMACOLOGYi 2353.

    Protein family/group databases

    MEROPSi C01.034.

    PTM databases

    PhosphoSitei P25774.

    Polymorphism databases

    DMDMi 88984046.

    Proteomic databases

    MaxQBi P25774.
    PaxDbi P25774.
    PeptideAtlasi P25774.
    PRIDEi P25774.

    Protocols and materials databases

    DNASUi 1520.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368985 ; ENSP00000357981 ; ENSG00000163131 . [P25774-1 ]
    ENST00000448301 ; ENSP00000408414 ; ENSG00000163131 . [P25774-2 ]
    GeneIDi 1520.
    KEGGi hsa:1520.
    UCSCi uc001evn.3. human. [P25774-1 ]
    uc010pcj.2. human. [P25774-2 ]

    Organism-specific databases

    CTDi 1520.
    GeneCardsi GC01M150702.
    HGNCi HGNC:2545. CTSS.
    HPAi CAB000460.
    HPA002988.
    MIMi 116845. gene.
    neXtProti NX_P25774.
    PharmGKBi PA27041.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000230774.
    HOVERGENi HBG011513.
    InParanoidi P25774.
    KOi K01368.
    OMAi MERTRVP.
    OrthoDBi EOG786H3P.
    PhylomeDBi P25774.
    TreeFami TF313739.

    Enzyme and pathway databases

    BRENDAi 3.4.22.27. 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.

    Miscellaneous databases

    ChiTaRSi CTSS. human.
    EvolutionaryTracei P25774.
    GeneWikii Cathepsin_S.
    GenomeRNAii 1520.
    NextBioi 6291.
    PMAP-CutDB P25774.
    PROi P25774.
    SOURCEi Search...

    Gene expression databases

    Bgeei P25774.
    CleanExi HS_CTSS.
    Genevestigatori P25774.

    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. "Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease."
      Shi G.-P., Munger J.S., Meara J.P., Rich D.H., Chapman H.A.
      J. Biol. Chem. 267:7258-7262(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-161.
      Tissue: Alveolar macrophage.
    2. "Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S."
      Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C.
      J. Biol. Chem. 267:13708-13713(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 211.
    4. "Human cathepsin S: chromosomal localization, gene structure, and tissue distribution."
      Shi G.-P., Webb A.C., Foster K.E., Knoll J.H.M., Lemere C.A., Munger J.S., Chapman H.A.
      J. Biol. Chem. 269:11530-11536(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-161.
    5. "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] (ISOFORM 1), VARIANT TRP-113.
    6. "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] (ISOFORMS 1 AND 2), VARIANT TRP-113.
      Tissue: Placenta and Synovium.
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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), VARIANT TRP-113.
      Tissue: Pancreas.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics."
      Fengler A., Brandt W.
      Protein Eng. 11:1007-1013(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 115-331.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 115-331.
    13. "Characterization and optimization of selective, nonpeptidic inhibitors of cathepsin S with an unprecedented binding mode."
      Inagaki H., Tsuruoka H., Hornsby M., Lesley S.A., Spraggon G., Ellman J.A.
      J. Med. Chem. 50:2693-2699(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 112-331 IN COMPLEX WITH INHIBITOR, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCATS_HUMAN
    AccessioniPrimary (citable) accession number: P25774
    Secondary accession number(s): B4DWC9
    , D3DV05, Q5T5I0, Q6FHS5, Q9BUG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: February 21, 2006
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 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, 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