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P07858

- CATB_HUMAN

UniProt

P07858 - CATB_HUMAN

Protein

Cathepsin B

Gene

CTSB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 3 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.

    Catalytic activityi

    Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei108 – 1081
    Active sitei278 – 2781
    Active sitei298 – 2981

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular response to thyroid hormone stimulus Source: UniProtKB
    2. collagen catabolic process Source: BHF-UCL
    3. epithelial cell differentiation Source: UniProt
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. innate immune response Source: Reactome
    7. proteolysis Source: UniProtKB
    8. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
    9. regulation of apoptotic process Source: UniProtKB
    10. regulation of catalytic activity Source: InterPro
    11. toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BRENDAi3.4.22.1. 2681.
    ReactomeiREACT_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

    MEROPSiC01.060.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin B (EC:3.4.22.1)
    Alternative name(s):
    APP secretase
    Short name:
    APPS
    Cathepsin B1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CTSB
    Synonyms:CPSB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2527. CTSB.

    Subcellular locationi

    Lysosome. Melanosome. Secretedextracellular space By similarity
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. endolysosome lumen Source: Reactome
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. intracellular Source: ProtInc
    6. intracellular membrane-bounded organelle Source: HPA
    7. lysosome Source: UniProtKB
    8. melanosome Source: UniProtKB-SubCell
    9. mitochondrion Source: Ensembl
    10. nucleolus Source: HPA
    11. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27027.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 7962Activation peptidePRO_0000026143Add
    BLAST
    Chaini80 – 333254Cathepsin BPRO_0000026144Add
    BLAST
    Chaini80 – 12647Cathepsin B light chainPRO_0000026145Add
    BLAST
    Chaini129 – 333205Cathepsin B heavy chainPRO_0000026146Add
    BLAST
    Propeptidei334 – 3396PRO_0000026147

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi93 ↔ 1221 Publication
    Disulfide bondi105 ↔ 1501 Publication
    Disulfide bondi141 ↔ 2071 Publication
    Disulfide bondi142 ↔ 1461 Publication
    Disulfide bondi179 ↔ 2111 Publication
    Disulfide bondi187 ↔ 1981 Publication
    Glycosylationi192 – 1921N-linked (GlcNAc...)1 Publication
    Modified residuei220 – 2201N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP07858.
    PaxDbiP07858.
    PeptideAtlasiP07858.
    PRIDEiP07858.

    2D gel databases

    SWISS-2DPAGEP07858.
    UCD-2DPAGEP07858.

    PTM databases

    PhosphoSiteiP07858.

    Miscellaneous databases

    PMAP-CutDBP07858.

    Expressioni

    Gene expression databases

    ArrayExpressiP07858.
    BgeeiP07858.
    CleanExiHS_CTSB.
    GenevestigatoriP07858.

    Organism-specific databases

    HPAiCAB000457.
    HPA018156.

    Interactioni

    Subunit structurei

    Dimer of a heavy chain and a light chain cross-linked by a disulfide bond. Interacts with SRPX2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAMTSL4Q6UY143EBI-715062,EBI-742002
    AMBPP027604EBI-715062,EBI-2115136
    MLH1P406927EBI-715062,EBI-744248
    SPHK1Q9NYA14EBI-715062,EBI-985303

    Protein-protein interaction databases

    BioGridi107888. 29 interactions.
    DIPiDIP-42785N.
    IntActiP07858. 23 interactions.
    MINTiMINT-1397666.
    STRINGi9606.ENSP00000342070.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi82 – 854
    Helixi86 – 894
    Helixi94 – 974
    Beta strandi104 – 1063
    Helixi108 – 12417
    Turni125 – 1273
    Beta strandi131 – 1333
    Helixi135 – 1417
    Helixi143 – 1464
    Helixi149 – 1513
    Helixi155 – 16410
    Beta strandi167 – 1704
    Turni173 – 1753
    Beta strandi178 – 1803
    Beta strandi188 – 1914
    Beta strandi193 – 1953
    Helixi220 – 2223
    Beta strandi226 – 2316
    Helixi236 – 24611
    Beta strandi249 – 2568
    Helixi257 – 2615
    Beta strandi264 – 2674
    Beta strandi274 – 28815
    Beta strandi291 – 2977
    Beta strandi302 – 3043
    Beta strandi309 – 3135
    Turni314 – 3174
    Helixi318 – 3203
    Turni321 – 3233
    Beta strandi326 – 3305

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CSBX-ray2.00A/D80-126[»]
    B/E129-333[»]
    1GMYX-ray1.90A/B/C79-339[»]
    1HUCX-ray2.10A/C80-126[»]
    B/D129-333[»]
    1PBHX-ray3.20A18-333[»]
    2IPPX-ray2.15A80-126[»]
    B129-333[»]
    2PBHX-ray3.30A18-333[»]
    3AI8X-ray2.11A/B78-333[»]
    3CBJX-ray1.80A74-339[»]
    3CBKX-ray2.67A74-339[»]
    3K9MX-ray2.61A/B80-333[»]
    3PBHX-ray2.50A18-333[»]
    ProteinModelPortaliP07858.
    SMRiP07858. Positions 18-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07858.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    HOGENOMiHOG000241341.
    HOVERGENiHBG003480.
    InParanoidiP07858.
    KOiK01363.
    OMAiCTGEGDT.
    OrthoDBiEOG7034HR.
    PhylomeDBiP07858.
    TreeFamiTF314576.

    Family and domain databases

    InterProiIPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR015643. Peptidase_C1A_cathepsin-B.
    IPR012599. Propeptide_C1A.
    [Graphical view]
    PANTHERiPTHR12411. PTHR12411. 1 hit.
    PTHR12411:SF285. PTHR12411:SF285. 1 hit.
    PfamiPF00112. Peptidase_C1. 1 hit.
    PF08127. Propeptide_C1. 1 hit.
    [Graphical view]
    PRINTSiPR00705. PAPAIN.
    SMARTiSM00645. 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.

    P07858-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWQLWASLCC LLVLANARSR PSFHPLSDEL VNYVNKRNTT WQAGHNFYNV    50
    DMSYLKRLCG TFLGGPKPPQ RVMFTEDLKL PASFDAREQW PQCPTIKEIR 100
    DQGSCGSCWA FGAVEAISDR ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC 150
    NGGYPAEAWN FWTRKGLVSG GLYESHVGCR PYSIPPCEHH VNGSRPPCTG 200
    EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM AEIYKNGPVE 250
    GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW 300
    NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI 339
    Length:339
    Mass (Da):37,822
    Last modified:June 21, 2005 - v3
    Checksum:i0FC818EA4C1F6D90
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti228 – 2281N → D AA sequence (PubMed:3972105)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261L → V.3 Publications
    Corresponds to variant rs12338 [ dbSNP | Ensembl ].
    VAR_006724
    Natural varianti53 – 531S → G.1 Publication
    Corresponds to variant rs1803250 [ dbSNP | Ensembl ].
    VAR_051511
    Natural varianti91 – 911P → L.
    Corresponds to variant rs11548596 [ dbSNP | Ensembl ].
    VAR_051512
    Natural varianti235 – 2351S → N.
    Corresponds to variant rs17573 [ dbSNP | Ensembl ].
    VAR_014696

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14221 mRNA. Translation: AAA52129.1.
    L16510 mRNA. Translation: AAC37547.1.
    AK092070 mRNA. Translation: BAG52477.1.
    AK075393 mRNA. Translation: BAG52127.1.
    CH471157 Genomic DNA. Translation: EAW65630.1.
    BC010240 mRNA. Translation: AAH10240.1.
    BC095408 mRNA. Translation: AAH95408.1.
    M13230 mRNA. Translation: AAA52125.1.
    CCDSiCCDS5986.1.
    PIRiA26498. KHHUB.
    RefSeqiNP_001899.1. NM_001908.3.
    NP_680090.1. NM_147780.2.
    NP_680091.1. NM_147781.2.
    NP_680092.1. NM_147782.2.
    NP_680093.1. NM_147783.2.
    XP_006716307.1. XM_006716244.1.
    XP_006716308.1. XM_006716245.1.
    UniGeneiHs.520898.

    Genome annotation databases

    EnsembliENST00000345125; ENSP00000342070; ENSG00000164733.
    ENST00000353047; ENSP00000345672; ENSG00000164733.
    ENST00000453527; ENSP00000409917; ENSG00000164733.
    ENST00000530640; ENSP00000435105; ENSG00000164733.
    ENST00000531089; ENSP00000433215; ENSG00000164733.
    ENST00000533455; ENSP00000432244; ENSG00000164733.
    ENST00000534510; ENSP00000434217; ENSG00000164733.
    GeneIDi1508.
    KEGGihsa:1508.
    UCSCiuc003wum.3. human.

    Polymorphism databases

    DMDMi68067549.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14221 mRNA. Translation: AAA52129.1 .
    L16510 mRNA. Translation: AAC37547.1 .
    AK092070 mRNA. Translation: BAG52477.1 .
    AK075393 mRNA. Translation: BAG52127.1 .
    CH471157 Genomic DNA. Translation: EAW65630.1 .
    BC010240 mRNA. Translation: AAH10240.1 .
    BC095408 mRNA. Translation: AAH95408.1 .
    M13230 mRNA. Translation: AAA52125.1 .
    CCDSi CCDS5986.1.
    PIRi A26498. KHHUB.
    RefSeqi NP_001899.1. NM_001908.3.
    NP_680090.1. NM_147780.2.
    NP_680091.1. NM_147781.2.
    NP_680092.1. NM_147782.2.
    NP_680093.1. NM_147783.2.
    XP_006716307.1. XM_006716244.1.
    XP_006716308.1. XM_006716245.1.
    UniGenei Hs.520898.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CSB X-ray 2.00 A/D 80-126 [» ]
    B/E 129-333 [» ]
    1GMY X-ray 1.90 A/B/C 79-339 [» ]
    1HUC X-ray 2.10 A/C 80-126 [» ]
    B/D 129-333 [» ]
    1PBH X-ray 3.20 A 18-333 [» ]
    2IPP X-ray 2.15 A 80-126 [» ]
    B 129-333 [» ]
    2PBH X-ray 3.30 A 18-333 [» ]
    3AI8 X-ray 2.11 A/B 78-333 [» ]
    3CBJ X-ray 1.80 A 74-339 [» ]
    3CBK X-ray 2.67 A 74-339 [» ]
    3K9M X-ray 2.61 A/B 80-333 [» ]
    3PBH X-ray 2.50 A 18-333 [» ]
    ProteinModelPortali P07858.
    SMRi P07858. Positions 18-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107888. 29 interactions.
    DIPi DIP-42785N.
    IntActi P07858. 23 interactions.
    MINTi MINT-1397666.
    STRINGi 9606.ENSP00000342070.

    Chemistry

    BindingDBi P07858.
    ChEMBLi CHEMBL2111396.
    GuidetoPHARMACOLOGYi 2343.

    Protein family/group databases

    MEROPSi C01.060.

    PTM databases

    PhosphoSitei P07858.

    Polymorphism databases

    DMDMi 68067549.

    2D gel databases

    SWISS-2DPAGE P07858.
    UCD-2DPAGE P07858.

    Proteomic databases

    MaxQBi P07858.
    PaxDbi P07858.
    PeptideAtlasi P07858.
    PRIDEi P07858.

    Protocols and materials databases

    DNASUi 1508.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345125 ; ENSP00000342070 ; ENSG00000164733 .
    ENST00000353047 ; ENSP00000345672 ; ENSG00000164733 .
    ENST00000453527 ; ENSP00000409917 ; ENSG00000164733 .
    ENST00000530640 ; ENSP00000435105 ; ENSG00000164733 .
    ENST00000531089 ; ENSP00000433215 ; ENSG00000164733 .
    ENST00000533455 ; ENSP00000432244 ; ENSG00000164733 .
    ENST00000534510 ; ENSP00000434217 ; ENSG00000164733 .
    GeneIDi 1508.
    KEGGi hsa:1508.
    UCSCi uc003wum.3. human.

    Organism-specific databases

    CTDi 1508.
    GeneCardsi GC08M011700.
    H-InvDB HIX0007320.
    HGNCi HGNC:2527. CTSB.
    HPAi CAB000457.
    HPA018156.
    MIMi 116810. gene.
    neXtProti NX_P07858.
    PharmGKBi PA27027.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4870.
    HOGENOMi HOG000241341.
    HOVERGENi HBG003480.
    InParanoidi P07858.
    KOi K01363.
    OMAi CTGEGDT.
    OrthoDBi EOG7034HR.
    PhylomeDBi P07858.
    TreeFami TF314576.

    Enzyme and pathway databases

    BRENDAi 3.4.22.1. 2681.
    Reactomei 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 CTSB. human.
    EvolutionaryTracei P07858.
    GeneWikii Cathepsin_B.
    GenomeRNAii 1508.
    NextBioi 6235.
    PMAP-CutDB P07858.
    PROi P07858.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07858.
    Bgeei P07858.
    CleanExi HS_CTSB.
    Genevestigatori P07858.

    Family and domain databases

    InterProi IPR025661. Pept_asp_AS.
    IPR000169. Pept_cys_AS.
    IPR025660. Pept_his_AS.
    IPR013128. Peptidase_C1A.
    IPR000668. Peptidase_C1A_C.
    IPR015643. Peptidase_C1A_cathepsin-B.
    IPR012599. Propeptide_C1A.
    [Graphical view ]
    PANTHERi PTHR12411. PTHR12411. 1 hit.
    PTHR12411:SF285. PTHR12411:SF285. 1 hit.
    Pfami PF00112. Peptidase_C1. 1 hit.
    PF08127. Propeptide_C1. 1 hit.
    [Graphical view ]
    PRINTSi PR00705. PAPAIN.
    SMARTi 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. "Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs."
      Chan S.J., San Segundo B., McCormick M.B., Steiner D.F.
      Proc. Natl. Acad. Sci. U.S.A. 83:7721-7725(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-26.
    2. "Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene."
      Cao L., Taggart R.T., Berquin I.M., Moin K., Fong D., Sloane B.F.
      Gene 139:163-169(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Gastric carcinoma.
    3. "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], VARIANT VAL-26.
      Tissue: Esophagus.
    4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. 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], VARIANTS VAL-26 AND GLY-53.
      Tissue: Brain and Placenta.
    7. Cited for: PROTEIN SEQUENCE OF 80-126 AND 129-333.
      Tissue: Liver.
    8. "Human tumour cathepsin B. Comparison with normal liver cathepsin B."
      Moin K., Day N.A., Sameni M., Hasnain S., Hirama T., Sloane B.F.
      Biochem. J. 285:427-434(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 80-91 AND 129-139.
      Tissue: Liver.
    9. "Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B."
      Fong D., Calhoun D.H., Hsieh W.-T., Lee B., Wells R.D.
      Proc. Natl. Acad. Sci. U.S.A. 83:2909-2913(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-339.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    12. "Epileptic and developmental disorders of the speech cortex: ligand/receptor interaction of wild-type and mutant SRPX2 with the plasminogen activator receptor uPAR."
      Royer-Zemmour B., Ponsole-Lenfant M., Gara H., Roll P., Leveque C., Massacrier A., Ferracci G., Cillario J., Robaglia-Schlupp A., Vincentelli R., Cau P., Szepetowski P.
      Hum. Mol. Genet. 17:3617-3630(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRPX2.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity."
      Musil D., Zucic D., Turk D., Engh R.A., Mayr I., Huber R., Popovic T., Turk V., Towatari T., Katunuma N., Bode W.
      EMBO J. 10:2321-2330(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
    15. "Crystal structures of human procathepsin B at 3.2- and 3.3-A resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide."
      Turk D., Podobnik M., Kuhelj R., Dolinar M., Turk V.
      FEBS Lett. 384:211-214(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
    16. "Crystal structure of the wild-type human procathepsin B at 2.5-A resolution reveals the native active site of a papain-like cysteine protease zymogen."
      Podobnik M., Kuhelj R., Turk V., Turk D.
      J. Mol. Biol. 271:774-788(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiCATB_HUMAN
    AccessioniPrimary (citable) accession number: P07858
    Secondary accession number(s): B3KQR5
    , B3KRR5, Q503A6, Q96D87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 177 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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