Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P10605

- CATB_MOUSE

UniProt

P10605 - CATB_MOUSE

Protein

Cathepsin B

Gene

Ctsb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 1081By similarity
    Active sitei278 – 2781By similarity
    Active sitei298 – 2981By similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. cellular response to thyroid hormone stimulus Source: Ensembl
    2. decidualization Source: MGI
    3. regulation of catalytic activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14810.
    BRENDAi3.4.22.1. 3474.
    ReactomeiREACT_198976. Trafficking and processing of endosomal TLR.
    REACT_199055. Collagen degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cathepsin B (EC:3.4.22.1)
    Alternative name(s):
    Cathepsin B1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Ctsb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:88561. Ctsb.

    Subcellular locationi

    Lysosome. Melanosome By similarity. Secretedextracellular space By similarity

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell
    2. lysosome Source: MGI
    3. melanosome Source: UniProtKB-SubCell
    4. mitochondrion Source: MGI
    5. nucleolus Source: Ensembl
    6. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Lysosome, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 7962Activation peptidePRO_0000026148Add
    BLAST
    Chaini80 – 333254Cathepsin BPRO_0000026149Add
    BLAST
    Chaini80 – 12647Cathepsin B light chainBy similarityPRO_0000026150Add
    BLAST
    Chaini129 – 333205Cathepsin B heavy chainBy similarityPRO_0000026151Add
    BLAST
    Propeptidei334 – 3396By similarityPRO_0000026152

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi93 ↔ 122By similarity
    Disulfide bondi105 ↔ 150By similarity
    Disulfide bondi141 ↔ 207By similarity
    Disulfide bondi142 ↔ 146By similarity
    Disulfide bondi179 ↔ 211By similarity
    Disulfide bondi187 ↔ 198By similarity
    Glycosylationi192 – 1921N-linked (GlcNAc...)Curated
    Modified residuei220 – 2201N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP10605.
    PaxDbiP10605.
    PRIDEiP10605.

    2D gel databases

    SWISS-2DPAGEP10605.

    PTM databases

    PhosphoSiteiP10605.

    Expressioni

    Gene expression databases

    BgeeiP10605.
    CleanExiMM_CTSB.
    GenevestigatoriP10605.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP10605. 9 interactions.
    MINTiMINT-4089890.

    Structurei

    3D structure databases

    ProteinModelPortaliP10605.
    SMRiP10605. Positions 27-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4870.
    GeneTreeiENSGT00730000110701.
    HOGENOMiHOG000241341.
    HOVERGENiHBG003480.
    InParanoidiP10605.
    KOiK01363.
    OMAiCTGEGDT.
    OrthoDBiEOG7034HR.
    PhylomeDBiP10605.
    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.

    P10605-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWWSLILLSC LLALTSAHDK PSFHPLSDDL INYINKQNTT WQAGRNFYNV    50
    DISYLKKLCG TVLGGPKLPG RVAFGEDIDL PETFDAREQW SNCPTIGQIR 100
    DQGSCGSCWA FGAVEAISDR TCIHTNGRVN VEVSAEDLLT CCGIQCGDGC 150
    NGGYPSGAWS FWTKKGLVSG GVYNSHVGCL PYTIPPCEHH VNGSRPPCTG 200
    EGDTPRCNKS CEAGYSPSYK EDKHFGYTSY SVSNSVKEIM AEIYKNGPVE 250
    GAFTVFSDFL TYKSGVYKHE AGDMMGGHAI RILGWGVENG VPYWLAANSW 300
    NLDWGDNGFF KILRGENHCG IESEIVAGIP RTDQYWGRF 339
    Length:339
    Mass (Da):37,280
    Last modified:February 1, 1991 - v2
    Checksum:i9F0A3CDF70A94040
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti160 – 1601S → N in AAA37494. (PubMed:3463996)Curated
    Sequence conflicti174 – 1741N → D in AAA37494. (PubMed:3463996)Curated
    Sequence conflicti177 – 1771V → I in AAA37494. (PubMed:3463996)Curated
    Sequence conflicti284 – 2841G → V in AAA37494. (PubMed:3463996)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65270
    , M65263, M65264, M65265, M65266, M65267, M65268, M65269 Genomic DNA. Translation: AAA37375.1.
    M14222 mRNA. Translation: AAA37494.1.
    X54966 mRNA. Translation: CAA38713.1.
    S69034 mRNA. Translation: AAB20536.1.
    AK083393 mRNA. Translation: BAC38900.1.
    AK147192 mRNA. Translation: BAE27751.1.
    AK149884 mRNA. Translation: BAE29144.1.
    AK151790 mRNA. Translation: BAE30691.1.
    AK167361 mRNA. Translation: BAE39458.1.
    BC006656 mRNA. Translation: AAH06656.1.
    CCDSiCCDS27197.1.
    PIRiA38458. KHMSB.
    RefSeqiNP_031824.1. NM_007798.3.
    UniGeneiMm.236553.

    Genome annotation databases

    EnsembliENSMUST00000006235; ENSMUSP00000006235; ENSMUSG00000021939.
    GeneIDi13030.
    KEGGimmu:13030.
    UCSCiuc007uhh.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M65270
    , M65263 , M65264 , M65265 , M65266 , M65267 , M65268 , M65269 Genomic DNA. Translation: AAA37375.1 .
    M14222 mRNA. Translation: AAA37494.1 .
    X54966 mRNA. Translation: CAA38713.1 .
    S69034 mRNA. Translation: AAB20536.1 .
    AK083393 mRNA. Translation: BAC38900.1 .
    AK147192 mRNA. Translation: BAE27751.1 .
    AK149884 mRNA. Translation: BAE29144.1 .
    AK151790 mRNA. Translation: BAE30691.1 .
    AK167361 mRNA. Translation: BAE39458.1 .
    BC006656 mRNA. Translation: AAH06656.1 .
    CCDSi CCDS27197.1.
    PIRi A38458. KHMSB.
    RefSeqi NP_031824.1. NM_007798.3.
    UniGenei Mm.236553.

    3D structure databases

    ProteinModelPortali P10605.
    SMRi P10605. Positions 27-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P10605. 9 interactions.
    MINTi MINT-4089890.

    Chemistry

    BindingDBi P10605.
    ChEMBLi CHEMBL5187.

    PTM databases

    PhosphoSitei P10605.

    2D gel databases

    SWISS-2DPAGE P10605.

    Proteomic databases

    MaxQBi P10605.
    PaxDbi P10605.
    PRIDEi P10605.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006235 ; ENSMUSP00000006235 ; ENSMUSG00000021939 .
    GeneIDi 13030.
    KEGGi mmu:13030.
    UCSCi uc007uhh.2. mouse.

    Organism-specific databases

    CTDi 1508.
    MGIi MGI:88561. Ctsb.

    Phylogenomic databases

    eggNOGi COG4870.
    GeneTreei ENSGT00730000110701.
    HOGENOMi HOG000241341.
    HOVERGENi HBG003480.
    InParanoidi P10605.
    KOi K01363.
    OMAi CTGEGDT.
    OrthoDBi EOG7034HR.
    PhylomeDBi P10605.
    TreeFami TF314576.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14810.
    BRENDAi 3.4.22.1. 3474.
    Reactomei REACT_198976. Trafficking and processing of endosomal TLR.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    ChiTaRSi CTSB. mouse.
    NextBioi 282900.
    PROi P10605.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10605.
    CleanExi MM_CTSB.
    Genevestigatori P10605.

    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. "The structure of the mouse cathepsin B gene and its putative promoter."
      Qian F., Frankfater A., Chan S.J., Steiner D.F.
      DNA Cell Biol. 10:159-168(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. Cited for: NUCLEOTIDE SEQUENCE.
    3. "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].
    4. "Characterization of multiple cathepsin B mRNAs in murine B16a melanoma."
      Qian F., Frankfater A., Steiner D.F., Bajkowski A.S., Chan S.J.
      Anticancer Res. 11:1445-1451(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Placenta and Thymus.
    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].
      Strain: FVB/N.
      Tissue: Mammary gland.
    7. "Isolation of a cathepsin B-encoding cDNA from murine osteogenic cells."
      Friemert C., Closs E.I., Silbermann M., Erfle V., Strauss P.G.
      Gene 103:259-261(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 314-339.
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiCATB_MOUSE
    AccessioniPrimary (citable) accession number: P10605
    Secondary accession number(s): Q3UDW7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3