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Protein

Cathepsin B

Gene

Ctsb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. collagen binding Source: MGI
  2. cysteine-type endopeptidase activity Source: MGI
  3. cysteine-type peptidase activity Source: MGI
  4. peptidase activity Source: MGI
  5. proteoglycan binding Source: MGI

GO - Biological processi

  1. cellular response to thyroid hormone stimulus Source: Ensembl
  2. collagen catabolic process Source: MGI
  3. decidualization Source: MGI
  4. epithelial cell differentiation Source: Ensembl
  5. proteolysis Source: MGI
  6. proteolysis involved in cellular protein catabolic process Source: MGI
  7. regulation of catalytic activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14810.
BRENDAi3.4.22.1. 3474.
3.4.23.5. 3474.
ReactomeiREACT_313067. Collagen degradation.
REACT_318656. Assembly of collagen fibrils and other multimeric structures.
REACT_338311. Trafficking and processing of endosomal TLR.

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 Componenti: 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: MGI
  2. extracellular vesicular exosome Source: MGI
  3. intracellular membrane-bounded organelle Source: MGI
  4. lysosome Source: MGI
  5. melanosome Source: UniProtKB-SubCell
  6. mitochondrion Source: MGI
  7. nucleolus Source: MGI
  8. perinuclear region of cytoplasm Source: MGI
Complete GO annotation...

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.
GeneTreeiENSGT00780000121937.
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

        10         20         30         40         50
MWWSLILLSC LLALTSAHDK PSFHPLSDDL INYINKQNTT WQAGRNFYNV
60 70 80 90 100
DISYLKKLCG TVLGGPKLPG RVAFGEDIDL PETFDAREQW SNCPTIGQIR
110 120 130 140 150
DQGSCGSCWA FGAVEAISDR TCIHTNGRVN VEVSAEDLLT CCGIQCGDGC
160 170 180 190 200
NGGYPSGAWS FWTKKGLVSG GVYNSHVGCL PYTIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGDTPRCNKS CEAGYSPSYK EDKHFGYTSY SVSNSVKEIM AEIYKNGPVE
260 270 280 290 300
GAFTVFSDFL TYKSGVYKHE AGDMMGGHAI RILGWGVENG VPYWLAANSW
310 320 330
NLDWGDNGFF KILRGENHCG IESEIVAGIP RTDQYWGRF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiP10605. 9 interactions.
MINTiMINT-4089890.

Chemistry

BindingDBiP10605.
ChEMBLiCHEMBL5187.

PTM databases

PhosphoSiteiP10605.

2D gel databases

SWISS-2DPAGEP10605.

Proteomic databases

MaxQBiP10605.
PaxDbiP10605.
PRIDEiP10605.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1508.
MGIiMGI:88561. Ctsb.

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00780000121937.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP10605.
KOiK01363.
OMAiCTGEGDT.
OrthoDBiEOG7034HR.
PhylomeDBiP10605.
TreeFamiTF314576.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14810.
BRENDAi3.4.22.1. 3474.
3.4.23.5. 3474.
ReactomeiREACT_313067. Collagen degradation.
REACT_318656. Assembly of collagen fibrils and other multimeric structures.
REACT_338311. Trafficking and processing of endosomal TLR.

Miscellaneous databases

ChiTaRSiCtsb. mouse.
NextBioi282900.
PROiP10605.
SOURCEiSearch...

Gene expression databases

BgeeiP10605.
CleanExiMM_CTSB.
GenevestigatoriP10605.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1990) [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(1985) [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(1990) [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(2004) [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(2003) [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(1990) [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(2012) [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: April 1, 2015
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.