SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P10605

- CATB_MOUSE

UniProt

P10605 - CATB_MOUSE

(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)

Protein
Cathepsin B
Gene
Ctsb
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 – 1081 By similarity
Active sitei278 – 2781 By similarity
Active sitei298 – 2981 By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. cellular response to thyroid hormone stimulus Source: Ensembl
  2. decidualization Source: MGI
  3. 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.
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
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Propeptidei18 – 7962Activation peptide
PRO_0000026148Add
BLAST
Chaini80 – 333254Cathepsin B
PRO_0000026149Add
BLAST
Chaini80 – 12647Cathepsin B light chain By similarity
PRO_0000026150Add
BLAST
Chaini129 – 333205Cathepsin B heavy chain By similarity
PRO_0000026151Add
BLAST
Propeptidei334 – 3396 By similarity
PRO_0000026152

Amino acid modifications

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

Protein-protein interaction databases

IntActiP10605. 3 interactions.
MINTiMINT-4089890.

Structurei

3D structure databases

ProteinModelPortaliP10605.
SMRiP10605. Positions 27-339.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601S → N in AAA37494. 1 Publication
Sequence conflicti174 – 1741N → D in AAA37494. 1 Publication
Sequence conflicti177 – 1771V → I in AAA37494. 1 Publication
Sequence conflicti284 – 2841G → V in AAA37494. 1 Publication

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...

Protein-protein interaction databases

IntActi P10605. 3 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

« 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(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: September 3, 2014
This is version 145 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