CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003811
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cathepsin B 
Protein Synonyms/Alias
 Cathepsin B1; Cathepsin B light chain; Cathepsin B heavy chain 
Gene Name
 Ctsb 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
220AGYSPSYKEDKHFGYacetylation[1, 2, 3, 4]
220AGYSPSYKEDKHFGYubiquitination[5]
223SPSYKEDKHFGYTSYacetylation[1]
245EIMAEIYKNGPVEGAacetylation[4]
268TYKSGVYKHEAGDMMacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. 
Sequence Annotation
 ACT_SITE 108 108 By similarity.
 ACT_SITE 278 278 By similarity.
 ACT_SITE 298 298 By similarity.
 CARBOHYD 192 192 N-linked (GlcNAc...) (Probable).
 DISULFID 93 122 By similarity.
 DISULFID 105 150 By similarity.
 DISULFID 141 207 By similarity.
 DISULFID 142 146 By similarity.
 DISULFID 179 211 By similarity.
 DISULFID 187 198 By similarity.  
Keyword
 Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome; Secreted; Signal; Thiol protease; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 339 AA 
Protein Sequence
MWWSLILLSC LLALTSAHDK PSFHPLSDDL INYINKQNTT WQAGRNFYNV DISYLKKLCG 60
TVLGGPKLPG RVAFGEDIDL PETFDAREQW SNCPTIGQIR DQGSCGSCWA FGAVEAISDR 120
TCIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWS FWTKKGLVSG GVYNSHVGCL 180
PYTIPPCEHH VNGSRPPCTG EGDTPRCNKS CEAGYSPSYK EDKHFGYTSY SVSNSVKEIM 240
AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDMMGGHAI RILGWGVENG VPYWLAANSW 300
NLDWGDNGFF KILRGENHCG IESEIVAGIP RTDQYWGRF 339 
Gene Ontology
 GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
 GO:0005764; C:lysosome; IDA:MGI.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
 GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Compara.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0050790; P:regulation of catalytic activity; IEA:InterPro. 
Interpro
 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. 
Pfam
 PF00112; Peptidase_C1
 PF08127; Propeptide_C1 
SMART
 SM00645; Pept_C1 
PROSITE
 PS00640; THIOL_PROTEASE_ASN
 PS00139; THIOL_PROTEASE_CYS
 PS00639; THIOL_PROTEASE_HIS 
PRINTS
 PR00705; PAPAIN.