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Protein

Cathepsin B

Gene

CTSB

Organism
Homo sapiens (Human)
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)DescriptionActionsGraphical viewLength
Active sitei1081
Active sitei2781
Active sitei2981

GO - Molecular functioni

  • collagen binding Source: BHF-UCL
  • cysteine-type endopeptidase activity Source: BHF-UCL
  • cysteine-type peptidase activity Source: UniProtKB
  • peptidase activity Source: BHF-UCL
  • proteoglycan binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: Reactome

GO - Biological processi

  • cellular response to thyroid hormone stimulus Source: UniProtKB
  • collagen catabolic process Source: BHF-UCL
  • decidualization Source: Ensembl
  • epithelial cell differentiation Source: UniProtKB
  • proteolysis Source: UniProtKB
  • proteolysis involved in cellular protein catabolic process Source: BHF-UCL
  • regulation of apoptotic process Source: UniProtKB
  • regulation of catalytic activity Source: InterPro
  • toll-like receptor signaling pathway Source: Reactome
  • viral entry into host cell Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciZFISH:HS09125-MONOMER.
BRENDAi3.4.22.1. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:2527. CTSB.

Subcellular locationi

GO - Cellular componenti

  • endolysosome lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • intracellular Source: ProtInc
  • intracellular membrane-bounded organelle Source: HPA
  • lysosome Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • mitochondrion Source: Ensembl
  • nucleolus Source: HPA
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi1508.
OpenTargetsiENSG00000164733.
PharmGKBiPA27027.

Chemistry databases

ChEMBLiCHEMBL4072.
GuidetoPHARMACOLOGYi2343.

Polymorphism and mutation databases

BioMutaiCTSB.
DMDMi68067549.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002614318 – 79Activation peptideAdd BLAST62
ChainiPRO_000002614480 – 333Cathepsin BAdd BLAST254
ChainiPRO_000002614580 – 126Cathepsin B light chainAdd BLAST47
ChainiPRO_0000026146129 – 333Cathepsin B heavy chainAdd BLAST205
PropeptideiPRO_0000026147334 – 3396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi93 ↔ 1221 Publication
Disulfide bondi105 ↔ 1501 Publication
Disulfide bondi141 ↔ 2071 Publication
Disulfide bondi142 ↔ 1461 Publication
Disulfide bondi179 ↔ 2111 Publication
Disulfide bondi187 ↔ 1981 Publication
Glycosylationi192N-linked (GlcNAc...)1 Publication1
Modified residuei220N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP07858.
MaxQBiP07858.
PaxDbiP07858.
PeptideAtlasiP07858.
PRIDEiP07858.
TopDownProteomicsiP07858.

2D gel databases

SWISS-2DPAGEP07858.
UCD-2DPAGEP07858.

PTM databases

iPTMnetiP07858.
PhosphoSitePlusiP07858.
SwissPalmiP07858.

Miscellaneous databases

PMAP-CutDBP07858.

Expressioni

Gene expression databases

BgeeiENSG00000164733.
CleanExiHS_CTSB.
ExpressionAtlasiP07858. baseline and differential.
GenevisibleiP07858. HS.

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

GO - Molecular functioni

  • collagen binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107888. 35 interactors.
DIPiDIP-42785N.
IntActiP07858. 39 interactors.
MINTiMINT-1397666.
STRINGi9606.ENSP00000342070.

Chemistry databases

BindingDBiP07858.

Structurei

Secondary structure

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi82 – 85Combined sources4
Helixi86 – 89Combined sources4
Helixi94 – 97Combined sources4
Beta strandi104 – 106Combined sources3
Helixi108 – 124Combined sources17
Turni125 – 127Combined sources3
Beta strandi131 – 133Combined sources3
Helixi135 – 141Combined sources7
Helixi143 – 146Combined sources4
Helixi149 – 151Combined sources3
Helixi155 – 164Combined sources10
Beta strandi167 – 170Combined sources4
Turni173 – 175Combined sources3
Beta strandi178 – 180Combined sources3
Beta strandi188 – 191Combined sources4
Beta strandi193 – 195Combined sources3
Helixi220 – 222Combined sources3
Beta strandi226 – 231Combined sources6
Helixi236 – 246Combined sources11
Beta strandi249 – 256Combined sources8
Helixi257 – 261Combined sources5
Beta strandi264 – 267Combined sources4
Beta strandi274 – 288Combined sources15
Beta strandi291 – 297Combined sources7
Beta strandi302 – 304Combined sources3
Beta strandi309 – 313Combined sources5
Turni314 – 317Combined sources4
Helixi318 – 320Combined sources3
Turni321 – 323Combined sources3
Beta strandi326 – 330Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07858.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00780000121937.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP07858.
KOiK01363.
OMAiEDMLTCC.
OrthoDBiEOG091G094Z.
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.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 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

        10         20         30         40         50
MWQLWASLCC LLVLANARSR PSFHPLSDEL VNYVNKRNTT WQAGHNFYNV
60 70 80 90 100
DMSYLKRLCG TFLGGPKPPQ RVMFTEDLKL PASFDAREQW PQCPTIKEIR
110 120 130 140 150
DQGSCGSCWA FGAVEAISDR ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC
160 170 180 190 200
NGGYPAEAWN FWTRKGLVSG GLYESHVGCR PYSIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM AEIYKNGPVE
260 270 280 290 300
GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW
310 320 330
NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI
Length:339
Mass (Da):37,822
Last modified:June 21, 2005 - v3
Checksum:i0FC818EA4C1F6D90
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti228N → D AA sequence (PubMed:3972105).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00672426L → V.3 PublicationsCorresponds to variant rs12338dbSNPEnsembl.1
Natural variantiVAR_05151153S → G.1 PublicationCorresponds to variant rs1803250dbSNPEnsembl.1
Natural variantiVAR_05151291P → L.Corresponds to variant rs11548596dbSNPEnsembl.1
Natural variantiVAR_014696235S → N.Corresponds to variant rs17573dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001908.4.
NP_680090.1. NM_147780.3.
NP_680091.1. NM_147781.3.
NP_680092.1. NM_147782.3.
NP_680093.1. NM_147783.3.
XP_006716307.1. XM_006716244.2.
XP_006716308.1. XM_006716245.2.
XP_011542114.1. XM_011543812.2.
XP_016868586.1. XM_017013097.1.
XP_016868587.1. XM_017013098.1.
XP_016868588.1. XM_017013099.1.
XP_016868589.1. XM_017013100.1.
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.
UCSCiuc003wun.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001908.4.
NP_680090.1. NM_147780.3.
NP_680091.1. NM_147781.3.
NP_680092.1. NM_147782.3.
NP_680093.1. NM_147783.3.
XP_006716307.1. XM_006716244.2.
XP_006716308.1. XM_006716245.2.
XP_011542114.1. XM_011543812.2.
XP_016868586.1. XM_017013097.1.
XP_016868587.1. XM_017013098.1.
XP_016868588.1. XM_017013099.1.
XP_016868589.1. XM_017013100.1.
UniGeneiHs.520898.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107888. 35 interactors.
DIPiDIP-42785N.
IntActiP07858. 39 interactors.
MINTiMINT-1397666.
STRINGi9606.ENSP00000342070.

Chemistry databases

BindingDBiP07858.
ChEMBLiCHEMBL4072.
GuidetoPHARMACOLOGYi2343.

Protein family/group databases

MEROPSiC01.060.

PTM databases

iPTMnetiP07858.
PhosphoSitePlusiP07858.
SwissPalmiP07858.

Polymorphism and mutation databases

BioMutaiCTSB.
DMDMi68067549.

2D gel databases

SWISS-2DPAGEP07858.
UCD-2DPAGEP07858.

Proteomic databases

EPDiP07858.
MaxQBiP07858.
PaxDbiP07858.
PeptideAtlasiP07858.
PRIDEiP07858.
TopDownProteomicsiP07858.

Protocols and materials databases

DNASUi1508.
Structural Biology KnowledgebaseSearch...

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.
UCSCiuc003wun.4. human.

Organism-specific databases

CTDi1508.
DisGeNETi1508.
GeneCardsiCTSB.
H-InvDBHIX0007320.
HGNCiHGNC:2527. CTSB.
HPAiCAB000457.
HPA018156.
MIMi116810. gene.
neXtProtiNX_P07858.
OpenTargetsiENSG00000164733.
PharmGKBiPA27027.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00780000121937.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP07858.
KOiK01363.
OMAiEDMLTCC.
OrthoDBiEOG091G094Z.
PhylomeDBiP07858.
TreeFamiTF314576.

Enzyme and pathway databases

BioCyciZFISH:HS09125-MONOMER.
BRENDAi3.4.22.1. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1679131. Trafficking and processing of endosomal TLR.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiCTSB. human.
EvolutionaryTraceiP07858.
GeneWikiiCathepsin_B.
GenomeRNAii1508.
PMAP-CutDBP07858.
PROiP07858.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164733.
CleanExiHS_CTSB.
ExpressionAtlasiP07858. baseline and differential.
GenevisibleiP07858. HS.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 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...

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: November 30, 2016
This is version 198 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

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 one 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.