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Protein

Cathepsin B

Gene

CTSB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 Publication1
Active sitei2781 Publication1
Active sitei2981 Publication1

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
  • neutrophil degranulation Source: Reactome
  • 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
  • viral entry into host cell Source: Ensembl

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000164733.20
HGNCiHGNC:2527 CTSB
MIMi116810 gene
neXtProtiNX_P07858

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi1508
MalaCardsiCTSB
OpenTargetsiENSG00000164733
PharmGKBiPA27027

Chemistry databases

ChEMBLiCHEMBL4072
DrugBankiDB02108 2-Aminoethanimidic Acid
DB03329 2-Pyridinethiol
DB02148 3-Amino-4-Oxybenzyl-2-Butanone
DB02685 3-Methylphenylalanine
DB03588 Diphenylacetic Acid
DB02855 N-(3-Propylcarbamoyloxirane-2-Carbonyl)-Isoleucyl-Proline
DB04126 N-[1-Hydroxycarboxyethyl-Carbonyl]Leucylamino-2-Methyl-Butane
GuidetoPHARMACOLOGYi2343

Polymorphism and mutation databases

BioMutaiCTSB
DMDMi68067549

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002614318 – 79Activation peptide1 PublicationAdd BLAST62
ChainiPRO_000002614480 – 333Cathepsin BAdd BLAST254
ChainiPRO_000002614580 – 126Cathepsin B light chain1 PublicationAdd BLAST47
ChainiPRO_0000026146129 – 333Cathepsin B heavy chain1 PublicationAdd 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...) asparagine1 Publication1
Modified residuei220N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP07858
MaxQBiP07858
PaxDbiP07858
PeptideAtlasiP07858
PRIDEiP07858
TopDownProteomicsiP07858

2D gel databases

SWISS-2DPAGEiP07858
UCD-2DPAGEiP07858

PTM databases

iPTMnetiP07858
PhosphoSitePlusiP07858
SwissPalmiP07858

Miscellaneous databases

PMAP-CutDBiP07858

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. Directly interacts with SHKBP1 (PubMed:16733801).2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • proteoglycan binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107888, 39 interactors
DIPiDIP-42785N
IntActiP07858, 45 interactors
MINTiP07858
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 strandi20 – 22Combined sources3
Helixi28 – 37Combined sources10
Beta strandi40 – 43Combined sources4
Helixi52 – 57Combined sources6
Beta strandi69 – 72Combined sources4
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 – 145Combined sources3
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
Helixi259 – 261Combined sources3
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[»]
5MBLX-ray1.81A78-333[»]
5MBMX-ray2.76A/B78-333[»]
6AY2X-ray1.60A/B79-333[»]
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
GeneTreeiENSGT00900000140859
HOGENOMiHOG000241341
HOVERGENiHBG003480
InParanoidiP07858
KOiK01363
OMAiHCGIESS
OrthoDBiEOG091G094Z
PhylomeDBiP07858
TreeFamiTF314576

Family and domain databases

InterProiView protein in InterPro
IPR025661 Pept_asp_AS
IPR000169 Pept_cys_AS
IPR025660 Pept_his_AS
IPR013128 Peptidase_C1A
IPR000668 Peptidase_C1A_C
IPR012599 Propeptide_C1A
PANTHERiPTHR12411 PTHR12411, 1 hit
PfamiView protein in Pfam
PF00112 Peptidase_C1, 1 hit
PF08127 Propeptide_C1, 1 hit
PRINTSiPR00705 PAPAIN
SMARTiView protein in SMART
SM00645 Pept_C1, 1 hit
PROSITEiView protein in PROSITE
PS00640 THIOL_PROTEASE_ASN, 1 hit
PS00139 THIOL_PROTEASE_CYS, 1 hit
PS00639 THIOL_PROTEASE_HIS, 1 hit

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 → V3 PublicationsCorresponds to variant dbSNP:rs12338Ensembl.1
Natural variantiVAR_05151153S → G1 PublicationCorresponds to variant dbSNP:rs1803250Ensembl.1
Natural variantiVAR_05151291P → L. Corresponds to variant dbSNP:rs11548596Ensembl.1
Natural variantiVAR_014696235S → N. Corresponds to variant dbSNP:rs17573Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiCATB_HUMAN
AccessioniPrimary (citable) accession number: P07858
Secondary accession number(s): B3KQR5
, B3KRR5, Q503A6, Q96D87
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 21, 2005
Last modified: May 23, 2018
This is version 211 of the entry and version 3 of the sequence. See 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

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