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Reviewed, UniProtKB/Swiss-Prot P07858 (CATB_HUMAN)

Last modified June 10, 2008. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesCathepsin B [Precursor]
Also known as:
     EC 3.4.22.1
     Cathepsin B1
     APP secretase
     APPS
Cleaved into:
     Cathepsin B light chain
     Cathepsin B heavy chain
Gene names
Name: CTSB
Synonyms: CPSB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.

Catalytic activity

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.

Subunit structure

Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.

Subcellular location

Lysosome. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Sequence similarities

Belongs to the peptidase C1 family.

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Ontologies

Keywords

   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMGlycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processproteolysis Ref.1

Traceable author statement. Source: ProtInc

regulation of apoptosis

Traceable author statement. Source: UniProtKB

   Cellular componentintracellular

Traceable author statement. Source: ProtInc

   Molecular functioncathepsin B activity

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 7962Activation peptide
Chain80 – 333254Cathepsin B
Chain80 – 12647Cathepsin B light chain
Chain129 – 333205Cathepsin B heavy chain
Propeptide334 – 3396

Sites

Active site1081
Active site2781
Active site2981

Amino acid modifications

Glycosylation1921N-linked (GlcNAc...)
Disulfide bond93 ↔ 122
Disulfide bond105 ↔ 150
Disulfide bond141 ↔ 207
Disulfide bond142 ↔ 146
Disulfide bond179 ↔ 211
Disulfide bond187 ↔ 198

Natural variations

Natural variant261L → V: dbSNP rs12338.
Natural variant2351S → N: dbSNP rs17573.

Experimental info

Sequence conflict531S → G in AAH10240. Ref.3
Sequence conflict2281N → D AA sequence Ref.4

Secondary structure

1 ......................................... 339
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P07858-1 [UniParc].

Last modified June 21, 2005. Version 3.
Checksum: 0FC818EA4C1F6D90

FASTA33937,822
        10         20         30         40         50         60 
MWQLWASLCC LLVLANARSR PSFHPLSDEL VNYVNKRNTT WQAGHNFYNV DMSYLKRLCG 

        70         80         90        100        110        120 
TFLGGPKPPQ RVMFTEDLKL PASFDAREQW PQCPTIKEIR DQGSCGSCWA FGAVEAISDR 

       130        140        150        160        170        180 
ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC NGGYPAEAWN FWTRKGLVSG GLYESHVGCR 

       190        200        210        220        230        240 
PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM 

       250        260        270        280        290        300 
AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW 

       310        320        330 
NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI

« Hide

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References

« Hide 'large scale' references
[1]"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: 3463996] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-26.
[2]"Human gastric adenocarcinoma cathepsin B: isolation and sequencing of full-length cDNAs and polymorphisms of the gene."
Cao L., Taggart R.T., Berquin I.M., Moin K., Fong D., Sloane B.F.
Gene 139:163-169(1994) [PubMed: 8112600] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Gastric carcinoma.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-26.
Tissue: Brain and Placenta.
[4]"Amino acid sequence of human liver cathepsin B."
Ritonja A., Popovic T., Turk V., Wiedenmann K., Machleidt W.
FEBS Lett. 181:169-172(1985) [PubMed: 3972105] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-126 AND 129-333.
Tissue: Liver.
[5]"Human tumour cathepsin B. Comparison with normal liver cathepsin B."
Moin K., Day N.A., Sameni M., Hasnain S., Hirama T., Sloane B.F.
Biochem. J. 285:427-434(1992) [PubMed: 1637335] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-91 AND 129-139.
Tissue: Liver.
[6]"Isolation of a cDNA clone for the human lysosomal proteinase cathepsin B."
Fong D., Calhoun D.H., Hsieh W.-T., Lee B., Wells R.D.
Proc. Natl. Acad. Sci. U.S.A. 83:2909-2913(1986) [PubMed: 3010323] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-339.
[7]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity."
Musil D., Zucic D., Turk D., Engh R.A., Mayr I., Huber R., Popovic T., Turk V., Towatari T., Katunuma N., Bode W.
EMBO J. 10:2321-2330(1991) [PubMed: 1868826] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[10]"Crystal structures of human procathepsin B at 3.2- and 3.3-A resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide."
Turk D., Podobnik M., Kuhelj R., Dolinar M., Turk V.
FEBS Lett. 384:211-214(1996) [PubMed: 8617355] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[11]"Crystal structure of the wild-type human procathepsin B at 2.5-A resolution reveals the native active site of a papain-like cysteine protease zymogen."
Podobnik M., Kuhelj R., Turk V., Turk D.
J. Mol. Biol. 271:774-788(1997) [PubMed: 9299326] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

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Cross-references

Sequence databases

M14221 mRNA. Translation: AAA52129.1.
L16510 mRNA. Translation: AAC37547.1.
BC010240 mRNA. Translation: AAH10240.1.
BC095408 mRNA. Translation: AAH95408.1.
M13230 mRNA. Translation: AAA52125.1.
PIRKHHUB. A26498.
RefSeqNP_001899.1.
NP_680090.1.
NP_680091.1.
NP_680092.1.
NP_680093.1.
UniGeneHs.520898

3D structure databases

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[»]
3PBHX-ray2.50A18-333[»]
SMRP07858. Positions 18-333.
ModBaseSearch...

Protein family/group databases

MEROPSC01.060.

PTM databases

PhosphoSiteP07858.

2-D gel databases

SWISS-2DPAGEP07858.

Proteomic databases

PeptideAtlasP07858.

Genome annotation databases

EnsemblENSG00000164733. Homo sapiens. [Contig view]
GeneID1508.
KEGGhsa:1508.

Organism-specific databases

H-InvDBHIX0007320.
HGNCHGNC:2527. CTSB.
HPACAB000457.
MIM116810. gene.
PharmGKBPA27027.
GenAtlasSearch...
GeneCardsSearch...
GeneLynxSearch...

Phylogenomic databases

HOGENOMP07858.
HOVERGENP07858.

Gene expression databases

ArrayExpressP07858.
CleanExHS_CTSB.
GermOnlineENSG00000164733. Homo sapiens.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR015643. Peptidase_C1A_cathepsin-B.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERPTHR12411:SF16. CathepsinB_like. 1 hit.
PTHR12411. Peptidase_C1A. 1 hit.
PfamPF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
BLOCKSSearch...

Other Resources

LinkHubP07858.
SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameCATB_HUMAN
AccessionPrimary (citable) accession number: P07858
Secondary accession number(s): Q503A6, Q96D87
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: June 21, 2005
Last modified: June 10, 2008
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents