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P07858

- CATB_HUMAN

UniProt

P07858 - CATB_HUMAN

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Protein

Cathepsin B

Gene

CTSB

Organism
Homo sapiens (Human)
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
Active sitei278 – 2781
Active sitei298 – 2981

GO - Molecular functioni

  1. collagen binding Source: BHF-UCL
  2. cysteine-type endopeptidase activity Source: BHF-UCL
  3. cysteine-type peptidase activity Source: UniProtKB
  4. peptidase activity Source: BHF-UCL
  5. proteoglycan binding Source: BHF-UCL

GO - Biological processi

  1. cellular response to thyroid hormone stimulus Source: UniProtKB
  2. collagen catabolic process Source: BHF-UCL
  3. decidualization Source: Ensembl
  4. epithelial cell differentiation Source: UniProt
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. innate immune response Source: Reactome
  8. proteolysis Source: UniProtKB
  9. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
  10. regulation of apoptotic process Source: UniProtKB
  11. regulation of catalytic activity Source: InterPro
  12. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.1. 2681.
ReactomeiREACT_118632. Trafficking and processing of endosomal TLR.
REACT_121399. MHC class II antigen presentation.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.

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
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:2527. CTSB.

Subcellular locationi

Lysosome. Melanosome. Secretedextracellular space By similarity
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. endolysosome lumen Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProtKB
  5. intracellular Source: ProtInc
  6. intracellular membrane-bounded organelle Source: HPA
  7. lysosome Source: UniProtKB
  8. mitochondrion Source: Ensembl
  9. nucleolus Source: HPA
  10. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27027.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 7962Activation peptidePRO_0000026143Add
BLAST
Chaini80 – 333254Cathepsin BPRO_0000026144Add
BLAST
Chaini80 – 12647Cathepsin B light chainPRO_0000026145Add
BLAST
Chaini129 – 333205Cathepsin B heavy chainPRO_0000026146Add
BLAST
Propeptidei334 – 3396PRO_0000026147

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi93 ↔ 1221 Publication
Disulfide bondi105 ↔ 1501 Publication
Disulfide bondi141 ↔ 2071 Publication
Disulfide bondi142 ↔ 1461 Publication
Disulfide bondi179 ↔ 2111 Publication
Disulfide bondi187 ↔ 1981 Publication
Glycosylationi192 – 1921N-linked (GlcNAc...)1 Publication
Modified residuei220 – 2201N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP07858.
PaxDbiP07858.
PeptideAtlasiP07858.
PRIDEiP07858.

2D gel databases

SWISS-2DPAGEP07858.
UCD-2DPAGEP07858.

PTM databases

PhosphoSiteiP07858.

Miscellaneous databases

PMAP-CutDBP07858.

Expressioni

Gene expression databases

BgeeiP07858.
CleanExiHS_CTSB.
ExpressionAtlasiP07858. baseline and differential.
GenevestigatoriP07858.

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

Protein-protein interaction databases

BioGridi107888. 30 interactions.
DIPiDIP-42785N.
IntActiP07858. 23 interactions.
MINTiMINT-1397666.
STRINGi9606.ENSP00000342070.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi82 – 854Combined sources
Helixi86 – 894Combined sources
Helixi94 – 974Combined sources
Beta strandi104 – 1063Combined sources
Helixi108 – 12417Combined sources
Turni125 – 1273Combined sources
Beta strandi131 – 1333Combined sources
Helixi135 – 1417Combined sources
Helixi143 – 1464Combined sources
Helixi149 – 1513Combined sources
Helixi155 – 16410Combined sources
Beta strandi167 – 1704Combined sources
Turni173 – 1753Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi193 – 1953Combined sources
Helixi220 – 2223Combined sources
Beta strandi226 – 2316Combined sources
Helixi236 – 24611Combined sources
Beta strandi249 – 2568Combined sources
Helixi257 – 2615Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi274 – 28815Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi302 – 3043Combined sources
Beta strandi309 – 3135Combined sources
Turni314 – 3174Combined sources
Helixi318 – 3203Combined sources
Turni321 – 3233Combined sources
Beta strandi326 – 3305Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 18-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07858.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP07858.
KOiK01363.
OMAiCTGEGDT.
OrthoDBiEOG7034HR.
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.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281N → D AA sequence (PubMed:3972105)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261L → V.3 Publications
Corresponds to variant rs12338 [ dbSNP | Ensembl ].
VAR_006724
Natural varianti53 – 531S → G.1 Publication
Corresponds to variant rs1803250 [ dbSNP | Ensembl ].
VAR_051511
Natural varianti91 – 911P → L.
Corresponds to variant rs11548596 [ dbSNP | Ensembl ].
VAR_051512
Natural varianti235 – 2351S → N.
Corresponds to variant rs17573 [ dbSNP | Ensembl ].
VAR_014696

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_001908.3.
NP_680090.1. NM_147780.2.
NP_680091.1. NM_147781.2.
NP_680092.1. NM_147782.2.
NP_680093.1. NM_147783.2.
XP_006716307.1. XM_006716244.1.
XP_006716308.1. XM_006716245.1.
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.
UCSCiuc003wum.3. human.

Polymorphism databases

DMDMi68067549.

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 .
CCDSi CCDS5986.1.
PIRi A26498. KHHUB.
RefSeqi NP_001899.1. NM_001908.3.
NP_680090.1. NM_147780.2.
NP_680091.1. NM_147781.2.
NP_680092.1. NM_147782.2.
NP_680093.1. NM_147783.2.
XP_006716307.1. XM_006716244.1.
XP_006716308.1. XM_006716245.1.
UniGenei Hs.520898.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CSB X-ray 2.00 A/D 80-126 [» ]
B/E 129-333 [» ]
1GMY X-ray 1.90 A/B/C 79-339 [» ]
1HUC X-ray 2.10 A/C 80-126 [» ]
B/D 129-333 [» ]
1PBH X-ray 3.20 A 18-333 [» ]
2IPP X-ray 2.15 A 80-126 [» ]
B 129-333 [» ]
2PBH X-ray 3.30 A 18-333 [» ]
3AI8 X-ray 2.11 A/B 78-333 [» ]
3CBJ X-ray 1.80 A 74-339 [» ]
3CBK X-ray 2.67 A 74-339 [» ]
3K9M X-ray 2.61 A/B 80-333 [» ]
3PBH X-ray 2.50 A 18-333 [» ]
ProteinModelPortali P07858.
SMRi P07858. Positions 18-333.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107888. 30 interactions.
DIPi DIP-42785N.
IntActi P07858. 23 interactions.
MINTi MINT-1397666.
STRINGi 9606.ENSP00000342070.

Chemistry

BindingDBi P07858.
ChEMBLi CHEMBL2111396.
GuidetoPHARMACOLOGYi 2343.

Protein family/group databases

MEROPSi C01.060.

PTM databases

PhosphoSitei P07858.

Polymorphism databases

DMDMi 68067549.

2D gel databases

SWISS-2DPAGE P07858.
UCD-2DPAGE P07858.

Proteomic databases

MaxQBi P07858.
PaxDbi P07858.
PeptideAtlasi P07858.
PRIDEi P07858.

Protocols and materials databases

DNASUi 1508.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000345125 ; ENSP00000342070 ; ENSG00000164733 .
ENST00000353047 ; ENSP00000345672 ; ENSG00000164733 .
ENST00000453527 ; ENSP00000409917 ; ENSG00000164733 .
ENST00000530640 ; ENSP00000435105 ; ENSG00000164733 .
ENST00000531089 ; ENSP00000433215 ; ENSG00000164733 .
ENST00000533455 ; ENSP00000432244 ; ENSG00000164733 .
ENST00000534510 ; ENSP00000434217 ; ENSG00000164733 .
GeneIDi 1508.
KEGGi hsa:1508.
UCSCi uc003wum.3. human.

Organism-specific databases

CTDi 1508.
GeneCardsi GC08M011700.
H-InvDB HIX0007320.
HGNCi HGNC:2527. CTSB.
HPAi CAB000457.
HPA018156.
MIMi 116810. gene.
neXtProti NX_P07858.
PharmGKBi PA27027.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4870.
GeneTreei ENSGT00760000118871.
HOGENOMi HOG000241341.
HOVERGENi HBG003480.
InParanoidi P07858.
KOi K01363.
OMAi CTGEGDT.
OrthoDBi EOG7034HR.
PhylomeDBi P07858.
TreeFami TF314576.

Enzyme and pathway databases

BRENDAi 3.4.22.1. 2681.
Reactomei REACT_118632. Trafficking and processing of endosomal TLR.
REACT_121399. MHC class II antigen presentation.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.

Miscellaneous databases

ChiTaRSi CTSB. human.
EvolutionaryTracei P07858.
GeneWikii Cathepsin_B.
GenomeRNAii 1508.
NextBioi 6235.
PMAP-CutDB P07858.
PROi P07858.
SOURCEi Search...

Gene expression databases

Bgeei P07858.
CleanExi HS_CTSB.
ExpressionAtlasi P07858. baseline and differential.
Genevestigatori P07858.

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. "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], 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Gastric carcinoma.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-26.
    Tissue: Esophagus.
  4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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], VARIANTS VAL-26 AND GLY-53.
    Tissue: Brain and Placenta.
  7. Cited for: PROTEIN SEQUENCE OF 80-126 AND 129-333.
    Tissue: Liver.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 80-91 AND 129-139.
    Tissue: Liver.
  9. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-339.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  12. "Epileptic and developmental disorders of the speech cortex: ligand/receptor interaction of wild-type and mutant SRPX2 with the plasminogen activator receptor uPAR."
    Royer-Zemmour B., Ponsole-Lenfant M., Gara H., Roll P., Leveque C., Massacrier A., Ferracci G., Cillario J., Robaglia-Schlupp A., Vincentelli R., Cau P., Szepetowski P.
    Hum. Mol. Genet. 17:3617-3630(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRPX2.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  15. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
  16. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

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 26, 2014
This is version 179 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

External Data

Dasty 3