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Cathepsin B (EC 3.4.22.1) (APP secretase) (APPS) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain]

 CATB_HUMAN              Reviewed;         339 AA.
P07858; B3KQR5; B3KRR5; Q503A6; Q96D87;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 3.
23-MAY-2018, entry version 211.
RecName: Full=Cathepsin B;
EC=3.4.22.1;
AltName: Full=APP secretase;
Short=APPS;
AltName: Full=Cathepsin B1;
Contains:
RecName: Full=Cathepsin B light chain;
Contains:
RecName: Full=Cathepsin B heavy chain;
Flags: Precursor;
Name=CTSB; Synonyms=CPSB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-26.
PubMed=3463996; DOI=10.1073/pnas.83.20.7721;
Chan S.J., San Segundo B., McCormick M.B., Steiner D.F.;
"Nucleotide and predicted amino acid sequences of cloned human and
mouse preprocathepsin B cDNAs.";
Proc. Natl. Acad. Sci. U.S.A. 83:7721-7725(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Gastric carcinoma;
PubMed=8112600; DOI=10.1016/0378-1119(94)90750-1;
Cao L., Taggart R.T., Berquin I.M., Moin K., Fong D., Sloane B.F.;
"Human gastric adenocarcinoma cathepsin B: isolation and sequencing of
full-length cDNAs and polymorphisms of the gene.";
Gene 139:163-169(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-26.
TISSUE=Esophagus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
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.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-26 AND
GLY-53.
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 80-126 AND 129-333.
TISSUE=Liver;
PubMed=3972105; DOI=10.1016/0014-5793(85)81136-4;
Ritonja A., Popovic T., Turk V., Wiedenmann K., Machleidt W.;
"Amino acid sequence of human liver cathepsin B.";
FEBS Lett. 181:169-172(1985).
[8]
PROTEIN SEQUENCE OF 80-91 AND 129-139.
TISSUE=Liver;
PubMed=1637335; DOI=10.1042/bj2850427;
Moin K., Day N.A., Sameni M., Hasnain S., Hirama T., Sloane B.F.;
"Human tumour cathepsin B. Comparison with normal liver cathepsin B.";
Biochem. J. 285:427-434(1992).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 131-339.
PubMed=3010323; DOI=10.1073/pnas.83.9.2909;
Fong D., Calhoun D.H., Hsieh W.-T., Lee B., Wells R.D.;
"Isolation of a cDNA clone for the human lysosomal proteinase
cathepsin B.";
Proc. Natl. Acad. Sci. U.S.A. 83:2909-2913(1986).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
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.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
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.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[12]
INTERACTION WITH SHKBP1, AND SUBCELLULAR LOCATION.
PubMed=16733801; DOI=10.1007/s11010-006-9214-7;
Liu J.P., Liu N.S., Yuan H.Y., Guo Q., Lu H., Li Y.Y.;
"Human homologue of SETA binding protein 1 interacts with cathepsin B
and participates in TNF-Induced apoptosis in ovarian cancer cells.";
Mol. Cell. Biochem. 292:189-195(2006).
[13]
INTERACTION WITH SRPX2.
PubMed=18718938; DOI=10.1093/hmg/ddn256;
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.;
"Epileptic and developmental disorders of the speech cortex:
ligand/receptor interaction of wild-type and mutant SRPX2 with the
plasminogen activator receptor uPAR.";
Hum. Mol. Genet. 17:3617-3630(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
PubMed=1868826;
Musil D., Zucic D., Turk D., Engh R.A., Mayr I., Huber R., Popovic T.,
Turk V., Towatari T., Katunuma N., Bode W.;
"The refined 2.15 A X-ray crystal structure of human liver cathepsin
B: the structural basis for its specificity.";
EMBO J. 10:2321-2330(1991).
[18]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
PubMed=8617355; DOI=10.1016/0014-5793(96)00309-2;
Turk D., Podobnik M., Kuhelj R., Dolinar M., Turk V.;
"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.";
FEBS Lett. 384:211-214(1996).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND ACTIVE SITE.
PubMed=9299326; DOI=10.1006/jmbi.1997.1218;
Podobnik M., Kuhelj R., Turk V., Turk D.;
"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.";
J. Mol. Biol. 271:774-788(1997).
-!- 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: Dimer of a heavy chain and a light chain cross-linked by
a disulfide bond. Interacts with SRPX2. Directly interacts with
SHKBP1 (PubMed:16733801). {ECO:0000269|PubMed:16733801,
ECO:0000269|PubMed:18718938}.
-!- INTERACTION:
Q6UY14:ADAMTSL4; NbExp=3; IntAct=EBI-715062, EBI-742002;
P02760:AMBP; NbExp=4; IntAct=EBI-715062, EBI-2115136;
P40692:MLH1; NbExp=7; IntAct=EBI-715062, EBI-744248;
Q9NYA1:SPHK1; NbExp=4; IntAct=EBI-715062, EBI-985303;
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:16733801}.
Melanosome. Secreted, extracellular space {ECO:0000250}.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CTSBID40202ch8p23.html";
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EMBL; M14221; AAA52129.1; -; mRNA.
EMBL; L16510; AAC37547.1; -; mRNA.
EMBL; AK092070; BAG52477.1; -; mRNA.
EMBL; AK075393; BAG52127.1; -; mRNA.
EMBL; CH471157; EAW65630.1; -; Genomic_DNA.
EMBL; BC010240; AAH10240.1; -; mRNA.
EMBL; BC095408; AAH95408.1; -; mRNA.
EMBL; M13230; AAA52125.1; -; mRNA.
CCDS; CCDS5986.1; -.
PIR; A26498; KHHUB.
RefSeq; NP_001899.1; NM_001908.4.
RefSeq; NP_680090.1; NM_147780.3.
RefSeq; NP_680091.1; NM_147781.3.
RefSeq; NP_680092.1; NM_147782.3.
RefSeq; NP_680093.1; NM_147783.3.
RefSeq; XP_006716307.1; XM_006716244.2.
RefSeq; XP_006716308.1; XM_006716245.2.
RefSeq; XP_011542114.1; XM_011543812.2.
RefSeq; XP_016868586.1; XM_017013097.1.
RefSeq; XP_016868587.1; XM_017013098.1.
RefSeq; XP_016868588.1; XM_017013099.1.
RefSeq; XP_016868589.1; XM_017013100.1.
UniGene; Hs.520898; -.
PDB; 1CSB; X-ray; 2.00 A; A/D=80-126, B/E=129-333.
PDB; 1GMY; X-ray; 1.90 A; A/B/C=79-339.
PDB; 1HUC; X-ray; 2.10 A; A/C=80-126, B/D=129-333.
PDB; 1PBH; X-ray; 3.20 A; A=18-333.
PDB; 2IPP; X-ray; 2.15 A; A=80-126, B=129-333.
PDB; 2PBH; X-ray; 3.30 A; A=18-333.
PDB; 3AI8; X-ray; 2.11 A; A/B=78-333.
PDB; 3CBJ; X-ray; 1.80 A; A=74-339.
PDB; 3CBK; X-ray; 2.67 A; A=74-339.
PDB; 3K9M; X-ray; 2.61 A; A/B=80-333.
PDB; 3PBH; X-ray; 2.50 A; A=18-333.
PDB; 5MBL; X-ray; 1.81 A; A=78-333.
PDB; 5MBM; X-ray; 2.76 A; A/B=78-333.
PDB; 6AY2; X-ray; 1.60 A; A/B=79-333.
PDBsum; 1CSB; -.
PDBsum; 1GMY; -.
PDBsum; 1HUC; -.
PDBsum; 1PBH; -.
PDBsum; 2IPP; -.
PDBsum; 2PBH; -.
PDBsum; 3AI8; -.
PDBsum; 3CBJ; -.
PDBsum; 3CBK; -.
PDBsum; 3K9M; -.
PDBsum; 3PBH; -.
PDBsum; 5MBL; -.
PDBsum; 5MBM; -.
PDBsum; 6AY2; -.
ProteinModelPortal; P07858; -.
SMR; P07858; -.
BioGrid; 107888; 39.
DIP; DIP-42785N; -.
IntAct; P07858; 45.
MINT; P07858; -.
STRING; 9606.ENSP00000342070; -.
BindingDB; P07858; -.
ChEMBL; CHEMBL4072; -.
DrugBank; DB02108; 2-Aminoethanimidic Acid.
DrugBank; DB03329; 2-Pyridinethiol.
DrugBank; DB02148; 3-Amino-4-Oxybenzyl-2-Butanone.
DrugBank; DB02685; 3-Methylphenylalanine.
DrugBank; DB03588; Diphenylacetic Acid.
DrugBank; DB02855; N-(3-Propylcarbamoyloxirane-2-Carbonyl)-Isoleucyl-Proline.
DrugBank; DB04126; N-[1-Hydroxycarboxyethyl-Carbonyl]Leucylamino-2-Methyl-Butane.
GuidetoPHARMACOLOGY; 2343; -.
MEROPS; C01.060; -.
iPTMnet; P07858; -.
PhosphoSitePlus; P07858; -.
SwissPalm; P07858; -.
BioMuta; CTSB; -.
DMDM; 68067549; -.
SWISS-2DPAGE; P07858; -.
UCD-2DPAGE; P07858; -.
EPD; P07858; -.
MaxQB; P07858; -.
PaxDb; P07858; -.
PeptideAtlas; P07858; -.
PRIDE; P07858; -.
TopDownProteomics; P07858; -.
DNASU; 1508; -.
Ensembl; ENST00000345125; ENSP00000342070; ENSG00000164733.
Ensembl; ENST00000353047; ENSP00000345672; ENSG00000164733.
Ensembl; ENST00000453527; ENSP00000409917; ENSG00000164733.
Ensembl; ENST00000530640; ENSP00000435105; ENSG00000164733.
Ensembl; ENST00000531089; ENSP00000433215; ENSG00000164733.
Ensembl; ENST00000533455; ENSP00000432244; ENSG00000164733.
Ensembl; ENST00000534510; ENSP00000434217; ENSG00000164733.
GeneID; 1508; -.
KEGG; hsa:1508; -.
UCSC; uc003wun.4; human.
CTD; 1508; -.
DisGeNET; 1508; -.
EuPathDB; HostDB:ENSG00000164733.20; -.
GeneCards; CTSB; -.
H-InvDB; HIX0007320; -.
HGNC; HGNC:2527; CTSB.
HPA; CAB000457; -.
HPA; HPA018156; -.
MalaCards; CTSB; -.
MIM; 116810; gene.
neXtProt; NX_P07858; -.
OpenTargets; ENSG00000164733; -.
PharmGKB; PA27027; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140859; -.
HOGENOM; HOG000241341; -.
HOVERGEN; HBG003480; -.
InParanoid; P07858; -.
KO; K01363; -.
OMA; HCGIESS; -.
OrthoDB; EOG091G094Z; -.
PhylomeDB; P07858; -.
TreeFam; TF314576; -.
BRENDA; 3.4.22.1; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1679131; Trafficking and processing of endosomal TLR.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; CTSB; human.
EvolutionaryTrace; P07858; -.
GeneWiki; Cathepsin_B; -.
GenomeRNAi; 1508; -.
PMAP-CutDB; P07858; -.
PRO; PR:P07858; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164733; -.
CleanEx; HS_CTSB; -.
ExpressionAtlas; P07858; baseline and differential.
Genevisible; P07858; HS.
GO; GO:0036021; C:endolysosome lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005622; C:intracellular; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005518; F:collagen binding; IDA:BHF-UCL.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL.
GO; GO:0043394; F:proteoglycan binding; IPI:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; IDA:BHF-UCL.
GO; GO:0046697; P:decidualization; IEA:Ensembl.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR012599; Propeptide_C1A.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF00112; Peptidase_C1; 1.
Pfam; PF08127; Propeptide_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Lysosome; Polymorphism; Protease; Reference proteome; Secreted;
Signal; Thiol protease; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 79 Activation peptide.
{ECO:0000269|PubMed:3972105}.
/FTId=PRO_0000026143.
CHAIN 80 333 Cathepsin B.
/FTId=PRO_0000026144.
CHAIN 80 126 Cathepsin B light chain.
{ECO:0000269|PubMed:3972105}.
/FTId=PRO_0000026145.
CHAIN 129 333 Cathepsin B heavy chain.
{ECO:0000269|PubMed:3972105}.
/FTId=PRO_0000026146.
PROPEP 334 339
/FTId=PRO_0000026147.
ACT_SITE 108 108 {ECO:0000269|PubMed:9299326}.
ACT_SITE 278 278 {ECO:0000269|PubMed:9299326}.
ACT_SITE 298 298 {ECO:0000269|PubMed:9299326}.
MOD_RES 220 220 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10605}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3463996}.
DISULFID 93 122 {ECO:0000269|PubMed:1868826}.
DISULFID 105 150 {ECO:0000269|PubMed:1868826}.
DISULFID 141 207 {ECO:0000269|PubMed:1868826}.
DISULFID 142 146 {ECO:0000269|PubMed:1868826}.
DISULFID 179 211 {ECO:0000269|PubMed:1868826}.
DISULFID 187 198 {ECO:0000269|PubMed:1868826}.
VARIANT 26 26 L -> V (in dbSNP:rs12338).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3463996}.
/FTId=VAR_006724.
VARIANT 53 53 S -> G (in dbSNP:rs1803250).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_051511.
VARIANT 91 91 P -> L (in dbSNP:rs11548596).
/FTId=VAR_051512.
VARIANT 235 235 S -> N (in dbSNP:rs17573).
/FTId=VAR_014696.
CONFLICT 228 228 N -> D (in Ref. 7; AA sequence).
{ECO:0000305}.
STRAND 20 22 {ECO:0000244|PDB:3PBH}.
HELIX 28 37 {ECO:0000244|PDB:3PBH}.
STRAND 40 43 {ECO:0000244|PDB:3PBH}.
HELIX 52 57 {ECO:0000244|PDB:3PBH}.
STRAND 69 72 {ECO:0000244|PDB:3PBH}.
STRAND 82 85 {ECO:0000244|PDB:1GMY}.
HELIX 86 89 {ECO:0000244|PDB:6AY2}.
HELIX 94 97 {ECO:0000244|PDB:6AY2}.
STRAND 104 106 {ECO:0000244|PDB:6AY2}.
HELIX 108 124 {ECO:0000244|PDB:6AY2}.
TURN 125 127 {ECO:0000244|PDB:6AY2}.
STRAND 131 133 {ECO:0000244|PDB:3K9M}.
HELIX 135 141 {ECO:0000244|PDB:6AY2}.
HELIX 143 145 {ECO:0000244|PDB:6AY2}.
HELIX 149 151 {ECO:0000244|PDB:1GMY}.
HELIX 155 164 {ECO:0000244|PDB:6AY2}.
STRAND 167 170 {ECO:0000244|PDB:3PBH}.
TURN 173 175 {ECO:0000244|PDB:3CBK}.
STRAND 178 180 {ECO:0000244|PDB:6AY2}.
STRAND 188 191 {ECO:0000244|PDB:6AY2}.
STRAND 193 195 {ECO:0000244|PDB:2IPP}.
HELIX 220 222 {ECO:0000244|PDB:6AY2}.
STRAND 226 231 {ECO:0000244|PDB:5MBL}.
HELIX 236 246 {ECO:0000244|PDB:6AY2}.
STRAND 249 256 {ECO:0000244|PDB:6AY2}.
HELIX 259 261 {ECO:0000244|PDB:6AY2}.
STRAND 264 267 {ECO:0000244|PDB:6AY2}.
STRAND 274 288 {ECO:0000244|PDB:6AY2}.
STRAND 291 297 {ECO:0000244|PDB:6AY2}.
STRAND 302 304 {ECO:0000244|PDB:2IPP}.
STRAND 309 313 {ECO:0000244|PDB:6AY2}.
TURN 314 317 {ECO:0000244|PDB:5MBM}.
HELIX 318 320 {ECO:0000244|PDB:6AY2}.
TURN 321 323 {ECO:0000244|PDB:3CBJ}.
STRAND 326 330 {ECO:0000244|PDB:5MBL}.
SEQUENCE 339 AA; 37822 MW; 0FC818EA4C1F6D90 CRC64;
MWQLWASLCC LLVLANARSR PSFHPLSDEL VNYVNKRNTT WQAGHNFYNV DMSYLKRLCG
TFLGGPKPPQ RVMFTEDLKL PASFDAREQW PQCPTIKEIR DQGSCGSCWA FGAVEAISDR
ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC NGGYPAEAWN FWTRKGLVSG GLYESHVGCR
PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM
AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW
NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI


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