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Cathepsin S (EC 3.4.22.27)

 CATS_HUMAN              Reviewed;         331 AA.
P25774; B4DWC9; D3DV05; Q5T5I0; Q6FHS5; Q9BUG3;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
21-FEB-2006, sequence version 3.
20-JUN-2018, entry version 185.
RecName: Full=Cathepsin S;
EC=3.4.22.27;
Flags: Precursor;
Name=CTSS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-161.
TISSUE=Alveolar macrophage;
PubMed=1373132;
Shi G.-P., Munger J.S., Meara J.P., Rich D.H., Chapman H.A.;
"Molecular cloning and expression of human alveolar macrophage
cathepsin S, an elastinolytic cysteine protease.";
J. Biol. Chem. 267:7258-7262(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=1377692;
Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B.,
Peters C.;
"Phylogenetic conservation of cysteine proteinases. Cloning and
expression of a cDNA coding for human cathepsin S.";
J. Biol. Chem. 267:13708-13713(1992).
[3]
SEQUENCE REVISION TO 211.
Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B.,
Peters C.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-161.
PubMed=8157683;
Shi G.-P., Webb A.C., Foster K.E., Knoll J.H.M., Lemere C.A.,
Munger J.S., Chapman H.A.;
"Human cathepsin S: chromosomal localization, gene structure, and
tissue distribution.";
J. Biol. Chem. 269:11530-11536(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TRP-113.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
TRP-113.
TISSUE=Placenta, and Synovium;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TRP-113.
TISSUE=Pancreas;
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).
[10]
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).
[11]
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).
[12]
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).
[13]
3D-STRUCTURE MODELING OF 115-331.
PubMed=9876921; DOI=10.1093/protein/11.11.1007;
Fengler A., Brandt W.;
"Three-dimensional structures of the cysteine proteases cathepsins K
and S deduced by knowledge-based modelling and active site
characteristics.";
Protein Eng. 11:1007-1013(1998).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 115-331.
PubMed=11856830; DOI=10.1107/S0907444901021825;
Turkenburg J.P., Lamers M.B., Brzozowski A.M., Wright L.M.,
Hubbard R.E., Sturt S.L., Williams D.H.;
"Structure of a Cys25-->Ser mutant of human cathepsin S.";
Acta Crystallogr. D 58:451-455(2002).
[15]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 112-331 IN COMPLEX WITH
INHIBITOR, AND DISULFIDE BONDS.
PubMed=17469812; DOI=10.1021/jm070111+;
Inagaki H., Tsuruoka H., Hornsby M., Lesley S.A., Spraggon G.,
Ellman J.A.;
"Characterization and optimization of selective, nonpeptidic
inhibitors of cathepsin S with an unprecedented binding mode.";
J. Med. Chem. 50:2693-2699(2007).
-!- FUNCTION: Thiol protease. Key protease responsible for the removal
of the invariant chain from MHC class II molecules. The bond-
specificity of this proteinase is in part similar to the
specificities of cathepsin L.
-!- CATALYTIC ACTIVITY: Similar to cathepsin L, but with much less
activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-
Arg-|-Xaa compound.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17469812}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P25774-1; Sequence=Displayed;
Name=2;
IsoId=P25774-2; Sequence=VSP_042712;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; S93414; AAB22005.1; -; mRNA.
EMBL; M86553; AAA35655.1; -; mRNA.
EMBL; M90696; AAC37592.1; -; mRNA.
EMBL; U07374; AAB60643.2; -; Genomic_DNA.
EMBL; U07370; AAB60643.2; JOINED; Genomic_DNA.
EMBL; U07371; AAB60643.2; JOINED; Genomic_DNA.
EMBL; U07372; AAB60643.2; JOINED; Genomic_DNA.
EMBL; U07373; AAB60643.2; JOINED; Genomic_DNA.
EMBL; CR541676; CAG46477.1; -; mRNA.
EMBL; AK301472; BAG62991.1; -; mRNA.
EMBL; AK314482; BAG37086.1; -; mRNA.
EMBL; AL356292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53518.1; -; Genomic_DNA.
EMBL; CH471121; EAW53519.1; -; Genomic_DNA.
EMBL; BC002642; AAH02642.1; -; mRNA.
CCDS; CCDS55634.1; -. [P25774-2]
CCDS; CCDS968.1; -. [P25774-1]
PIR; A42482; A42482.
RefSeq; NP_001186668.1; NM_001199739.1. [P25774-2]
RefSeq; NP_004070.3; NM_004079.4. [P25774-1]
UniGene; Hs.181301; -.
PDB; 1BXF; Model; -; A=115-331.
PDB; 1GLO; X-ray; 2.20 A; A=115-331.
PDB; 1MS6; X-ray; 1.90 A; A=115-331.
PDB; 1NPZ; X-ray; 2.00 A; A/B=115-331.
PDB; 1NQC; X-ray; 1.80 A; A=115-331.
PDB; 2C0Y; X-ray; 2.10 A; A=17-331.
PDB; 2F1G; X-ray; 1.90 A; A/B=112-331.
PDB; 2FQ9; X-ray; 1.65 A; A/B=114-331.
PDB; 2FRA; X-ray; 1.90 A; A/B=114-330.
PDB; 2FRQ; X-ray; 1.60 A; A/B=114-331.
PDB; 2FT2; X-ray; 1.70 A; A/B=114-331.
PDB; 2FUD; X-ray; 1.95 A; A/B=114-331.
PDB; 2FYE; X-ray; 2.20 A; A=115-331.
PDB; 2G6D; X-ray; 2.50 A; A=115-331.
PDB; 2G7Y; X-ray; 2.00 A; A/B=114-330.
PDB; 2H7J; X-ray; 1.50 A; A/B=112-331.
PDB; 2HH5; X-ray; 1.80 A; A/B=112-331.
PDB; 2HHN; X-ray; 1.55 A; A/B=112-331.
PDB; 2HXZ; X-ray; 1.90 A; A/B/C=112-331.
PDB; 2OP3; X-ray; 1.60 A; A/B=112-331.
PDB; 2R9M; X-ray; 1.97 A; A/B=115-331.
PDB; 2R9N; X-ray; 2.00 A; A/B=115-331.
PDB; 2R9O; X-ray; 2.00 A; A/B=115-331.
PDB; 3IEJ; X-ray; 2.18 A; A/B=115-331.
PDB; 3N3G; X-ray; 1.60 A; A/B=115-331.
PDB; 3N4C; X-ray; 1.90 A; A/B=115-331.
PDB; 3OVX; X-ray; 1.49 A; A/B=114-331.
PDB; 4P6E; X-ray; 1.80 A; A/B=109-331.
PDB; 4P6G; X-ray; 1.58 A; A/B/C/D=114-331.
PDB; 5QBU; X-ray; 2.78 A; A/B=114-331.
PDB; 5QBV; X-ray; 1.80 A; A/B=115-331.
PDB; 5QBW; X-ray; 3.01 A; A=114-331.
PDB; 5QBX; X-ray; 2.10 A; A/B=114-331.
PDB; 5QBY; X-ray; 2.25 A; A/B=114-331.
PDB; 5QBZ; X-ray; 2.80 A; A=114-331.
PDB; 5QC0; X-ray; 1.90 A; A/B=114-331.
PDB; 5QC1; X-ray; 2.08 A; A/B=114-331.
PDB; 5QC2; X-ray; 2.26 A; A/B=114-331.
PDB; 5QC3; X-ray; 2.00 A; A/B=114-331.
PDB; 5QC4; X-ray; 2.00 A; A/B=115-331.
PDB; 5QC5; X-ray; 2.40 A; A/B=114-331.
PDB; 5QC6; X-ray; 2.10 A; A/B=114-331.
PDB; 5QC7; X-ray; 1.90 A; A/B=114-331.
PDB; 5QC8; X-ray; 1.74 A; A/B=114-331.
PDB; 5QC9; X-ray; 2.00 A; A/B=114-331.
PDB; 5QCA; X-ray; 2.29 A; A/B=114-331.
PDB; 5QCB; X-ray; 2.20 A; A/B=114-331.
PDB; 5QCC; X-ray; 1.80 A; A/B=114-331.
PDB; 5QCD; X-ray; 1.95 A; A=114-331.
PDB; 5QCE; X-ray; 2.78 A; A/B=114-331.
PDB; 5QCF; X-ray; 2.10 A; A=114-331.
PDB; 5QCG; X-ray; 2.69 A; A/B=114-331.
PDB; 5QCH; X-ray; 2.20 A; A/B/C/D=114-331.
PDB; 5QCI; X-ray; 2.18 A; A=114-331.
PDB; 5QCJ; X-ray; 2.00 A; A/B/C=114-331.
PDBsum; 1BXF; -.
PDBsum; 1GLO; -.
PDBsum; 1MS6; -.
PDBsum; 1NPZ; -.
PDBsum; 1NQC; -.
PDBsum; 2C0Y; -.
PDBsum; 2F1G; -.
PDBsum; 2FQ9; -.
PDBsum; 2FRA; -.
PDBsum; 2FRQ; -.
PDBsum; 2FT2; -.
PDBsum; 2FUD; -.
PDBsum; 2FYE; -.
PDBsum; 2G6D; -.
PDBsum; 2G7Y; -.
PDBsum; 2H7J; -.
PDBsum; 2HH5; -.
PDBsum; 2HHN; -.
PDBsum; 2HXZ; -.
PDBsum; 2OP3; -.
PDBsum; 2R9M; -.
PDBsum; 2R9N; -.
PDBsum; 2R9O; -.
PDBsum; 3IEJ; -.
PDBsum; 3N3G; -.
PDBsum; 3N4C; -.
PDBsum; 3OVX; -.
PDBsum; 4P6E; -.
PDBsum; 4P6G; -.
PDBsum; 5QBU; -.
PDBsum; 5QBV; -.
PDBsum; 5QBW; -.
PDBsum; 5QBX; -.
PDBsum; 5QBY; -.
PDBsum; 5QBZ; -.
PDBsum; 5QC0; -.
PDBsum; 5QC1; -.
PDBsum; 5QC2; -.
PDBsum; 5QC3; -.
PDBsum; 5QC4; -.
PDBsum; 5QC5; -.
PDBsum; 5QC6; -.
PDBsum; 5QC7; -.
PDBsum; 5QC8; -.
PDBsum; 5QC9; -.
PDBsum; 5QCA; -.
PDBsum; 5QCB; -.
PDBsum; 5QCC; -.
PDBsum; 5QCD; -.
PDBsum; 5QCE; -.
PDBsum; 5QCF; -.
PDBsum; 5QCG; -.
PDBsum; 5QCH; -.
PDBsum; 5QCI; -.
PDBsum; 5QCJ; -.
ProteinModelPortal; P25774; -.
SMR; P25774; -.
BioGrid; 107900; 3.
DIP; DIP-61077N; -.
IntAct; P25774; 7.
STRING; 9606.ENSP00000357981; -.
BindingDB; P25774; -.
ChEMBL; CHEMBL2954; -.
DrugBank; DB08195; (1R)-2-[(CYANOMETHYL)AMINO]-1-({[2-(DIFLUOROMETHOXY)BENZYL]SULFONYL}METHYL)-2-OXOETHYL MORPHOLINE-4-CARBOXYLATE.
DrugBank; DB03837; Morpholine-4-Carboxylic Acid (1-(3-Benzenesulfonyl-1-Phenethylallylcarbamoyl)-3-Methylbutyl)-Amide.
DrugBank; DB03984; Morpholine-4-Carboxylic Acid [1-(2-Benzylsulfanyl-1-Formyl-Ethylcarbamoyl)-2-Phenyl-Ethyl]-Amide.
DrugBank; DB03767; Morpholine-4-Carboxylic Acid [1s-(2-Benzyloxy-1r-Cyano-Ethylcarbamoyl)-3-Methyl-Butyl]Amide.
DrugBank; DB08752; N-[(1S)-2-[(4-cyano-1-methylpiperidin-4-yl)amino]-1-(cyclohexylmethyl)-2-oxoethyl]morpholine-4-carboxamide.
DrugBank; DB08755; N-[(1S)-2-{[(1R)-2-(benzyloxy)-1-cyano-1-methylethyl]amino}-1-(cyclohexylmethyl)-2-oxoethyl]morpholine-4-carboxamide.
GuidetoPHARMACOLOGY; 2353; -.
MEROPS; I29.004; -.
iPTMnet; P25774; -.
PhosphoSitePlus; P25774; -.
BioMuta; CTSS; -.
DMDM; 88984046; -.
EPD; P25774; -.
MaxQB; P25774; -.
PaxDb; P25774; -.
PeptideAtlas; P25774; -.
PRIDE; P25774; -.
ProteomicsDB; 54285; -.
ProteomicsDB; 54286; -. [P25774-2]
DNASU; 1520; -.
Ensembl; ENST00000368985; ENSP00000357981; ENSG00000163131. [P25774-1]
Ensembl; ENST00000448301; ENSP00000408414; ENSG00000163131. [P25774-2]
GeneID; 1520; -.
KEGG; hsa:1520; -.
UCSC; uc001evn.3; human. [P25774-1]
CTD; 1520; -.
DisGeNET; 1520; -.
EuPathDB; HostDB:ENSG00000163131.10; -.
GeneCards; CTSS; -.
HGNC; HGNC:2545; CTSS.
HPA; CAB000460; -.
HPA; HPA002988; -.
MIM; 116845; gene.
neXtProt; NX_P25774; -.
OpenTargets; ENSG00000163131; -.
PharmGKB; PA27041; -.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140823; -.
HOGENOM; HOG000230774; -.
HOVERGEN; HBG011513; -.
InParanoid; P25774; -.
KO; K01368; -.
OMA; KYQGSCG; -.
OrthoDB; EOG091G0AKT; -.
PhylomeDB; P25774; -.
TreeFam; TF313739; -.
BRENDA; 3.4.22.27; 2681.
Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
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.
SIGNOR; P25774; -.
ChiTaRS; CTSS; human.
EvolutionaryTrace; P25774; -.
GeneWiki; Cathepsin_S; -.
GenomeRNAi; 1520; -.
PMAP-CutDB; P25774; -.
PRO; PR:P25774; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163131; -.
CleanEx; HS_CTSS; -.
ExpressionAtlas; P25774; baseline and differential.
Genevisible; P25774; HS.
GO; GO:0036021; C:endolysosome lumen; TAS:Reactome.
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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0005518; F:collagen binding; IDA:BHF-UCL.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:CAFA.
GO; GO:0001968; F:fibronectin binding; IPI:BHF-UCL.
GO; GO:0043236; F:laminin binding; IDA:BHF-UCL.
GO; GO:0043394; F:proteoglycan binding; IPI:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0002250; P:adaptive immune response; IEP:UniProtKB.
GO; GO:0019882; P:antigen processing and presentation; TAS:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IDA:CACAO.
GO; GO:0034769; P:basement membrane disassembly; IDA:BHF-UCL.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; IDA:BHF-UCL.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2001259; P:positive regulation of cation channel activity; IDA:CACAO.
GO; GO:0016485; P:protein processing; IDA:CACAO.
GO; GO:0006508; P:proteolysis; IDA:CAFA.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
GO; GO:0010447; P:response to acidic pH; IDA:CACAO.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
InterPro; IPR038765; Papain_like_cys_pep_sf.
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; IPR013201; Prot_inhib_I29.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08246; Inhibitor_I29; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00848; Inhibitor_I29; 1.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF54001; SSF54001; 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; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Hydrolase; Lysosome; Polymorphism; Protease;
Reference proteome; Signal; Thiol protease; Zymogen.
SIGNAL 1 16 {ECO:0000255}.
PROPEP 17 114 Activation peptide.
/FTId=PRO_0000026313.
CHAIN 115 331 Cathepsin S.
/FTId=PRO_0000026314.
ACT_SITE 139 139 {ECO:0000250}.
ACT_SITE 278 278 {ECO:0000250}.
ACT_SITE 298 298 {ECO:0000250}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 126 224 {ECO:0000269|PubMed:17469812}.
DISULFID 136 180 {ECO:0000269|PubMed:17469812}.
DISULFID 170 213 {ECO:0000269|PubMed:17469812}.
DISULFID 272 320 {ECO:0000269|PubMed:17469812}.
VAR_SEQ 84 133 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042712.
VARIANT 113 113 R -> W (in dbSNP:rs2230061).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_025385.
VARIANT 161 161 S -> T (in dbSNP:rs1059604).
{ECO:0000269|PubMed:1373132,
ECO:0000269|PubMed:8157683}.
/FTId=VAR_025386.
CONFLICT 92 92 M -> T (in Ref. 1 and 4). {ECO:0000305}.
HELIX 22 24 {ECO:0000244|PDB:2C0Y}.
HELIX 25 35 {ECO:0000244|PDB:2C0Y}.
HELIX 44 67 {ECO:0000244|PDB:2C0Y}.
STRAND 72 75 {ECO:0000244|PDB:2C0Y}.
HELIX 79 82 {ECO:0000244|PDB:2C0Y}.
HELIX 85 91 {ECO:0000244|PDB:2C0Y}.
HELIX 100 102 {ECO:0000244|PDB:2C0Y}.
HELIX 121 124 {ECO:0000244|PDB:3OVX}.
STRAND 135 137 {ECO:0000244|PDB:2HH5}.
HELIX 139 156 {ECO:0000244|PDB:3OVX}.
HELIX 164 170 {ECO:0000244|PDB:3OVX}.
HELIX 173 175 {ECO:0000244|PDB:3OVX}.
HELIX 179 181 {ECO:0000244|PDB:3OVX}.
HELIX 185 195 {ECO:0000244|PDB:3OVX}.
STRAND 198 200 {ECO:0000244|PDB:3OVX}.
TURN 201 203 {ECO:0000244|PDB:3OVX}.
HELIX 217 219 {ECO:0000244|PDB:3OVX}.
STRAND 220 222 {ECO:0000244|PDB:3OVX}.
STRAND 226 229 {ECO:0000244|PDB:3OVX}.
HELIX 235 244 {ECO:0000244|PDB:3OVX}.
STRAND 248 252 {ECO:0000244|PDB:3OVX}.
HELIX 257 261 {ECO:0000244|PDB:3OVX}.
STRAND 264 267 {ECO:0000244|PDB:3OVX}.
STRAND 278 288 {ECO:0000244|PDB:3OVX}.
STRAND 291 297 {ECO:0000244|PDB:3OVX}.
TURN 302 305 {ECO:0000244|PDB:5QCA}.
STRAND 309 313 {ECO:0000244|PDB:3OVX}.
STRAND 315 318 {ECO:0000244|PDB:3OVX}.
HELIX 319 321 {ECO:0000244|PDB:3OVX}.
TURN 322 324 {ECO:0000244|PDB:3OVX}.
STRAND 327 330 {ECO:0000244|PDB:3OVX}.
SEQUENCE 331 AA; 37496 MW; 86093619DB6F0269 CRC64;
MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL IWEKNLKFVM
LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LMSSLRVPSQ WQRNITYKSN PNRILPDSVD
WREKGCVTEV KYQGSCGACW AFSAVGALEA QLKLKTGKLV SLSAQNLVDC STEKYGNKGC
NGGFMTTAFQ YIIDNKGIDS DASYPYKAMD QKCQYDSKYR AATCSKYTEL PYGREDVLKE
AVANKGPVSV GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG KEYWLVKNSW
GHNFGEEGYI RMARNKGNHC GIASFPSYPE I


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