HUMAN:CATS

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CTSS
Protein Name(s)	Cathepsin S
External Links
UniProt	P25774
EMBL	S93414 M86553 M90696 U07374 U07370 U07371 U07372 U07373 CR541676 AK301472 AK314482 AL356292 CH471121 CH471121 BC002642
CCDS	CCDS55634.1 CCDS968.1
PIR	A42482
RefSeq	NP_001186668.1 NP_004070.3
UniGene	Hs.181301
PDB	1BXF 1GLO 1MS6 1NPZ 1NQC 2C0Y 2F1G 2FQ9 2FRA 2FRQ 2FT2 2FUD 2FYE 2G6D 2G7Y 2H7J 2HH5 2HHN 2HXZ 2OP3 2R9M 2R9N 2R9O 3IEJ 3KWN 3MPE 3MPF 3N3G 3N4C 3OVX 4P6E 4P6G
PDBsum	1BXF 1GLO 1MS6 1NPZ 1NQC 2C0Y 2F1G 2FQ9 2FRA 2FRQ 2FT2 2FUD 2FYE 2G6D 2G7Y 2H7J 2HH5 2HHN 2HXZ 2OP3 2R9M 2R9N 2R9O 3IEJ 3KWN 3MPE 3MPF 3N3G 3N4C 3OVX 4P6E 4P6G
ProteinModelPortal	P25774
SMR	P25774
BioGrid	107900
IntAct	P25774
STRING	9606.ENSP00000357981
BindingDB	P25774
ChEMBL	CHEMBL2954
GuidetoPHARMACOLOGY	2353
MEROPS	C01.034
PhosphoSite	P25774
DMDM	88984046
MaxQB	P25774
PaxDb	P25774
PeptideAtlas	P25774
PRIDE	P25774
DNASU	1520
Ensembl	ENST00000368985 ENST00000448301
GeneID	1520
KEGG	hsa:1520
UCSC	uc001evn.3 uc010pcj.2
CTD	1520
GeneCards	GC01M150702
HGNC	HGNC:2545
HPA	CAB000460 HPA002988
MIM	116845
neXtProt	NX_P25774
PharmGKB	PA27041
eggNOG	COG4870
GeneTree	ENSGT00760000118871
HOGENOM	HOG000230774
HOVERGEN	HBG011513
InParanoid	P25774
KO	K01368
OMA	ICHGADP
OrthoDB	EOG786H3P
PhylomeDB	P25774
TreeFam	TF313739
BRENDA	3.4.22.27
Reactome	REACT_111168 REACT_118572 REACT_118632 REACT_121399 REACT_150180
ChiTaRS	CTSS
EvolutionaryTrace	P25774
GeneWiki	Cathepsin_S
GenomeRNAi	1520
NextBio	6291
PMAP-CutDB	P25774
PRO	PR:P25774
Proteomes	UP000005640
Bgee	P25774
CleanEx	HS_CTSS
ExpressionAtlas	P25774
Genevestigator	P25774
GO	GO:0036021 GO:0005576 GO:0005615 GO:0043231 GO:0043202 GO:0005764 GO:0016020 GO:0005518 GO:0004197 GO:0001968 GO:0043236 GO:0043394 GO:0002250 GO:0019882 GO:0042590 GO:0002480 GO:0019886 GO:0002474 GO:0034769 GO:0097067 GO:0030574 GO:0022617 GO:0030198 GO:0006955 GO:0045087 GO:0050729 GO:0006508 GO:0051603 GO:0002224
InterPro	IPR025661 IPR000169 IPR025660 IPR013128 IPR000668 IPR013201
PANTHER	PTHR12411
Pfam	PF08246 PF00112
PRINTS	PR00705
SMART	SM00848 SM00645
PROSITE	PS00640 PS00139 PS00639

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004197	cysteine-type endopeptidase activity	PMID:8612130^[1]	ECO:0000314			F		Fig. 2, Fig. 4A, Fig. 5, and Fig. 6	complete CACAO 2088
	GO:0048002	antigen processing and presentation of peptide antigen	PMID:8612130^[1]	ECO:0000314			P		Fig. 2, Fig. 5, and Fig. 6	complete CACAO 2117
	GO:2001259	positive regulation of cation channel activity	PMID:22864553^[2]	ECO:0000314			P		Figure 2: ENaC (cation channel) activation by Cathepsin S	complete CACAO 5172
	GO:2001258	negative regulation of cation channel activity	PMID:22864553^[2]	ECO:0000314			P		Figure 3: ENaC (cation channel) inhibition by cathepsin-S inhibitor LHVS	complete CACAO 5178
	GO:2001258	negative regulation of cation channel activity	PMID:22864553^[2]	ECO:0000315			P		Figure 8: Mutating two putative neutrophil elastase cleavage sites prevents proteolytic activation of ENaC by cathepsin-S.	complete CACAO 5191
	GO:0008234	cysteine-type peptidase activity	PMID:22864553^[2]	ECO:0000314			F		Figure 2: Cysteine protease cathepsin-S activates ENaC (cation channel).	complete CACAO 5196
	GO:0097179	protease inhibitor complex	PMID:22864553^[2]	ECO:0000314			C		Figure 3: Cysteine protease Cathepsin-S covalently binds to the vinylsulfone residue and inhibits ENaC (cation channel) activation.	complete CACAO 5204
	GO:0010447	response to acidity	PMID:22864553^[2]	ECO:0000314			P		Figure 5: Cathepsin-S can activate ENaC in an acidic environment.	complete CACAO 5210
	GO:0006508	proteolysis	PMID:22864553^[2]	ECO:0000314			P		Figure 7	complete CACAO 5504
	GO:0030162	regulation of proteolysis	PMID:22864553^[2]	ECO:0000314			P		Figure 6.	complete CACAO 5723
	GO:0016485	protein processing	PMID:22864553^[2]	ECO:0000314			P		Figure 6	complete CACAO 5777
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:28344315^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002371)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002107)	Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:22365146^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:8612130^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010447	response to acidic pH	PMID:22864553^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016485	protein processing	PMID:22864553^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048002	antigen processing and presentation of peptide antigen	PMID:8612130^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001259	positive regulation of cation channel activity	PMID:22864553^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:22864553^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	PMID:22952693^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P98160)\|has_input:(UniProtKB:P02751)	Seeded From UniProt	complete
enables	GO:0043394	proteoglycan binding	PMID:22952693^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q05793	F		Seeded From UniProt	complete
enables	GO:0043236	laminin binding	PMID:22952693^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0034769	basement membrane disassembly	PMID:22952693^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030574	collagen catabolic process	PMID:22952693^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22952693^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000312)	Seeded From UniProt	complete
enables	GO:0005518	collagen binding	PMID:22952693^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:22952693^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(UniProtKB:P98160)\|has_input:(UniProtKB:P02751)	Seeded From UniProt	complete
enables	GO:0001968	fibronectin binding	PMID:22952693^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02751	F		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:16502470^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001914)	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:12788072^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:12788072^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097067	cellular response to thyroid hormone stimulus	PMID:21217776^[9]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:15196205^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0009039)\|part_of:(CL:0000887)\|part_of:(CL:0000888)	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:14718574^[11]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002250	adaptive immune response	PMID:15196205^[10]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:107341 PANTHER:PTN000274640 UniProtKB:P07711 UniProtKB:P07858 UniProtKB:P25774 UniProtKB:P43235	P		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0013770 MGI:MGI:107341 MGI:MGI:1860262 MGI:MGI:88561 MGI:MGI:88564 PANTHER:PTN000274640 RGD:2445 RGD:2447 RGD:2448 RGD:61810 RGD:621509 UniProtKB:P07711 UniProtKB:P07858 UniProtKB:P09668 UniProtKB:P25774 UniProtKB:Q9UBR2 WB:WBGene00000786 dictyBase:DDB_G0279187	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0034229 FB:FBgn0034709 MGI:MGI:88564 PANTHER:PTN000274640 RGD:2447 RGD:61810 RGD:621509 RGD:708479 UniProtKB:P07711 UniProtKB:P07858 UniProtKB:P09668 UniProtKB:P25774 UniProtKB:P43235 UniProtKB:Q9UBR2	C		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0013770 FB:FBgn0030521 MGI:MGI:107285 MGI:MGI:107341 PANTHER:PTN000274640 RGD:2448 RGD:621509 TAIR:locus:2133402 TAIR:locus:2157712 TAIR:locus:2204873 TAIR:locus:505006093 UniProtKB:P07711 UniProtKB:P07858 UniProtKB:P09668 UniProtKB:P25774 UniProtKB:P43235 UniProtKB:Q8IIL0	F		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000668	P		Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000668 InterPro:IPR013128	F		Seeded From UniProt	complete
involved_in	GO:0006955	immune response	PMID:8157683^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:1373132^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:1373132^[14] Reactome:R-HSA-1678981	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0019882	antigen processing and presentation	PMID:15196205^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1904724	tertiary granule lumen	Reactome:R-HSA-6798745	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043202	lysosomal lumen	Reactome:R-HSA-2130706 Reactome:R-HSA-2130504 Reactome:R-HSA-2130349	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0036021	endolysosome lumen	Reactome:R-HSA-1678981 Reactome:R-HSA-1678920	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0022617	extracellular matrix disassembly	Reactome:R-HSA-1474228	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019886	antigen processing and presentation of exogenous peptide antigen via MHC class II	Reactome:R-HSA-2132295	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6800434 Reactome:R-HSA-6798745 Reactome:R-HSA-1566981	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002224	toll-like receptor signaling pathway	Reactome:R-HSA-168898	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0788	F		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0458 UniProtKB-SubCell:SL-0158	C		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Riese, RJ et al. (1996) Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 4 357-66 PubMed GONUTS page
↑ ^2.00 ^2.01 ^2.02 ^2.03 ^2.04 ^2.05 ^2.06 ^2.07 ^2.08 ^2.09 ^2.10 ^2.11 ^2.12 Haerteis, S et al. (2012) Proteolytic activation of the epithelial sodium channel (ENaC) by the cysteine protease cathepsin-S. Pflugers Arch. 464 353-65 PubMed GONUTS page
↑ Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page
↑ Naba, A et al. (2014) Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. BMC Cancer 14 518 PubMed GONUTS page
↑ Magister, S et al. (2012) Regulation of cathepsins S and L by cystatin F during maturation of dendritic cells. Eur. J. Cell Biol. 91 391-401 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 ^6.6 ^6.7 ^6.8 Sage, J et al. (2012) Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners. PLoS ONE 7 e43494 PubMed GONUTS page
↑ Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page
↑ ^8.0 ^8.1 Ohashi, A et al. (2003) New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors. Biochem. Biophys. Res. Commun. 306 98-103 PubMed GONUTS page
↑ Wu, SM et al. (2011) Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells. Oncogene 30 2057-69 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Zavasnik-Bergant, V et al. (2004) Inhibitory p41 isoform of invariant chain and its potential target enzymes cathepsins L and H in distinct populations of macrophages in human lymph nodes. Immunology 112 378-85 PubMed GONUTS page
↑ Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Shi, GP et al. (1994) Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. J. Biol. Chem. 269 11530-6 PubMed GONUTS page
↑ ^14.0 ^14.1 Shi, GP et al. (1992) Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J. Biol. Chem. 267 7258-62 PubMed GONUTS page

[PMID:8612130-1] 1.0 ^1.1 ^1.2 ^1.3 Riese, RJ et al. (1996) Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 4 357-66 PubMed GONUTS page

[PMID:22864553-2] 2.00 ^2.01 ^2.02 ^2.03 ^2.04 ^2.05 ^2.06 ^2.07 ^2.08 ^2.09 ^2.10 ^2.11 ^2.12 Haerteis, S et al. (2012) Proteolytic activation of the epithelial sodium channel (ENaC) by the cysteine protease cathepsin-S. Pflugers Arch. 464 353-65 PubMed GONUTS page

[PMID:28344315-3] Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page

[PMID:25037231-4] Naba, A et al. (2014) Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. BMC Cancer 14 518 PubMed GONUTS page

[PMID:22365146-5] Magister, S et al. (2012) Regulation of cathepsins S and L by cystatin F during maturation of dendritic cells. Eur. J. Cell Biol. 91 391-401 PubMed GONUTS page

[PMID:22952693-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 ^6.6 ^6.7 ^6.8 Sage, J et al. (2012) Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners. PLoS ONE 7 e43494 PubMed GONUTS page

[PMID:16502470-7] Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page

[PMID:12788072-8] 8.0 ^8.1 Ohashi, A et al. (2003) New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors. Biochem. Biophys. Res. Commun. 306 98-103 PubMed GONUTS page

[PMID:21217776-9] Wu, SM et al. (2011) Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells. Oncogene 30 2057-69 PubMed GONUTS page

[PMID:15196205-10] 10.0 ^10.1 ^10.2 Zavasnik-Bergant, V et al. (2004) Inhibitory p41 isoform of invariant chain and its potential target enzymes cathepsins L and H in distinct populations of macrophages in human lymph nodes. Immunology 112 378-85 PubMed GONUTS page

[PMID:14718574-11] Anderson, NL et al. (2004) The human plasma proteome: a nonredundant list developed by combination of four separate sources. Mol. Cell Proteomics 3 311-26 PubMed GONUTS page

[PMID:21873635-12] 12.0 ^12.1 ^12.2 ^12.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:8157683-13] Shi, GP et al. (1994) Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. J. Biol. Chem. 269 11530-6 PubMed GONUTS page

[PMID:1373132-14] 14.0 ^14.1 Shi, GP et al. (1992) Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J. Biol. Chem. 267 7258-62 PubMed GONUTS page

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HUMAN:CATS

Contents

Annotations

Notes

References

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