HUMAN:CATB

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CTSB (synonyms: CPSB)
Protein Name(s)	Cathepsin B APP secretase APPS Cathepsin B1 Cathepsin B light chain Cathepsin B heavy chain
External Links
UniProt	P07858
EMBL	M14221 L16510 AK092070 AK075393 CH471157 BC010240 BC095408 M13230
CCDS	CCDS5986.1
PIR	A26498
RefSeq	NP_001899.1 NP_680090.1 NP_680091.1 NP_680092.1 NP_680093.1 XP_006716307.1 XP_006716308.1
UniGene	Hs.520898
PDB	1CSB 1GMY 1HUC 1PBH 2IPP 2PBH 3AI8 3CBJ 3CBK 3K9M 3PBH
PDBsum	1CSB 1GMY 1HUC 1PBH 2IPP 2PBH 3AI8 3CBJ 3CBK 3K9M 3PBH
ProteinModelPortal	P07858
SMR	P07858
BioGrid	107888
DIP	DIP-42785N
IntAct	P07858
MINT	MINT-1397666
STRING	9606.ENSP00000342070
BindingDB	P07858
ChEMBL	CHEMBL2111396
GuidetoPHARMACOLOGY	2343
MEROPS	C01.060
PhosphoSite	P07858
DMDM	68067549
SWISS-2DPAGE	P07858
UCD-2DPAGE	P07858
MaxQB	P07858
PaxDb	P07858
PeptideAtlas	P07858
PRIDE	P07858
DNASU	1508
Ensembl	ENST00000345125 ENST00000353047 ENST00000453527 ENST00000530640 ENST00000531089 ENST00000533455 ENST00000534510
GeneID	1508
KEGG	hsa:1508
UCSC	uc003wum.3
CTD	1508
GeneCards	GC08M011700
H-InvDB	HIX0007320
HGNC	HGNC:2527
HPA	CAB000457 HPA018156
MIM	116810
neXtProt	NX_P07858
PharmGKB	PA27027
eggNOG	COG4870
GeneTree	ENSGT00760000118871
HOGENOM	HOG000241341
HOVERGEN	HBG003480
InParanoid	P07858
KO	K01363
OMA	CTGEGDT
OrthoDB	EOG7034HR
PhylomeDB	P07858
TreeFam	TF314576
BRENDA	3.4.22.1
Reactome	REACT_118632 REACT_121399 REACT_150180 REACT_150401
ChiTaRS	CTSB
EvolutionaryTrace	P07858
GeneWiki	Cathepsin_B
GenomeRNAi	1508
NextBio	6235
PMAP-CutDB	P07858
PRO	PR:P07858
Proteomes	UP000005640
Bgee	P07858
CleanEx	HS_CTSB
ExpressionAtlas	P07858
Genevestigator	P07858
GO	GO:0036021 GO:0005576 GO:0005615 GO:0070062 GO:0005622 GO:0043231 GO:0005764 GO:0042470 GO:0005739 GO:0005730 GO:0048471 GO:0005518 GO:0004197 GO:0008234 GO:0008233 GO:0043394 GO:0097067 GO:0030574 GO:0046697 GO:0030855 GO:0022617 GO:0030198 GO:0045087 GO:0006508 GO:0051603 GO:0042981 GO:0050790 GO:0002224
InterPro	IPR025661 IPR000169 IPR025660 IPR013128 IPR000668 IPR015643 IPR012599
PANTHER	PTHR12411 PTHR12411:SF285
Pfam	PF00112 PF08127
PRINTS	PR00705
SMART	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:0008234	cysteine-type peptidase activity	PMID:8612130^[1]	ECO:0000314			F		Fig. 1A	complete CACAO 2099
colocalizes_with	GO:0062023	collagen-containing extracellular matrix	PMID:28327460^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002540)	Seeded From UniProt	complete
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:28675934^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0003688)	Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0002107)	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:2350688^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0062023	collagen-containing extracellular matrix	PMID:25037231^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001155)	Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	PMID:8612130^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	PMID:22952693^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:Q05793)	Seeded From UniProt	complete
enables	GO:0043394	proteoglycan binding	PMID:22952693^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q05793	F		Seeded From UniProt	complete
involved_in	GO:0030574	collagen catabolic process	PMID:22952693^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22952693^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0001003)	Seeded From UniProt	complete
enables	GO:0005518	collagen binding	PMID:22952693^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:22952693^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(UniProtKB:P98160)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
involved_in	GO:0030855	epithelial cell differentiation	PMID:21492153^[10]	ECO:0000270	expression pattern evidence used in manual assertion		P	results_in_acquisition_of_features_of:(CL:1000334)	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	PMID:7890620^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:7890620^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22261194^[12]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:A1E295	C	part_of:(UBERON:0002084)	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:6203523^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0097067	cellular response to thyroid hormone stimulus	PMID:21217776^[14]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:15614436^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	PMID:8811434^[16]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_in:(UBERON:0002113)	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:8811434^[16]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0002113)	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:1837142^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000530)	Seeded From UniProt	complete
involved_in	GO:0051603	proteolysis involved in cellular protein catabolic process	PMID:21873635^[18]	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^[18]	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^[18]	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^[18]	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
part_of	GO:0005730	nucleolus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0046718	viral entry into host cell	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P10605 ensembl:ENSMUSP00000006235	P		Seeded From UniProt	complete
involved_in	GO:0046697	decidualization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P10605 ensembl:ENSMUSP00000006235	P		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P10605 ensembl:ENSMUSP00000006235	C		Seeded From UniProt	complete
enables	GO:0004175	endopeptidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P10605 ensembl:ENSMUSP00000006235	F		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012599	F		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:0050790	regulation of catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012599	P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:3463996^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005622	intracellular	PMID:1645961^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:1645961^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	PMID:16130169^[21]	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
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:0036021	endolysosome lumen	Reactome:R-HSA-1678920	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030574	collagen catabolic process	Reactome:R-HSA-1442490	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-2471621 Reactome:R-HSA-2168923	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
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: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
part_of	GO:0005576	extracellular region	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964	C		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
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
part_of	GO:0042470	melanosome	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0161	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0112	C		Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 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
↑ Ragelle, H et al. (2017) Comprehensive proteomic characterization of stem cell-derived extracellular matrices. Biomaterials 128 147-159 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. (2017) Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. J. Proteome Res. 16 3083-3091 PubMed GONUTS page
↑ ^5.0 ^5.1 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
↑ Cataldo, AM et al. (1990) Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin. Brain Res. 513 181-92 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 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
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ Buhrke, T et al. (2011) Analysis of proteomic changes induced upon cellular differentiation of the human intestinal cell line Caco-2. Dev. Growth Differ. 53 411-26 PubMed GONUTS page
↑ ^11.0 ^11.1 Hall, A et al. (1995) Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases. J. Biol. Chem. 270 5115-21 PubMed GONUTS page
↑ Barallobre-Barreiro, J et al. (2012) Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury. Circulation 125 789-802 PubMed GONUTS page
↑ Barrett, AJ et al. (1984) The place of human gamma-trace (cystatin C) amongst the cysteine proteinase inhibitors. Biochem. Biophys. Res. Commun. 120 631-6 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
↑ Zhang, JL et al. (2005) Human hepatitis B virus X protein promotes cell proliferation and inhibits cell apoptosis through interacting with a serine protease Hepsin. Arch. Virol. 150 721-41 PubMed GONUTS page
↑ ^16.0 ^16.1 Popovic, T et al. (1996) Simultaneous isolation of human kidney cathepsins B, H, L and C and their characterisation. J. Chromatogr. B, Biomed. Appl. 681 251-62 PubMed GONUTS page
↑ Cataldo, AM et al. (1991) Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 88 10998-1002 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Chan, SJ et al. (1986) Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc. Natl. Acad. Sci. U.S.A. 83 7721-5 PubMed GONUTS page
↑ ^20.0 ^20.1 Tagawa, K et al. (1991) Alzheimer's disease amyloid beta-clipping enzyme (APP secretase): identification, purification, and characterization of the enzyme. Biochem. Biophys. Res. Commun. 177 377-87 PubMed GONUTS page
↑ Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:8612130-1] 1.0 ^1.1 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:28327460-2] Ragelle, H et al. (2017) Comprehensive proteomic characterization of stem cell-derived extracellular matrices. Biomaterials 128 147-159 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:28675934-4] Naba, A et al. (2017) Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. J. Proteome Res. 16 3083-3091 PubMed GONUTS page

[PMID:25037231-5] 5.0 ^5.1 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:2350688-6] Cataldo, AM et al. (1990) Lysosomal proteinase antigens are prominently localized within senile plaques of Alzheimer's disease: evidence for a neuronal origin. Brain Res. 513 181-92 PubMed GONUTS page

[PMID:23533145-7] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:22952693-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 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:19199708-9] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:21492153-10] Buhrke, T et al. (2011) Analysis of proteomic changes induced upon cellular differentiation of the human intestinal cell line Caco-2. Dev. Growth Differ. 53 411-26 PubMed GONUTS page

[PMID:7890620-11] 11.0 ^11.1 Hall, A et al. (1995) Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases. J. Biol. Chem. 270 5115-21 PubMed GONUTS page

[PMID:22261194-12] Barallobre-Barreiro, J et al. (2012) Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury. Circulation 125 789-802 PubMed GONUTS page

[PMID:6203523-13] Barrett, AJ et al. (1984) The place of human gamma-trace (cystatin C) amongst the cysteine proteinase inhibitors. Biochem. Biophys. Res. Commun. 120 631-6 PubMed GONUTS page

[PMID:21217776-14] 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:15614436-15] Zhang, JL et al. (2005) Human hepatitis B virus X protein promotes cell proliferation and inhibits cell apoptosis through interacting with a serine protease Hepsin. Arch. Virol. 150 721-41 PubMed GONUTS page

[PMID:8811434-16] 16.0 ^16.1 Popovic, T et al. (1996) Simultaneous isolation of human kidney cathepsins B, H, L and C and their characterisation. J. Chromatogr. B, Biomed. Appl. 681 251-62 PubMed GONUTS page

[PMID:1837142-17] Cataldo, AM et al. (1991) Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 88 10998-1002 PubMed GONUTS page

[PMID:21873635-18] 18.0 ^18.1 ^18.2 ^18.3 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:3463996-19] Chan, SJ et al. (1986) Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc. Natl. Acad. Sci. U.S.A. 83 7721-5 PubMed GONUTS page

[PMID:1645961-20] 20.0 ^20.1 Tagawa, K et al. (1991) Alzheimer's disease amyloid beta-clipping enzyme (APP secretase): identification, purification, and characterization of the enzyme. Biochem. Biophys. Res. Commun. 177 377-87 PubMed GONUTS page

[PMID:16130169-21] Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

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HUMAN:CATB

Contents

Annotations

Notes

References

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