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HUMAN:CATD

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) CTSD (synonyms: CPSD)
Protein Name(s) Cathepsin D

Cathepsin D light chain Cathepsin D heavy chain

External Links
UniProt P07339
EMBL M11233
X05344
M63138
M63134
M63135
M63136
M63137
CR456947
BT006910
BT020155
BC016320
L12980
S74689
S52557
CCDS CCDS7725.1
PIR A25771
RefSeq NP_001900.1
UniGene Hs.654447
PDB 1LYA
1LYB
1LYW
4OBZ
4OC6
4OD9
PDBsum 1LYA
1LYB
1LYW
4OBZ
4OC6
4OD9
ProteinModelPortal P07339
SMR P07339
BioGrid 107889
DIP DIP-43906N
IntAct P07339
MINT MINT-3005628
STRING 9606.ENSP00000236671
BindingDB P07339
ChEMBL CHEMBL2581
DrugBank DB00071
DB00030
GuidetoPHARMACOLOGY 2345
MEROPS A01.009
PhosphoSite P07339
DMDM 115717
DOSAC-COBS-2DPAGE P07339
REPRODUCTION-2DPAGE IPI00011229
SWISS-2DPAGE P07339
UCD-2DPAGE P07339
MaxQB P07339
PaxDb P07339
PeptideAtlas P07339
PRIDE P07339
DNASU 1509
Ensembl ENST00000236671
GeneID 1509
KEGG hsa:1509
UCSC uc001luc.2
CTD 1509
GeneCards GC11M001773
GeneReviews CTSD
H-InvDB HIX0009359
HGNC HGNC:2529
HPA CAB000109
HPA003001
MIM 116840
610127
neXtProt NX_P07339
Orphanet 228337
PharmGKB PA27029
eggNOG NOG248684
HOGENOM HOG000197681
HOVERGEN HBG000482
InParanoid P07339
KO K01379
OMA TEGPIPE
PhylomeDB P07339
TreeFam TF314990
BioCyc MetaCyc:HS04183-MONOMER
Reactome REACT_121399
REACT_147707
REACT_150401
EvolutionaryTrace P07339
GeneWiki Cathepsin_D
GenomeRNAi 1509
NextBio 6247
PMAP-CutDB P07339
PRO PR:P07339
Proteomes UP000005640
Bgee P07339
CleanEx HS_CTSD
ExpressionAtlas P07339
Genevestigator P07339
GO GO:0005576
GO:0005615
GO:0070062
GO:0043202
GO:0005764
GO:0042470
GO:0004190
GO:0019886
GO:0030574
GO:0022617
GO:0030198
Gene3D 2.40.70.10
InterPro IPR001461
IPR001969
IPR012848
IPR021109
PANTHER PTHR13683
Pfam PF07966
PF00026
PRINTS PR00792
SUPFAM SSF50630
PROSITE PS00141

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004190

aspartic-type endopeptidase activity

PMID:8612130[1]

ECO:0000314

F

Fig. 7

complete
CACAO 2100

part_of

GO:0062023

collagen-containing extracellular matrix

PMID:28344315[2]

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[3]

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[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0002107)

Seeded From UniProt

complete

enables

GO:0070001

aspartic-type peptidase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P18242

F

Seeded From UniProt

complete

part_of

GO:0010008

endosome membrane

PMID:17188016[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005765

lysosomal membrane

PMID:17188016[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:17188016[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

PMID:17188016[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043280

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

PMID:12107093[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070201

regulation of establishment of protein localization

PMID:12107093[6]

ECO:0000314

direct assay evidence used in manual assertion

P

has_input:(UniProtKB:P99999)|has_end_location(GO:0005829)

Seeded From UniProt

complete

involved_in

GO:0043065

positive regulation of apoptotic process

PMID:12107093[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042159

lipoprotein catabolic process

PMID:16997486[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:16997486[7]

ECO:0000314

direct assay evidence used in manual assertion

P

has_input:(UniProtKB:P02649)

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

PMID:16997486[7]

ECO:0000314

direct assay evidence used in manual assertion

F

has_input:(UniProtKB:P02649)

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

PMID:1692625[8]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(CL:0000540)

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

PMID:2350688[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:27068509[10]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0007318)

Seeded From UniProt

complete

part_of

GO:0045121

membrane raft

PMID:25204797[11]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(CL:0002618)

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:23533145[12]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:19056867[13]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001088)

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:16502470[14]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001914)

Seeded From UniProt

complete

colocalizes_with

GO:0062023

collagen-containing extracellular matrix

PMID:20551380[15]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001496)

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:20551380[15]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001496)

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:22261194[16]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P00795

C

part_of:(UBERON:0002084)

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)|part_of:(CL:0000127)

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:14718574[18]

ECO:0000303

author statement without traceable support used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0030163

protein catabolic process

PMID:21873635[19]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201569
PANTHER:PTN000342793
UniProtKB:P0CY27
UniProtKB:Q5A8N2
UniProtKB:Q5AC08

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:21873635[19]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000190503
CGD:CAL0000194661
CGD:CAL0000196689
CGD:CAL0000201140
MGI:MGI:1346542
PANTHER:PTN000342793
RGD:621511
SGD:S000002551
TAIR:locus:2008940
UniProtKB:P00797
UniProtKB:P0CY27
UniProtKB:P41748
UniProtKB:P43094
UniProtKB:P56817
UniProtKB:Q59VH7
UniProtKB:Q5AC08
UniProtKB:Q8I6Z5
WB:WBGene00000217

P

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

PMID:21873635[19]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:88562
PANTHER:PTN002671460
RGD:621511
UniProtKB:P07339
UniProtKB:Q05744

C

Seeded From UniProt

complete

enables

GO:0004190

aspartic-type endopeptidase activity

PMID:21873635[19]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000196689
MGI:MGI:107361
MGI:MGI:1915935
MGI:MGI:88562
PANTHER:PTN000342793
PomBase:SPCC1795.09
RGD:2446
SGD:S000001277
SGD:S000002551
SGD:S000004110
SGD:S000004111
TAIR:locus:2145954
UniProtKB:P00797
UniProtKB:P0CY27
UniProtKB:P14091
UniProtKB:P20142
UniProtKB:P56817
UniProtKB:Q4WNV0
UniProtKB:Q5AC08
UniProtKB:Q8I6Z5
UniProtKB:Q9LTW4
UniProtKB:Q9Y5Z0

F

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

PMID:19723497[20]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004190

aspartic-type endopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001461
InterPro:IPR001969
InterPro:IPR012848
InterPro:IPR033144

F

Seeded From UniProt

complete

part_of

GO:0005764

lysosome

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR033144

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:IPR001461
InterPro:IPR001969
InterPro:IPR012848
InterPro:IPR033144

P

Seeded From UniProt

complete

enables

GO:0004190

aspartic-type endopeptidase activity

PMID:3927292[21]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

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-9023846
Reactome:R-HSA-2130706
Reactome:R-HSA-2130349

ECO:0000304

author statement supported by traceable reference used in manual assertion



C

Seeded From UniProt

complete

part_of

GO:0035580

specific granule lumen

Reactome:R-HSA-6798749

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

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-6798749
Reactome:R-HSA-6798745
Reactome:R-HSA-2471621

ECO:0000304

author statement supported by traceable reference used in manual assertion




C

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: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: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

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

enables

GO:0004190

aspartic-type endopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0064

F

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

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

edit table

Notes

References

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

  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
  2. ↑ Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page
  3. ↑ 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
  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
  5. ↑ 5.0 5.1 5.2 5.3 Follo, C et al. (2007) Folding, activity and targeting of mutated human cathepsin D that cannot be processed into the double-chain form. Int. J. Biochem. Cell Biol. 39 638-49 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 Roberg, K et al. (2002) Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts. Am. J. Pathol. 161 89-96 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 Zhou, W et al. (2006) Cathepsin D-mediated proteolysis of apolipoprotein E: possible role in Alzheimer's disease. Neuroscience 143 689-701 PubMed GONUTS page
  8. ↑ Cataldo, AM & Nixon, RA (1990) Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc. Natl. Acad. Sci. U.S.A. 87 3861-5 PubMed GONUTS page
  9. ↑ 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
  10. ↑ Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page
  11. ↑ Fork, C et al. (2014) Flotillin-1 facilitates toll-like receptor 3 signaling in human endothelial cells. Basic Res. Cardiol. 109 439 PubMed GONUTS page
  12. ↑ 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
  13. ↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
  14. ↑ Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page
  15. ↑ 15.0 15.1 Didangelos, A et al. (2010) Proteomics characterization of extracellular space components in the human aorta. Mol. Cell Proteomics 9 2048-62 PubMed GONUTS page
  16. ↑ 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
  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
  18. ↑ 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
  19. ↑ 19.0 19.1 19.2 19.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  20. ↑ Harrison, KD et al. (2009) Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking. Cell Metab. 10 208-18 PubMed GONUTS page
  21. ↑ Faust, PL et al. (1985) Cloning and sequence analysis of cDNA for human cathepsin D. Proc. Natl. Acad. Sci. U.S.A. 82 4910-4 PubMed GONUTS page
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