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Protein

Cathepsin D

Gene

CTSD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acid protease active in intracellular protein breakdown. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.

Catalytic activityi

Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei97 – 971PROSITE-ProRule annotation1 Publication
Active sitei295 – 2951PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: ProtInc

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. collagen catabolic process Source: Reactome
  3. extracellular matrix disassembly Source: Reactome
  4. extracellular matrix organization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciMetaCyc:HS04183-MONOMER.
BRENDAi3.4.23.5. 2681.
ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiA01.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin D (EC:3.4.23.5)
Cleaved into the following 2 chains:
Gene namesi
Name:CTSD
Synonyms:CPSD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2529. CTSD.

Subcellular locationi

  1. Lysosome
  2. Melanosome
  3. Secretedextracellular space

  4. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. In aortic samples, detected as an extracellular protein loosely bound to the matrix (PubMed:20551380).1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. lysosomal lumen Source: Reactome
  5. lysosome Source: UniProtKB
  6. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Involvement in diseasei

Ceroid lipofuscinosis, neuronal, 10 (CLN10)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of neuronal ceroid lipofuscinosis with onset at birth or early childhood. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.

See also OMIM:610127
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti229 – 2291F → I in CLN10. 2 Publications
VAR_029362
Natural varianti383 – 3831W → C in CLN10. 1 Publication
VAR_029363

Keywords - Diseasei

Alzheimer disease, Disease mutation, Neurodegeneration, Neuronal ceroid lipofuscinosis

Organism-specific databases

MIMi610127. phenotype.
Orphaneti228337. CLN10 disease.
PharmGKBiPA27029.

Chemistry

DrugBankiDB00030. Insulin Regular.

Polymorphism and mutation databases

BioMutaiCTSD.
DMDMi115717.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Propeptidei19 – 6446Activation peptidePRO_0000025949Add
BLAST
Chaini65 – 412348Cathepsin DPRO_0000025950Add
BLAST
Chaini65 – 16197Cathepsin D light chainCuratedPRO_0000025951Add
BLAST
Chaini169 – 412244Cathepsin D heavy chainCuratedPRO_0000025952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631O-linked (GalNAc...)1 Publication
Disulfide bondi91 ↔ 1601 Publication
Disulfide bondi110 ↔ 1171 Publication
Glycosylationi134 – 1341N-linked (GlcNAc...)1 Publication
Glycosylationi263 – 2631N-linked (GlcNAc...)5 Publications
Disulfide bondi286 ↔ 2901 Publication
Disulfide bondi329 ↔ 366

Post-translational modificationi

N- and O-glycosylated.5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP07339.
PaxDbiP07339.
PeptideAtlasiP07339.
PRIDEiP07339.

2D gel databases

DOSAC-COBS-2DPAGEP07339.
REPRODUCTION-2DPAGEIPI00011229.
SWISS-2DPAGEP07339.
UCD-2DPAGEP07339.

PTM databases

PhosphoSiteiP07339.

Miscellaneous databases

PMAP-CutDBP07339.

Expressioni

Tissue specificityi

Expressed in the aorta extrcellular space (at protein level).1 Publication

Gene expression databases

BgeeiP07339.
CleanExiHS_CTSD.
ExpressionAtlasiP07339. baseline and differential.
GenevestigatoriP07339.

Organism-specific databases

HPAiCAB000109.
HPA003001.

Interactioni

Subunit structurei

Consists of a light chain and a heavy chain.

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP050672EBI-2115097,EBI-77613

Protein-protein interaction databases

BioGridi107889. 17 interactions.
DIPiDIP-43906N.
IntActiP07339. 18 interactions.
MINTiMINT-3005628.
STRINGi9606.ENSP00000236671.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 748Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 858Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 978Combined sources
Beta strandi103 – 1075Combined sources
Helixi115 – 1184Combined sources
Helixi125 – 1273Combined sources
Beta strandi132 – 14110Combined sources
Beta strandi146 – 15914Combined sources
Beta strandi172 – 18413Combined sources
Helixi189 – 1924Combined sources
Beta strandi194 – 2007Combined sources
Helixi204 – 2063Combined sources
Helixi208 – 2103Combined sources
Helixi214 – 2207Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi228 – 2336Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi239 – 24911Combined sources
Helixi252 – 2543Combined sources
Beta strandi255 – 2639Combined sources
Turni267 – 2704Combined sources
Beta strandi271 – 2744Combined sources
Beta strandi276 – 2794Combined sources
Turni280 – 2823Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi299 – 3035Combined sources
Helixi305 – 31410Combined sources
Beta strandi318 – 3214Combined sources
Beta strandi325 – 3273Combined sources
Helixi329 – 3346Combined sources
Beta strandi338 – 3425Combined sources
Beta strandi345 – 3495Combined sources
Helixi351 – 3544Combined sources
Beta strandi355 – 3606Combined sources
Beta strandi363 – 37210Combined sources
Turni377 – 3793Combined sources
Beta strandi383 – 3853Combined sources
Helixi387 – 3926Combined sources
Beta strandi393 – 3986Combined sources
Turni399 – 4024Combined sources
Beta strandi403 – 4097Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LYAX-ray2.50A/C65-161[»]
B/D170-410[»]
1LYBX-ray2.50A/C65-161[»]
B/D170-410[»]
1LYWX-ray2.50A/C/E/G65-161[»]
B/D/F/H170-410[»]
4OBZX-ray2.90A/C60-162[»]
B/D170-412[»]
4OC6X-ray2.64A60-162[»]
B170-412[»]
4OD9X-ray1.90A/C60-162[»]
B/D170-412[»]
ProteinModelPortaliP07339.
SMRiP07339. Positions 23-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07339.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG248684.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP07339.
KOiK01379.
OMAiTEGPIPE.
PhylomeDBiP07339.
TreeFamiTF314990.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07339-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPSSLLPLA LCLLAAPASA LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG
60 70 80 90 100
PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS
110 120 130 140 150
SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY
160 170 180 190 200
LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG
210 220 230 240 250
MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT
260 270 280 290 300
DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL
310 320 330 340 350
MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS
360 370 380 390 400
PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD
410
NNRVGFAEAA RL
Length:412
Mass (Da):44,552
Last modified:April 1, 1988 - v1
Checksum:i903FB8412E0CF0B0
GO

Polymorphismi

The Val-58 allele is significantly overrepresented in demented patients (11.8%) compared with non-demented controls (4.9%). Carriers of the Val-58 allele have a 3.1-fold increased risk for developing AD than non-carriers.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581A → V Associated with increased risk for AD; possibly influences secretion and intracellular maturation. 1 Publication
Corresponds to variant rs17571 [ dbSNP | Ensembl ].
VAR_011621
Natural varianti229 – 2291F → I in CLN10. 2 Publications
VAR_029362
Natural varianti282 – 2821G → R.1 Publication
Corresponds to variant rs147278302 [ dbSNP | Ensembl ].
VAR_058490
Natural varianti383 – 3831W → C in CLN10. 1 Publication
VAR_029363

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11233 mRNA. Translation: AAB59529.1.
X05344 mRNA. Translation: CAA28955.1.
M63138
, M63134, M63135, M63136, M63137 Genomic DNA. Translation: AAA51922.1.
CR456947 mRNA. Translation: CAG33228.1.
BT006910 mRNA. Translation: AAP35556.1.
BT020155 mRNA. Translation: AAV38957.1.
BC016320 mRNA. Translation: AAH16320.1.
L12980 Genomic DNA. Translation: AAA16314.1.
S74689 Genomic DNA. Translation: AAD14156.1.
S52557 Genomic DNA. Translation: AAD13868.1.
CCDSiCCDS7725.1.
PIRiA25771. KHHUD.
RefSeqiNP_001900.1. NM_001909.4.
UniGeneiHs.654447.

Genome annotation databases

EnsembliENST00000236671; ENSP00000236671; ENSG00000117984.
GeneIDi1509.
KEGGihsa:1509.
UCSCiuc001luc.2. human.

Polymorphism and mutation databases

BioMutaiCTSD.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NCL CTSD

Neural Ceroid Lipofuscinoses mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11233 mRNA. Translation: AAB59529.1.
X05344 mRNA. Translation: CAA28955.1.
M63138
, M63134, M63135, M63136, M63137 Genomic DNA. Translation: AAA51922.1.
CR456947 mRNA. Translation: CAG33228.1.
BT006910 mRNA. Translation: AAP35556.1.
BT020155 mRNA. Translation: AAV38957.1.
BC016320 mRNA. Translation: AAH16320.1.
L12980 Genomic DNA. Translation: AAA16314.1.
S74689 Genomic DNA. Translation: AAD14156.1.
S52557 Genomic DNA. Translation: AAD13868.1.
CCDSiCCDS7725.1.
PIRiA25771. KHHUD.
RefSeqiNP_001900.1. NM_001909.4.
UniGeneiHs.654447.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LYAX-ray2.50A/C65-161[»]
B/D170-410[»]
1LYBX-ray2.50A/C65-161[»]
B/D170-410[»]
1LYWX-ray2.50A/C/E/G65-161[»]
B/D/F/H170-410[»]
4OBZX-ray2.90A/C60-162[»]
B/D170-412[»]
4OC6X-ray2.64A60-162[»]
B170-412[»]
4OD9X-ray1.90A/C60-162[»]
B/D170-412[»]
ProteinModelPortaliP07339.
SMRiP07339. Positions 23-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107889. 17 interactions.
DIPiDIP-43906N.
IntActiP07339. 18 interactions.
MINTiMINT-3005628.
STRINGi9606.ENSP00000236671.

Chemistry

BindingDBiP07339.
ChEMBLiCHEMBL2581.
DrugBankiDB00030. Insulin Regular.
GuidetoPHARMACOLOGYi2345.

Protein family/group databases

MEROPSiA01.009.

PTM databases

PhosphoSiteiP07339.

Polymorphism and mutation databases

BioMutaiCTSD.
DMDMi115717.

2D gel databases

DOSAC-COBS-2DPAGEP07339.
REPRODUCTION-2DPAGEIPI00011229.
SWISS-2DPAGEP07339.
UCD-2DPAGEP07339.

Proteomic databases

MaxQBiP07339.
PaxDbiP07339.
PeptideAtlasiP07339.
PRIDEiP07339.

Protocols and materials databases

DNASUi1509.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236671; ENSP00000236671; ENSG00000117984.
GeneIDi1509.
KEGGihsa:1509.
UCSCiuc001luc.2. human.

Organism-specific databases

CTDi1509.
GeneCardsiGC11M001773.
GeneReviewsiCTSD.
H-InvDBHIX0009359.
HGNCiHGNC:2529. CTSD.
HPAiCAB000109.
HPA003001.
MIMi116840. gene.
610127. phenotype.
neXtProtiNX_P07339.
Orphaneti228337. CLN10 disease.
PharmGKBiPA27029.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG248684.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP07339.
KOiK01379.
OMAiTEGPIPE.
PhylomeDBiP07339.
TreeFamiTF314990.

Enzyme and pathway databases

BioCyciMetaCyc:HS04183-MONOMER.
BRENDAi3.4.23.5. 2681.
ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
REACT_150401. Collagen degradation.

Miscellaneous databases

EvolutionaryTraceiP07339.
GeneWikiiCathepsin_D.
GenomeRNAii1509.
NextBioi6247.
PMAP-CutDBP07339.
PROiP07339.
SOURCEiSearch...

Gene expression databases

BgeeiP07339.
CleanExiHS_CTSD.
ExpressionAtlasiP07339. baseline and differential.
GenevestigatoriP07339.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of cDNA for human cathepsin D."
    Faust P.L., Kornfeld S., Chirgwin J.M.
    Proc. Natl. Acad. Sci. U.S.A. 82:4910-4914(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells."
    Westley B.R., May F.E.B.
    Nucleic Acids Res. 15:3773-3786(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  7. "The human cathepsin D-encoding gene is transcribed from an estrogen-regulated and a constitutive start point."
    May F.E., Smith D.J., Westley B.R.
    Gene 134:277-282(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  8. "Characterization of the proximal estrogen-responsive element of human cathepsin D gene."
    Augereau P., Miralles F., Cavailles V., Gaudelet C., Parker M., Rochefort H.
    Mol. Endocrinol. 8:693-703(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  9. Cited for: PROTEIN SEQUENCE OF 170-180.
    Tissue: Liver.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  11. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-263.
  12. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-263.
    Tissue: Plasma.
  13. "Cathepsin D deficiency underlies congenital human neuronal ceroid-lipofuscinosis."
    Siintola E., Partanen S., Stromme P., Haapanen A., Haltia M., Maehlen J., Lehesjoki A.E., Tyynela J.
    Brain 129:1438-1445(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CLN10, VARIANT ARG-282.
  14. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  15. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-263.
    Tissue: Platelet.
  16. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-263.
    Tissue: Liver.
  17. "Proteomics characterization of extracellular space components in the human aorta."
    Didangelos A., Yin X., Mandal K., Baumert M., Jahangiri M., Mayr M.
    Mol. Cell. Proteomics 9:2048-2062(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
    Halim A., Ruetschi U., Larson G., Nilsson J.
    J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-63, IDENTIFICATION BY MASS SPECTROMETRY.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "Two crystal structures for cathepsin D: the lysosomal targeting signal and active site."
    Metcalf P., Fusek M.
    EMBO J. 12:1293-1302(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
    Tissue: Spleen.
  22. "Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design."
    Baldwin E.T., Bhat T.N., Gulnik S., Hosur M.V., Sowder R.C. II, Cachau R.E., Collins J., Silva A.M., Erickson J.W.
    Proc. Natl. Acad. Sci. U.S.A. 90:6796-6800(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Tissue: Liver.
  23. "A genetic variation of cathepsin D is a major risk factor for Alzheimer's disease."
    Papassotiropoulos A., Bagli M., Kurz A., Kornhuber J., Forstl H., Maier W., Pauls J., Lautenschlager N., Heun R.
    Ann. Neurol. 47:399-403(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-58.
  24. "Cathepsin D deficiency is associated with a human neurodegenerative disorder."
    Steinfeld R., Reinhardt K., Schreiber K., Hillebrand M., Kraetzner R., Bruck W., Saftig P., Gartner J.
    Am. J. Hum. Genet. 78:988-998(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CLN10 ILE-229 AND CYS-383.
  25. "Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses."
    Kousi M., Lehesjoki A.E., Mole S.E.
    Hum. Mutat. 33:42-63(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CLN10 ILE-229.

Entry informationi

Entry nameiCATD_HUMAN
AccessioniPrimary (citable) accession number: P07339
Secondary accession number(s): Q6IB57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 29, 2015
This is version 182 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.