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P07339

- CATD_HUMAN

UniProt

P07339 - CATD_HUMAN

Protein

Cathepsin D

Gene

CTSD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    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 – 9711 PublicationPROSITE-ProRule annotation
    Active sitei295 – 29511 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: ProtInc
    2. protein binding Source: IntAct

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. autophagic vacuole assembly Source: Ensembl
    3. cell death Source: UniProtKB-KW
    4. collagen catabolic process Source: Reactome
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04183-MONOMER.
    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: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2529. CTSD.

    Subcellular locationi

    Lysosome. Melanosome. Secretedextracellular space
    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: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. lysosomal lumen Source: Reactome
    5. lysosome Source: UniProtKB
    6. melanosome Source: UniProtKB-SubCell
    7. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Lysosome, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ceroid lipofuscinosis, neuronal, 10 (CLN10) [MIM:610127]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP07339.
    BgeeiP07339.
    CleanExiHS_CTSD.
    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 – 748
    Turni75 – 773
    Beta strandi78 – 858
    Turni86 – 894
    Beta strandi90 – 978
    Beta strandi103 – 1075
    Helixi115 – 1184
    Helixi125 – 1273
    Beta strandi132 – 14110
    Beta strandi146 – 15914
    Beta strandi172 – 18413
    Turni189 – 1913
    Beta strandi194 – 2007
    Helixi204 – 2063
    Helixi208 – 2103
    Helixi214 – 2207
    Beta strandi224 – 23310
    Beta strandi236 – 2383
    Beta strandi243 – 2475
    Helixi252 – 2543
    Beta strandi255 – 2639
    Turni267 – 2704
    Beta strandi271 – 2799
    Turni280 – 2823
    Beta strandi284 – 2863
    Beta strandi290 – 2945
    Beta strandi299 – 3035
    Helixi305 – 31511
    Beta strandi318 – 3214
    Beta strandi324 – 3285
    Helixi329 – 3346
    Beta strandi338 – 3425
    Beta strandi345 – 3495
    Turni351 – 3533
    Beta strandi354 – 3585
    Turni359 – 3624
    Beta strandi363 – 37210
    Turni377 – 3793
    Beta strandi383 – 3853
    Helixi387 – 3904
    Beta strandi393 – 3986
    Turni399 – 4024
    Beta strandi403 – 4097

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    OMAiNIACLMH.
    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

    MQPSSLLPLA LCLLAAPASA LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG    50
    PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS 100
    SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY 150
    LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG 200
    MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT 250
    DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL 300
    MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS 350
    PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD 400
    NNRVGFAEAA RL 412
    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:
    EMBL
    GenBank
    DDBJ
    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 databases

    DMDMi115717.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NCL CTSD

    Neural Ceroid Lipofuscinoses mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS7725.1.
    PIRi A25771. KHHUD.
    RefSeqi NP_001900.1. NM_001909.4.
    UniGenei Hs.654447.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LYA X-ray 2.50 A/C 65-161 [» ]
    B/D 170-410 [» ]
    1LYB X-ray 2.50 A/C 65-161 [» ]
    B/D 170-410 [» ]
    1LYW X-ray 2.50 A/C/E/G 65-161 [» ]
    B/D/F/H 170-410 [» ]
    ProteinModelPortali P07339.
    SMRi P07339. Positions 23-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107889. 17 interactions.
    DIPi DIP-43906N.
    IntActi P07339. 18 interactions.
    MINTi MINT-3005628.
    STRINGi 9606.ENSP00000236671.

    Chemistry

    BindingDBi P07339.
    ChEMBLi CHEMBL2581.
    DrugBanki DB00047. Insulin Glargine recombinant.
    DB00046. Insulin Lyspro recombinant.
    DB00030. Insulin recombinant.
    DB00071. Insulin, porcine.
    GuidetoPHARMACOLOGYi 2345.

    Protein family/group databases

    MEROPSi A01.009.

    PTM databases

    PhosphoSitei P07339.

    Polymorphism databases

    DMDMi 115717.

    2D gel databases

    DOSAC-COBS-2DPAGE P07339.
    REPRODUCTION-2DPAGE IPI00011229.
    SWISS-2DPAGE P07339.
    UCD-2DPAGE P07339.

    Proteomic databases

    MaxQBi P07339.
    PaxDbi P07339.
    PeptideAtlasi P07339.
    PRIDEi P07339.

    Protocols and materials databases

    DNASUi 1509.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000236671 ; ENSP00000236671 ; ENSG00000117984 .
    GeneIDi 1509.
    KEGGi hsa:1509.
    UCSCi uc001luc.2. human.

    Organism-specific databases

    CTDi 1509.
    GeneCardsi GC11M001773.
    GeneReviewsi CTSD.
    H-InvDB HIX0009359.
    HGNCi HGNC:2529. CTSD.
    HPAi CAB000109.
    HPA003001.
    MIMi 116840. gene.
    610127. phenotype.
    neXtProti NX_P07339.
    Orphaneti 228337. CLN10 disease.
    PharmGKBi PA27029.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248684.
    HOGENOMi HOG000197681.
    HOVERGENi HBG000482.
    InParanoidi P07339.
    KOi K01379.
    OMAi NIACLMH.
    PhylomeDBi P07339.
    TreeFami TF314990.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04183-MONOMER.
    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei P07339.
    GeneWikii Cathepsin_D.
    GenomeRNAii 1509.
    NextBioi 6247.
    PMAP-CutDB P07339.
    PROi P07339.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07339.
    Bgeei P07339.
    CleanExi HS_CTSD.
    Genevestigatori P07339.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    21. "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.
    22. "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.
    23. "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.
    24. "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: October 1, 2014
    This is version 175 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