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P10619

- PPGB_HUMAN

UniProt

P10619 - PPGB_HUMAN

Protein

Lysosomal protective protein

Gene

CTSA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.1 Publication

    Catalytic activityi

    Release of a C-terminal amino acid with broad specificity.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei178 – 1781
    Active sitei400 – 4001By similarity
    Active sitei457 – 4571

    GO - Molecular functioni

    1. carboxypeptidase activity Source: ProtInc
    2. enzyme activator activity Source: ProtInc
    3. serine-type carboxypeptidase activity Source: InterPro

    GO - Biological processi

    1. glycosphingolipid metabolic process Source: Reactome
    2. intracellular protein transport Source: ProtInc
    3. positive regulation of catalytic activity Source: GOC
    4. small molecule metabolic process Source: Reactome
    5. sphingolipid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Protease

    Enzyme and pathway databases

    ReactomeiREACT_116105. Glycosphingolipid metabolism.
    REACT_121399. MHC class II antigen presentation.
    REACT_200874. Sialic acid metabolism.
    SignaLinkiP10619.

    Protein family/group databases

    MEROPSiS10.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysosomal protective protein (EC:3.4.16.5)
    Alternative name(s):
    Carboxypeptidase C
    Carboxypeptidase L
    Cathepsin A
    Protective protein cathepsin A
    Short name:
    PPCA
    Protective protein for beta-galactosidase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CTSA
    Synonyms:PPGB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:9251. CTSA.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: ProtInc
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular membrane-bounded organelle Source: HPA
    4. lysosomal lumen Source: Reactome
    5. lysosome Source: UniProtKB
    6. membrane Source: UniProtKB
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Galactosialidosis (GSL) [MIM:256540]: A lysosomal storage disease associated with a combined deficiency of beta-galactosidase and neuraminidase, secondary to a defect in cathepsin A. All patients have clinical manifestations typical of a lysosomal disorder, such as coarse facies, cherry red spots, vertebral changes, foam cells in the bone marrow, and vacuolated lymphocytes. Three phenotypic subtypes are recognized. The early infantile form is associated with fetal hydrops, edema, ascites, visceromegaly, skeletal dysplasia, and early death. The late infantile type is characterized by hepatosplenomegaly, growth retardation, cardiac involvement, and a normal or mildly affected mental state. The juvenile/adult form is characterized by myoclonus, ataxia, angiokeratoma, mental retardation, neurologic deterioration, absence of visceromegaly, and long survival.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491Q → R in GSL. 1 Publication
    VAR_001385
    Natural varianti51 – 511S → Y in GSL. 1 Publication
    VAR_063018
    Natural varianti65 – 651W → R in GSL. 1 Publication
    Corresponds to variant rs28934603 [ dbSNP | Ensembl ].
    VAR_001386
    Natural varianti90 – 901S → L in GSL. 1 Publication
    VAR_001387
    Natural varianti132 – 1321V → M in GSL. 1 Publication
    VAR_063019
    Natural varianti236 – 2361L → P in GSL. 1 Publication
    VAR_063020
    Natural varianti249 – 2491Y → N in GSL; small amount of activity. 2 Publications
    VAR_001388
    Natural varianti395 – 3951Y → C in GSL; loss of activity. 1 Publication
    VAR_001389
    Natural varianti406 – 4061M → T in GSL. 1 Publication
    VAR_063021
    Natural varianti439 – 4391G → S in GSL. 1 Publication
    VAR_063022
    Natural varianti440 – 4401F → V in GSL. 2 Publications
    VAR_001390
    Natural varianti453 – 4531K → E in GSL. 1 Publication
    VAR_063023

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi178 – 1781S → A: Inactivates the enzyme. 1 Publication
    Mutagenesisi457 – 4571H → Q: Inactivates the enzyme. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi256540. phenotype.
    Orphaneti351. Galactosialidosis.
    PharmGKBiPA33572.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28282 PublicationsAdd
    BLAST
    Chaini29 – 480452Lysosomal protective proteinPRO_0000004274Add
    BLAST
    Chaini29 – 326298Lysosomal protective protein 32 kDa chainPRO_0000004275Add
    BLAST
    Chaini327 – 480154Lysosomal protective protein 20 kDa chainPRO_0000004276Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi88 ↔ 362
    Glycosylationi145 – 1451N-linked (GlcNAc...)2 Publications
    Disulfide bondi240 ↔ 256
    Disulfide bondi241 ↔ 246
    Disulfide bondi281 ↔ 331
    Glycosylationi333 – 3331N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP10619.
    PaxDbiP10619.
    PRIDEiP10619.

    2D gel databases

    OGPiP10619.

    PTM databases

    PhosphoSiteiP10619.

    Expressioni

    Gene expression databases

    ArrayExpressiP10619.
    BgeeiP10619.
    CleanExiHS_CTSA.
    GenevestigatoriP10619.

    Organism-specific databases

    HPAiCAB024930.
    HPA031068.

    Interactioni

    Subunit structurei

    Heterodimer of a 32 kDa chain and a 20 kDa chain; disulfide-linked.

    Protein-protein interaction databases

    BioGridi111472. 20 interactions.
    IntActiP10619. 8 interactions.
    MINTiMINT-3007366.
    STRINGi9606.ENSP00000361562.

    Structurei

    Secondary structure

    1
    480
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 333
    Beta strandi41 – 433
    Beta strandi49 – 557
    Beta strandi60 – 678
    Turni73 – 753
    Beta strandi78 – 825
    Turni85 – 873
    Helixi91 – 966
    Beta strandi99 – 1035
    Beta strandi110 – 1123
    Helixi117 – 1193
    Beta strandi120 – 1267
    Beta strandi136 – 1394
    Helixi146 – 16318
    Helixi165 – 1673
    Beta strandi168 – 1703
    Beta strandi172 – 1776
    Helixi180 – 19213
    Beta strandi199 – 2068
    Helixi211 – 22414
    Helixi230 – 24011
    Helixi254 – 26815
    Beta strandi269 – 2713
    Beta strandi286 – 2927
    Beta strandi295 – 2984
    Helixi315 – 3173
    Helixi318 – 3214
    Beta strandi324 – 3274
    Helixi335 – 3417
    Helixi344 – 3496
    Helixi364 – 3696
    Beta strandi375 – 3773
    Helixi378 – 3869
    Beta strandi391 – 3977
    Beta strandi401 – 4033
    Helixi405 – 41410
    Beta strandi424 – 4296
    Helixi431 – 4333
    Beta strandi435 – 44410
    Beta strandi447 – 4526
    Helixi459 – 4624
    Helixi464 – 47512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IVYX-ray2.20A/B29-480[»]
    3BP4X-ray1.85C2-10[»]
    3BP7X-ray1.80C2-10[»]
    3BXNX-ray1.86C2-10[»]
    4AZ0X-ray2.17A29-326[»]
    B327-480[»]
    4AZ3X-ray2.04A29-326[»]
    B327-480[»]
    4CI9X-ray1.58A29-480[»]
    4CIAX-ray1.98A29-480[»]
    4CIBX-ray1.89A29-480[»]
    4MWSX-ray2.80A/B29-480[»]
    4MWTX-ray3.85A/B29-480[»]
    ProteinModelPortaliP10619.
    SMRiP10619. Positions 29-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10619.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S10 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2939.
    HOVERGENiHBG053652.
    InParanoidiP10619.
    KOiK13289.
    OrthoDBiEOG7KQ21H.
    PhylomeDBiP10619.
    TreeFamiTF323769.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view]
    PANTHERiPTHR11802. PTHR11802. 1 hit.
    PfamiPF00450. Peptidase_S10. 1 hit.
    [Graphical view]
    PRINTSiPR00724. CRBOXYPTASEC.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P10619-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MIRAAPPPLF LLLLLLLLLV SWASRGEAAP DQDEIQRLPG LAKQPSFRQY    50
    SGYLKGSGSK HLHYWFVESQ KDPENSPVVL WLNGGPGCSS LDGLLTEHGP 100
    FLVQPDGVTL EYNPYSWNLI ANVLYLESPA GVGFSYSDDK FYATNDTEVA 150
    QSNFEALQDF FRLFPEYKNN KLFLTGESYA GIYIPTLAVL VMQDPSMNLQ 200
    GLAVGNGLSS YEQNDNSLVY FAYYHGLLGN RLWSSLQTHC CSQNKCNFYD 250
    NKDLECVTNL QEVARIVGNS GLNIYNLYAP CAGGVPSHFR YEKDTVVVQD 300
    LGNIFTRLPL KRMWHQALLR SGDKVRMDPP CTNTTAASTY LNNPYVRKAL 350
    NIPEQLPQWD MCNFLVNLQY RRLYRSMNSQ YLKLLSSQKY QILLYNGDVD 400
    MACNFMGDEW FVDSLNQKME VQRRPWLVKY GDSGEQIAGF VKEFSHIAFL 450
    TIKGAGHMVP TDKPLAAFTM FSRFLNKQPY 480
    Length:480
    Mass (Da):54,466
    Last modified:April 16, 2002 - v2
    Checksum:i46B737DEE775C508
    GO
    Isoform 2 (identifier: P10619-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         102-118: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:463
    Mass (Da):52,489
    Checksum:i7342A76945E40684
    GO

    Sequence cautioni

    The sequence CAI20248.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191Missing in AAH00597. (PubMed:15489334)Curated
    Sequence conflicti56 – 561G → S in AAA36476. (PubMed:3136930)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491Q → R in GSL. 1 Publication
    VAR_001385
    Natural varianti51 – 511S → Y in GSL. 1 Publication
    VAR_063018
    Natural varianti65 – 651W → R in GSL. 1 Publication
    Corresponds to variant rs28934603 [ dbSNP | Ensembl ].
    VAR_001386
    Natural varianti90 – 901S → L in GSL. 1 Publication
    VAR_001387
    Natural varianti132 – 1321V → M in GSL. 1 Publication
    VAR_063019
    Natural varianti236 – 2361L → P in GSL. 1 Publication
    VAR_063020
    Natural varianti249 – 2491Y → N in GSL; small amount of activity. 2 Publications
    VAR_001388
    Natural varianti395 – 3951Y → C in GSL; loss of activity. 1 Publication
    VAR_001389
    Natural varianti406 – 4061M → T in GSL. 1 Publication
    VAR_063021
    Natural varianti439 – 4391G → S in GSL. 1 Publication
    VAR_063022
    Natural varianti440 – 4401F → V in GSL. 2 Publications
    VAR_001390
    Natural varianti453 – 4531K → E in GSL. 1 Publication
    VAR_063023

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei102 – 11817Missing in isoform 2. CuratedVSP_054832Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22960 mRNA. Translation: AAA36476.1.
    AK312898 mRNA. Translation: BAG35745.1.
    AL008726 Genomic DNA. Translation: CAA15501.1.
    AL008726 Genomic DNA. Translation: CAI20248.1. Different initiation.
    BC000597 mRNA. Translation: AAH00597.1.
    BC093009 mRNA. Translation: AAH93009.1.
    CCDSiCCDS46609.1. [P10619-1]
    PIRiA31589.
    RefSeqiNP_000299.2. NM_000308.2.
    NP_001121167.1. NM_001127695.1. [P10619-1]
    NP_001161066.1. NM_001167594.1.
    UniGeneiHs.609336.

    Genome annotation databases

    EnsembliENST00000191018; ENSP00000191018; ENSG00000064601. [P10619-1]
    ENST00000372459; ENSP00000361537; ENSG00000064601. [P10619-1]
    GeneIDi5476.
    KEGGihsa:5476.
    UCSCiuc002xqh.3. human. [P10619-1]

    Polymorphism databases

    DMDMi20178316.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22960 mRNA. Translation: AAA36476.1 .
    AK312898 mRNA. Translation: BAG35745.1 .
    AL008726 Genomic DNA. Translation: CAA15501.1 .
    AL008726 Genomic DNA. Translation: CAI20248.1 . Different initiation.
    BC000597 mRNA. Translation: AAH00597.1 .
    BC093009 mRNA. Translation: AAH93009.1 .
    CCDSi CCDS46609.1. [P10619-1 ]
    PIRi A31589.
    RefSeqi NP_000299.2. NM_000308.2.
    NP_001121167.1. NM_001127695.1. [P10619-1 ]
    NP_001161066.1. NM_001167594.1.
    UniGenei Hs.609336.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IVY X-ray 2.20 A/B 29-480 [» ]
    3BP4 X-ray 1.85 C 2-10 [» ]
    3BP7 X-ray 1.80 C 2-10 [» ]
    3BXN X-ray 1.86 C 2-10 [» ]
    4AZ0 X-ray 2.17 A 29-326 [» ]
    B 327-480 [» ]
    4AZ3 X-ray 2.04 A 29-326 [» ]
    B 327-480 [» ]
    4CI9 X-ray 1.58 A 29-480 [» ]
    4CIA X-ray 1.98 A 29-480 [» ]
    4CIB X-ray 1.89 A 29-480 [» ]
    4MWS X-ray 2.80 A/B 29-480 [» ]
    4MWT X-ray 3.85 A/B 29-480 [» ]
    ProteinModelPortali P10619.
    SMRi P10619. Positions 29-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111472. 20 interactions.
    IntActi P10619. 8 interactions.
    MINTi MINT-3007366.
    STRINGi 9606.ENSP00000361562.

    Chemistry

    BindingDBi P10619.
    ChEMBLi CHEMBL6115.

    Protein family/group databases

    MEROPSi S10.002.

    PTM databases

    PhosphoSitei P10619.

    Polymorphism databases

    DMDMi 20178316.

    2D gel databases

    OGPi P10619.

    Proteomic databases

    MaxQBi P10619.
    PaxDbi P10619.
    PRIDEi P10619.

    Protocols and materials databases

    DNASUi 5476.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000191018 ; ENSP00000191018 ; ENSG00000064601 . [P10619-1 ]
    ENST00000372459 ; ENSP00000361537 ; ENSG00000064601 . [P10619-1 ]
    GeneIDi 5476.
    KEGGi hsa:5476.
    UCSCi uc002xqh.3. human. [P10619-1 ]

    Organism-specific databases

    CTDi 5476.
    GeneCardsi GC20P044519.
    HGNCi HGNC:9251. CTSA.
    HPAi CAB024930.
    HPA031068.
    MIMi 256540. phenotype.
    613111. gene.
    neXtProti NX_P10619.
    Orphaneti 351. Galactosialidosis.
    PharmGKBi PA33572.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2939.
    HOVERGENi HBG053652.
    InParanoidi P10619.
    KOi K13289.
    OrthoDBi EOG7KQ21H.
    PhylomeDBi P10619.
    TreeFami TF323769.

    Enzyme and pathway databases

    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_121399. MHC class II antigen presentation.
    REACT_200874. Sialic acid metabolism.
    SignaLinki P10619.

    Miscellaneous databases

    ChiTaRSi CTSA. human.
    EvolutionaryTracei P10619.
    GeneWikii Cathepsin_A.
    GenomeRNAii 5476.
    NextBioi 21202.
    PROi P10619.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10619.
    Bgeei P10619.
    CleanExi HS_CTSA.
    Genevestigatori P10619.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR001563. Peptidase_S10.
    IPR018202. Peptidase_S10_AS.
    [Graphical view ]
    PANTHERi PTHR11802. PTHR11802. 1 hit.
    Pfami PF00450. Peptidase_S10. 1 hit.
    [Graphical view ]
    PRINTSi PR00724. CRBOXYPTASEC.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
    PS00131. CARBOXYPEPT_SER_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of cDNA encoding the human 'protective protein' associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases."
      Galjart N.J., Gillemans N., Harris A., van de Horst G.T.J., Verheijen F.W., Galjaard H., D'Azzo A.
      Cell 54:755-764(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Placenta and Skin.
    5. "A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal 'protective protein'."
      Jackman H.L., Tan F., Tamei H., Beurling-Harbury C., Li X.-Y., Skidgel R.A., Erdoes E.G.
      J. Biol. Chem. 265:11265-11272(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-53 AND 327-351.
      Tissue: Platelet.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-37.
      Tissue: Platelet.
    7. "Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function."
      Galjart N.J., Morreau H., Willemsen R., Gillemans N., Bonten E.J., D'Azzo A.
      J. Biol. Chem. 266:14754-14762(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS.
    8. "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-145.
      Tissue: Platelet.
    9. "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-145 AND ASN-333.
      Tissue: Liver.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism."
      Rudenko G., Bonten E., D'Azzo A., Hol W.G.J.
      Structure 3:1249-1259(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    12. "A mutation in a mild form of galactosialidosis impairs dimerization of the protective protein and renders it unstable."
      Zhou X.Y., Galjart N.J., Willemsen R., Gillemans N., Galjaard H., D'Azzo A.
      EMBO J. 10:4041-4048(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSL VAL-440.
    13. Cited for: VARIANTS GSL ARG-49; ARG-65; LEU-90; ASN-249 AND CYS-395.
    14. "Molecular and biochemical analysis of protective protein/cathepsin A mutations: correlation with clinical severity in galactosialidosis."
      Zhou X.Y., van der Spoel A., Rottier R., Hale G., Willemsen R., Berry G.T., Strisciuglio P., Morrone A., Zammarchi E., Andria G., d'Azzo A.
      Hum. Mol. Genet. 5:1977-1987(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GSL TYR-51; MET-132; PRO-236; ASN-249; THR-406; SER-439 AND VAL-440.
    15. "Structural and functional study of K453E mutant protective protein/cathepsin A causing the late infantile form of galactosialidosis."
      Takiguchi K., Itoh K., Shimmoto M., Ozand P.T., Doi H., Sakuraba H.
      J. Hum. Genet. 45:200-206(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSL GLU-453.

    Entry informationi

    Entry nameiPPGB_HUMAN
    AccessioniPrimary (citable) accession number: P10619
    Secondary accession number(s): B2R798
    , Q561W6, Q5JZH1, Q96KJ2, Q9BR08, Q9BW68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 180 of the entry and version 2 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 20
      Human chromosome 20: 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