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P20933

- ASPG_HUMAN

UniProt

P20933 - ASPG_HUMAN

Protein

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase

Gene

AGA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.

    Catalytic activityi

    N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei206 – 2061Nucleophile1 Publication

    GO - Molecular functioni

    1. N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Source: UniProtKB
    2. peptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. protein deglycosylation Source: UniProtKB
    2. protein maturation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease

    Enzyme and pathway databases

    BRENDAi3.5.1.26. 2681.
    SABIO-RKP20933.

    Protein family/group databases

    MEROPSiT02.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase (EC:3.5.1.26)
    Alternative name(s):
    Aspartylglucosaminidase
    Glycosylasparaginase
    N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:AGA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:318. AGA.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. lysosome Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Aspartylglucosaminuria (AGU) [MIM:208400]: An inborn lysosomal storage disease causing excess accumulation of glycoasparagine in the body tissues and its increased excretion in urine. Clinical features include mild to severe mental retardation manifesting from the age of two, coarse facial features and mild connective tissue abnormalities.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121V → L in AGU; uncertain pathological significance. 1 Publication
    Corresponds to variant rs74626221 [ dbSNP | Ensembl ].
    VAR_015427
    Natural varianti60 – 601G → D in AGU.
    VAR_005069
    Natural varianti72 – 721S → P in AGU; specifically prevents the proteolytic activation cleavage of AGA in the endoplasmic reticulum. 1 Publication
    VAR_005070
    Natural varianti100 – 1001G → E in AGU. 1 Publication
    VAR_015428
    Natural varianti101 – 1011A → V in AGU.
    VAR_005071
    Natural varianti135 – 1351F → S in AGU. 1 Publication
    VAR_015429
    Natural varianti161 – 1611R → Q in AGU. 3 Publications
    Corresponds to variant rs192195150 [ dbSNP | Ensembl ].
    VAR_005072
    Natural varianti163 – 1631C → S in AGU; most frequent mutation; abolishes autocatalytic cleavage and enzyme activity. 3 Publications
    Corresponds to variant rs121964904 [ dbSNP | Ensembl ].
    VAR_005073
    Natural varianti252 – 2521G → E in AGU. 1 Publication
    VAR_015430
    Natural varianti252 – 2521G → R in AGU. 1 Publication
    VAR_015431
    Natural varianti257 – 2571T → I in AGU. 1 Publication
    VAR_015432
    Natural varianti302 – 3021G → R in AGU.
    VAR_005074
    Natural varianti306 – 3061C → R in AGU.
    VAR_005075

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi208400. phenotype.
    Orphaneti93. Aspartylglucosaminuria.
    PharmGKBiPA24615.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Chaini24 – 205182Glycosylasparaginase alpha chainPRO_0000002333Add
    BLAST
    Chaini206 – 346141Glycosylasparaginase beta chainPRO_0000002334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Blocked amino end (Ser)
    Glycosylationi38 – 381N-linked (GlcNAc...)3 Publications
    Disulfide bondi64 ↔ 691 Publication
    Disulfide bondi163 ↔ 1791 Publication
    Disulfide bondi286 ↔ 3061 Publication
    Glycosylationi308 – 3081N-linked (GlcNAc...)1 Publication
    Disulfide bondi317 ↔ 3451 Publication

    Post-translational modificationi

    Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP20933.
    PaxDbiP20933.
    PRIDEiP20933.

    PTM databases

    PhosphoSiteiP20933.

    Miscellaneous databases

    PMAP-CutDBP20933.

    Expressioni

    Gene expression databases

    ArrayExpressiP20933.
    BgeeiP20933.
    CleanExiHS_AGA.
    GenevestigatoriP20933.

    Organism-specific databases

    HPAiHPA031415.
    HPA031417.

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.1 Publication

    Protein-protein interaction databases

    BioGridi106683. 3 interactions.
    IntActiP20933. 2 interactions.
    STRINGi9606.ENSP00000264595.

    Structurei

    Secondary structure

    1
    346
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 358
    Helixi37 – 4812
    Helixi53 – 6715
    Helixi69 – 713
    Beta strandi72 – 776
    Beta strandi87 – 937
    Turni94 – 963
    Beta strandi99 – 1057
    Beta strandi107 – 1093
    Helixi111 – 12111
    Beta strandi125 – 1284
    Helixi129 – 13810
    Helixi149 – 16012
    Turni175 – 1773
    Beta strandi207 – 2126
    Beta strandi214 – 2163
    Beta strandi218 – 2247
    Turni241 – 2433
    Beta strandi244 – 2485
    Turni249 – 2513
    Beta strandi252 – 2587
    Helixi260 – 2634
    Helixi264 – 2663
    Helixi268 – 27710
    Helixi282 – 29615
    Beta strandi302 – 3087
    Beta strandi313 – 3186
    Beta strandi325 – 3317
    Turni333 – 3353
    Beta strandi339 – 3446

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1APYX-ray2.00A/C24-185[»]
    B/D206-346[»]
    1APZX-ray2.30A/C24-185[»]
    B/D206-346[»]
    ProteinModelPortaliP20933.
    SMRiP20933. Positions 25-185, 206-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20933.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni234 – 2374Substrate binding
    Regioni257 – 2604Substrate binding

    Sequence similaritiesi

    Belongs to the Ntn-hydrolase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1446.
    HOVERGENiHBG004289.
    InParanoidiP20933.
    KOiK01444.
    OMAiKFFGAVI.
    OrthoDBiEOG7RV9GJ.
    PhylomeDBiP20933.
    TreeFamiTF300756.

    Family and domain databases

    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000246. Peptidase_T2.
    [Graphical view]
    PANTHERiPTHR10188. PTHR10188. 1 hit.
    PfamiPF01112. Asparaginase_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P20933-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARKSNLPVL LVPFLLCQAL VRCSSPLPLV VNTWPFKNAT EAAWRALASG    50
    GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG 100
    AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA 150
    SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED 200
    DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT 250
    AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF 300
    FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCI 346
    Length:346
    Mass (Da):37,208
    Last modified:February 9, 2010 - v2
    Checksum:i766F1690B5B62FFA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211V → A in AAB60655. (PubMed:1840528)Curated
    Sequence conflicti21 – 211V → A in CAA43958. (PubMed:1840528)Curated
    Sequence conflicti25 – 251S → C AA sequence (PubMed:2011603)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121V → L in AGU; uncertain pathological significance. 1 Publication
    Corresponds to variant rs74626221 [ dbSNP | Ensembl ].
    VAR_015427
    Natural varianti60 – 601G → D in AGU.
    VAR_005069
    Natural varianti72 – 721S → P in AGU; specifically prevents the proteolytic activation cleavage of AGA in the endoplasmic reticulum. 1 Publication
    VAR_005070
    Natural varianti100 – 1001G → E in AGU. 1 Publication
    VAR_015428
    Natural varianti101 – 1011A → V in AGU.
    VAR_005071
    Natural varianti135 – 1351F → S in AGU. 1 Publication
    VAR_015429
    Natural varianti149 – 1491T → S.8 Publications
    Corresponds to variant rs2228119 [ dbSNP | Ensembl ].
    VAR_033533
    Natural varianti161 – 1611R → Q in AGU. 3 Publications
    Corresponds to variant rs192195150 [ dbSNP | Ensembl ].
    VAR_005072
    Natural varianti163 – 1631C → S in AGU; most frequent mutation; abolishes autocatalytic cleavage and enzyme activity. 3 Publications
    Corresponds to variant rs121964904 [ dbSNP | Ensembl ].
    VAR_005073
    Natural varianti252 – 2521G → E in AGU. 1 Publication
    VAR_015430
    Natural varianti252 – 2521G → R in AGU. 1 Publication
    VAR_015431
    Natural varianti257 – 2571T → I in AGU. 1 Publication
    VAR_015432
    Natural varianti302 – 3021G → R in AGU.
    VAR_005074
    Natural varianti306 – 3061C → R in AGU.
    VAR_005075
    Natural varianti322 – 3221T → I.
    Corresponds to variant rs56849061 [ dbSNP | Ensembl ].
    VAR_061026

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55762 mRNA. Translation: CAA39288.1.
    X55330 mRNA. Translation: CAA39029.1.
    U21281
    , U21273, U21274, U21275, U21277, U21278, U21279, U21280 Genomic DNA. Translation: AAB60655.1.
    X61959 Genomic DNA. Translation: CAA43958.1.
    M64073 mRNA. Translation: AAA35903.1.
    M64075 mRNA. Translation: AAA35904.1. Sequence problems.
    M64076 mRNA. Translation: AAA35905.1. Sequence problems.
    M60808 mRNA. Translation: AAA35901.1.
    M60809 mRNA. Translation: AAA35902.1.
    AK312982 mRNA. Translation: BAG35819.1.
    CR541715 mRNA. Translation: CAG46516.1.
    AC078881 Genomic DNA. Translation: AAY40915.1.
    AC027627 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04714.1.
    CH471056 Genomic DNA. Translation: EAX04715.1.
    BC012392 mRNA. Translation: AAH12392.1.
    CCDSiCCDS3829.1.
    PIRiS11343. MUHUGD.
    RefSeqiNP_000018.2. NM_000027.3.
    NP_001165459.1. NM_001171988.1.
    UniGeneiHs.207776.

    Genome annotation databases

    EnsembliENST00000264595; ENSP00000264595; ENSG00000038002.
    GeneIDi175.
    KEGGihsa:175.
    UCSCiuc003iuu.2. human.

    Polymorphism databases

    DMDMi288558804.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55762 mRNA. Translation: CAA39288.1 .
    X55330 mRNA. Translation: CAA39029.1 .
    U21281
    , U21273 , U21274 , U21275 , U21277 , U21278 , U21279 , U21280 Genomic DNA. Translation: AAB60655.1 .
    X61959 Genomic DNA. Translation: CAA43958.1 .
    M64073 mRNA. Translation: AAA35903.1 .
    M64075 mRNA. Translation: AAA35904.1 . Sequence problems.
    M64076 mRNA. Translation: AAA35905.1 . Sequence problems.
    M60808 mRNA. Translation: AAA35901.1 .
    M60809 mRNA. Translation: AAA35902.1 .
    AK312982 mRNA. Translation: BAG35819.1 .
    CR541715 mRNA. Translation: CAG46516.1 .
    AC078881 Genomic DNA. Translation: AAY40915.1 .
    AC027627 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04714.1 .
    CH471056 Genomic DNA. Translation: EAX04715.1 .
    BC012392 mRNA. Translation: AAH12392.1 .
    CCDSi CCDS3829.1.
    PIRi S11343. MUHUGD.
    RefSeqi NP_000018.2. NM_000027.3.
    NP_001165459.1. NM_001171988.1.
    UniGenei Hs.207776.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1APY X-ray 2.00 A/C 24-185 [» ]
    B/D 206-346 [» ]
    1APZ X-ray 2.30 A/C 24-185 [» ]
    B/D 206-346 [» ]
    ProteinModelPortali P20933.
    SMRi P20933. Positions 25-185, 206-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106683. 3 interactions.
    IntActi P20933. 2 interactions.
    STRINGi 9606.ENSP00000264595.

    Chemistry

    BindingDBi P20933.

    Protein family/group databases

    MEROPSi T02.001.

    PTM databases

    PhosphoSitei P20933.

    Polymorphism databases

    DMDMi 288558804.

    Proteomic databases

    MaxQBi P20933.
    PaxDbi P20933.
    PRIDEi P20933.

    Protocols and materials databases

    DNASUi 175.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264595 ; ENSP00000264595 ; ENSG00000038002 .
    GeneIDi 175.
    KEGGi hsa:175.
    UCSCi uc003iuu.2. human.

    Organism-specific databases

    CTDi 175.
    GeneCardsi GC04M178351.
    H-InvDB HIX0004652.
    HGNCi HGNC:318. AGA.
    HPAi HPA031415.
    HPA031417.
    MIMi 208400. phenotype.
    613228. gene.
    neXtProti NX_P20933.
    Orphaneti 93. Aspartylglucosaminuria.
    PharmGKBi PA24615.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1446.
    HOVERGENi HBG004289.
    InParanoidi P20933.
    KOi K01444.
    OMAi KFFGAVI.
    OrthoDBi EOG7RV9GJ.
    PhylomeDBi P20933.
    TreeFami TF300756.

    Enzyme and pathway databases

    BRENDAi 3.5.1.26. 2681.
    SABIO-RK P20933.

    Miscellaneous databases

    ChiTaRSi AGA. human.
    EvolutionaryTracei P20933.
    GeneWikii Aspartylglucosaminidase.
    GenomeRNAii 175.
    NextBioi 702.
    PMAP-CutDB P20933.
    PROi P20933.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20933.
    Bgeei P20933.
    CleanExi HS_AGA.
    Genevestigatori P20933.

    Family and domain databases

    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000246. Peptidase_T2.
    [Graphical view ]
    PANTHERi PTHR10188. PTHR10188. 1 hit.
    Pfami PF01112. Asparaginase_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase."
      Fisher K.J., Tollersrud O.-K., Aronson N.N. Jr.
      FEBS Lett. 269:440-444(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-149.
    2. Erratum
      Fisher K.J., Tollersrud O.-K., Aronson N.N. Jr.
      FEBS Lett. 276:232-232(1990) [PubMed] [Europe PMC] [Abstract]
    3. "Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease."
      Ikonen E., Baumann M., Groen K., Syvaenen A.-C., Enomaa N., Halila R., Aula P., Peltonen L.
      EMBO J. 10:51-58(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 206-235, ACTIVATION BY CLEAVAGE, CATALYTIC ACTIVITY, VARIANTS SER-149; AGU GLN-161 AND SER-163, CHARACTERIZATION OF VARIANT AGU SER-163.
      Tissue: Fetal liver.
    4. "Genomic structure of human lysosomal glycosylasparaginase."
      Park H., Fisher K.J., Aronson N.N. Jr.
      FEBS Lett. 288:168-172(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-149.
    5. "Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163-->Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits."
      Fisher K.J., Aronson N.N. Jr.
      J. Biol. Chem. 266:12105-12113(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], AUTOCATALYTIC CLEAVAGE, CATALYTIC ACTIVITY, VARIANTS SER-149; AGU GLN-161 AND SER-163.
    6. "Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase."
      Mononen I., Heisterkamp N., Kaartinen V., Williams J.C., Yates J.R. III, Griffin P.R., Hood L.E., Groffen J.
      Proc. Natl. Acad. Sci. U.S.A. 88:2941-2945(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-45; 47-60; 67-84; 98-120; 123-190; 206-314 AND 320-343, VARIANTS AGU GLN-161 AND SER-163.
    7. "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], VARIANT SER-149.
      Tissue: Urinary bladder.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-149.
    9. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-149.
    11. "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], VARIANT SER-149.
      Tissue: Ovary.
    12. "Purification and structure of human liver aspartylglucosaminidase."
      Rip J.W., Coulter-Mackie M.B., Rupar C.A., Gordon B.A.
      Biochem. J. 288:1005-1010(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-44 AND 206-231, GLYCOSYLATION AT ASN-38.
      Tissue: Liver.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Three-dimensional structure of human lysosomal aspartylglucosaminidase."
      Oinonen C., Tikkanen R., Rouvinen J., Peltonen L.
      Nat. Struct. Biol. 2:1102-1108(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-185 IN COMPLEX WITH ASPARTIC ACID, SUBUNIT, ACTIVE SITE, GLYCOSYLATION AT ASN-38 AND ASN-308, DISULFIDE BONDS.
    15. "Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease."
      Ikonen E., Peltonen L.
      Hum. Mutat. 1:361-365(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON AGU VARIANTS.
    16. "Ser72-->Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation."
      Peltola M., Tikkanen R., Peltonen L., Jalanko A.
      Hum. Mol. Genet. 5:737-743(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AGU PRO-72.
    17. "Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation."
      Laitinen A., Hietala M., Haworth J.C., Schroeder M.L., Seargeant L.E., Greenberg C.R., Aula P.
      Clin. Genet. 51:174-178(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AGU GLU-100 AND SER-135.
    18. "Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations."
      Saarela J., Laine M., Oinonen C., Schantz C., Jalanko A., Rouvinen J., Peltonen L.
      Hum. Mol. Genet. 10:983-995(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS AGU LEU-12; ARG-252; GLU-252 AND ILE-257.

    Entry informationi

    Entry nameiASPG_HUMAN
    AccessioniPrimary (citable) accession number: P20933
    Secondary accession number(s): B2R7H2
    , D3DP47, Q4W5Q2, Q6FHN6, Q9UCK6, Q9UCK7, Q9UCK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 153 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 4
      Human chromosome 4: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3