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Q9UK23

- NAGPA_HUMAN

UniProt

Q9UK23 - NAGPA_HUMAN

Protein

N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase

Gene

NAGPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases.1 Publication

    Catalytic activityi

    Glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose.

    Pathwayi

    GO - Molecular functioni

    1. N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: ProtInc
    2. cellular protein modification process Source: ProtInc
    3. lysosome organization Source: ProtInc
    4. protein glycosylation Source: UniProtKB-UniPathway
    5. protein targeting to lysosome Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (EC:3.1.4.45)
    Alternative name(s):
    Mannose 6-phosphate-uncovering enzyme
    Phosphodiester alpha-GlcNAcase
    Gene namesi
    Name:NAGPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:17378. NAGPA.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Golgi apparatustrans-Golgi network 1 Publication
    Note: Cis/medial Golgi.

    GO - Cellular componenti

    1. Golgi cisterna membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: ProtInc

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511C → M: 65% of wild-type of activity. 1 Publication
    Mutagenesisi115 – 1151C → S: 15% of wild-type of activity, and almost no traffic to Golgi. 1 Publication
    Mutagenesisi132 – 1321C → V: No traffic to Golgi. 1 Publication
    Mutagenesisi137 – 1371N → A: 11% of wild-type of activity. 1 Publication
    Mutagenesisi221 – 2211C → L: 10% of wild-type of activity; when associated with M-51. 1 Publication
    Mutagenesisi225 – 2251Q → H: 6% of wild-type of activity. 1 Publication
    Mutagenesisi227 – 2271T → R: Complete loss of activity. 1 Publication
    Mutagenesisi247 – 2471R → A: 87% of wild-type of activity. 1 Publication
    Mutagenesisi284 – 2841N → A: 22% of wild-type of activity. 1 Publication
    Mutagenesisi286 – 2861D → A: Complete loss of activity. 1 Publication
    Mutagenesisi287 – 2871G → A: 16% of wild-type of activity. 1 Publication
    Mutagenesisi288 – 2881G → A: Complete loss of activity. 1 Publication
    Mutagenesisi289 – 2891G → A: Complete loss of activity. 1 Publication
    Mutagenesisi290 – 2901S → A: Complete loss of activity. 1 Publication
    Mutagenesisi320 – 3201T → A: 43% of wild-type of activity. 1 Publication
    Mutagenesisi322 – 3221V → A: 67% of wild-type of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134940049.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Propeptidei26 – 4924Removed in mature formPRO_0000424659Add
    BLAST
    Chaini50 – 515466N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidasePRO_0000021788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi115 ↔ 1481 Publication
    Disulfide bondi132 ↔ 3231 PublicationPROSITE-ProRule annotation
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi307 ↔ 3141 Publication
    Disulfide bondi362 ↔ 373PROSITE-ProRule annotation
    Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi380 ↔ 389PROSITE-ProRule annotation
    Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi420 – 4201N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved and activated in the trans-Golgi network by a furin endopeptidase.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ9UK23.
    PaxDbiQ9UK23.
    PRIDEiQ9UK23.

    PTM databases

    PhosphoSiteiQ9UK23.

    Expressioni

    Tissue specificityi

    Isoform 2 may be brain-specific.

    Gene expression databases

    ArrayExpressiQ9UK23.
    BgeeiQ9UK23.
    CleanExiHS_NAGPA.
    GenevestigatoriQ9UK23.

    Interactioni

    Subunit structurei

    Homotetramer arranged as two disulfide-linked homodimers.By similarity

    Protein-protein interaction databases

    BioGridi119351. 4 interactions.
    IntActiQ9UK23. 2 interactions.
    STRINGi9606.ENSP00000310998.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UK23.
    SMRiQ9UK23. Positions 314-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini50 – 448399LumenalSequence AnalysisAdd
    BLAST
    Topological domaini470 – 51546CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei449 – 46921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini358 – 39033EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi488 – 4914Tyrosine-based internalization motif
    Motifi511 – 5155NPF internalization motif

    Domaini

    The tyrosine-based internalization signal may be essential for its retrieval from the plasma membrane to the TGN.
    The C-terminal NPFKD sequence is an attractive candidate for either an endocytosis signal acting at the plasma membrane or a retrieval signal acting at the TGN to return the enzyme to the cis/medial-Golgi.

    Sequence similaritiesi

    Contains 1 EGF-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG126864.
    HOGENOMiHOG000059612.
    HOVERGENiHBG052571.
    InParanoidiQ9UK23.
    KOiK01125.
    OMAiPSDHCQD.
    OrthoDBiEOG7R2BJP.
    PhylomeDBiQ9UK23.
    TreeFamiTF331920.

    Family and domain databases

    InterProiIPR018711. DUF2233.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    [Graphical view]
    PfamiPF09992. DUF2233. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UK23-1) [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

    MATSTGRWLL LRLALFGFLW EASGGLDSGA SRDDDLLLPY PRARARLPRD    50
    CTRVRAGNRE HESWPPPPAT PGAGGLAVRT FVSHFRDRAV AGHLTRAVEP 100
    LRTFSVLEPG GPGGCAARRR ATVEETARAA DCRVAQNGGF FRMNSGECLG 150
    NVVSDERRVS SSGGLQNAQF GIRRDGTLVT GYLSEEEVLD TENPFVQLLS 200
    GVVWLIRNGS IYINESQATE CDETQETGSF SKFVNVISAR TAIGHDRKGQ 250
    LVLFHADGQT EQRGINLWEM AEFLLKQDVV NAINLDGGGS ATFVLNGTLA 300
    SYPSDHCQDN MWRCPRQVST VVCVHEPRCQ PPDCHGHGTC VDGHCQCTGH 350
    FWRGPGCDEL DCGPSNCSQH GLCTETGCRC DAGWTGSNCS EECPLGWHGP 400
    GCQRPCKCEH HCPCDPKTGN CSVSRVKQCL QPPEATLRAG ELSFFTRTAW 450
    LALTLALAFL LLISTAANLS LLLSRAERNR RLHGDYAYHP LQEMNGEPLA 500
    AEKEQPGGAH NPFKD 515
    Length:515
    Mass (Da):56,073
    Last modified:May 18, 2010 - v2
    Checksum:i9B80335E7F9DBAA9
    GO
    Isoform 2 (identifier: Q9UK23-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         392-425: Missing.

    Show »
    Length:481
    Mass (Da):52,368
    Checksum:i2FC910C7DB777505
    GO
    Isoform 3 (identifier: Q9UK23-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         307-309: CQD → WQA
         310-515: Missing.

    Show »
    Length:309
    Mass (Da):33,577
    Checksum:i270763749113C946
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti259 – 2591Q → H in AAF08273. (PubMed:10551838)Curated
    Sequence conflicti405 – 4051P → R in AAF08273. (PubMed:10551838)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti465 – 4651T → I.1 Publication
    Corresponds to variant rs7188856 [ dbSNP | Ensembl ].
    VAR_020609

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei307 – 3093CQD → WQA in isoform 3. 1 PublicationVSP_012267
    Alternative sequencei310 – 515206Missing in isoform 3. 1 PublicationVSP_012268Add
    BLAST
    Alternative sequencei392 – 42534Missing in isoform 2. 1 PublicationVSP_012269Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF187072 mRNA. Translation: AAF08273.1.
    AK127952 mRNA. Translation: BAG54605.1.
    AK314320 mRNA. Translation: BAG36968.1.
    AC026458 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85245.1.
    BC012194 mRNA. Translation: AAH12194.1.
    CCDSiCCDS10527.1. [Q9UK23-1]
    RefSeqiNP_057340.2. NM_016256.3. [Q9UK23-1]
    UniGeneiHs.21334.

    Genome annotation databases

    EnsembliENST00000312251; ENSP00000310998; ENSG00000103174. [Q9UK23-1]
    ENST00000381955; ENSP00000371381; ENSG00000103174. [Q9UK23-2]
    ENST00000562746; ENSP00000455900; ENSG00000103174. [Q9UK23-3]
    GeneIDi51172.
    KEGGihsa:51172.
    UCSCiuc002cyg.3. human. [Q9UK23-1]

    Polymorphism databases

    DMDMi296439239.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF187072 mRNA. Translation: AAF08273.1 .
    AK127952 mRNA. Translation: BAG54605.1 .
    AK314320 mRNA. Translation: BAG36968.1 .
    AC026458 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85245.1 .
    BC012194 mRNA. Translation: AAH12194.1 .
    CCDSi CCDS10527.1. [Q9UK23-1 ]
    RefSeqi NP_057340.2. NM_016256.3. [Q9UK23-1 ]
    UniGenei Hs.21334.

    3D structure databases

    ProteinModelPortali Q9UK23.
    SMRi Q9UK23. Positions 314-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119351. 4 interactions.
    IntActi Q9UK23. 2 interactions.
    STRINGi 9606.ENSP00000310998.

    Chemistry

    ChEMBLi CHEMBL5920.
    DrugBanki DB00141. N-Acetyl-D-glucosamine.

    PTM databases

    PhosphoSitei Q9UK23.

    Polymorphism databases

    DMDMi 296439239.

    Proteomic databases

    MaxQBi Q9UK23.
    PaxDbi Q9UK23.
    PRIDEi Q9UK23.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312251 ; ENSP00000310998 ; ENSG00000103174 . [Q9UK23-1 ]
    ENST00000381955 ; ENSP00000371381 ; ENSG00000103174 . [Q9UK23-2 ]
    ENST00000562746 ; ENSP00000455900 ; ENSG00000103174 . [Q9UK23-3 ]
    GeneIDi 51172.
    KEGGi hsa:51172.
    UCSCi uc002cyg.3. human. [Q9UK23-1 ]

    Organism-specific databases

    CTDi 51172.
    GeneCardsi GC16M005014.
    H-InvDB HIX0013112.
    HGNCi HGNC:17378. NAGPA.
    MIMi 607985. gene.
    neXtProti NX_Q9UK23.
    PharmGKBi PA134940049.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG126864.
    HOGENOMi HOG000059612.
    HOVERGENi HBG052571.
    InParanoidi Q9UK23.
    KOi K01125.
    OMAi PSDHCQD.
    OrthoDBi EOG7R2BJP.
    PhylomeDBi Q9UK23.
    TreeFami TF331920.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    GeneWikii NAGPA.
    GenomeRNAii 51172.
    NextBioi 54121.
    PROi Q9UK23.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UK23.
    Bgeei Q9UK23.
    CleanExi HS_NAGPA.
    Genevestigatori Q9UK23.

    Family and domain databases

    InterProi IPR018711. DUF2233.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    [Graphical view ]
    Pfami PF09992. DUF2233. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional expression of two splice forms of human N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase."
      Kornfeld R.H., Bao M., Brewer K., Noll C., Canfield W.M.
      J. Biol. Chem. 274:32778-32785(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ILE-465.
    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: Mammary gland and Tongue.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 3).
      Tissue: Colon.
    6. "Human mannose 6-phosphate-uncovering enzyme is synthesized as a proenzyme that is activated by the endoprotease furin."
      Do H., Lee W.S., Ghosh P., Hollowell T., Canfield W., Kornfeld S.
      J. Biol. Chem. 277:29737-29744(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-36, SIGNAL SEQUENCE CLEAVAGE SITE, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
    7. "Structure and function of the DUF2233 domain in bacteria and in the human mannose 6-phosphate uncovering enzyme."
      Das D., Lee W.S., Grant J.C., Chiu H.J., Farr C.L., Vance J., Klock H.E., Knuth M.W., Miller M.D., Elsliger M.A., Deacon A.M., Godzik A., Lesley S.A., Kornfeld S., Wilson I.A.
      J. Biol. Chem. 288:16789-16799(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-51; CYS-115; CYS-132; ASN-137; CYS-221; GLN-225; THR-227; ARG-247; ASN-284; ASP-286; GLY-287; GLY-288; GLY-289; SER-290; THR-320 AND VAL-322, 3D-STRUCTURE MODELING, DISULFIDE BONDS, FUNCTION.

    Entry informationi

    Entry nameiNAGPA_HUMAN
    AccessioniPrimary (citable) accession number: Q9UK23
    Secondary accession number(s): B2RAS1, Q96EJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 118 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3