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Q9UJJ9

- GNPTG_HUMAN

UniProt

Q9UJJ9 - GNPTG_HUMAN

Protein

N-acetylglucosamine-1-phosphotransferase subunit gamma

Gene

GNPTG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Non-catalytic subunit of the N-acetylglucosamine-1-phosphotransferase complex, an enzyme that catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. Binds and presents the high mannose glycans of the acceptor to the catalytic alpha and beta subunits (GNPTAB). Enhances the rate of N-acetylglucosamine-1-phosphate transfer to the oligosaccharides of acid hydrolase acceptors.2 Publications

    GO - Molecular functioni

    1. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate phosphorylation Source: UniProtKB
    2. N-glycan processing to lysosome Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetylglucosamine-1-phosphotransferase subunit gamma
    Alternative name(s):
    GlcNAc-1-phosphotransferase subunit gamma
    UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma
    Gene namesi
    Name:GNPTG
    Synonyms:C16orf27, GNPTAG
    ORF Names:CAB56184, LP2537
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:23026. GNPTG.

    Subcellular locationi

    Secreted 1 Publication. Golgi apparatus 1 Publication

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. Golgi apparatus Source: UniProtKB
    3. Golgi membrane Source: Ensembl

    Keywords - Cellular componenti

    Golgi apparatus, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Mucolipidosis type III complementation group C (MLIIIC) [MIM:252605]: Autosomal recessive disease of lysosomal hydrolase trafficking. Unlike the related diseases, mucolipidosis II and IIIA, the enzyme affected in mucolipidosis IIIC (GlcNAc-phosphotransferase) retains full transferase activity on synthetic substrates but lacks activity on lysosomal hydrolases. Typical clinical findings include stiffness of the hands and shoulders, claw-hand deformity, scoliosis, short stature, coarse facies, and mild mental retardation. Radiographically, severe dysostosis multiplex of the hip is characteristic and frequently disabling. The clinical diagnosis can be confirmed by finding elevated serum lysosomal enzyme levels and/or decreased lysosomal enzyme levels in cultured fibroblasts.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti115 – 1151Missing in MLIIIC. 1 Publication
    VAR_070815
    Natural varianti142 – 1421C → Y in MLIIIC. 1 Publication
    VAR_070816

    Keywords - Diseasei

    Disease mutation, Mucolipidosis

    Organism-specific databases

    MIMi252605. phenotype.
    Orphaneti577. Mucolipidosis type 3.
    PharmGKBiPA134990433.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 305281N-acetylglucosamine-1-phosphotransferase subunit gammaPRO_0000019577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi88 – 881N-linked (GlcNAc...)By similarity
    Glycosylationi115 – 1151N-linked (GlcNAc...)2 Publications
    Disulfide bondi245 – 245InterchainBy similarity

    Post-translational modificationi

    Cys-245 mediates the formation of the interchain disulfide bond for formation of the homofimer. Cys-142, Cys-157 and Cys-169 are involved in intramolecular disulfide bonds formation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9UJJ9.
    PaxDbiQ9UJJ9.
    PRIDEiQ9UJJ9.

    PTM databases

    PhosphoSiteiQ9UJJ9.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9UJJ9.
    BgeeiQ9UJJ9.
    CleanExiHS_GNPTG.
    GenevestigatoriQ9UJJ9.

    Organism-specific databases

    HPAiHPA004055.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Hexamer of two alpha (GNPTAB), two beta (GNPTAB) and two gamma (GNPTG) subunits; disulfide-linked. The alpha and/or the beta subunits of the enzyme constitute the catalytic subunits.2 Publications

    Protein-protein interaction databases

    BioGridi124144. 3 interactions.
    IntActiQ9UJJ9. 4 interactions.
    STRINGi9606.ENSP00000204679.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJJ9.
    SMRiQ9UJJ9. Positions 71-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini69 – 12658PRKCSHAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PRKCSH domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG291062.
    HOVERGENiHBG054262.
    InParanoidiQ9UJJ9.
    KOiK10087.
    OMAiRLAGKCF.
    OrthoDBiEOG7D59P4.
    PhylomeDBiQ9UJJ9.
    TreeFamiTF329550.

    Family and domain databases

    Gene3Di2.70.130.10. 1 hit.
    InterProiIPR009011. Man6P_isomerase_rcpt-bd_dom.
    [Graphical view]
    SUPFAMiSSF50911. SSF50911. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9UJJ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAGLARLLL LLGLSAGGPA PAGAAKMKVV EEPNAFGVNN PFLPQASRLQ    50
    AKRDPSPVSG PVHLFRLSGK CFSLVESTYK YEFCPFHNVT QHEQTFRWNA 100
    YSGILGIWHE WEIANNTFTG MWMRDGDACR SRSRQSKVEL ACGKSNRLAH 150
    VSEPSTCVYA LTFETPLVCH PHALLVYPTL PEALQRQWDQ VEQDLADELI 200
    TPQGHEKLLR TLFEDAGYLK TPEENEPTQL EGGPDSLGFE TLENCRKAHK 250
    ELSKEIKRLK GLLTQHGIPY TRPTETSNLE HLGHETPRAK SPEQLRGDPG 300
    LRGSL 305
    Length:305
    Mass (Da):33,974
    Last modified:May 1, 2000 - v1
    Checksum:i7774BBC0911DA1C2
    GO

    Sequence cautioni

    The sequence AAP34456.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231Missing in AAH14592. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti115 – 1151Missing in MLIIIC. 1 Publication
    VAR_070815
    Natural varianti142 – 1421C → Y in MLIIIC. 1 Publication
    VAR_070816

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF302786 mRNA. Translation: AAG27706.1.
    AL031709 Genomic DNA. Translation: CAB56184.1.
    AK312067 mRNA. Translation: BAG35003.1.
    CH471112 Genomic DNA. Translation: EAW85668.1.
    BC014592 mRNA. Translation: AAH14592.1.
    AY203933 mRNA. Translation: AAP34456.1. Different initiation.
    CCDSiCCDS10436.1.
    PIRiT45062.
    RefSeqiNP_115909.1. NM_032520.4.
    UniGeneiHs.241575.

    Genome annotation databases

    EnsembliENST00000204679; ENSP00000204679; ENSG00000090581.
    GeneIDi84572.
    KEGGihsa:84572.
    UCSCiuc002clm.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF302786 mRNA. Translation: AAG27706.1 .
    AL031709 Genomic DNA. Translation: CAB56184.1 .
    AK312067 mRNA. Translation: BAG35003.1 .
    CH471112 Genomic DNA. Translation: EAW85668.1 .
    BC014592 mRNA. Translation: AAH14592.1 .
    AY203933 mRNA. Translation: AAP34456.1 . Different initiation.
    CCDSi CCDS10436.1.
    PIRi T45062.
    RefSeqi NP_115909.1. NM_032520.4.
    UniGenei Hs.241575.

    3D structure databases

    ProteinModelPortali Q9UJJ9.
    SMRi Q9UJJ9. Positions 71-172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124144. 3 interactions.
    IntActi Q9UJJ9. 4 interactions.
    STRINGi 9606.ENSP00000204679.

    PTM databases

    PhosphoSitei Q9UJJ9.

    Proteomic databases

    MaxQBi Q9UJJ9.
    PaxDbi Q9UJJ9.
    PRIDEi Q9UJJ9.

    Protocols and materials databases

    DNASUi 84572.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000204679 ; ENSP00000204679 ; ENSG00000090581 .
    GeneIDi 84572.
    KEGGi hsa:84572.
    UCSCi uc002clm.3. human.

    Organism-specific databases

    CTDi 84572.
    GeneCardsi GC16P001401.
    GeneReviewsi GNPTG.
    HGNCi HGNC:23026. GNPTG.
    HPAi HPA004055.
    MIMi 252605. phenotype.
    607838. gene.
    neXtProti NX_Q9UJJ9.
    Orphaneti 577. Mucolipidosis type 3.
    PharmGKBi PA134990433.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291062.
    HOVERGENi HBG054262.
    InParanoidi Q9UJJ9.
    KOi K10087.
    OMAi RLAGKCF.
    OrthoDBi EOG7D59P4.
    PhylomeDBi Q9UJJ9.
    TreeFami TF329550.

    Miscellaneous databases

    ChiTaRSi GNPTG. human.
    GenomeRNAii 84572.
    NextBioi 74470.
    PROi Q9UJJ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJJ9.
    Bgeei Q9UJJ9.
    CleanExi HS_GNPTG.
    Genevestigatori Q9UJJ9.

    Family and domain databases

    Gene3Di 2.70.130.10. 1 hit.
    InterProi IPR009011. Man6P_isomerase_rcpt-bd_dom.
    [Graphical view ]
    SUPFAMi SSF50911. SSF50911. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, INVOLVEMENT IN MLIIIC.
      Tissue: Brain.
    2. "cDNA from human fetal brain."
      Fitzgerald P., Amarante-Mendes G.P., Li W., Green D.R.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    3. "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].
      Tissue: Tongue.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Testis.
    7. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-305.
    8. "Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase."
      Qian Y., Lee I., Lee W.S., Qian M., Kudo M., Canfield W.M., Lobel P., Kornfeld S.
      J. Biol. Chem. 285:3360-3370(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    9. "Post-translational modifications of the gamma-subunit affect intracellular trafficking and complex assembly of GlcNAc-1-phosphotransferase."
      Encarnacao M., Kollmann K., Trusch M., Braulke T., Pohl S.
      J. Biol. Chem. 286:5311-5318(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION.
    10. "A novel mutation in UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTAG) in two siblings with mucolipidosis type III alters a used glycosylation site."
      Tiede S., Cantz M., Raas-Rothschild A., Muschol N., Buerger F., Ullrich K., Braulke T.
      Hum. Mutat. 24:535-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MLIIIC ASN-115 DEL, HOMODIMERIZATION, GLYCOSYLATION AT ASN-115, SUBCELLULAR LOCATION.
    11. "Three novel homozygous mutations in the GNPTG gene that cause mucolipidosis type III gamma."
      Liu S., Zhang W., Shi H., Meng Y., Qiu Z.
      Gene 535:294-298(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MLIIIC TYR-142.

    Entry informationi

    Entry nameiGNPTG_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJJ9
    Secondary accession number(s): B2R556, Q6XYD7, Q96L13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 95 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

    Caution

    The MLIIIC 'Tyr-142' variant is reported as a 'Val-142' variant due to a typo.1 Publication

    Keywords - Technical termi

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3