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Q9UJJ9 (GNPTG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylglucosamine-1-phosphotransferase subunit gamma
Alternative name(s):
GlcNAc-1-phosphotransferase subunit gamma
UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma
Gene names
Name:GNPTG
Synonyms:C16orf27, GNPTAG
ORF Names:CAB56184, LP2537
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8

Subunit structure

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. Ref.1 Ref.8 Ref.10

Subcellular location

Secreted. Golgi apparatus Ref.10.

Tissue specificity

Widely expressed. Ref.1

Post-translational modification

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.10 Ref.11

Sequence similarities

Contains 1 PRKCSH domain.

Caution

The MLIIIC 'Tyr-142' variant is reported as a 'Val-142' variant due to a typo (Ref.11).

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 305281N-acetylglucosamine-1-phosphotransferase subunit gamma
PRO_0000019577

Regions

Domain69 – 12658PRKCSH

Amino acid modifications

Glycosylation881N-linked (GlcNAc...) By similarity
Glycosylation1151N-linked (GlcNAc...) Probable
Disulfide bond245Interchain By similarity

Natural variations

Natural variant1151Missing in MLIIIC. Ref.10
VAR_070815
Natural variant1421C → Y in MLIIIC. Ref.11
VAR_070816

Experimental info

Sequence conflict2231Missing in AAH14592. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9UJJ9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7774BBC0911DA1C2

FASTA30533,974
        10         20         30         40         50         60 
MAAGLARLLL LLGLSAGGPA PAGAAKMKVV EEPNAFGVNN PFLPQASRLQ AKRDPSPVSG 

        70         80         90        100        110        120 
PVHLFRLSGK CFSLVESTYK YEFCPFHNVT QHEQTFRWNA YSGILGIWHE WEIANNTFTG 

       130        140        150        160        170        180 
MWMRDGDACR SRSRQSKVEL ACGKSNRLAH VSEPSTCVYA LTFETPLVCH PHALLVYPTL 

       190        200        210        220        230        240 
PEALQRQWDQ VEQDLADELI TPQGHEKLLR TLFEDAGYLK TPEENEPTQL EGGPDSLGFE 

       250        260        270        280        290        300 
TLENCRKAHK ELSKEIKRLK GLLTQHGIPY TRPTETSNLE HLGHETPRAK SPEQLRGDPG 


LRGSL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular basis of variant pseudo-Hurler polydystrophy (mucolipidosis IIIC)."
Raas-Rothschild A., Cormier-Daire V., Bao M., Genin E., Salomon R., Brewer K., Zeigler M., Mandel H., Toth S., Roe B., Munnich A., Canfield W.M.
J. Clin. Invest. 105:673-681(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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. 24:0-0(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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT45062.
RefSeqNP_115909.1. NM_032520.4.
UniGeneHs.241575.

3D structure databases

ProteinModelPortalQ9UJJ9.
SMRQ9UJJ9. Positions 71-172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124144. 3 interactions.
IntActQ9UJJ9. 4 interactions.
STRING9606.ENSP00000204679.

PTM databases

PhosphoSiteQ9UJJ9.

Proteomic databases

PaxDbQ9UJJ9.
PRIDEQ9UJJ9.

Protocols and materials databases

DNASU84572.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000204679; ENSP00000204679; ENSG00000090581.
GeneID84572.
KEGGhsa:84572.
UCSCuc002clm.3. human.

Organism-specific databases

CTD84572.
GeneCardsGC16P001401.
HGNCHGNC:23026. GNPTG.
HPAHPA004055.
MIM252605. phenotype.
607838. gene.
neXtProtNX_Q9UJJ9.
Orphanet577. Mucolipidosis type 3.
PharmGKBPA134990433.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291062.
HOVERGENHBG054262.
InParanoidQ9UJJ9.
KOK10087.
OMARLAGKCF.
OrthoDBEOG7D59P4.
PhylomeDBQ9UJJ9.
TreeFamTF329550.

Gene expression databases

ArrayExpressQ9UJJ9.
BgeeQ9UJJ9.
CleanExHS_GNPTG.
GenevestigatorQ9UJJ9.

Family and domain databases

Gene3D2.70.130.10. 1 hit.
InterProIPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view]
SUPFAMSSF50911. SSF50911. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGNPTG. human.
GenomeRNAi84572.
NextBio74470.
PROQ9UJJ9.
SOURCESearch...

Entry information

Entry nameGNPTG_HUMAN
AccessionPrimary (citable) accession number: Q9UJJ9
Secondary accession number(s): B2R556, Q6XYD7, Q96L13
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM