SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UJJ9

- GNPTG_HUMAN

UniProt

Q9UJJ9 - GNPTG_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
N-acetylglucosamine-1-phosphotransferase subunit gamma
Gene
GNPTG, C16orf27, GNPTAG, CAB56184, LP2537
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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. Golgi apparatus 1 Publication

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
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 – 2424 Reviewed prediction
Add
BLAST
Chaini25 – 305281N-acetylglucosamine-1-phosphotransferase subunit gamma
PRO_0000019577Add
BLAST

Amino acid modifications

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

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.3 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9UJJ9.
SMRiQ9UJJ9. Positions 71-172.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 PRKCSH domain.

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231Missing in AAH14592. 1 Publication

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 94 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

Similar proteinsi