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Protein

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase

Gene

DPAGT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.

Catalytic activityi

UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol.

Pathway:iprotein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
REACT_268849. Defective DPAGT1 causes DPAGT1-CDG (CDG-1j) and CMSTA2.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC:2.7.8.15)
Alternative name(s):
GlcNAc-1-P transferase
Short name:
G1PT
Short name:
GPT
N-acetylglucosamine-1-phosphate transferase
Gene namesi
Name:DPAGT1
Synonyms:DPAGT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2995. DPAGT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66LumenalSequence Analysis
Transmembranei7 – 3226HelicalSequence AnalysisAdd
BLAST
Topological domaini33 – 5725CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei58 – 7922HelicalSequence AnalysisAdd
BLAST
Topological domaini80 – 9415LumenalSequence AnalysisAdd
BLAST
Transmembranei95 – 11420HelicalSequence AnalysisAdd
BLAST
Topological domaini115 – 12511CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei126 – 14520HelicalSequence AnalysisAdd
BLAST
Topological domaini146 – 16419LumenalSequence AnalysisAdd
BLAST
Transmembranei165 – 18420HelicalSequence AnalysisAdd
BLAST
Topological domaini185 – 19410CytoplasmicSequence Analysis
Transmembranei195 – 21117HelicalSequence AnalysisAdd
BLAST
Topological domaini212 – 22110LumenalSequence Analysis
Transmembranei222 – 24019HelicalSequence AnalysisAdd
BLAST
Topological domaini241 – 25212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei253 – 26917HelicalSequence AnalysisAdd
BLAST
Topological domaini270 – 2745LumenalSequence Analysis
Transmembranei275 – 29420HelicalSequence AnalysisAdd
BLAST
Topological domaini295 – 37884CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei379 – 39719HelicalSequence AnalysisAdd
BLAST
Topological domaini398 – 40811LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1J (CDG1J)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.

See also OMIM:608093
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701Y → C in CDG1J. 1 Publication
Corresponds to variant rs28934876 [ dbSNP | Ensembl ].
VAR_017243
Myasthenic syndrome, congenital, 13 (CMS13)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS13 is characterized by muscle weakness mostly affecting proximal limb muscles, minimal involvement of facial, ocular and bulbar muscles, and tubular aggregates present on muscle biopsy. Symptoms include difficulty walking and frequent falls. Younger patients show hypotonia and poor head control. Neurophysiological features indicate a disorder of neuromuscular transmission on electromyography.

See also OMIM:614750
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti108 – 1081M → I in CMS13. 1 Publication
VAR_068810
Natural varianti117 – 1171V → I in CMS13. 1 Publication
VAR_068811
Natural varianti120 – 1201L → M in CMS13. 1 Publication
VAR_068812
Natural varianti160 – 1601G → S in CMS13. 1 Publication
VAR_068813
Natural varianti192 – 1921G → S in CMS13. 1 Publication
VAR_068814
Natural varianti264 – 2641V → G in CMS13. 1 Publication
VAR_068815

Keywords - Diseasei

Congenital disorder of glycosylation, Congenital myasthenic syndrome, Disease mutation

Organism-specific databases

MIMi608093. phenotype.
614750. phenotype.
Orphaneti353327. Congenital myasthenic syndromes with glycosylation defect.
86309. DPAGT1-CDG.
PharmGKBiPA27460.

Polymorphism and mutation databases

BioMutaiDPAGT1.
DMDMi18202943.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferasePRO_0000108761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9H3H5.
PaxDbiQ9H3H5.
PRIDEiQ9H3H5.

PTM databases

PhosphoSiteiQ9H3H5.

Expressioni

Gene expression databases

BgeeiQ9H3H5.
CleanExiHS_DPAGT1.
ExpressionAtlasiQ9H3H5. baseline and differential.
GenevisibleiQ9H3H5. HS.

Organism-specific databases

HPAiHPA053878.

Interactioni

Protein-protein interaction databases

BioGridi108133. 3 interactions.
IntActiQ9H3H5. 1 interaction.
STRINGi9606.ENSP00000346142.

Structurei

3D structure databases

ProteinModelPortaliQ9H3H5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi67 – 7913Dolichol recognitionAdd
BLAST
Motifi222 – 23413Dolichol recognitionAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 4 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0472.
GeneTreeiENSGT00390000011424.
HOGENOMiHOG000163915.
HOVERGENiHBG000846.
InParanoidiQ9H3H5.
KOiK01001.
OMAiWAFPELP.
OrthoDBiEOG73804W.
PhylomeDBiQ9H3H5.
TreeFamiTF313734.

Family and domain databases

InterProiIPR000715. Glycosyl_transferase_4.
[Graphical view]
PfamiPF00953. Glycos_transf_4. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H3H5-1) [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

        10         20         30         40         50
MWAFSELPMP LLINLIVSLL GFVATVTLIP AFRGHFIAAR LCGQDLNKTS
60 70 80 90 100
RQQIPESQGV ISGAVFLIIL FCFIPFPFLN CFVKEQCKAF PHHEFVALIG
110 120 130 140 150
ALLAICCMIF LGFADDVLNL RWRHKLLLPT AASLPLLMVY FTNFGNTTIV
160 170 180 190 200
VPKPFRPILG LHLDLGILYY VYMGLLAVFC TNAINILAGI NGLEAGQSLV
210 220 230 240 250
ISASIIVFNL VELEGDCRDD HVFSLYFMIP FFFTTLGLLY HNWYPSRVFV
260 270 280 290 300
GDTFCYFAGM TFAVVGILGH FSKTMLLFFM PQVFNFLYSL PQLLHIIPCP
310 320 330 340 350
RHRIPRLNIK TGKLEMSYSK FKTKSLSFLG TFILKVAESL QLVTVHQSET
360 370 380 390 400
EDGEFTECNN MTLINLLLKV LGPIHERNLT LLLLLLQILG SAITFSIRYQ

LVRLFYDV
Length:408
Mass (Da):46,090
Last modified:August 29, 2001 - v2
Checksum:i0AE10EFE55E7B9E0
GO
Isoform 2 (identifier: Q9H3H5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.

Note: No experimental confirmation available.
Show »
Length:400
Mass (Da):45,128
Checksum:i54D3A9DCCCA14F6B
GO
Isoform 3 (identifier: Q9H3H5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: Missing.

Note: No experimental confirmation available.
Show »
Length:301
Mass (Da):34,270
Checksum:iC605449414F020C3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331R → L in CAB04787 (PubMed:9451016).Curated
Sequence conflicti129 – 1291P → H in AAG43168 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91M → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_036422
Natural varianti108 – 1081M → I in CMS13. 1 Publication
VAR_068810
Natural varianti117 – 1171V → I in CMS13. 1 Publication
VAR_068811
Natural varianti120 – 1201L → M in CMS13. 1 Publication
VAR_068812
Natural varianti160 – 1601G → S in CMS13. 1 Publication
VAR_068813
Natural varianti170 – 1701Y → C in CDG1J. 1 Publication
Corresponds to variant rs28934876 [ dbSNP | Ensembl ].
VAR_017243
Natural varianti192 – 1921G → S in CMS13. 1 Publication
VAR_068814
Natural varianti264 – 2641V → G in CMS13. 1 Publication
VAR_068815
Natural varianti393 – 3931I → V.1 Publication
Corresponds to variant rs643788 [ dbSNP | Ensembl ].
VAR_011391

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 107107Missing in isoform 3. 1 PublicationVSP_008886Add
BLAST
Alternative sequencei1 – 88Missing in isoform 2. 1 PublicationVSP_001803

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z82022 mRNA. Translation: CAB04787.1.
AF070443, AF069061 Genomic DNA. Translation: AAG43168.1.
BT006802 mRNA. Translation: AAP35448.1.
BC000325 mRNA. Translation: AAH00325.1.
BC047771 mRNA. Translation: AAH47771.1.
CCDSiCCDS8411.1. [Q9H3H5-1]
RefSeqiNP_001373.2. NM_001382.3. [Q9H3H5-1]
UniGeneiHs.524081.

Genome annotation databases

EnsembliENST00000354202; ENSP00000346142; ENSG00000172269.
ENST00000409993; ENSP00000386597; ENSG00000172269.
GeneIDi1798.
KEGGihsa:1798.
UCSCiuc001pvi.3. human. [Q9H3H5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z82022 mRNA. Translation: CAB04787.1.
AF070443, AF069061 Genomic DNA. Translation: AAG43168.1.
BT006802 mRNA. Translation: AAP35448.1.
BC000325 mRNA. Translation: AAH00325.1.
BC047771 mRNA. Translation: AAH47771.1.
CCDSiCCDS8411.1. [Q9H3H5-1]
RefSeqiNP_001373.2. NM_001382.3. [Q9H3H5-1]
UniGeneiHs.524081.

3D structure databases

ProteinModelPortaliQ9H3H5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108133. 3 interactions.
IntActiQ9H3H5. 1 interaction.
STRINGi9606.ENSP00000346142.

PTM databases

PhosphoSiteiQ9H3H5.

Polymorphism and mutation databases

BioMutaiDPAGT1.
DMDMi18202943.

Proteomic databases

MaxQBiQ9H3H5.
PaxDbiQ9H3H5.
PRIDEiQ9H3H5.

Protocols and materials databases

DNASUi1798.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354202; ENSP00000346142; ENSG00000172269.
ENST00000409993; ENSP00000386597; ENSG00000172269.
GeneIDi1798.
KEGGihsa:1798.
UCSCiuc001pvi.3. human. [Q9H3H5-1]

Organism-specific databases

CTDi1798.
GeneCardsiGC11M118973.
GeneReviewsiDPAGT1.
H-InvDBHIX0019316.
HGNCiHGNC:2995. DPAGT1.
HPAiHPA053878.
MIMi191350. gene.
608093. phenotype.
614750. phenotype.
neXtProtiNX_Q9H3H5.
Orphaneti353327. Congenital myasthenic syndromes with glycosylation defect.
86309. DPAGT1-CDG.
PharmGKBiPA27460.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0472.
GeneTreeiENSGT00390000011424.
HOGENOMiHOG000163915.
HOVERGENiHBG000846.
InParanoidiQ9H3H5.
KOiK01001.
OMAiWAFPELP.
OrthoDBiEOG73804W.
PhylomeDBiQ9H3H5.
TreeFamiTF313734.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
REACT_268849. Defective DPAGT1 causes DPAGT1-CDG (CDG-1j) and CMSTA2.

Miscellaneous databases

GeneWikiiDPAGT1.
GenomeRNAii1798.
NextBioi7325.
PROiQ9H3H5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H3H5.
CleanExiHS_DPAGT1.
ExpressionAtlasiQ9H3H5. baseline and differential.
GenevisibleiQ9H3H5. HS.

Family and domain databases

InterProiIPR000715. Glycosyl_transferase_4.
[Graphical view]
PfamiPF00953. Glycos_transf_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae."
    Eckert V., Blank M., Mazhari-Tabrizi R., Mumberg D., Funk M., Schwarz R.T.
    Glycobiology 8:77-85(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Lung.
  2. "Putative genomic sequence of GlcNAc-1-P transferase on chromosome 11q23."
    Dagnino F., Regis S., Filocamo M., Gatti R.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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] (ISOFORMS 1 AND 3), VARIANT VAL-393.
    Tissue: Lung.
  5. "Deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij."
    Wu X., Rush J.S., Karaoglu D., Krasnewich D., Lubinsky M.S., Waechter C.J., Gilmore R., Freeze H.H.
    Hum. Mutat. 22:144-150(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG1J CYS-170.
  6. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-9.
  7. Cited for: VARIANTS CMS13 ILE-108; ILE-117; MET-120; SER-160; SER-192 AND GLY-264.

Entry informationi

Entry nameiGPT_HUMAN
AccessioniPrimary (citable) accession number: Q9H3H5
Secondary accession number(s): O15216, Q86WV9, Q9BWE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 29, 2001
Last modified: July 22, 2015
This is version 140 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.