Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9H3H5 (GPT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DPAGT1
Synonyms:DPAGT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Involvement in disease

Congenital disorder of glycosylation 1J (CDG1J) [MIM:608093]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Myasthenic syndrome, congenital, with tubular aggregates, 2 (CMSTA2) [MIM:614750]: A congenital myasthenic syndrome 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the glycosyltransferase 4 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCongenital disorder of glycosylation
Congenital myasthenic syndrome
Disease mutation
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUDP-N-acetylglucosamine metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

dolichol biosynthetic process

Inferred from direct assay PubMed 8179616. Source: UniProtKB

dolichol-linked oligosaccharide biosynthetic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation

Inferred from mutant phenotype PubMed 19549906. Source: UniProtKB

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

protein oligomerization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay Ref.5. Source: UniProtKB

membrane

Inferred from direct assay PubMed 8179616. Source: UniProtKB

   Molecular_functionUDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity

Inferred from direct assay PubMed 8179616. Source: UniProtKB

phospho-N-acetylmuramoyl-pentapeptide-transferase activity

Inferred from electronic annotation. Source: InterPro

transferase activity, transferring glycosyl groups

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H3H5-1)

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.
Isoform 2 (identifier: Q9H3H5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9H3H5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
PRO_0000108761

Regions

Topological domain1 – 66Lumenal Potential
Transmembrane7 – 3226Helical; Potential
Topological domain33 – 5725Cytoplasmic Potential
Transmembrane58 – 7922Helical; Potential
Topological domain80 – 9415Lumenal Potential
Transmembrane95 – 11420Helical; Potential
Topological domain115 – 12511Cytoplasmic Potential
Transmembrane126 – 14520Helical; Potential
Topological domain146 – 16419Lumenal Potential
Transmembrane165 – 18420Helical; Potential
Topological domain185 – 19410Cytoplasmic Potential
Transmembrane195 – 21117Helical; Potential
Topological domain212 – 22110Lumenal Potential
Transmembrane222 – 24019Helical; Potential
Topological domain241 – 25212Cytoplasmic Potential
Transmembrane253 – 26917Helical; Potential
Topological domain270 – 2745Lumenal Potential
Transmembrane275 – 29420Helical; Potential
Topological domain295 – 37884Cytoplasmic Potential
Transmembrane379 – 39719Helical; Potential
Topological domain398 – 40811Lumenal Potential
Motif67 – 7913Dolichol recognition
Motif222 – 23413Dolichol recognition

Amino acid modifications

Glycosylation1461N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 107107Missing in isoform 3.
VSP_008886
Alternative sequence1 – 88Missing in isoform 2.
VSP_001803
Natural variant91M → I in a breast cancer sample; somatic mutation. Ref.6
VAR_036422
Natural variant1081M → I in CMSTA2. Ref.7
VAR_068810
Natural variant1171V → I in CMSTA2. Ref.7
VAR_068811
Natural variant1201L → M in CMSTA2. Ref.7
VAR_068812
Natural variant1601G → S in CMSTA2. Ref.7
VAR_068813
Natural variant1701Y → C in CDG1J. Ref.5
Corresponds to variant rs28934876 [ dbSNP | Ensembl ].
VAR_017243
Natural variant1921G → S in CMSTA2. Ref.7
VAR_068814
Natural variant2641V → G in CMSTA2. Ref.7
VAR_068815
Natural variant3931I → V. Ref.4
Corresponds to variant rs643788 [ dbSNP | Ensembl ].
VAR_011391

Experimental info

Sequence conflict331R → L in CAB04787. Ref.1
Sequence conflict1291P → H in AAG43168. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: 0AE10EFE55E7B9E0

FASTA40846,090
        10         20         30         40         50         60 
MWAFSELPMP LLINLIVSLL GFVATVTLIP AFRGHFIAAR LCGQDLNKTS RQQIPESQGV 

        70         80         90        100        110        120 
ISGAVFLIIL FCFIPFPFLN CFVKEQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL 

       130        140        150        160        170        180 
RWRHKLLLPT AASLPLLMVY FTNFGNTTIV VPKPFRPILG LHLDLGILYY VYMGLLAVFC 

       190        200        210        220        230        240 
TNAINILAGI NGLEAGQSLV ISASIIVFNL VELEGDCRDD HVFSLYFMIP FFFTTLGLLY 

       250        260        270        280        290        300 
HNWYPSRVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFM PQVFNFLYSL PQLLHIIPCP 

       310        320        330        340        350        360 
RHRIPRLNIK TGKLEMSYSK FKTKSLSFLG TFILKVAESL QLVTVHQSET EDGEFTECNN 

       370        380        390        400 
MTLINLLLKV LGPIHERNLT LLLLLLQILG SAITFSIRYQ LVRLFYDV 

« Hide

Isoform 2 [UniParc].

Checksum: 54D3A9DCCCA14F6B
Show »

FASTA40045,128
Isoform 3 [UniParc].

Checksum: C605449414F020C3
Show »

FASTA30134,270

References

« Hide 'large scale' references
[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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-9.
[7]"Mutations in DPAGT1 cause a limb-girdle congenital myasthenic syndrome with tubular aggregates."
Belaya K., Finlayson S., Slater C.R., Cossins J., Liu W.W., Maxwell S., McGowan S.J., Maslau S., Twigg S.R., Walls T.J., Pascual Pascual S.I., Palace J., Beeson D.
Am. J. Hum. Genet. 91:193-201(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMSTA2 ILE-108; ILE-117; MET-120; SER-160; SER-192 AND GLY-264.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001373.2. NM_001382.3.
UniGeneHs.524081.

3D structure databases

ProteinModelPortalQ9H3H5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108133. 4 interactions.
IntActQ9H3H5. 1 interaction.
STRING9606.ENSP00000346142.

PTM databases

PhosphoSiteQ9H3H5.

Polymorphism databases

DMDM18202943.

Proteomic databases

PaxDbQ9H3H5.
PRIDEQ9H3H5.

Protocols and materials databases

DNASU1798.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354202; ENSP00000346142; ENSG00000172269. [Q9H3H5-1]
ENST00000409993; ENSP00000386597; ENSG00000172269. [Q9H3H5-1]
GeneID1798.
KEGGhsa:1798.
UCSCuc001pvi.3. human. [Q9H3H5-1]

Organism-specific databases

CTD1798.
GeneCardsGC11M119001.
H-InvDBHIX0019316.
HGNCHGNC:2995. DPAGT1.
HPAHPA053878.
MIM191350. gene.
608093. phenotype.
614750. phenotype.
neXtProtNX_Q9H3H5.
Orphanet353327. Congenital myasthenic syndromes with glycosylation defect.
86309. DPAGT1-CDG.
PharmGKBPA27460.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0472.
HOGENOMHOG000163915.
HOVERGENHBG000846.
InParanoidQ9H3H5.
KOK01001.
OMAIHERNLT.
OrthoDBEOG73804W.
PhylomeDBQ9H3H5.
TreeFamTF313734.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9H3H5.
BgeeQ9H3H5.
CleanExHS_DPAGT1.
GenevestigatorQ9H3H5.

Family and domain databases

InterProIPR000715. Glycosyl_transferase_4.
[Graphical view]
PfamPF00953. Glycos_transf_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDPAGT1.
GenomeRNAi1798.
NextBio7325.
PROQ9H3H5.
SOURCESearch...

Entry information

Entry nameGPT_HUMAN
AccessionPrimary (citable) accession number: Q9H3H5
Secondary accession number(s): O15216, Q86WV9, Q9BWE6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: August 29, 2001
Last modified: April 16, 2014
This is version 129 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 11

Human chromosome 11: entries, gene names and cross-references to MIM