Q9H3H5 (GPT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DPAGT1
Synonyms:	DPAGT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Congenital disorder of glycosylation Congenital myasthenic syndrome Disease mutation
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine metabolic process Inferred from electronic annotation. Source: Compara 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 via asparagine Traceable author statement. Source: Reactome protein oligomerization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	integral to endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	UDP-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 408	408	UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase		PRO_0000108761
Regions
	Topological domain	1 – 6	6	Lumenal Potential
	Transmembrane	7 – 32	26	Helical; Potential
	Topological domain	33 – 57	25	Cytoplasmic Potential
	Transmembrane	58 – 79	22	Helical; Potential
	Topological domain	80 – 94	15	Lumenal Potential
	Transmembrane	95 – 114	20	Helical; Potential
	Topological domain	115 – 125	11	Cytoplasmic Potential
	Transmembrane	126 – 145	20	Helical; Potential
	Topological domain	146 – 164	19	Lumenal Potential
	Transmembrane	165 – 184	20	Helical; Potential
	Topological domain	185 – 194	10	Cytoplasmic Potential
	Transmembrane	195 – 211	17	Helical; Potential
	Topological domain	212 – 221	10	Lumenal Potential
	Transmembrane	222 – 240	19	Helical; Potential
	Topological domain	241 – 252	12	Cytoplasmic Potential
	Transmembrane	253 – 269	17	Helical; Potential
	Topological domain	270 – 274	5	Lumenal Potential
	Transmembrane	275 – 294	20	Helical; Potential
	Topological domain	295 – 378	84	Cytoplasmic Potential
	Transmembrane	379 – 397	19	Helical; Potential
	Topological domain	398 – 408	11	Lumenal Potential
	Motif	67 – 79	13	Dolichol recognition
	Motif	222 – 234	13	Dolichol recognition
Amino acid modifications
	Glycosylation	146	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 107	107	Missing in isoform 3.		VSP_008886
	Alternative sequence	1 – 8	8	Missing in isoform 2.		VSP_001803
	Natural variant	9	1	M → I in a breast cancer sample; somatic mutation. Ref.6		VAR_036422
	Natural variant	108	1	M → I in CMSTA2. Ref.7		VAR_068810
	Natural variant	117	1	V → I in CMSTA2. Ref.7		VAR_068811
	Natural variant	120	1	L → M in CMSTA2. Ref.7		VAR_068812
	Natural variant	160	1	G → S in CMSTA2. Ref.7		VAR_068813
	Natural variant	170	1	Y → C in CDG1J. Ref.5 Corresponds to variant rs28934876 [ dbSNP | Ensembl ].		VAR_017243
	Natural variant	192	1	G → S in CMSTA2. Ref.7		VAR_068814
	Natural variant	264	1	V → G in CMSTA2. Ref.7		VAR_068815
	Natural variant	393	1	I → V. Ref.4 Corresponds to variant rs643788 [ dbSNP | Ensembl ].		VAR_011391
Experimental info
	Sequence conflict	33	1	R → L in CAB04787. Ref.1
	Sequence conflict	129	1	P → H in AAG43168. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 29, 2001. Version 2. Checksum: 0AE10EFE55E7B9E0	FASTA	408	46,090
	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
	Isoform 2 [UniParc]. Checksum: 54D3A9DCCCA14F6B	FASTA	400	45,128
	10 20 30 40 50 60 MPLLINLIVS LLGFVATVTL IPAFRGHFIA ARLCGQDLNK TSRQQIPESQ GVISGAVFLI 70 80 90 100 110 120 ILFCFIPFPF LNCFVKEQCK AFPHHEFVAL IGALLAICCM IFLGFADDVL NLRWRHKLLL 130 140 150 160 170 180 PTAASLPLLM VYFTNFGNTT IVVPKPFRPI LGLHLDLGIL YYVYMGLLAV FCTNAINILA 190 200 210 220 230 240 GINGLEAGQS LVISASIIVF NLVELEGDCR DDHVFSLYFM IPFFFTTLGL LYHNWYPSRV 250 260 270 280 290 300 FVGDTFCYFA GMTFAVVGIL GHFSKTMLLF FMPQVFNFLY SLPQLLHIIP CPRHRIPRLN 310 320 330 340 350 360 IKTGKLEMSY SKFKTKSLSF LGTFILKVAE SLQLVTVHQS ETEDGEFTEC NNMTLINLLL 370 380 390 400 KVLGPIHERN LTLLLLLLQI LGSAITFSIR YQLVRLFYDV
	Isoform 3 [UniParc]. Checksum: C605449414F020C3	FASTA	301	34,270
	10 20 30 40 50 60 MIFLGFADDV LNLRWRHKLL LPTAASLPLL MVYFTNFGNT TIVVPKPFRP ILGLHLDLGI 70 80 90 100 110 120 LYYVYMGLLA VFCTNAINIL AGINGLEAGQ SLVISASIIV FNLVELEGDC RDDHVFSLYF 130 140 150 160 170 180 MIPFFFTTLG LLYHNWYPSR VFVGDTFCYF AGMTFAVVGI LGHFSKTMLL FFMPQVFNFL 190 200 210 220 230 240 YSLPQLLHII PCPRHRIPRL NIKTGKLEMS YSKFKTKSLS FLGTFILKVA ESLQLVTVHQ 250 260 270 280 290 300 SETEDGEFTE CNNMTLINLL LKVLGPIHER NLTLLLLLLQ ILGSAITFSI RYQLVRLFYD V

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00023500. IPI00219736. IPI00394961.
RefSeq	NP_001373.2. NM_001382.3.
UniGene	Hs.524081.
3D structure databases
ProteinModelPortal	Q9H3H5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H3H5. 1 interaction.
STRING	9606.ENSP00000346142.
PTM databases
PhosphoSite	Q9H3H5.
Polymorphism databases
DMDM	18202943.
Proteomic databases
PaxDb	Q9H3H5.
PRIDE	Q9H3H5.
Protocols and materials databases
DNASU	1798.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354202; ENSP00000346142; ENSG00000172269. ENST00000409993; ENSP00000386597; ENSG00000172269.
GeneID	1798.
KEGG	hsa:1798.
UCSC	uc001pvi.3. human.
Organism-specific databases
CTD	1798.
GeneCards	GC11M119001.
H-InvDB	HIX0019316.
HGNC	HGNC:2995. DPAGT1.
HPA	HPA053878.
MIM	191350. gene. 608093. phenotype. 614750. phenotype.
neXtProt	NX_Q9H3H5.
Orphanet	590. Congenital myasthenic syndromes. 86309. DPAGT1-CDG syndrome.
PharmGKB	PA27460.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0472.
HOGENOM	HOG000163915.
HOVERGEN	HBG000846.
InParanoid	Q9H3H5.
KO	K01001.
OMA	PFLNCFV.
OrthoDB	EOG4868CQ.
PhylomeDB	Q9H3H5.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q9H3H5.
Bgee	Q9H3H5.
CleanEx	HS_DPAGT1.
Genevestigator	Q9H3H5.
GermOnline	ENSG00000172269. Homo sapiens.
Family and domain databases
InterPro	IPR000715. Glycosyl_transferase_4. [Graphical view]
Pfam	PF00953. Glycos_transf_4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1798.
NextBio	7325.
SOURCE	Search...

Entry information

Entry name

GPT_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.