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UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) (GlcNAc-1-P transferase) (G1PT) (GPT) (N-acetylglucosamine-1-phosphate transferase)

 GPT_HUMAN               Reviewed;         408 AA.
Q9H3H5; O15216; Q86WV9; Q9BWE6;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
29-AUG-2001, sequence version 2.
12-SEP-2018, entry version 166.
RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase;
EC=2.7.8.15 {ECO:0000269|PubMed:29459785};
AltName: Full=GlcNAc-1-P transferase {ECO:0000303|PubMed:29459785};
Short=G1PT;
Short=GPT {ECO:0000303|PubMed:29459785};
AltName: Full=N-acetylglucosamine-1-phosphate transferase;
Name=DPAGT1 {ECO:0000303|PubMed:12872255, ECO:0000303|PubMed:22742743,
ECO:0000303|PubMed:29459785, ECO:0000312|HGNC:HGNC:2995};
Synonyms=DPAGT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=9451016; DOI=10.1093/glycob/8.1.77;
Eckert V., Blank M., Mazhari-Tabrizi R., Mumberg D., Funk M.,
Schwarz R.T.;
"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.";
Glycobiology 8:77-85(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Dagnino F., Regis S., Filocamo M., Gatti R.;
"Putative genomic sequence of GlcNAc-1-P transferase on chromosome
11q23.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR,
FUNCTION, SUBUNIT, TOPOLOGY, ACTIVITY REGULATION, COFACTOR, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF ASP-252.
PubMed=29459785; DOI=10.1038/s41594-018-0031-y;
Yoo J., Mashalidis E.H., Kuk A.C.Y., Yamamoto K., Kaeser B.,
Ichikawa S., Lee S.Y.;
"GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis
for inhibition of N-glycosylation.";
Nat. Struct. Mol. Biol. 25:217-224(2018).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
VAL-393.
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
VARIANT CDG1J CYS-170.
PubMed=12872255; DOI=10.1002/humu.10239;
Wu X., Rush J.S., Karaoglu D., Krasnewich D., Lubinsky M.S.,
Waechter C.J., Gilmore R., Freeze H.H.;
"Deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1
phosphate transferase (DPAGT1) causes a novel congenital disorder of
glycosylation type Ij.";
Hum. Mutat. 22:144-150(2003).
[7]
VARIANT [LARGE SCALE ANALYSIS] ILE-9.
PubMed=16959974; DOI=10.1126/science.1133427;
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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[8]
VARIANTS CMS13 ILE-108; ILE-117; MET-120; SER-160; SER-192 AND
GLY-264.
PubMed=22742743; DOI=10.1016/j.ajhg.2012.05.022;
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.;
"Mutations in DPAGT1 cause a limb-girdle congenital myasthenic
syndrome with tubular aggregates.";
Am. J. Hum. Genet. 91:193-201(2012).
-!- FUNCTION: Catalyzes the initial step of dolichol-linked
oligosaccharide biosynthesis in N-linked protein glycosylation
pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier
lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-
dolichol. {ECO:0000269|PubMed:29459785}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + dolichyl
phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol.
{ECO:0000269|PubMed:29459785}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:29459785};
-!- ACTIVITY REGULATION: Activated by mannosylphosphoryldolichol and
phospholipids such as phosphatidylglycerol and phosphatidylcholine
(Probable). Inhibited by natural nucleoside antibiotic
tunicamycin, which acts as a structural analog and competitor of
UDP-GlcNAc (PubMed:29459785). {ECO:0000269|PubMed:29459785,
ECO:0000305|PubMed:29459785}.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29459785}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein {ECO:0000269|PubMed:29459785}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H3H5-1; Sequence=Displayed;
Name=2;
IsoId=Q9H3H5-2; Sequence=VSP_001803;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9H3H5-3; Sequence=VSP_008886;
Note=No experimental confirmation available.;
-!- DISEASE: Congenital disorder of glycosylation 1J (CDG1J)
[MIM:608093]: A form of congenital disorder of glycosylation, 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. {ECO:0000269|PubMed:12872255}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Myasthenic syndrome, congenital, 13 (CMS13) [MIM:614750]:
A 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. {ECO:0000269|PubMed:22742743}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 4 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=UDP-
N-acetylglucosamine--dolichyl-phosphate N-
acetylglucosaminephosphotransferase;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_543";
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EMBL; Z82022; CAB04787.1; -; mRNA.
EMBL; AF070443; AAG43168.1; -; Genomic_DNA.
EMBL; AF069061; AAG43168.1; JOINED; Genomic_DNA.
EMBL; BT006802; AAP35448.1; -; mRNA.
EMBL; BC000325; AAH00325.1; -; mRNA.
EMBL; BC047771; AAH47771.1; -; mRNA.
CCDS; CCDS8411.1; -. [Q9H3H5-1]
RefSeq; NP_001373.2; NM_001382.3. [Q9H3H5-1]
RefSeq; XP_016872782.1; XM_017017293.1. [Q9H3H5-3]
UniGene; Hs.524081; -.
PDB; 5LEV; X-ray; 3.20 A; A=1-408.
PDB; 5O5E; X-ray; 3.40 A; A=1-408.
PDB; 6BW5; X-ray; 3.10 A; A/B/C/D=1-408.
PDB; 6BW6; X-ray; 2.95 A; A/B/C/D=1-408.
PDB; 6FM9; X-ray; 3.60 A; A=1-408.
PDBsum; 5LEV; -.
PDBsum; 5O5E; -.
PDBsum; 6BW5; -.
PDBsum; 6BW6; -.
PDBsum; 6FM9; -.
ProteinModelPortal; Q9H3H5; -.
SMR; Q9H3H5; -.
BioGrid; 108133; 11.
IntAct; Q9H3H5; 1.
STRING; 9606.ENSP00000346142; -.
iPTMnet; Q9H3H5; -.
PhosphoSitePlus; Q9H3H5; -.
BioMuta; DPAGT1; -.
DMDM; 18202943; -.
EPD; Q9H3H5; -.
MaxQB; Q9H3H5; -.
PaxDb; Q9H3H5; -.
PeptideAtlas; Q9H3H5; -.
PRIDE; Q9H3H5; -.
ProteomicsDB; 80717; -.
ProteomicsDB; 80718; -. [Q9H3H5-2]
ProteomicsDB; 80719; -. [Q9H3H5-3]
DNASU; 1798; -.
Ensembl; ENST00000354202; ENSP00000346142; ENSG00000172269. [Q9H3H5-1]
Ensembl; ENST00000409993; ENSP00000386597; ENSG00000172269. [Q9H3H5-1]
GeneID; 1798; -.
KEGG; hsa:1798; -.
UCSC; uc001pvi.4; human. [Q9H3H5-1]
CTD; 1798; -.
DisGeNET; 1798; -.
EuPathDB; HostDB:ENSG00000172269.16; -.
GeneCards; DPAGT1; -.
GeneReviews; DPAGT1; -.
H-InvDB; HIX0019316; -.
HGNC; HGNC:2995; DPAGT1.
HPA; HPA053878; -.
MalaCards; DPAGT1; -.
MIM; 191350; gene.
MIM; 608093; phenotype.
MIM; 614750; phenotype.
neXtProt; NX_Q9H3H5; -.
OpenTargets; ENSG00000172269; -.
Orphanet; 353327; Congenital myasthenic syndromes with glycosylation defect.
Orphanet; 86309; DPAGT1-CDG.
PharmGKB; PA27460; -.
eggNOG; KOG2788; Eukaryota.
eggNOG; COG0472; LUCA.
GeneTree; ENSGT00390000011424; -.
HOGENOM; HOG000163915; -.
HOVERGEN; HBG000846; -.
InParanoid; Q9H3H5; -.
KO; K01001; -.
OMA; GDYRDDH; -.
OrthoDB; EOG091G0A0M; -.
PhylomeDB; Q9H3H5; -.
TreeFam; TF313734; -.
Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
Reactome; R-HSA-4549356; Defective DPAGT1 causes DPAGT1-CDG (CDG-1j) and CMSTA2.
UniPathway; UPA00378; -.
GeneWiki; DPAGT1; -.
GenomeRNAi; 1798; -.
PRO; PR:Q9H3H5; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000172269; Expressed in 207 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_DPAGT1; -.
ExpressionAtlas; Q9H3H5; baseline and differential.
Genevisible; Q9H3H5; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IDA:UniProtKB.
GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; IDA:MGI.
GO; GO:0019348; P:dolichol metabolic process; IEA:Ensembl.
GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IDA:UniProtKB.
GO; GO:0006489; P:dolichyl diphosphate biosynthetic process; IBA:GO_Central.
GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:Ensembl.
CDD; cd06855; GT_GPT_euk; 1.
InterPro; IPR000715; Glycosyl_transferase_4.
InterPro; IPR033895; GPT.
PANTHER; PTHR10571; PTHR10571; 1.
Pfam; PF00953; Glycos_transf_4; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Congenital disorder of glycosylation; Congenital myasthenic syndrome;
Disease mutation; Endoplasmic reticulum; Glycoprotein;
Glycosyltransferase; Magnesium; Membrane; Polymorphism;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 408 UDP-N-acetylglucosamine--dolichyl-
phosphate N-
acetylglucosaminephosphotransferase.
/FTId=PRO_0000108761.
TOPO_DOM 1 10 Lumenal. {ECO:0000269|PubMed:29459785}.
TRANSMEM 11 38 Helical; Name=Helix 1.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 39 58 Cytoplasmic.
{ECO:0000269|PubMed:29459785}.
TRANSMEM 59 78 Helical; Name=Helix 2.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 79 91 Lumenal. {ECO:0000269|PubMed:29459785}.
TRANSMEM 92 118 Helical; Name=Helix 3.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 119 121 Cytoplasmic.
{ECO:0000269|PubMed:29459785}.
TRANSMEM 122 143 Helical; Name=Helix 4.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 144 166 Lumenal. {ECO:0000269|PubMed:29459785}.
TRANSMEM 167 186 Helical; Name=Helix 5.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 187 192 Cytoplasmic.
{ECO:0000269|PubMed:29459785}.
TRANSMEM 193 213 Helical; Name=Helix 6.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 214 218 Lumenal. {ECO:0000269|PubMed:29459785}.
TRANSMEM 219 242 Helical; Name=Helix 7.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 243 250 Cytoplasmic.
{ECO:0000269|PubMed:29459785}.
TRANSMEM 251 269 Helical; Name=Helix 8.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 270 271 Lumenal. {ECO:0000269|PubMed:29459785}.
TRANSMEM 272 293 Helical; Name=Helix 9.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 294 375 Cytoplasmic.
{ECO:0000269|PubMed:29459785}.
TRANSMEM 376 400 Helical; Name=Helix 10.
{ECO:0000269|PubMed:29459785}.
TOPO_DOM 401 408 Lumenal. {ECO:0000269|PubMed:29459785}.
MOTIF 67 79 Dolichol recognition.
MOTIF 222 234 Dolichol recognition.
BINDING 46 46 Inhibitor; via amide nitrogen.
{ECO:0000244|PDB:6BW5,
ECO:0000244|PDB:6BW6,
ECO:0000269|PubMed:29459785}.
BINDING 119 119 Inhibitor. {ECO:0000244|PDB:6BW5,
ECO:0000269|PubMed:29459785}.
BINDING 185 185 Inhibitor. {ECO:0000244|PDB:6BW5,
ECO:0000244|PDB:6BW6,
ECO:0000269|PubMed:29459785}.
BINDING 252 252 Inhibitor. {ECO:0000244|PDB:6BW5,
ECO:0000269|PubMed:29459785}.
BINDING 303 303 Inhibitor. {ECO:0000244|PDB:6BW5,
ECO:0000244|PDB:6BW6,
ECO:0000269|PubMed:29459785}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 107 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_008886.
VAR_SEQ 1 8 Missing (in isoform 2).
{ECO:0000303|PubMed:9451016}.
/FTId=VSP_001803.
VARIANT 9 9 M -> I (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036422.
VARIANT 108 108 M -> I (in CMS13; dbSNP:rs376039938).
{ECO:0000269|PubMed:22742743}.
/FTId=VAR_068810.
VARIANT 117 117 V -> I (in CMS13; dbSNP:rs387907243).
{ECO:0000269|PubMed:22742743}.
/FTId=VAR_068811.
VARIANT 120 120 L -> M (in CMS13; dbSNP:rs387907244).
{ECO:0000269|PubMed:22742743}.
/FTId=VAR_068812.
VARIANT 160 160 G -> S (in CMS13; dbSNP:rs762676399).
{ECO:0000269|PubMed:22742743}.
/FTId=VAR_068813.
VARIANT 170 170 Y -> C (in CDG1J; dbSNP:rs28934876).
{ECO:0000269|PubMed:12872255}.
/FTId=VAR_017243.
VARIANT 192 192 G -> S (in CMS13; dbSNP:rs768464558).
{ECO:0000269|PubMed:22742743}.
/FTId=VAR_068814.
VARIANT 264 264 V -> G (in CMS13; dbSNP:rs387907245).
{ECO:0000269|PubMed:22742743}.
/FTId=VAR_068815.
VARIANT 393 393 I -> V (in dbSNP:rs643788).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_011391.
MUTAGEN 252 252 D->A: Reduces binding to inhibitor.
{ECO:0000269|PubMed:29459785}.
CONFLICT 33 33 R -> L (in Ref. 1; CAB04787).
{ECO:0000305}.
CONFLICT 129 129 P -> H (in Ref. 2; AAG43168).
{ECO:0000305}.
HELIX 9 31 {ECO:0000244|PDB:6BW6}.
HELIX 33 38 {ECO:0000244|PDB:6BW6}.
STRAND 42 44 {ECO:0000244|PDB:6BW6}.
STRAND 53 55 {ECO:0000244|PDB:6BW6}.
HELIX 59 73 {ECO:0000244|PDB:6BW6}.
HELIX 76 78 {ECO:0000244|PDB:6BW6}.
HELIX 92 118 {ECO:0000244|PDB:6BW6}.
HELIX 122 143 {ECO:0000244|PDB:6BW6}.
TURN 155 157 {ECO:0000244|PDB:5O5E}.
HELIX 167 186 {ECO:0000244|PDB:6BW6}.
HELIX 193 213 {ECO:0000244|PDB:6BW6}.
STRAND 214 216 {ECO:0000244|PDB:6BW6}.
HELIX 219 242 {ECO:0000244|PDB:6BW6}.
STRAND 243 245 {ECO:0000244|PDB:6BW6}.
HELIX 251 269 {ECO:0000244|PDB:6BW6}.
HELIX 272 278 {ECO:0000244|PDB:6BW6}.
HELIX 280 288 {ECO:0000244|PDB:6BW6}.
HELIX 290 293 {ECO:0000244|PDB:6BW6}.
STRAND 306 308 {ECO:0000244|PDB:6BW6}.
TURN 309 312 {ECO:0000244|PDB:6BW6}.
STRAND 313 315 {ECO:0000244|PDB:6BW6}.
STRAND 318 321 {ECO:0000244|PDB:6BW6}.
TURN 323 325 {ECO:0000244|PDB:6BW6}.
HELIX 328 339 {ECO:0000244|PDB:6BW6}.
STRAND 345 349 {ECO:0000244|PDB:6BW5}.
STRAND 356 359 {ECO:0000244|PDB:6BW6}.
HELIX 363 371 {ECO:0000244|PDB:6BW6}.
HELIX 376 398 {ECO:0000244|PDB:6BW6}.
SEQUENCE 408 AA; 46090 MW; 0AE10EFE55E7B9E0 CRC64;
MWAFSELPMP LLINLIVSLL GFVATVTLIP AFRGHFIAAR LCGQDLNKTS RQQIPESQGV
ISGAVFLIIL FCFIPFPFLN CFVKEQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL
RWRHKLLLPT AASLPLLMVY FTNFGNTTIV VPKPFRPILG LHLDLGILYY VYMGLLAVFC
TNAINILAGI NGLEAGQSLV ISASIIVFNL VELEGDCRDD HVFSLYFMIP FFFTTLGLLY
HNWYPSRVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFM PQVFNFLYSL PQLLHIIPCP
RHRIPRLNIK TGKLEMSYSK FKTKSLSFLG TFILKVAESL QLVTVHQSET EDGEFTECNN
MTLINLLLKV LGPIHERNLT LLLLLLQILG SAITFSIRYQ LVRLFYDV


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CSB-EL007121BO Bovine UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit 96T
CSB-EL007121MO Mouse UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit 96T
I0600 UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1), Mouse, ELISA Kit 96T
CSB-EL007121HU Human UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit 96T
I0598 UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1), Bovine, ELISA Kit 96T
I0599 UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1), Human, ELISA Kit 96T
CSB-EL007121MO Mouse UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit SpeciesMouse 96T
CSB-EL007121HU Human UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit SpeciesHuman 96T
CSB-EL007121BO Bovine UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit SpeciesBovine 96T
EIAAB28725 Homo sapiens,Human,O-GlcNAc transferase subunit p110,OGT,O-linked N-acetylglucosamine transferase 110 kDa subunit,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
EIAAB28729 Mouse,Mus musculus,O-GlcNAc transferase subunit p110,Ogt,O-linked N-acetylglucosamine transferase 110 kDa subunit,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
EIAAB28727 O-GlcNAc transferase subunit p110,Ogt,O-linked N-acetylglucosamine transferase 110 kDa subunit,Rat,Rattus norvegicus,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
CSB-PA016315GA01HU Rabbit anti-human O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul


 

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