Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC 2.4.1.255) (O-GlcNAc transferase subunit p110) (O-linked N-acetylglucosamine transferase 110 kDa subunit) (OGT)

 OGT1_RAT                Reviewed;        1036 AA.
P56558;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 1.
10-OCT-2018, entry version 145.
RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
EC=2.4.1.255 {ECO:0000269|PubMed:24995978};
AltName: Full=O-GlcNAc transferase subunit p110;
AltName: Full=O-linked N-acetylglucosamine transferase 110 kDa subunit;
Short=OGT;
Name=Ogt;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE
SPECIFICITY, PHOSPHORYLATION AT TYR-979, GLYCOSYLATION, AND
SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=9083067; DOI=10.1074/jbc.272.14.9308;
Kreppel L.K., Blomberg M.A., Hart G.W.;
"Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and
characterization of a unique O-GlcNAc transferase with multiple
tetratricopeptide repeats.";
J. Biol. Chem. 272:9308-9315(1997).
[2]
TISSUE SPECIFICITY.
PubMed=10580430; DOI=10.2337/diabetes.48.12.2407;
Akimoto Y., Kreppel L.K., Hirano H., Hart G.W.;
"Localization of the O-linked N-acetylglucosamine transferase in rat
pancreas.";
Diabetes 48:2407-2413(1999).
[3]
SUBCELLULAR LOCATION, INTERACTION WITH ATXN10, SUBUNIT, TISSUE
SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16714295; DOI=10.1074/jbc.M601563200;
Maerz P., Stetefeld J., Bendfeldt K., Nitsch C., Reinstein J.,
Shoeman R.L., Dimitriades-Schmutz B., Schwager M., Leiser D.,
Ozcan S., Otten U., Ozbek S.;
"Ataxin-10 interacts with O-linked beta-N-acetylglucosamine
transferase in the brain.";
J. Biol. Chem. 281:20263-20270(2006).
[4]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL-BINDING, AND
MUTAGENESIS OF 981-LYS-LYS-982; ARG-984; LYS-986; LYS-989; ARG-991 AND
LYS-1000.
PubMed=18288188; DOI=10.1038/nature06668;
Yang X., Ongusaha P.P., Miles P.D., Havstad J.C., Zhang F., So W.V.,
Kudlow J.E., Michell R.H., Olefsky J.M., Field S.J., Evans R.M.;
"Phosphoinositide signalling links O-GlcNAc transferase to insulin
resistance.";
Nature 451:964-969(2008).
[5]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH KIF5B; RHOT1;
RHOT2 AND TRAK1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
2-MET--MET-129; 2-MET--HIS-248 AND HIS-498.
PubMed=24995978; DOI=10.1016/j.cell.2014.06.007;
Pekkurnaz G., Trinidad J.C., Wang X., Kong D., Schwarz T.L.;
"Glucose regulates mitochondrial motility via Milton modification by
O-GlcNAc transferase.";
Cell 158:54-68(2014).
-!- FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine
from UDP-GlcNAc to a serine or threonine residue in cytoplasmic
and nuclear proteins resulting in their modification with a beta-
linked N-acetylglucosamine (O-GlcNAc) (PubMed:24995978).
Glycosylates a large and diverse number of proteins including
histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can
regulate their cellular processes via cross-talk between
glycosylation and phosphorylation or by affecting proteolytic
processing. Probably by glycosylating KMT2E/MLL5, stabilizes
KMT2E/MLL5 by preventing its ubiquitination (By similarity).
Involved in insulin resistance in muscle and adipocyte cells via
glycosylating insulin signaling components and inhibiting the
'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation
and attenuating insulin signaling (PubMed:18288188). Involved in
glycolysis regulation by mediating glycosylation of 6-
phosphofructokinase PFKL, inhibiting its activity. Component of a
THAP1/THAP3-HCFC1-OGT complex that is required for the regulation
of the transcriptional activity of RRM1. Plays a key role in
chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of
histone H2B: recruited to CpG-rich transcription start sites of
active genes via its interaction with TET proteins (TET1, TET2 or
TET3). As part of the NSL complex indirectly involved in
acetylation of nucleosomal histone H4 on several lysine residues.
O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and
facilitating the formation of H3K27me3 by the PRC2/EED-EZH2
complex. Regulates circadian oscillation of the clock genes and
glucose homeostasis in the liver. Stabilizes clock proteins
ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents
their ubiquitination and subsequent degradation. Promotes the
CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative
loop of the circadian clock such as PER1/2 and CRY1/2. O-
glycosylates HCFC1 and regulates its proteolytic processing and
transcriptional activity (By similarity). Regulates mitochondrial
motility in neurons by mediating glycosylation of TRAK1
(PubMed:24995978). Glycosylates HOXA1 (By similarity).
{ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:Q8CGY8,
ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:24995978}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-
serine. {ECO:0000269|PubMed:24995978}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-threonine. {ECO:0000269|PubMed:24995978}.
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:24995978}.
-!- SUBUNIT: Heterotrimer; consists of one 78 kDa subunit and two 110
kDa subunits dimerized via TPR repeats 6 and 7. Component of a
THAP1/THAP3-HCFC1-OGT complex. Component of the NSL complex at
least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20,
OGT1/OGT, WDR5 and HCFC1. Interacts directly with HCFC1; the
interaction O-glycosylates HCFC1, regulates its proteolytic
processing and transcriptional activity and, in turn, stabilizes
OGT in the nucleus. Interacts (via TPRs 1-6) with SIN3A; the
interaction mediates transcriptional repression in parallel with
histone deacetylase. Interacts (via TPR 5-6) with TET1, TET2 and
TET3 (By similarity). Interacts (via TPR repeats 6 and 7) with
ATXN10 (PubMed:16714295). Interacts with histone H2B (By
similarity). Interacts with ARNTL/BMAL1. Found in a complex
composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and
TET1. Interacts with SINHCAF (By similarity). Component of a
complex composed of KMT2E/MLL5, OGT and USP7; the complex
stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination and
proteosomal-mediated degradation. Interacts (via TRP repeats) with
KMT2E (via N-terminus). Interacts with USP7 (By similarity).
Interacts with TRAK1; this interaction is not required for
glycosylation of TRAK1 by this protein. Found in a complex with
KIF5B, RHOT1, RHOT2 and TRAK1 (PubMed:24995978). Interacts (via
TPR repeats domain) with HOXA1; the interaction takes place mainly
in the nucleus (By similarity). {ECO:0000250|UniProtKB:O15294,
ECO:0000250|UniProtKB:Q8CGY8, ECO:0000269|PubMed:16714295,
ECO:0000269|PubMed:24995978}.
-!- INTERACTION:
Q9WVH3:Foxo4 (xeno); NbExp=2; IntAct=EBI-7614183, EBI-4567305;
Q9WU00:Nrf1 (xeno); NbExp=2; IntAct=EBI-7614183, EBI-11291138;
Q9UPV9:TRAK1 (xeno); NbExp=6; IntAct=EBI-7614183, EBI-1105048;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16714295,
ECO:0000269|PubMed:24995978, ECO:0000269|PubMed:9083067}. Nucleus
{ECO:0000269|PubMed:18288188, ECO:0000269|PubMed:24995978,
ECO:0000269|PubMed:9083067}. Cell membrane
{ECO:0000269|PubMed:18288188}. Mitochondrion membrane
{ECO:0000269|PubMed:24995978}. Cell projection
{ECO:0000269|PubMed:24995978}. Note=Mostly in the nucleus.
Retained in the nucleus via interaction with HCFC1 (By
similarity). After insulin induction, translocated from the
nucleus to the cell membrane via phophatidylinositide binding.
Colocalizes with AKT1 at the plasma membrane (PubMed:18288188).
TRAK1 recruits this protein to mitochondria. In the absence of
TRAK1, localizes in cytosol and nucleus (PubMed:24995978).
{ECO:0000250|UniProtKB:O15294, ECO:0000269|PubMed:18288188,
ECO:0000269|PubMed:24995978}.
-!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, thymus,
lung, pancreas, spleen, uterus and ovary. In the pancreas,
expressed in both exocrine acinar cells and in endocrine cells of
the islets of Langerhans. {ECO:0000269|PubMed:10580430,
ECO:0000269|PubMed:16714295, ECO:0000269|PubMed:9083067}.
-!- DOMAIN: The TPR repeat domain is required for substrate binding
and oligomerization. {ECO:0000250|UniProtKB:O15294,
ECO:0000269|PubMed:24995978}.
-!- PTM: O-glycosylated; contains O-GlcNAc.
{ECO:0000269|PubMed:9083067}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
{ECO:0000250}.
-!- PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively
regulates its activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
transferase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U76557; AAC53121.1; -; mRNA.
PIR; T31673; T31673.
RefSeq; NP_058803.2; NM_017107.2.
UniGene; Rn.82705; -.
ProteinModelPortal; P56558; -.
SMR; P56558; -.
BioGrid; 247798; 5.
IntAct; P56558; 4.
MINT; P56558; -.
STRING; 10116.ENSRNOP00000004692; -.
CAZy; GT41; Glycosyltransferase Family 41.
iPTMnet; P56558; -.
PhosphoSitePlus; P56558; -.
PaxDb; P56558; -.
PRIDE; P56558; -.
GeneID; 26295; -.
KEGG; rno:26295; -.
UCSC; RGD:62060; rat.
CTD; 8473; -.
RGD; 62060; Ogt.
eggNOG; KOG1124; Eukaryota.
eggNOG; KOG4626; Eukaryota.
eggNOG; COG3914; LUCA.
HOGENOM; HOG000003765; -.
HOVERGEN; HBG000351; -.
InParanoid; P56558; -.
KO; K09667; -.
PhylomeDB; P56558; -.
BRENDA; 2.4.1.255; 5301.
UniPathway; UPA00378; -.
PRO; PR:P56558; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0000791; C:euchromatin; IDA:RGD.
GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0042588; C:zymogen granule; IDA:RGD.
GO; GO:0048029; F:monosaccharide binding; IDA:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:RGD.
GO; GO:0097363; F:protein O-GlcNAc transferase activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IMP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:RGD.
GO; GO:0097237; P:cellular response to toxic substance; IEP:RGD.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEP:RGD.
GO; GO:0006041; P:glucosamine metabolic process; IDA:RGD.
GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:RGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IMP:RGD.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:RGD.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
GO; GO:0090315; P:negative regulation of protein targeting to membrane; IMP:RGD.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:0045793; P:positive regulation of cell size; IMP:RGD.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0070208; P:protein heterotrimerization; IDA:RGD.
GO; GO:0070207; P:protein homotrimerization; IDA:RGD.
GO; GO:0006493; P:protein O-linked glycosylation; IDA:RGD.
GO; GO:0016485; P:protein processing; ISS:UniProtKB.
GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
Gene3D; 1.25.40.10; -; 2.
InterPro; IPR037919; OGT.
InterPro; IPR029489; OGT/SEC/SPY_C.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR001440; TPR_1.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR44366; PTHR44366; 1.
Pfam; PF13844; Glyco_transf_41; 1.
Pfam; PF00515; TPR_1; 2.
Pfam; PF13181; TPR_8; 2.
SMART; SM00028; TPR; 12.
SUPFAM; SSF48452; SSF48452; 5.
PROSITE; PS50005; TPR; 12.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Acetylation; Biological rhythms; Cell membrane; Cell projection;
Chromatin regulator; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycoprotein; Glycosyltransferase;
Lipid-binding; Membrane; Mitochondrion; Nucleus; Phosphoprotein;
Reference proteome; Repeat; TPR repeat; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O15294}.
CHAIN 2 1036 UDP-N-acetylglucosamine--peptide N-
acetylglucosaminyltransferase 110 kDa
subunit.
/FTId=PRO_0000191774.
REPEAT 11 44 TPR 1.
REPEAT 79 112 TPR 2.
REPEAT 113 146 TPR 3.
REPEAT 147 180 TPR 4.
REPEAT 181 214 TPR 5.
REPEAT 215 248 TPR 6.
REPEAT 249 282 TPR 7.
REPEAT 283 316 TPR 8.
REPEAT 317 350 TPR 9.
REPEAT 351 384 TPR 10.
REPEAT 385 418 TPR 11.
REPEAT 419 452 TPR 12.
REPEAT 453 463 TPR 13; truncated.
NP_BIND 896 898 UDP. {ECO:0000250|UniProtKB:O15294}.
NP_BIND 901 904 UDP. {ECO:0000250|UniProtKB:O15294}.
NP_BIND 920 922 UDP. {ECO:0000250|UniProtKB:O15294}.
REGION 981 1000 Required for phosphatidylinositol 3,4,5-
triphosphate binding.
MOTIF 478 493 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 498 498 Proton acceptor.
{ECO:0000269|PubMed:24995978}.
BINDING 839 839 UDP. {ECO:0000250|UniProtKB:O15294}.
BINDING 842 842 UDP. {ECO:0000250|UniProtKB:O15294}.
BINDING 925 925 UDP. {ECO:0000250|UniProtKB:O15294}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O15294}.
MOD_RES 3 3 Phosphoserine; by GSK3-beta; alternate.
{ECO:0000250|UniProtKB:Q8CGY8}.
MOD_RES 4 4 Phosphoserine; by GSK3-beta; alternate.
{ECO:0000250|UniProtKB:Q8CGY8}.
MOD_RES 979 979 Phosphotyrosine.
{ECO:0000305|PubMed:9083067}.
CARBOHYD 3 3 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 4 4 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
MUTAGEN 2 248 Missing: Decreased TRAK1 O-glycosylation
by this protein.
{ECO:0000269|PubMed:24995978}.
MUTAGEN 2 129 Missing: Decreased ability to reduce
neuronal mitochondrial motility in both
anterograde and retrograde directions.
{ECO:0000269|PubMed:24995978}.
MUTAGEN 498 498 H->N: Loss of glycosylation activity.
Loss of ability to reduce mitochondrial
motility. {ECO:0000269|PubMed:24995978}.
MUTAGEN 981 982 KK->AA: Abolishes phosphatidylinisitol
binding, no translocation to the cell
membrane, and no effect on
phosphorylation of AKT1 nor IRS1.
{ECO:0000269|PubMed:18288188}.
MUTAGEN 984 984 R->A: No effect on phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
MUTAGEN 986 986 K->A: Reduced phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
MUTAGEN 989 989 K->A: Reduced phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
MUTAGEN 991 991 R->A: No effect on phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
MUTAGEN 1000 1000 K->A: No effect on phosphatidylinisitol
binding. {ECO:0000269|PubMed:18288188}.
SEQUENCE 1036 AA; 115606 MW; 3F057CABDD019BD6 CRC64;
MASSVGNVAD STGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL LSSIHFQCRR
LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP DFIDGYINLA
AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF
AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAAYLR
ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA NALKEKGSVA
EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF AAAHSNLASV
LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR AIQINPAFAD
AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV
SIVAEQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK PPYEHPKDLK
LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN FRVKVMAEAN
HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA MWLGYPGTSG
ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV IDFKSNGHIY
DNRIVLNGID LKAFLDSLPD VKIVKMKCPD GGDNADTTNT ALNMPVIPMN TIAEAVIEMI
NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL
YKIDPSTLQM GANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI IFSPVAPKEE
HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL TCLGCLELIA
KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ RISSPLFNTK QYTMELERLY LQMWEHYAAG
NKPDHMIKPV EVTESA


Related products :

Catalog number Product name Quantity
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
EIAAB28726 O-GlcNAc transferase subunit p110,OGT,O-linked N-acetylglucosamine transferase 110 kDa subunit,Pig,Sus scrofa,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
EIAAB28728 O-GlcNAc transferase subunit p110,OGT,O-linked N-acetylglucosamine transferase 110 kDa subunit,Oryctolagus cuniculus,Rabbit,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa sub
CSB-EL016315PI Pig O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine polypeptide-N-acetylglucosaminyl transferase) (OGT) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL016315RA Rat O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine polypeptide-N-acetylglucosaminyl transferase) (OGT) ELISA kit, Species Rat, Sample Type serum, plasma 96T
OIP5 OGT Gene O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine polypeptide-N-acetylglucosaminyl transferase)
CSB-EL016315HU Human O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine polypeptide-N-acetylglucosaminyl transferase) (OGT) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL016315RB Rabbit O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine polypeptide-N-acetylglucosaminyl transferase) (OGT) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-EL016315MO Mouse O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine polypeptide-N-acetylglucosaminyl transferase) (OGT) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
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 50ul
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
201-20-3947 OGT{O-linked N-acetylglucosamine (GlcNAc) transferase }rabbit.pAb 0.2ml
GS-1515a O-linked N-acetylglucosamine (GlcNAc) transferase primary antibody, Host: Rabbit 200ul
GNRH2 GNPTG Gene N-acetylglucosamine-1-phosphate transferase, gamma subunit
ALG14_HUMAN Human ELISA Kit FOR UDP-N-acetylglucosamine transferase subunit ALG14 homolog 96T
I0605 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (OGT), Rat, ELISA Kit 96T
I0603 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (OGT), Pig, ELISA Kit 96T
CSB-EL016315RA Rat UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit(OGT) ELISA kit 96T
I0602 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (OGT), Mouse, ELISA Kit 96T
CSB-EL016315PI Pig UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit(OGT) ELISA kit SpeciesPig 96T
CSB-EL016315RA Rat UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit(OGT) ELISA kit SpeciesRat 96T
I0604 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (OGT), Rabbit, ELISA Kit 96T
I0601 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (OGT), Human, ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur