Protein name:
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit ;
Alternative:
O-linked N-acetylglucosamine transferase 110 kDa subunit (OGT) ;O-GlcNAc transferase subunit p110 ;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Heterotrimer of two 110 kDa and one 70 kDa subunits. It is not known if the 70 kDa subunit is encoded by a separate gene or is the product of either of a proteolytic degradation or an alternative initiation of the 110 kDa subunit (By similarity). Interacts with ATXN10 (By similarity). Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts directly with HCFC1.
Function:
Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Mediates the O-glycosylation of MLL5 and HCFC1. Promotes proteolytic maturation of HCFC1.
Subcellular Location:
Cytoplasm
Nucleus
Mostly in the nucleus.
Protein Attributes:
50:
MASSVGNVAD | STEPTKRMLS | FQGLAELAHR | EYQAGDFEAA | ERHCMQLWRQ |
100:
EPDNTGVLLL | LSSIHFQCRR | LDRSAHFSTL | AIKQNPLLAE | AYSNLGNVYK |
150:
ERGQLQEAIE | HYRHALRLKP | DFIDGYINLA | AALVAAGDME | GAVQAYVSAL |
200:
QYNPDLYCVR | SDLGNLLKAL | GRLEEAKACY | LKAIETQPNF | AVAWSNLGCV |
250:
FNAQGEIWLA | IHHFEKAVTL | DPNFLDAYIN | LGNVLKEARI | FDRAVAAYLR |
300:
ALSLSPNHAV | VHGNLACVYY | EQGLIDLAID | TYRRAIELQP | HFPDAYCNLA |
350:
NALKEKGSVA | EAEDCYNTAL | RLCPTHADSL | NNLANIKREQ | GNIEEAVRLY |
400:
RKALEVFPEF | AAAHSNLASV | LQQQGKLQEA | LMHYKEAIRI | SPTFADAYSN |
450:
MGNTLKEMQD | VQGALQCYTR | AIQINPAFAD | AHSNLASIHK | DSGNIPEAIA |
500:
SYRTALKLKP | DFPDAYCNLA | HCLQIVCDWT | DYDERMKKLV | SIVADQLEKN |
550:
RLPSVHPHHS | MLYPLSHGFR | KAIAERHGNL | CLDKINVLHK | PPYEHPKDLK |
600:
LSDGRLRVGY | VSSDFGNHPT | SHLMQSIPGM | HNPDKFEVFC | YALSPDDGTN |
650:
FRVKVMAEAN | HFIDLSQIPC | NGKAADRIHQ | DGIHILVNMN | GYTKGARNEL |
700:
FALRPAPIQA | MWLGYPGTSG | ALFMDYIITD | QETSPAEVAE | QYSEKLAYMP |
750:
HTFFIGDHAN | MFPHLKKKAV | IDFKSNGHIY | DNRIVLNGID | LKAFLDSLPD |
800:
VKIVKMKCPD | GGDNADSSNT | ALNMPVIPMN | TIAEAVIEMI | NRGQIQITIN |
850:
GFSISNGLAT | TQINNKAATG | EEVPRTIIVT | TRSQYGLPED | AIVYCNFNQL |
900:
YKIDPSTLQM | WANILKRVPN | SVLWLLRFPA | VGEPNIQQYA | QNMGLPQNRI |
950:
IFSPVAPKEE | HVRRGQLADV | CLDTPLCNGH | TTGMDVLWAG | TPMVTMPGET |
1000:
LASRVAASQL | TCLGCLELIA | KNRQEYEDIA | VKLGTDLEYL | KKVRGKVWKQ |
1046:
RISSPLFNTK | QYTMELERLY | LQMWEHYAAG | NKPDHMIKPV | EVTESA
Vaild Sequence:
Related Databases
Uniprot:
ELISA Kit
CLIA Kit
Polyclonal Antibody
Monoclonal Antibody
Protein
FOR
Human
Rabbit
Rat
Pig
Mouse
ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
R&D Technical Data
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Precision
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Recovery
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Linearity
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References
1.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2);PROTEIN SEQUENCE OF 227-236 AND 955-971;TISSUE SPECIFICITY
tissue :
Liver .
2.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3)
3.
"The full-ORF clone resource of the German cDNA consortium."
Bechtel S.
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Duda A.
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Schmidt C.P.
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Ernst U.
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BMC Genomics8:399-399(2007)
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PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4)
tissue :
Endometrium .
tissue :
Fetal brain .
tissue :
Spinal cord .
4.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3)
tissue :
Colon .
tissue :
Pancreas .
5.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : PROTEIN SEQUENCE OF 2-17; 31-42; 161-168; 244-250; 339-348; 734-752; 868-877 AND 1002-1010;CLEAVAGE OF INITIATOR METHIONINE;ACETYLATION AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY
tissue :
Hepatoma .
6.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH SIN3A;FUNCTION
7.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INTERACTION WITH HCFC1
8.
"Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance."
Yang X.
,
Ongusaha P.P.
,
Miles P.D.
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Havstad J.C.
,
Zhang F.
,
So W.V.
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Kudlow J.E.
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Michell R.H.
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Olefsky J.M.
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Field S.J.
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Evans R.M.
Nature451:964-969(2008)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : SUBCELLULAR LOCATION;FUNCTION;PHOSPHATIDYLINOSITOL-BINDING;MUTAGENESIS OF 991-LYS-LYS-992; ARG-994; LYS-996; LYS-999; ARG-1001 AND LYS-1010
9.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
tissue :
Cervix carcinoma .
10.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
11.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;ASSOCIATION WITH ALZHEIMER DISEASE
12.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : INDUCTION
13.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;CATALYTIC ACTIVITY;IDENTIFICATION IN THE MLL5-L COMPLEX
14.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION IN HISTONE H4 ACETYLATION;IDENTIFICATION IN NSL COMPLEX;SUBCELLULAR LOCATION
15.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;POSSIBLE ASSOCIATION WITH DIABETES
16.
"The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias."
Mazars R.
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Gonzalez-de-Peredo A.
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Cayrol C.
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Lavigne A.C.
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Vogel J.L.
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Ortega N.
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Kristie T.M.
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Girard J.P.
J. Biol. Chem.285:13364-13371(2010)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX;INTERACTION WITH HCFC1; THAP1 AND THAP3;FUNCTION
17.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION (ISOFORM 2)
18.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
19.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;CATALYTIC ACTIVITY;SUBCELLULAR LOCATION;UBIQUITINATION;INTERACTION WITH HCFC1
20.
"GlcNAcylation of histone H2B facilitates its monoubiquitination."
Fujiki R.
,
Hashiba W.
,
Sekine H.
,
Yokoyama A.
,
Chikanishi T.
,
Ito S.
,
Imai Y.
,
Kim J.
,
He H.H.
,
Igarashi K.
,
Kanno J.
,
Ohtake F.
,
Kitagawa H.
,
Roeder R.G.
,
Brown M.
,
Kato S.
Nature480:557-560(2011)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;INTERACTION WITH H2B
21.
"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P.
,
Lasa M.
,
Polevoda B.
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Gazquez C.
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Elosegui-Artola A.
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Kim D.S.
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De Juan-Pardo E.
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Demeyer K.
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Prieto J.
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Gevaert K.
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Proc. Natl. Acad. Sci. U.S.A.109:12449-12454(2012)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
22.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION
23.
"TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS."
Deplus R.
,
Delatte B.
,
Schwinn M.K.
,
Defrance M.
,
Mendez J.
,
Murphy N.
,
Dawson M.A.
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Volkmar M.
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Putmans P.
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Calonne E.
,
Shih A.H.
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Levine R.L.
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Bernard O.
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Mercher T.
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Solary E.
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Urh M.
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Daniels D.L.
,
Fuks F.
EMBO J.32:645-655(2013)
[
PubMed ]
[
Europe PMC ]
[
Abstract ]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;INTERACTION WITH HCFC1; TET2 AND TET3
24.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION;INTERACTION WITH TET2 AND TET3
25.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : FUNCTION
26.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 26-400;FUNCTION;CATALYTIC ACTIVITY;DOMAIN;MUTAGENESIS OF TRP-208 AND ILE-211
27.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 323-1041 IN COMPLEXES WITH UDP AND PEPTIDE SUBSTRATE;FUNCTION;CATALYTIC ACTIVITY;ENZYME REGULATION;BIOPHYSICOCHEMICAL PROPERTIES;ACTIVE SITE;MUTAGENESIS OF HIS-508; HIS-568 AND HIS-911