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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.
20-JUN-2018, entry version 143.
RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
EC=2.4.1.255 {ECO:0000250|UniProtKB:O15294};
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).
-!- 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). Glycosylates a large and
diverse number of proteins including histone H2B, AKT1, EZH2,
PFKL, KMT2E, 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, stabilizes KMT2E by preventing its ubiquitination. 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. 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.
{ECO:0000250|UniProtKB:O15294}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-
serine. {ECO:0000250|UniProtKB:O15294}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-threonine. {ECO:0000250|UniProtKB:O15294}.
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Heterotrimer; consists of one 78 kDa subunit and two 110
kDa subunits dimerized via TPR repeats 6 and 7 (By similarity).
Component of a THAP1/THAP3-HCFC1-OGT complex (By similarity).
Component of the NSL complex at least composed of MOF/KAT8,
KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (By
similarity). Interacts directly with HCFC1; the interaction O-
glycosylates HCFC1, regulates its proteolytic processing and
transcriptional activity and, in turn, stabilizes OGT in the
nucleus (By similarity). Interacts (via TPRs 1-6) with SIN3A; the
interaction mediates transcriptional repression in parallel with
histone deacetylase (By similarity). 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 (By similarity). Found
in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30,
RBBP4, OGT and TET1 (By similarity). Interacts with SINHCAF (By
similarity). Component of a complex composed of KMT2E, OGT and
USP7; the complex stabilizes KMT2E, preventing KMT2E
ubiquitination and proteosomal-mediated degradation (By
similarity). Interacts (via TRP repeats) with KMT2E (via N-
terminus) (By similarity). Interacts with USP7 (By similarity).
{ECO:0000250|UniProtKB:O15294, ECO:0000250|UniProtKB:Q8CGY8,
ECO:0000269|PubMed:16714295}.
-!- 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. Nucleus. Cell membrane.
Note=Mostly in the nucleus. Retained in the nucleus via
interaction with HCFC1. After insulin induction, translocated from
the nucleus to the cell membrane via phophatidylinisotide binding.
Colocalizes with AKT1 at the plasma membrane (By similarity).
{ECO:0000250}.
-!- 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.
-!- 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}.
-----------------------------------------------------------------------
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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: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; Chromatin regulator;
Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein;
Glycosyltransferase; Lipid-binding; Membrane; 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 895 898 UDP. {ECO:0000250}.
NP_BIND 901 904 UDP. {ECO:0000250}.
NP_BIND 919 921 UDP. {ECO:0000250}.
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:0000250}.
BINDING 839 839 UDP. {ECO:0000250}.
BINDING 842 842 UDP. {ECO:0000250}.
BINDING 925 925 UDP. {ECO:0000250}.
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}.
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


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