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Protein

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Gene

Ogt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. 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.By similarity

Catalytic activityi

UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine.By similarity
UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine.By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei498Proton acceptorBy similarity1
Binding sitei839UDPBy similarity1
Binding sitei842UDPBy similarity1
Binding sitei925UDPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi895 – 898UDPBy similarity4
Nucleotide bindingi901 – 904UDPBy similarity4
Nucleotide bindingi919 – 921UDPBy similarity3

GO - Molecular functioni

  • monosaccharide binding Source: RGD
  • peptide binding Source: RGD
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • protein domain specific binding Source: RGD
  • protein N-acetylglucosaminyltransferase activity Source: RGD
  • protein O-GlcNAc transferase activity Source: UniProtKB
  • transcription factor binding Source: RGD

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cellular response to glucose stimulus Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to toxic substance Source: RGD
  • circadian regulation of gene expression Source: UniProtKB
  • forebrain development Source: RGD
  • glucosamine metabolic process Source: RGD
  • histone H3-K4 trimethylation Source: UniProtKB
  • histone H4-K16 acetylation Source: UniProtKB
  • histone H4-K5 acetylation Source: UniProtKB
  • histone H4-K8 acetylation Source: UniProtKB
  • intracellular distribution of mitochondria Source: RGD
  • negative regulation of cell death Source: RGD
  • negative regulation of cellular response to hypoxia Source: RGD
  • negative regulation of peptidyl-serine phosphorylation Source: RGD
  • negative regulation of peptidyl-threonine phosphorylation Source: RGD
  • negative regulation of protein phosphorylation Source: RGD
  • negative regulation of protein targeting to membrane Source: RGD
  • negative regulation of protein ubiquitination Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: UniProtKB
  • positive regulation of cell size Source: RGD
  • positive regulation of gene expression Source: RGD
  • positive regulation of histone H3-K27 methylation Source: UniProtKB
  • positive regulation of protein localization to nucleus Source: RGD
  • positive regulation of protein phosphorylation Source: RGD
  • positive regulation of proteolysis Source: UniProtKB
  • positive regulation of reactive oxygen species biosynthetic process Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein heterotrimerization Source: RGD
  • protein homotrimerization Source: RGD
  • protein O-linked glycosylation Source: RGD
  • regulation of gluconeogenesis involved in cellular glucose homeostasis Source: UniProtKB
  • regulation of glycolytic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Glycosyltransferase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BRENDAi2.4.1.255. 5301.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT41. Glycosyltransferase Family 41.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC:2.4.1.255By similarity)
Alternative name(s):
O-GlcNAc transferase subunit p110
O-linked N-acetylglucosamine transferase 110 kDa subunit
Short name:
OGT
Gene namesi
Name:Ogt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62060. Ogt.

Subcellular locationi

  • 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).By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • euchromatin Source: RGD
  • histone acetyltransferase complex Source: UniProtKB
  • mitochondrion Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: UniProtKB
  • zymogen granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001917742 – 1036UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunitAdd BLAST1035

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei3Phosphoserine; by GSK3-beta; alternateBy similarity1
Glycosylationi3O-linked (GlcNAc); alternateBy similarity1
Modified residuei4Phosphoserine; by GSK3-beta; alternateBy similarity1
Glycosylationi4O-linked (GlcNAc); alternateBy similarity1
Modified residuei979Phosphotyrosine1 Publication1

Post-translational modificationi

O-glycosylated; contains O-GlcNAc.1 Publication
Ubiquitinated, leading to its proteasomal degradation.By similarity
Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP56558.
PRIDEiP56558.

PTM databases

iPTMnetiP56558.
PhosphoSitePlusiP56558.

Expressioni

Tissue specificityi

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.3 Publications

Interactioni

Subunit structurei

Heterotrimer; consists of one 78 kDa subunit and two 110 kDa subunits dimerized via TPR repeats 6 and 7. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, HCFC1, PPP1CC and ACTB. 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. Interacts with ARNTL/BMAL1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Foxo4Q9WVH32EBI-7614183,EBI-4567305From a different organism.
Nrf1Q9WU002EBI-7614183,EBI-11291138From a different organism.
TRAK1Q9UPV96EBI-7614183,EBI-1105048From a different organism.

GO - Molecular functioni

  • protein domain specific binding Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi247798. 4 interactors.
IntActiP56558. 4 interactors.
STRINGi10116.ENSRNOP00000004692.

Structurei

3D structure databases

ProteinModelPortaliP56558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati11 – 44TPR 1Add BLAST34
Repeati79 – 112TPR 2Add BLAST34
Repeati113 – 146TPR 3Add BLAST34
Repeati147 – 180TPR 4Add BLAST34
Repeati181 – 214TPR 5Add BLAST34
Repeati215 – 248TPR 6Add BLAST34
Repeati249 – 282TPR 7Add BLAST34
Repeati283 – 316TPR 8Add BLAST34
Repeati317 – 350TPR 9Add BLAST34
Repeati351 – 384TPR 10Add BLAST34
Repeati385 – 418TPR 11Add BLAST34
Repeati419 – 452TPR 12Add BLAST34
Repeati453 – 463TPR 13; truncatedAdd BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni981 – 1000Required for phosphatidylinositol 3,4,5-triphosphate bindingAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi478 – 493Nuclear localization signalSequence analysisAdd BLAST16

Domaini

The TPR repeat domain is required for substrate binding and oligomerization.

Sequence similaritiesi

Contains 13 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1124. Eukaryota.
KOG4626. Eukaryota.
COG3914. LUCA.
HOGENOMiHOG000003765.
HOVERGENiHBG000351.
InParanoidiP56558.
KOiK09667.
PhylomeDBiP56558.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR029489. OGT/SEC/SPY_C.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13844. Glyco_transf_41. 1 hit.
PF00515. TPR_1. 2 hits.
PF13414. TPR_11. 3 hits.
PF13181. TPR_8. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 12 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 5 hits.
PROSITEiPS50005. TPR. 12 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56558-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSVGNVAD STGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL
60 70 80 90 100
LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE
110 120 130 140 150
HYRHALRLKP DFIDGYINLA AALVAAGDME GAVQAYVSAL QYNPDLYCVR
160 170 180 190 200
SDLGNLLKAL GRLEEAKACY LKAIETQPNF AVAWSNLGCV FNAQGEIWLA
210 220 230 240 250
IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAAYLR ALSLSPNHAV
260 270 280 290 300
VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA NALKEKGSVA
310 320 330 340 350
EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF
360 370 380 390 400
AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD
410 420 430 440 450
VQGALQCYTR AIQINPAFAD AHSNLASIHK DSGNIPEAIA SYRTALKLKP
460 470 480 490 500
DFPDAYCNLA HCLQIVCDWT DYDERMKKLV SIVAEQLEKN RLPSVHPHHS
510 520 530 540 550
MLYPLSHGFR KAIAERHGNL CLDKINVLHK PPYEHPKDLK LSDGRLRVGY
560 570 580 590 600
VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN FRVKVMAEAN
610 620 630 640 650
HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA
660 670 680 690 700
MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN
710 720 730 740 750
MFPHLKKKAV IDFKSNGHIY DNRIVLNGID LKAFLDSLPD VKIVKMKCPD
760 770 780 790 800
GGDNADTTNT ALNMPVIPMN TIAEAVIEMI NRGQIQITIN GFSISNGLAT
810 820 830 840 850
TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL YKIDPSTLQM
860 870 880 890 900
GANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI IFSPVAPKEE
910 920 930 940 950
HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL
960 970 980 990 1000
TCLGCLELIA KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ RISSPLFNTK
1010 1020 1030
QYTMELERLY LQMWEHYAAG NKPDHMIKPV EVTESA
Length:1,036
Mass (Da):115,606
Last modified:December 15, 1998 - v1
Checksum:i3F057CABDD019BD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76557 mRNA. Translation: AAC53121.1.
PIRiT31673.
RefSeqiNP_058803.2. NM_017107.2.
UniGeneiRn.82705.

Genome annotation databases

GeneIDi26295.
KEGGirno:26295.
UCSCiRGD:62060. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76557 mRNA. Translation: AAC53121.1.
PIRiT31673.
RefSeqiNP_058803.2. NM_017107.2.
UniGeneiRn.82705.

3D structure databases

ProteinModelPortaliP56558.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247798. 4 interactors.
IntActiP56558. 4 interactors.
STRINGi10116.ENSRNOP00000004692.

Protein family/group databases

CAZyiGT41. Glycosyltransferase Family 41.

PTM databases

iPTMnetiP56558.
PhosphoSitePlusiP56558.

Proteomic databases

PaxDbiP56558.
PRIDEiP56558.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi26295.
KEGGirno:26295.
UCSCiRGD:62060. rat.

Organism-specific databases

CTDi8473.
RGDi62060. Ogt.

Phylogenomic databases

eggNOGiKOG1124. Eukaryota.
KOG4626. Eukaryota.
COG3914. LUCA.
HOGENOMiHOG000003765.
HOVERGENiHBG000351.
InParanoidiP56558.
KOiK09667.
PhylomeDBiP56558.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.255. 5301.

Miscellaneous databases

PROiP56558.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR029489. OGT/SEC/SPY_C.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13844. Glyco_transf_41. 1 hit.
PF00515. TPR_1. 2 hits.
PF13414. TPR_11. 3 hits.
PF13181. TPR_8. 2 hits.
[Graphical view]
SMARTiSM00028. TPR. 12 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 5 hits.
PROSITEiPS50005. TPR. 12 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOGT1_RAT
AccessioniPrimary (citable) accession number: P56558
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: November 2, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.