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Protein

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

Gene

OGT

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei508 – 5081Proton acceptorBy similarity
Binding sitei849 – 8491UDPBy similarity
Binding sitei852 – 8521UDPBy similarity
Binding sitei935 – 9351UDPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi905 – 9084UDPBy similarity
Nucleotide bindingi911 – 9144UDPBy similarity
Nucleotide bindingi929 – 9313UDPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Glycosyltransferase, Transferase

Keywords - Biological processi

Biological rhythms

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cell membrane By similarity

  • 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10461045UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunitPRO_0000289993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei3 – 31Phosphoserine; by GSK3-beta; alternateBy similarity
Glycosylationi3 – 31O-linked (GlcNAc); alternateBy similarity
Modified residuei4 – 41Phosphoserine; by GSK3-beta; alternateBy similarity
Glycosylationi4 – 41O-linked (GlcNAc); alternateBy similarity
Modified residuei20 – 201PhosphoserineBy similarity

Post-translational modificationi

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

PaxDbiQ27HV0.
PeptideAtlasiQ27HV0.

Interactioni

Subunit structurei

Heterotrimer; consists of one 78 kDa subunit and two 110 kDa subunits dimerized via TPR repeats 6 and 7 (By similarity). 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 repeats 6 and 7) with ATXN10. Interacts (via TPR 5-6) with TET1, TET2 and TET3 (By similarity). Interacts with ARNTL/BMAL1 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000030900.

Structurei

3D structure databases

ProteinModelPortaliQ27HV0.
SMRiQ27HV0. Positions 23-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati21 – 5434TPR 1Add
BLAST
Repeati89 – 12234TPR 2Add
BLAST
Repeati123 – 15634TPR 3Add
BLAST
Repeati157 – 19034TPR 4Add
BLAST
Repeati191 – 22434TPR 5Add
BLAST
Repeati225 – 25834TPR 6Add
BLAST
Repeati259 – 29234TPR 7Add
BLAST
Repeati293 – 32634TPR 8Add
BLAST
Repeati327 – 36034TPR 9Add
BLAST
Repeati361 – 39434TPR 10Add
BLAST
Repeati395 – 42834TPR 11Add
BLAST
Repeati429 – 46234TPR 12Add
BLAST
Repeati463 – 47311TPR 13; truncatedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni991 – 101020Required for phosphatidylinositol 3,4,5-triphosphate bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi487 – 50317Nuclear localization signalSequence analysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 13 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1124. Eukaryota.
KOG4626. Eukaryota.
COG3914. LUCA.
HOGENOMiHOG000003765.
HOVERGENiHBG000351.
InParanoidiQ27HV0.
KOiK09667.

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.

Q27HV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ
60 70 80 90 100
EPDNTGVLLL LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK
110 120 130 140 150
ERGQLQEAIE HYRHALRLKP DFIDGYINLA AALVAAGDME GAVQAYVSAL
160 170 180 190 200
QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF AVAWSNLGCV
210 220 230 240 250
FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAAYLR
260 270 280 290 300
ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA
310 320 330 340 350
NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY
360 370 380 390 400
RKALEVFPEF AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN
410 420 430 440 450
MGNTLKEMQD VQGALQCYTR AIQINPAFAD AHSNLASIHK DSGNIPEAIA
460 470 480 490 500
SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV SIVADQLEKN
510 520 530 540 550
RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK PPYEHPKDLK
560 570 580 590 600
LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN
610 620 630 640 650
FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL
660 670 680 690 700
FALRPAPIQA MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP
710 720 730 740 750
HTFFIGDHAN MFPHLKKKAV IDFKSNGHIY DNRIVLNGID LKAFLDSLPD
760 770 780 790 800
VKIVKMKCPD GGDNADSSNT ALNMPVIPMN TIAEAVIEMI NRGQIQITIN
810 820 830 840 850
GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL
860 870 880 890 900
YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI
910 920 930 940 950
IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET
960 970 980 990 1000
LASRVAASQL TCLGCLELIA KNRQEFEDIA VKLGTDLEYL KKIRGKVWKQ
1010 1020 1030 1040
RISSPLFNTK QYTMELERLY LQMWEHYAAG NKPDHMIKPV EVTESA
Length:1,046
Mass (Da):116,923
Last modified:April 4, 2006 - v1
Checksum:iA9296D28DDF12A8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ400859 mRNA. Translation: ABD61726.1.
RefSeqiNP_001034837.1. NM_001039748.2.
UniGeneiSsc.27417.

Genome annotation databases

GeneIDi664652.
KEGGissc:664652.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ400859 mRNA. Translation: ABD61726.1.
RefSeqiNP_001034837.1. NM_001039748.2.
UniGeneiSsc.27417.

3D structure databases

ProteinModelPortaliQ27HV0.
SMRiQ27HV0. Positions 23-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000030900.

Protein family/group databases

CAZyiGT41. Glycosyltransferase Family 41.

Proteomic databases

PaxDbiQ27HV0.
PeptideAtlasiQ27HV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi664652.
KEGGissc:664652.

Organism-specific databases

CTDi8473.

Phylogenomic databases

eggNOGiKOG1124. Eukaryota.
KOG4626. Eukaryota.
COG3914. LUCA.
HOGENOMiHOG000003765.
HOVERGENiHBG000351.
InParanoidiQ27HV0.
KOiK09667.

Enzyme and pathway databases

UniPathwayiUPA00378.

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_PIG
AccessioniPrimary (citable) accession number: Q27HV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: April 4, 2006
Last modified: July 6, 2016
This is version 75 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, 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.