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O15294

- OGT1_HUMAN

UniProt

O15294 - OGT1_HUMAN

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Protein

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

Gene

OGT

Organism
Homo sapiens (Human)
Status
Reviewed - 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 (PubMed:22923583). 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) (PubMed:22121020, PubMed:23353889). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (PubMed:24474760). 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 (PubMed:12150998, PubMed:18288188, PubMed:19377461, PubMed:19451179, PubMed:20018868, PubMed:20200153, PubMed:21285374, PubMed:15361863).13 Publications
Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.

Catalytic activityi

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

Enzyme regulationi

Subject to product inhibition by UDP.1 Publication

Kineticsi

  1. KM=1.8 µM for UDP-N-acetyl-D-glucosamine1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei508 – 5081Proton acceptor1 Publication
Binding sitei849 – 8491UDP
Binding sitei852 – 8521UDP
Binding sitei935 – 9351UDP

Regions

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

GO - Molecular functioni

  1. acetylglucosaminyltransferase activity Source: ProtInc
  2. enzyme activator activity Source: BHF-UCL
  3. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  4. protein N-acetylglucosaminyltransferase activity Source: UniProtKB
  5. protein O-GlcNAc transferase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cellular response to retinoic acid Source: BHF-UCL
  3. chromatin organization Source: Reactome
  4. circadian regulation of gene expression Source: UniProtKB
  5. histone H3-K4 trimethylation Source: UniProtKB
  6. histone H4-K16 acetylation Source: UniProtKB
  7. histone H4-K5 acetylation Source: UniProtKB
  8. histone H4-K8 acetylation Source: UniProtKB
  9. negative regulation of protein ubiquitination Source: UniProtKB
  10. phosphatidylinositol-mediated signaling Source: UniProtKB
  11. positive regulation of catalytic activity Source: GOC
  12. positive regulation of granulocyte differentiation Source: BHF-UCL
  13. positive regulation of histone H3-K27 methylation Source: UniProtKB
  14. positive regulation of histone H3-K4 methylation Source: BHF-UCL
  15. positive regulation of proteolysis Source: UniProtKB
  16. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  17. protein O-linked glycosylation Source: UniProtKB
  18. regulation of gluconeogenesis involved in cellular glucose homeostasis Source: UniProtKB
  19. regulation of glycolytic process Source: UniProtKB
  20. regulation of insulin receptor signaling pathway Source: UniProtKB
  21. regulation of Rac protein signal transduction Source: UniProtKB
  22. response to insulin Source: UniProtKB
  23. response to nutrient Source: ProtInc
  24. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Glycosyltransferase, Transferase

Keywords - Biological processi

Apoptosis, Biological rhythms

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000147162-MONOMER.
ReactomeiREACT_172610. HATs acetylate histones.
SABIO-RKO15294.
SignaLinkiO15294.
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:2.4.1.255)
Alternative name(s):
O-GlcNAc transferase subunit p110
O-linked N-acetylglucosamine transferase 110 kDa subunit
Short name:
OGT
Gene namesi
Name:OGT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8127. OGT.

Subcellular locationi

Isoform 2 : Mitochondrion. Membrane
Note: Associates with the mitochondrial inner membrane.
Isoform 3 : 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.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. histone acetyltransferase complex Source: UniProtKB
  4. microtubule organizing center Source: HPA
  5. mitochondrion Source: UniProtKB-KW
  6. MLL5-L complex Source: UniProtKB
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Regulation of OGT activity and altered O-GlcNAcylations are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of AKT1 affects insulin signaling and, possibly diabetes. Reduced O-GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are observed in Alzheimer disease (AD) brain cerebrum.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081W → E: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with D-211. 1 Publication
Mutagenesisi211 – 2111I → D: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with E-208. 1 Publication
Mutagenesisi508 – 5081H → A: Loss of enzyme activity. 1 Publication
Mutagenesisi568 – 5681H → A: Reduces enzyme activity by about 95%. 1 Publication
Mutagenesisi911 – 9111H → A: Reduces enzyme activity by over 90%. 1 Publication
Mutagenesisi991 – 9922KK → AA: Abolishes phosphatidylinisitol binding, no translocation to the cell membrane, and no effect on phosphorylation of AKT1 nor IRS1. 1 Publication
Mutagenesisi994 – 9941R → A: No effect on phosphatidylinisitol binding. 1 Publication
Mutagenesisi996 – 9961K → A: Reduced phosphatidylinisitol binding. 1 Publication
Mutagenesisi999 – 9991K → A: Reduced phosphatidylinisitol binding. 1 Publication
Mutagenesisi1001 – 10011R → A: No effect on phosphatidylinisitol binding. 1 Publication
Mutagenesisi1010 – 10101K → A: No effect on phosphatidylinisitol binding. 1 Publication

Organism-specific databases

PharmGKBiPA31914.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 10461045UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunitPRO_0000191772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei3 – 31Phosphoserine; by GSK3-betaBy similarity
Glycosylationi3 – 31O-linked (GlcNAc)By similarity
Modified residuei4 – 41Phosphoserine; by GSK3-betaBy similarity
Glycosylationi4 – 41O-linked (GlcNAc)By similarity

Post-translational modificationi

Ubiquitinated, leading to its proteasomal degradation.1 Publication
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

MaxQBiO15294.
PaxDbiO15294.
PRIDEiO15294.

PTM databases

PhosphoSiteiO15294.

Expressioni

Tissue specificityi

Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver.1 Publication

Inductioni

Induction of the nucleocytoplasmic OGT (ncOGT) isoform in the liver on glucose deprivation is mediated by the decreased hexosamine biosynthesis pathway (HBP) flux.1 Publication

Gene expression databases

BgeeiO15294.
CleanExiHS_OGT.
ExpressionAtlasiO15294. baseline and differential.
GenevestigatoriO15294.

Organism-specific databases

HPAiCAB034099.
HPA030751.
HPA030752.
HPA030753.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
HCFC1P516109EBI-539828,EBI-396176
Hoxa1P090223EBI-539828,EBI-3957603From a different organism.
NFATC1O956442EBI-539828,EBI-6907210
RELAQ042062EBI-539828,EBI-73886
TET2Q6N0217EBI-539828,EBI-310727
TET3O431514EBI-539828,EBI-2831148
Tet3Q8BG872EBI-539828,EBI-9031997From a different organism.

Protein-protein interaction databases

BioGridi114049. 63 interactions.
DIPiDIP-33491N.
IntActiO15294. 34 interactions.
MINTiMINT-2998811.
STRINGi9606.ENSP00000362824.

Structurei

Secondary structure

1
1046
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 348Combined sources
Helixi37 – 5014Combined sources
Helixi55 – 6713Combined sources
Helixi71 – 8414Combined sources
Helixi89 – 10214Combined sources
Helixi105 – 11814Combined sources
Helixi123 – 13614Combined sources
Helixi141 – 15212Combined sources
Helixi158 – 16811Combined sources
Helixi173 – 18614Combined sources
Helixi191 – 20212Combined sources
Turni203 – 2053Combined sources
Helixi207 – 22014Combined sources
Helixi225 – 23612Combined sources
Turni237 – 2393Combined sources
Helixi243 – 25412Combined sources
Helixi259 – 27113Combined sources
Helixi275 – 28713Combined sources
Helixi293 – 30614Combined sources
Helixi309 – 32214Combined sources
Helixi325 – 33915Combined sources
Helixi343 – 35614Combined sources
Helixi361 – 37313Combined sources
Helixi377 – 39014Combined sources
Helixi395 – 40713Combined sources
Helixi411 – 42414Combined sources
Helixi429 – 44113Combined sources
Helixi445 – 45814Combined sources
Helixi463 – 47513Combined sources
Helixi482 – 49817Combined sources
Helixi509 – 5124Combined sources
Helixi517 – 53620Combined sources
Turni537 – 5393Combined sources
Beta strandi547 – 5493Combined sources
Turni550 – 5545Combined sources
Beta strandi556 – 5638Combined sources
Beta strandi565 – 5684Combined sources
Helixi569 – 5746Combined sources
Helixi577 – 5804Combined sources
Turni583 – 5853Combined sources
Beta strandi586 – 5949Combined sources
Helixi600 – 6089Combined sources
Beta strandi609 – 6146Combined sources
Helixi615 – 6173Combined sources
Helixi621 – 63010Combined sources
Beta strandi634 – 6396Combined sources
Beta strandi641 – 6433Combined sources
Helixi649 – 6524Combined sources
Beta strandi656 – 6616Combined sources
Beta strandi676 – 6794Combined sources
Turni681 – 6833Combined sources
Helixi686 – 6916Combined sources
Beta strandi693 – 6986Combined sources
Helixi708 – 7114Combined sources
Helixi713 – 7153Combined sources
Beta strandi719 – 7213Combined sources
Beta strandi731 – 7377Combined sources
Helixi741 – 7466Combined sources
Beta strandi748 – 7503Combined sources
Beta strandi752 – 7543Combined sources
Beta strandi774 – 7774Combined sources
Helixi781 – 79212Combined sources
Beta strandi796 – 7994Combined sources
Beta strandi802 – 8065Combined sources
Helixi807 – 8093Combined sources
Helixi810 – 8134Combined sources
Helixi815 – 8184Combined sources
Beta strandi820 – 8223Combined sources
Beta strandi826 – 8316Combined sources
Helixi832 – 8354Combined sources
Beta strandi841 – 8455Combined sources
Helixi850 – 8523Combined sources
Helixi855 – 86713Combined sources
Beta strandi869 – 8779Combined sources
Helixi880 – 8823Combined sources
Helixi883 – 89210Combined sources
Helixi897 – 8993Combined sources
Beta strandi900 – 9045Combined sources
Helixi908 – 9147Combined sources
Helixi915 – 9173Combined sources
Beta strandi919 – 9224Combined sources
Beta strandi925 – 9273Combined sources
Helixi931 – 9388Combined sources
Beta strandi943 – 9453Combined sources
Helixi951 – 9533Combined sources
Helixi955 – 9639Combined sources
Helixi966 – 9683Combined sources
Helixi973 – 98513Combined sources
Helixi987 – 100317Combined sources
Helixi1005 – 10073Combined sources
Helixi1009 – 102820Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W3BX-ray2.85A/B26-410[»]
3PE3X-ray2.78A/B/C/D323-1041[»]
3PE4X-ray1.95A/C323-1041[»]
3TAXX-ray1.88A/C323-1041[»]
4AY5X-ray3.15A/B/C/D323-1041[»]
4AY6X-ray3.30A/B/C/D323-1041[»]
4CDRX-ray3.15A/B/C/D323-1041[»]
4GYWX-ray1.70A/C323-1041[»]
4GYYX-ray1.85A/C323-1041[»]
4GZ3X-ray1.90A/C323-1041[»]
4GZ5X-ray3.08A/B/C/D323-1041[»]
4GZ6X-ray2.98A/B/C/D323-1041[»]
4N39X-ray1.76A323-1041[»]
4N3AX-ray1.88A323-1041[»]
4N3BX-ray2.17A323-1041[»]
4N3CX-ray2.55A323-1041[»]
ProteinModelPortaliO15294.
SMRiO15294. Positions 23-1038.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15294.

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.1 Publication

Sequence similaritiesi

Contains 13 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG3914.
GeneTreeiENSGT00550000074327.
HOGENOMiHOG000003765.
HOVERGENiHBG000351.
InParanoidiO15294.
KOiK09667.
OMAiLAYMPNT.
OrthoDBiEOG71K624.
PhylomeDBiO15294.
TreeFamiTF105785.

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. 9 hits.
[Graphical view]
SMARTiSM00028. TPR. 12 hits.
[Graphical view]
PROSITEiPS50005. TPR. 12 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 3 (identifier: O15294-1) [UniParc]FASTAAdd to Basket

Also known as: Nucleocytoplasmic isoform, ncOGT

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 KNRQEYEDIA VKLGTDLEYL KKVRGKVWKQ
1010 1020 1030 1040
RISSPLFNTK QYTMELERLY LQMWEHYAAG NKPDHMIKPV EVTESA
Length:1,046
Mass (Da):116,925
Last modified:June 21, 2005 - v3
Checksum:i852ED68BDDE63363
GO
Isoform 2 (identifier: O15294-2) [UniParc]FASTAAdd to Basket

Also known as: Mitochondrial isoform, mOGT

The sequence of this isoform differs from the canonical sequence as follows:
     1-176: MASSVGNVAD...LKALGRLEEA → MLQGHFWLVR...PSHLLSLTPP

Show »
Length:920
Mass (Da):103,012
Checksum:i766BF416ABD547C4
GO
Isoform 1 (identifier: O15294-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     13-22: Missing.

Show »
Length:1,036
Mass (Da):115,706
Checksum:iC3BD67340925A2C2
GO
Isoform 4 (identifier: O15294-4) [UniParc]FASTAAdd to Basket

Also known as: Short isoform, sOGT

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: Missing.

Note: No experimental confirmation available.

Show »
Length:665
Mass (Da):74,536
Checksum:i181B846A6B09E63A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti308 – 3081S → Q in CAB62528. (PubMed:17974005)Curated
Sequence conflicti663 – 6631L → P in CAD97853. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti538 – 5381L → P Found in a renal cell carcinoma sample; somatic mutation.
VAR_064736

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 381381Missing in isoform 4. 1 PublicationVSP_040764Add
BLAST
Alternative sequencei1 – 176176MASSV…RLEEA → MLQGHFWLVREGIMISPSSP PPPNLFFFPLQIFPFPFTSF PSHLLSLTPP in isoform 2. 1 PublicationVSP_006553Add
BLAST
Alternative sequencei13 – 2210Missing in isoform 1. 2 PublicationsVSP_014164

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U77413 mRNA. Translation: AAB63466.1.
AJ315767 Genomic DNA. Translation: CAC86127.1.
AJ315767 Genomic DNA. Translation: CAC86128.1.
AJ315767 Genomic DNA. Translation: CAC86129.1.
AL050366 mRNA. Translation: CAB62528.1.
AL833085 mRNA. Translation: CAD89970.1.
BX537844 mRNA. Translation: CAD97853.1.
BC014434 mRNA. Translation: AAH14434.1.
BC038180 mRNA. Translation: AAH38180.1.
CCDSiCCDS14414.1. [O15294-1]
CCDS35502.1. [O15294-3]
RefSeqiNP_858058.1. NM_181672.2. [O15294-1]
NP_858059.1. NM_181673.2. [O15294-3]
XP_005262365.1. XM_005262308.1. [O15294-4]
UniGeneiHs.405410.

Genome annotation databases

EnsembliENST00000373701; ENSP00000362805; ENSG00000147162. [O15294-3]
ENST00000373719; ENSP00000362824; ENSG00000147162. [O15294-1]
GeneIDi8473.
KEGGihsa:8473.
UCSCiuc004eaa.2. human. [O15294-1]
uc004eab.2. human. [O15294-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U77413 mRNA. Translation: AAB63466.1 .
AJ315767 Genomic DNA. Translation: CAC86127.1 .
AJ315767 Genomic DNA. Translation: CAC86128.1 .
AJ315767 Genomic DNA. Translation: CAC86129.1 .
AL050366 mRNA. Translation: CAB62528.1 .
AL833085 mRNA. Translation: CAD89970.1 .
BX537844 mRNA. Translation: CAD97853.1 .
BC014434 mRNA. Translation: AAH14434.1 .
BC038180 mRNA. Translation: AAH38180.1 .
CCDSi CCDS14414.1. [O15294-1 ]
CCDS35502.1. [O15294-3 ]
RefSeqi NP_858058.1. NM_181672.2. [O15294-1 ]
NP_858059.1. NM_181673.2. [O15294-3 ]
XP_005262365.1. XM_005262308.1. [O15294-4 ]
UniGenei Hs.405410.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W3B X-ray 2.85 A/B 26-410 [» ]
3PE3 X-ray 2.78 A/B/C/D 323-1041 [» ]
3PE4 X-ray 1.95 A/C 323-1041 [» ]
3TAX X-ray 1.88 A/C 323-1041 [» ]
4AY5 X-ray 3.15 A/B/C/D 323-1041 [» ]
4AY6 X-ray 3.30 A/B/C/D 323-1041 [» ]
4CDR X-ray 3.15 A/B/C/D 323-1041 [» ]
4GYW X-ray 1.70 A/C 323-1041 [» ]
4GYY X-ray 1.85 A/C 323-1041 [» ]
4GZ3 X-ray 1.90 A/C 323-1041 [» ]
4GZ5 X-ray 3.08 A/B/C/D 323-1041 [» ]
4GZ6 X-ray 2.98 A/B/C/D 323-1041 [» ]
4N39 X-ray 1.76 A 323-1041 [» ]
4N3A X-ray 1.88 A 323-1041 [» ]
4N3B X-ray 2.17 A 323-1041 [» ]
4N3C X-ray 2.55 A 323-1041 [» ]
ProteinModelPortali O15294.
SMRi O15294. Positions 23-1038.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114049. 63 interactions.
DIPi DIP-33491N.
IntActi O15294. 34 interactions.
MINTi MINT-2998811.
STRINGi 9606.ENSP00000362824.

Chemistry

BindingDBi O15294.
ChEMBLi CHEMBL5955.

Protein family/group databases

CAZyi GT41. Glycosyltransferase Family 41.

PTM databases

PhosphoSitei O15294.

Proteomic databases

MaxQBi O15294.
PaxDbi O15294.
PRIDEi O15294.

Protocols and materials databases

DNASUi 8473.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373701 ; ENSP00000362805 ; ENSG00000147162 . [O15294-3 ]
ENST00000373719 ; ENSP00000362824 ; ENSG00000147162 . [O15294-1 ]
GeneIDi 8473.
KEGGi hsa:8473.
UCSCi uc004eaa.2. human. [O15294-1 ]
uc004eab.2. human. [O15294-3 ]

Organism-specific databases

CTDi 8473.
GeneCardsi GC0XP070752.
HGNCi HGNC:8127. OGT.
HPAi CAB034099.
HPA030751.
HPA030752.
HPA030753.
MIMi 300255. gene.
neXtProti NX_O15294.
PharmGKBi PA31914.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3914.
GeneTreei ENSGT00550000074327.
HOGENOMi HOG000003765.
HOVERGENi HBG000351.
InParanoidi O15294.
KOi K09667.
OMAi LAYMPNT.
OrthoDBi EOG71K624.
PhylomeDBi O15294.
TreeFami TF105785.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci MetaCyc:ENSG00000147162-MONOMER.
Reactomei REACT_172610. HATs acetylate histones.
SABIO-RK O15294.
SignaLinki O15294.

Miscellaneous databases

EvolutionaryTracei O15294.
GeneWikii OGT_(gene).
GenomeRNAii 8473.
NextBioi 31706.
PROi O15294.
SOURCEi Search...

Gene expression databases

Bgeei O15294.
CleanExi HS_OGT.
ExpressionAtlasi O15294. baseline and differential.
Genevestigatori O15294.

Family and domain databases

Gene3Di 1.25.40.10. 5 hits.
InterProi IPR029489. OGT/SEC/SPY_C.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF13844. Glyco_transf_41. 1 hit.
PF00515. TPR_1. 9 hits.
[Graphical view ]
SMARTi SM00028. TPR. 12 hits.
[Graphical view ]
PROSITEi PS50005. TPR. 12 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats."
    Lubas W.A., Frank D.W., Krause M., Hanover J.A.
    J. Biol. Chem. 272:9316-9324(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 227-236 AND 955-971, TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1."
    Nolte D., Muller U.
    Mamm. Genome 13:62-64(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Endometrium, Fetal brain and Spinal cord.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Colon and Pancreas.
  5. Bienvenut W.V., Dhillon A.S., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    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. "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression."
    Yang X., Zhang F., Kudlow J.E.
    Cell 110:69-80(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIN3A, FUNCTION.
  7. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
    Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
    Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCFC1.
  8. "Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance."
    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.
    Nature 451:964-969(2008) [PubMed] [Europe PMC] [Abstract]
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease."
    Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K., Gong C.X.
    Brain 132:1820-1832(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH ALZHEIMER DISEASE.
  12. "Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux."
    Taylor R.P., Geisler T.S., Chambers J.H., McClain D.A.
    J. Biol. Chem. 284:3425-3432(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  13. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
    Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
    Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE MLL5-L COMPLEX.
  14. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
    Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
    J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
  15. "Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes."
    Whelan S.A., Dias W.B., Thiruneelakantapillai L., Lane M.D., Hart G.W.
    J. Biol. Chem. 285:5204-5211(2010) [PubMed] [Europe PMC] [Abstract]
    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., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L., Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B., Kristie T.M., Girard J.P.
    J. Biol. Chem. 285:13364-13371(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX, INTERACTION WITH HCFC1; THAP1 AND THAP3, FUNCTION.
  17. "Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis."
    Shin S.H., Love D.C., Hanover J.A.
    Amino Acids 40:885-893(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2).
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway."
    Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G., Vogel J.L., Kristie T.M., Affar E.B.
    Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH HCFC1.
  20. Cited for: FUNCTION, INTERACTION WITH H2B.
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Phosphofructokinase 1 glycosylation regulates cell growth and metabolism."
    Yi W., Clark P.M., Mason D.E., Keenan M.C., Hill C., Goddard W.A. III, Peters E.C., Driggers E.M., Hsieh-Wilson L.C.
    Science 337:975-980(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. Cited for: FUNCTION, INTERACTION WITH HCFC1; TET2 AND TET3.
  24. "TET2 promotes histone O-GlcNAcylation during gene transcription."
    Chen Q., Chen Y., Bian C., Fujiki R., Yu X.
    Nature 493:561-564(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TET2 AND TET3.
  25. Cited for: FUNCTION.
  26. "The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha."
    Jinek M., Rehwinkel J., Lazarus B.D., Izaurralde E., Hanover J.A., Conti E.
    Nat. Struct. Mol. Biol. 11:1001-1007(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 26-400, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, MUTAGENESIS OF TRP-208 AND ILE-211.
  27. "Structure of human O-GlcNAc transferase and its complex with a peptide substrate."
    Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S.
    Nature 469:564-567(2011) [PubMed] [Europe PMC] [Abstract]
    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.

Entry informationi

Entry nameiOGT1_HUMAN
AccessioniPrimary (citable) accession number: O15294
Secondary accession number(s): Q7Z3K0
, Q8WWM8, Q96CC1, Q9UG57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 21, 2005
Last modified: October 29, 2014
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3