Search Results

Overview

Uniprot IDO15294
Protein NameUDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Gene NameOGT
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
16 ADSTEPTKRMLSFQG

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) (PubMed:12150998, PubMed:15361863, PubMed:19451179, PubMed:20018868, PubMed:21240259, PubMed:21285374, PubMed:23103939, PubMed:26237509, PubMed:26369908, PubMed:26678539, PubMed:27713473, PubMed:37541260, PubMed:37962578). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, AMPK, ATG4B, CAPRIN1, EZH2, FNIP1, GSDMD, KRT7, LMNA, LMNB1, LMNB2, RPTOR, HOXA1, PFKL, KMT2E/MLL5, MAPT/TAU, TET2, RBL2, RET, NOD2 and HCFC1 (PubMed:19451179, PubMed:20200153, PubMed:21285374, PubMed:22923583, PubMed:23353889, PubMed:24474760, PubMed:26237509, PubMed:26369908, PubMed:26678539, PubMed:27527864, PubMed:30699359, PubMed:34074792, PubMed:34667079, PubMed:37541260, PubMed:37962578). Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing (PubMed:21285374). 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 (By similarity). Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity (PubMed:22923583). 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). Stabilizes KMT2E/MLL5 by mediating its glycosylation, thereby preventing KMT2E/MLL5 ubiquitination (PubMed:26678539). Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver (By similarity). Stabilizes clock proteins BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation (By similarity). Promotes the CLOCK-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 (PubMed:21285374, PubMed:28302723, PubMed:28584052). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (PubMed:20200153). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Promotes autophagy by mediating O-glycosylation of ATG4B (PubMed:27527864). Acts as a regulator of mTORC1 signaling by mediating O-glycosylation of RPTOR and FNIP1: O-GlcNAcylation of RPTOR in response to glucose sufficiency promotes activation of the mTORC1 complex (PubMed:30699359, PubMed:37541260)

Protein Sequence

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

Gene Ontology

Classification GO ID Description
Cellular Component GO:0042995 cell projection
Cellular Component GO:0005829 cytosol
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0000123 histone acetyltransferase complex
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0017122 protein N-acetylglucosaminyltransferase complex
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0008375 acetylglucosaminyltransferase activity
Molecular Function GO:0031490 chromatin DNA binding
Molecular Function GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding
Molecular Function GO:0097363 protein O-acetylglucosaminyltransferase activity
Biological Process GO:0006915 apoptotic process
Biological Process GO:0071333 cellular response to glucose stimulus
Biological Process GO:0006325 chromatin organization
Biological Process GO:0032922 circadian regulation of gene expression
Biological Process GO:0030097 hemopoiesis
Biological Process GO:0000423 mitophagy
Biological Process GO:0030336 negative regulation of cell migration
Biological Process GO:0160076 negative regulation of non-canonical inflammasome complex assembly
Biological Process GO:0032435 negative regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Process GO:0031397 negative regulation of protein ubiquitination
Biological Process GO:1902455 negative regulation of stem cell population maintenance
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
Biological Process GO:0120162 positive regulation of cold-induced thermogenesis
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0045862 positive regulation of proteolysis
Biological Process GO:1902459 positive regulation of stem cell population maintenance
Biological Process GO:1904263 positive regulation of TORC1 signaling
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0000432 positive regulation of transcription from RNA polymerase II promoter by glucose
Biological Process GO:0045727 positive regulation of translation
Biological Process GO:0006493 protein O-linked glycosylation
Biological Process GO:0016485 protein processing
Biological Process GO:0006111 regulation of gluconeogenesis
Biological Process GO:0006110 regulation of glycolytic process
Biological Process GO:0046626 regulation of insulin receptor signaling pathway
Biological Process GO:0060544 regulation of necroptotic process
Biological Process GO:0098696 regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
Biological Process GO:0035020 regulation of Rac protein signal transduction
Biological Process GO:0051963 regulation of synapse assembly
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0032868 response to insulin
Biological Process GO:0007584 response to nutrient
Biological Process GO:0007165 signal transduction

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.