UniProt Accession

 OGT1_HUMAN; O15294; Q7Z3K0; Q8WWM8; Q96CC1; Q9UG57 

Genbank Protein ID

 U77413; AJ315767; AJ315767; AJ315767; AL050366; AL833085; BX537844; BC014434; BC038180 

Genbank Nucleotide ID

 AAB63466.1; CAC86127.1; CAC86128.1; CAC86129.1; CAB62528.1; CAD89970.1; CAD97853.1; AAH14434.1; AAH38180.1 

Protein Name

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

Protein Synonyms/Alias

 O-GlcNAc transferase subunit p110; O-linked N-acetylglucosamine transferase 110 kDa subunit; OGT 

Gene Name

 OGT 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
16	ADSTEPTKRMLSFQG	ubiquitination	[1, 2, 3, 4, 5, 6]
83	HFSTLAIKQNPLLAE	ubiquitination	[1, 2, 3, 4, 5, 7, 8]
100	SNLGNVYKERGQLQE	ubiquitination	[1, 2, 3, 4, 5, 7, 9]
168	SDLGNLLKALGRLEE	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9, 10]
236	INLGNVLKEARIFDR	ubiquitination	[7, 9]
306	LANALKEKGSVAEAE	ubiquitination	[4]
337	LNNLANIKREQGNIE	ubiquitination	[4]
352	EAVRLYRKALEVFPE	ubiquitination	[4]
385	QEALMHYKEAIRISP	ubiquitination	[2, 4]
440	SNLASIHKDSGNIPE	ubiquitination	[4]
488	DYDERMKKLVSIVAD	ubiquitination	[4, 6]
499	IVADQLEKNRLPSVH	ubiquitination	[6]
550	YEHPKDLKLSDGRLR	ubiquitination	[4, 6]
604	DGTNFRVKVMAEANH	ubiquitination	[4]
623	SQIPCNGKAADRIHQ	ubiquitination	[4, 6]
644	VNMNGYTKGARNELF	ubiquitination	[4]
716	ANMFPHLKKKAVIDF	ubiquitination	[1, 5, 7, 11, 12]
717	NMFPHLKKKAVIDFK	ubiquitination	[4]
718	MFPHLKKKAVIDFKS	ubiquitination	[4]
724	KKAVIDFKSNGHIYD	ubiquitination	[4]
742	VLNGIDLKAFLDSLP	ubiquitination	[4, 7, 9, 12]
752	LDSLPDVKIVKMKCP	ubiquitination	[4, 7]
866	QMWANILKRVPNSVL	ubiquitination	[4, 7]
908	IFSPVAPKEEHVRRG	ubiquitination	[4]
971	GCLELIAKNRQEYED	ubiquitination	[4]
991	GTDLEYLKKVRGKVW	acetylation	[6, 13]
991	GTDLEYLKKVRGKVW	ubiquitination	[2, 4]
992	TDLEYLKKVRGKVWK	ubiquitination	[4]
1010	SSPLFNTKQYTMELE	ubiquitination	[1, 2, 3, 4, 5, 6, 12]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [11] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [12] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [13] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 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, 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. 

Sequence Annotation

 REPEAT 21 54 TPR 1.
 REPEAT 89 122 TPR 2.
 REPEAT 123 156 TPR 3.
 REPEAT 157 190 TPR 4.
 REPEAT 191 224 TPR 5.
 REPEAT 225 258 TPR 6.
 REPEAT 259 292 TPR 7.
 REPEAT 293 326 TPR 8.
 REPEAT 327 360 TPR 9.
 REPEAT 361 394 TPR 10.
 REPEAT 395 428 TPR 11.
 REPEAT 429 462 TPR 12.
 REPEAT 463 473 TPR 13; truncated.
 NP_BIND 905 908 UDP.
 NP_BIND 911 914 UDP.
 NP_BIND 929 931 UDP.
 REGION 991 1010 Required for phosphatidylinositol 3,4,5-
 MOTIF 487 503 Nuclear localization signal (Potential).
 ACT_SITE 508 508 Proton acceptor (Probable).
 BINDING 849 849 UDP.
 BINDING 852 852 UDP.
 BINDING 935 935 UDP.
 MOD_RES 2 2 N-acetylalanine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell membrane; Chromatin regulator; Complete proteome; Cytoplasm; Direct protein sequencing; Glycosyltransferase; Lipid-binding; Membrane; Mitochondrion; Nucleus; Polymorphism; Reference proteome; Repeat; TPR repeat; Transferase; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1046 AA 

Protein Sequence

Gene Ontology

 GO:0005813; C:centrosome; IDA:HPA.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0008047; F:enzyme activator activity; IDA:BHF-UCL.
 GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
 GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
 GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
 GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
 GO:0006917; P:induction of apoptosis; IDA:UniProtKB.
 GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
 GO:0030854; P:positive regulation of granulocyte differentiation; IMP:BHF-UCL.
 GO:0051571; P:positive regulation of histone H3-K4 methylation; IDA:BHF-UCL.
 GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
 GO:0006110; P:regulation of glycolysis; IDA:UniProtKB.
 GO:0046626; P:regulation of insulin receptor signaling pathway; IDA:UniProtKB.
 GO:0035020; P:regulation of Rac protein signal transduction; IDA:UniProtKB.
 GO:0032868; P:response to insulin stimulus; IDA:UniProtKB.
 GO:0007584; P:response to nutrient; TAS:ProtInc. 

Interpro

 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 

Pfam

 PF00515; TPR_1 

SMART

 SM00028; TPR 

PROSITE

 PS50005; TPR
 PS50293; TPR_REGION 

PRINTS