CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000425
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
73HFSTLAIKQNPLLAEubiquitination[1]
90SNLGNVYKERGQLQEubiquitination[1]
158SDLGNLLKALGRLEEubiquitination[1]
706ANMFPHLKKKAVIDFubiquitination[1]
732VLNGIDLKAFLDSLPubiquitination[1]
1000SSPLFNTKQYTMELEubiquitination[1]
Reference
 [1] 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] 
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
MASSVGNVAD STGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL LSSIHFQCRR 60
LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP DFIDGYINLA 120
AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF 180
AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAAYLR 240
ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA NALKEKGSVA 300
EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF AAAHSNLASV 360
LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR AIQINPAFAD 420
AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV 480
SIVADQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK PPYEHPKDLK 540
LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN FRVKVMAEAN 600
HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA MWLGYPGTSG 660
ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV IDFKSNGHIY 720
DNRIVLNGID LKAFLDSLPD VKIVKMKCPD GGDNADSSNT ALNMPVIPMN TIAEAVIEMI 780
NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL 840
YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI IFSPVAPKEE 900
HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL TCLGCLELIA 960
KNRQEYEDIA VKLGTDLEYL KKVRGKVWKQ RISSPLFNTK QYTMELERLY LQMWEHYAAG 1020
NKPDHMIKPV EVTESA 1036 
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