OGT1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: OGT1_RAT
• UniProt AC: P56558
• Protein Name: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
• Gene Name: Ogt
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1036
• Subcellular Localization: Cytoplasm. Nucleus. Cell membrane. 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 p
• Protein 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, EZH2, PFKL, KMT2E, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Probably by glycosylating KMT2E, stabilizes KMT2E by preventing its ubiquitination. 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. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity..
• Protein Sequence: MASSVGNVADSTGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVAEQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADTTNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMGANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKSRQEYEDIAVKLGTDLEYLKKIRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASSVGNVA ------CCCCCCCCC	23.09	-
3	Phosphorylation	-----MASSVGNVAD -----CCCCCCCCCC	37.10	-
3	O-linked_Glycosylation	-----MASSVGNVAD -----CCCCCCCCCC	37.10	-
4	Phosphorylation	----MASSVGNVADS ----CCCCCCCCCCC	40.89	-
4	O-linked_Glycosylation	----MASSVGNVADS ----CCCCCCCCCCC	40.89	-
158	Acetylation	SDLGNLLKALGRLEE HHHHHHHHHHCCHHH	44.74	22902405
375	Acetylation	QEALMHYKEAIRISP HHHHHHHHHHHHHCH	26.45	22902405
444	Phosphorylation	EAIASYRTALKLKPD HHHHHHHHHHHCCCC	28.27	-
540	Ubiquitination	YEHPKDLKLSDGRLR CCCCCCCCCCCCCEE	56.96	-
610	S-nitrosylation	IDLSQIPCNGKAADR EEHHHCCCCCCHHHH	12.85	22178444
610	S-nitrosocysteine	IDLSQIPCNGKAADR EEHHHCCCCCCHHHH	12.85	-
706	Ubiquitination	ANMFPHLKKKAVIDF CCCCHHCCCCEEEEE	49.55	-
707	Ubiquitination	NMFPHLKKKAVIDFK CCCHHCCCCEEEEEC	52.93	-
708	Acetylation	MFPHLKKKAVIDFKS CCHHCCCCEEEEECC	46.42	22902405
732	Acetylation	VLNGIDLKAFLDSLP EECCCCHHHHHHCCC	33.09	22902405
732	Ubiquitination	VLNGIDLKAFLDSLP EECCCCHHHHHHCCC	33.09	-
834	Phosphorylation	LPEDAIVYCNFNQLY CCCCCEEEECCCCEE	3.89	-
966	Phosphorylation	IAKSRQEYEDIAVKL HHHCHHHHHHHHHHH	15.57	-
979	Phosphorylation	KLGTDLEYLKKIRGK HHCCCHHHHHHHCCH	30.99	18288188
981	Acetylation	GTDLEYLKKIRGKVW CCCHHHHHHHCCHHH	45.30	22902405
1000	Ubiquitination	SSPLFNTKQYTMELE CCCCCCCHHHHHHHH	42.27	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
3	S	Phosphorylation	Kinase	GSK3-BETA	P18266	Uniprot
4	S	Phosphorylation	Kinase	GSK3-BETA	P18266	Uniprot
444	T	Phosphorylation	Kinase	AMPKA1	Q13131	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
3	S	Phosphorylation	Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity.	-
4	S	Phosphorylation	Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of OGT1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRAK2_RAT	Trak2	physical	12435728
ATX10_RAT	Atxn10	physical	16714295

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.