OGT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: OGT1_MOUSE
• UniProt AC: Q8CGY8
• Protein Name: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
• Gene Name: Ogt
• Organism: Mus musculus (Mouse).
• Sequence Length: 1046
• 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 th
• 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 (By similarity).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 (By similarity). 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: 23337503]
• Protein Sequence: MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVAEQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNPDSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKSRQEYEDIAVKLGTDLEYLKKIRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA

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	23395175
3	O-linked_Glycosylation	-----MASSVGNVAD -----CCCCCCCCCC	37.10	28528544
4	O-linked_Glycosylation	----MASSVGNVADS ----CCCCCCCCCCC	40.89	28528544
4	Phosphorylation	----MASSVGNVADS ----CCCCCCCCCCC	40.89	23395175
20	Phosphorylation	EPTKRMLSFQGLAEL CCCHHHHHHHHHHHH	13.23	29899451
90	Ubiquitination	KQNPLLAEAYSNLGN HCCHHHHHHHHCHHH	48.38	27667366
100	Ubiquitination	SNLGNVYKERGQLQE HCHHHHHHHHCHHHH	36.33	22790023
158	Ubiquitination	QYNPDLYCVRSDLGN HHCCCEEEEHHHHHH	2.39	27667366
168	Ubiquitination	SDLGNLLKALGRLEE HHHHHHHHHHCCHHH	44.74	22790023
236	Ubiquitination	INLGNVLKEARIFDR HCHHHHHHHHHHHHH	45.07	-
488	Ubiquitination	DYDERMKKLVSIVAE CHHHHHHHHHHHHHH	44.79	22790023
504	Phosphorylation	LEKNRLPSVHPHHSM HHHCCCCCCCCCCCH	37.34	29233185
510	Phosphorylation	PSVHPHHSMLYPLSH CCCCCCCCHHHHCCH	13.88	29233185
540	Ubiquitination	DKINVLHKPPYEHPK HHCCCCCCCCCCCCC	43.45	27667366
550	Ubiquitination	YEHPKDLKLSDGRLR CCCCCCCCCCCCCEE	56.96	22790023
716	Ubiquitination	ANMFPHLKKKAVIDF CCCCHHCCCCEEEEE	49.55	22790023
717	Ubiquitination	NMFPHLKKKAVIDFK CCCHHCCCCEEEEEC	52.93	-
742	Ubiquitination	VLNGIDLKAFLDSLP EECCCCHHHHHHCCC	33.09	22790023
742	Acetylation	VLNGIDLKAFLDSLP EECCCCHHHHHHCCC	33.09	23954790
752	Ubiquitination	LDSLPDVKIVKMKCP HHCCCCCEEEEEECC	49.51	22790023
819	Phosphorylation	QINNKAATGEEVPRT EECCCCCCCCCCCCE	50.41	30635358
826	Phosphorylation	TGEEVPRTIIVTTRS CCCCCCCEEEEEECH	14.69	30635358
830	Phosphorylation	VPRTIIVTTRSQYGL CCCEEEEEECHHCCC	13.19	30635358
831	Phosphorylation	PRTIIVTTRSQYGLP CCEEEEEECHHCCCC	19.89	30635358
857	Phosphorylation	LYKIDPSTLQMWANI EECCCHHHHHHHHHH	26.80	-
989	Phosphorylation	KLGTDLEYLKKIRGK HHCCCHHHHHHHCCH	30.99	-
991	Acetylation	GTDLEYLKKIRGKVW CCCHHHHHHHCCHHH	45.30	23236377
1000	Ubiquitination	IRGKVWKQRISSPLF HCCHHHHHHCCCCCC	32.02	27667366
1010	Ubiquitination	SSPLFNTKQYTMELE CCCCCCCHHHHHHHH	42.27	22790023
1043	O-linked_Glycosylation	MIKPVEVTESA---- CCCCCEECCCC----	15.66	28528544
1045	Phosphorylation	KPVEVTESA------ CCCEECCCC------	29.88	27841257

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	Q9WV60	Uniprot
4	S	Phosphorylation	Kinase	GSK3-BETA	Q9WV60	Uniprot

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.	23395175
4	S	Phosphorylation	Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity.	23395175

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PO5F1_MOUSE	Pou5f1	physical	22608532
SOX2_MOUSE	Sox2	physical	22608532

Drug and Disease Associations

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