dbPTM

OGT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	OGT1_HUMAN
UniProt AC	O15294
Protein Name	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Gene Name	OGT
Organism	Homo sapiens (Human).
Sequence Length	1046
Subcellular Localization	Nucleus . Cytoplasm . Predominantly localizes to the nucleus. Isoform 2: Mitochondrion. Membrane. Associates with the mitochondrial inner membrane. Isoform 3: Cytoplasm. Nucleus. Cell membrane. Mostly in the nucleus. Retained in the nucle
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). [PubMed: 26678539 Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1]
Protein Sequence	MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASSVGNVA ------CCCCCCCCC	23.09	22814378
3	O-linked_Glycosylation	-----MASSVGNVAD -----CCCCCCCCCC	37.10	UniProtKB CARBOHYD
3	Phosphorylation	-----MASSVGNVAD -----CCCCCCCCCC	37.10	20068231
4	O-linked_Glycosylation	----MASSVGNVADS ----CCCCCCCCCCC	40.89	UniProtKB CARBOHYD
4	Phosphorylation	----MASSVGNVADS ----CCCCCCCCCCC	40.89	20068231
10 (in isoform 4)	O-linked_Glycosylation	-	52.38	23301498
11	Phosphorylation	SVGNVADSTEPTKRM CCCCCCCCCCCCHHH	25.57	20068231
12 (in isoform 4)	O-linked_Glycosylation	-	46.67	23301498
12	Phosphorylation	VGNVADSTEPTKRML CCCCCCCCCCCHHHH	46.67	20068231
15	Phosphorylation	VADSTEPTKRMLSFQ CCCCCCCCHHHHHHH	25.67	20068231
16	Ubiquitination	ADSTEPTKRMLSFQG CCCCCCCHHHHHHHH	46.67	23000965
16	Acetylation	ADSTEPTKRMLSFQG CCCCCCCHHHHHHHH	46.67	25953088
18	Sulfoxidation	STEPTKRMLSFQGLA CCCCCHHHHHHHHHH	3.81	28183972
18 (in isoform 4)	O-linked_Glycosylation	-	3.81	23301498
20	Phosphorylation	EPTKRMLSFQGLAEL CCCHHHHHHHHHHHH	13.23	30266825
32	Phosphorylation	AELAHREYQAGDFEA HHHHCHHHHCCCHHH	12.01	27642862
38 (in isoform 4)	O-linked_Glycosylation	-	52.27	23301498
52 (in isoform 4)	O-linked_Glycosylation	-	31.64	23301498
56 (in isoform 4)	O-linked_Glycosylation	-	17.84	23301498
73	Ubiquitination	FQCRRLDRSAHFSTL HHHHCCCCCCCHHHH	40.09	23000965
73 (in isoform 3)	Ubiquitination	-	40.09	21890473
74	Phosphorylation	QCRRLDRSAHFSTLA HHHCCCCCCCHHHHH	26.26	20873877
78	Phosphorylation	LDRSAHFSTLAIKQN CCCCCCHHHHHHHCC	16.79	28857561
79	Phosphorylation	DRSAHFSTLAIKQNP CCCCCHHHHHHHCCH	21.18	20873877
83	Ubiquitination	HFSTLAIKQNPLLAE CHHHHHHHCCHHHHH	38.11	23000965
83 (in isoform 1)	Ubiquitination	-	38.11	21890473
90	Ubiquitination	KQNPLLAEAYSNLGN HCCHHHHHHHHCHHH	48.38	23000965
90 (in isoform 3)	Ubiquitination	-	48.38	21890473
92	Phosphorylation	NPLLAEAYSNLGNVY CHHHHHHHHCHHHHH	6.92	27642862
100	Ubiquitination	SNLGNVYKERGQLQE HCHHHHHHHHCHHHH	36.33	23000965
100 (in isoform 1)	Ubiquitination	-	36.33	21890473
110 (in isoform 2)	Ubiquitination	-	41.75	21890473
119	Sumoylation	YRHALRLKPDFIDGY HHHHHHCCHHHHHHH	35.79	-
119	Sumoylation	YRHALRLKPDFIDGY HHHHHHCCHHHHHHH	35.79	17000644
158	Ubiquitination	QYNPDLYCVRSDLGN HHCCCEEEEHHHHHH	2.39	23000965
158 (in isoform 3)	Ubiquitination	-	2.39	21890473
161	Phosphorylation	PDLYCVRSDLGNLLK CCEEEEHHHHHHHHH	19.45	28634120
167	Ubiquitination	RSDLGNLLKALGRLE HHHHHHHHHHHCCHH	3.37	32015554
168	Ubiquitination	SDLGNLLKALGRLEE HHHHHHHHHHCCHHH	44.74	23000965
168	Acetylation	SDLGNLLKALGRLEE HHHHHHHHHHCCHHH	44.74	25953088
168 (in isoform 1)	Ubiquitination	-	44.74	21890473
177	Ubiquitination	LGRLEEAKACYLKAI HCCHHHHHHHHHHHH	42.12	32015554
226	Ubiquitination	TLDPNFLDAYINLGN CCCCCHHHHHHCHHH	32.94	22817900
226 (in isoform 3)	Ubiquitination	-	32.94	21890473
236	Ubiquitination	INLGNVLKEARIFDR HCHHHHHHHHHHHHH	45.07	21906983
236 (in isoform 1)	Ubiquitination	-	45.07	21890473
296	Ubiquitination	QPHFPDAYCNLANAL CCCCCHHHHHHHHHH	6.83	29967540
306	Ubiquitination	LANALKEKGSVAEAE HHHHHHHCCCCCCHH	55.70	29967540
316	Phosphorylation	VAEAEDCYNTALRLC CCCHHHHHHHHHHHC	28.06	27642862
325	Phosphorylation	TALRLCPTHADSLNN HHHHHCCCCHHHHHH	28.79	20068231
327	Ubiquitination	LRLCPTHADSLNNLA HHHCCCCHHHHHHHH	15.57	30230243
329	Phosphorylation	LCPTHADSLNNLANI HCCCCHHHHHHHHHH	33.51	20068231
335	Ubiquitination	DSLNNLANIKREQGN HHHHHHHHHHHHHCC	43.40	21963094
336	Ubiquitination	SLNNLANIKREQGNI HHHHHHHHHHHHCCH	3.56	22817900
337	Sumoylation	LNNLANIKREQGNIE HHHHHHHHHHHCCHH	50.09	-
337	Ubiquitination	LNNLANIKREQGNIE HHHHHHHHHHHCCHH	50.09	22817900
337	Sumoylation	LNNLANIKREQGNIE HHHHHHHHHHHCCHH	50.09	17000644
352	Ubiquitination	EAVRLYRKALEVFPE HHHHHHHHHHHHCHH	43.71	-
361	Ubiquitination	LEVFPEFAAAHSNLA HHHCHHHHHHHHCHH	11.32	22817900
365	Phosphorylation	PEFAAAHSNLASVLQ HHHHHHHHCHHHHHH	28.89	-
369	Phosphorylation	AAHSNLASVLQQQGK HHHHCHHHHHHHCCC	26.90	-
371	Ubiquitination	HSNLASVLQQQGKLQ HHCHHHHHHHCCCHH	3.35	22817900
374	Ubiquitination	LASVLQQQGKLQEAL HHHHHHHCCCHHHHH	37.72	22817900
375	Ubiquitination	ASVLQQQGKLQEALM HHHHHHCCCHHHHHH	28.44	22505724
376	Ubiquitination	SVLQQQGKLQEALMH HHHHHCCCHHHHHHH	42.53	22817900
384	Phosphorylation	LQEALMHYKEAIRIS HHHHHHHHHHHHHHC	9.14	-
385	Ubiquitination	QEALMHYKEAIRISP HHHHHHHHHHHHHCH	26.45	22505724
385	Acetylation	QEALMHYKEAIRISP HHHHHHHHHHHHHCH	26.45	26051181
430	Ubiquitination	QINPAFADAHSNLAS HCCHHHHHCCCCHHH	38.06	30230243
433	Phosphorylation	PAFADAHSNLASIHK HHHHHCCCCHHHHHC	34.95	27080861
437	Phosphorylation	DAHSNLASIHKDSGN HCCCCHHHHHCCCCC	28.52	27080861
440	Ubiquitination	SNLASIHKDSGNIPE CCHHHHHCCCCCHHH	52.50	30230243
449 (in isoform 4)	O-linked_Glycosylation	-	2.20	23301498
452	Phosphorylation	IPEAIASYRTALKLK HHHHHHHHHHHHHCC	11.71	25627689
454	Phosphorylation	EAIASYRTALKLKPD HHHHHHHHHHHCCCC	28.27	-
459	Sumoylation	YRTALKLKPDFPDAY HHHHHHCCCCCCHHH	40.74	-
459	Sumoylation	YRTALKLKPDFPDAY HHHHHHCCCCCCHHH	40.74	17000644
478	Ubiquitination	HCLQIVCDWTDYDER HHHHHHCCCCCHHHH	40.18	30230243
488	Ubiquitination	DYDERMKKLVSIVAD CHHHHHHHHHHHHHH	44.79	30230243
488	Acetylation	DYDERMKKLVSIVAD CHHHHHHHHHHHHHH	44.79	26051181
489	Ubiquitination	YDERMKKLVSIVADQ HHHHHHHHHHHHHHH	2.81	30230243
491	Phosphorylation	ERMKKLVSIVADQLE HHHHHHHHHHHHHHH	23.06	-
499	Ubiquitination	IVADQLEKNRLPSVH HHHHHHHHCCCCCCC	56.83	30230243
524	Ubiquitination	HGFRKAIAERHGNLC HHHHHHHHHHHCCCC	16.78	29967540
530	Ubiquitination	IAERHGNLCLDKINV HHHHHCCCCCHHCCC	3.48	29967540
534	Ubiquitination	HGNLCLDKINVLHKP HCCCCCHHCCCCCCC	24.19	29967540
534	Acetylation	HGNLCLDKINVLHKP HCCCCCHHCCCCCCC	24.19	26051181
537	Ubiquitination	LCLDKINVLHKPPYE CCCHHCCCCCCCCCC	7.25	29967540
540	Ubiquitination	DKINVLHKPPYEHPK HHCCCCCCCCCCCCC	43.45	32015554
547	Ubiquitination	KPPYEHPKDLKLSDG CCCCCCCCCCCCCCC	77.06	29967540
550	Ubiquitination	YEHPKDLKLSDGRLR CCCCCCCCCCCCCEE	56.96	32015554
590 (in isoform 2)	Ubiquitination	-	2.04	21890473
604	Ubiquitination	DGTNFRVKVMAEANH CCCCEEEEEEEECCC	23.26	-
610	Ubiquitination	VKVMAEANHFIDLSQ EEEEEECCCCEEHHH	23.31	22505724
613	Ubiquitination	MAEANHFIDLSQIPC EEECCCCEEHHHCCC	3.97	30230243
616 (in isoform 2)	Ubiquitination	-	23.47	21890473
623	Ubiquitination	SQIPCNGKAADRIHQ HHCCCCCCHHHHCCC	26.81	30230243
626 (in isoform 2)	Ubiquitination	-	55.73	21890473
629	Ubiquitination	GKAADRIHQDGIHIL CCHHHHCCCCCCEEE	22.15	23000965
634	Ubiquitination	RIHQDGIHILVNMNG HCCCCCCEEEEECCC	16.92	30230243
644	Ubiquitination	VNMNGYTKGARNELF EECCCCCCCCCHHHE	41.93	30230243
706	Ubiquitination	MPHTFFIGDHANMFP CCCCEECCCCCCCCH	18.59	21963094
706 (in isoform 3)	Ubiquitination	-	18.59	21890473
707	Ubiquitination	PHTFFIGDHANMFPH CCCEECCCCCCCCHH	32.67	22817900
708	Ubiquitination	HTFFIGDHANMFPHL CCEECCCCCCCCHHC	17.50	22817900
714	Ubiquitination	DHANMFPHLKKKAVI CCCCCCHHCCCCEEE	38.73	30230243
716	Ubiquitination	ANMFPHLKKKAVIDF CCCCHHCCCCEEEEE	49.55	21906983
716 (in isoform 1)	Ubiquitination	-	49.55	21890473
717	Ubiquitination	NMFPHLKKKAVIDFK CCCHHCCCCEEEEEC	52.93	22817900
718	Ubiquitination	MFPHLKKKAVIDFKS CCHHCCCCEEEEECC	46.42	22817900
724	Ubiquitination	KKAVIDFKSNGHIYD CCEEEEECCCCEEEC	38.98	30230243
732	Ubiquitination	SNGHIYDNRIVLNGI CCCEEECCEEEECCC	20.71	22817900
732 (in isoform 3)	Ubiquitination	-	20.71	21890473
742	Ubiquitination	VLNGIDLKAFLDSLP EECCCCHHHHHHCCC	33.09	21906983
742 (in isoform 1)	Ubiquitination	-	33.09	21890473
742 (in isoform 3)	Ubiquitination	-	33.09	21890473
745	Ubiquitination	GIDLKAFLDSLPDVK CCCHHHHHHCCCCCE	5.37	22817900
747	Ubiquitination	DLKAFLDSLPDVKIV CHHHHHHCCCCCEEE	43.90	22817900
752	Ubiquitination	LDSLPDVKIVKMKCP HHCCCCCEEEEEECC	49.51	21906983
752	Sumoylation	LDSLPDVKIVKMKCP HHCCCCCEEEEEECC	49.51	-
752 (in isoform 1)	Ubiquitination	-	49.51	21890473
755	Ubiquitination	LPDVKIVKMKCPDGG CCCCEEEEEECCCCC	35.79	22817900
757	Ubiquitination	DVKIVKMKCPDGGDN CCEEEEEECCCCCCC	36.58	22817900
819	Phosphorylation	QINNKAATGEEVPRT EECCCCCCCCCCCCE	50.41	29457462
866	Ubiquitination	QMWANILKRVPNSVL HHHHHHHHHCCCCHH	47.77	-
884 (in isoform 2)	Ubiquitination	-	36.98	21890473
893	Sulfoxidation	IQQYAQNMGLPQNRI HHHHHHHCCCCCCCE	3.76	28183972
898	Ubiquitination	QNMGLPQNRIIFSPV HHCCCCCCCEEEECC	34.87	30230243
903	Phosphorylation	PQNRIIFSPVAPKEE CCCCEEEECCCCCHH	14.20	27067055
908	Ubiquitination	IFSPVAPKEEHVRRG EEECCCCCHHHHCCC	67.03	30230243
961	Ubiquitination	RVAASQLTCLGCLEL HHHHHHHHHHHHHHH	9.69	30230243
971	Ubiquitination	GCLELIAKNRQEYED HHHHHHHHCHHHHHH	45.74	30230243
972	Ubiquitination	CLELIAKNRQEYEDI HHHHHHHCHHHHHHH	41.67	30230243
976	Phosphorylation	IAKNRQEYEDIAVKL HHHCHHHHHHHHHHH	15.57	21406692
981	Ubiquitination	QEYEDIAVKLGTDLE HHHHHHHHHHCCCHH	5.55	22505724
982	Ubiquitination	EYEDIAVKLGTDLEY HHHHHHHHHCCCHHH	31.98	30230243
985	Phosphorylation	DIAVKLGTDLEYLKK HHHHHHCCCHHHHHH	48.09	-
989	Phosphorylation	KLGTDLEYLKKVRGK HHCCCHHHHHHHCCH	30.99	-
991	Acetylation	GTDLEYLKKVRGKVW CCCHHHHHHHCCHHH	48.60	23749302
991	Ubiquitination	GTDLEYLKKVRGKVW CCCHHHHHHHCCHHH	48.60	22505724
992	Ubiquitination	TDLEYLKKVRGKVWK CCHHHHHHHCCHHHH	34.27	-
1000	Ubiquitination	VRGKVWKQRISSPLF HCCHHHHHHCCCCCC	32.02	23000965
1000 (in isoform 3)	Ubiquitination	-	32.02	21890473
1004	Phosphorylation	VWKQRISSPLFNTKQ HHHHHCCCCCCCCHH	24.21	-
1010	Ubiquitination	SSPLFNTKQYTMELE CCCCCCCHHHHHHHH	42.27	23000965
1010 (in isoform 1)	Ubiquitination	-	42.27	21890473
1045	Phosphorylation	KPVEVTESA------ CCCEECCCC------	29.88	25159151

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	GSK3B	P49841	PSP
4	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
20	S	Phosphorylation	Kinase	CHEK1	O14757	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of OGT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
N62CL_HUMAN	NUP62CL	physical	16189514
TRAK1_HUMAN	TRAK1	physical	12724313
SIN3A_HUMAN	SIN3A	physical	12150998
OGA_HUMAN	MGEA5	physical	16505006
NUP62_HUMAN	NUP62	physical	16434389
OGA_HUMAN	MGEA5	physical	16434389
CSK21_HUMAN	CSNK2A1	physical	16434389
TAU_HUMAN	MAPT	physical	16434389
YES_HUMAN	YES1	physical	16434389
TAB1_HUMAN	TAB1	physical	22307082
HCFC1_HUMAN	HCFC1	physical	21295698
PP1A_HUMAN	PPP1CA	physical	22939629
PP1B_HUMAN	PPP1CB	physical	22939629
NUP62_RAT	Nup62	physical	17882263
NFAC1_HUMAN	NFATC1	physical	17882263
TF65_HUMAN	RELA	physical	17882263
FOXO4_HUMAN	FOXO4	physical	19932102
TET2_HUMAN	TET2	physical	25416956
N62CL_HUMAN	NUP62CL	physical	25416956
PHC3_HUMAN	PHC3	physical	25416956
CRKL_HUMAN	CRKL	physical	26344197
SYFA_HUMAN	FARSA	physical	26344197
PA1B2_HUMAN	PAFAH1B2	physical	26344197
NUP62_HUMAN	NUP62	physical	10753899
CSK21_HUMAN	CSNK2A1	physical	10753899
CSK2B_HUMAN	CSNK2B	physical	10753899
KMT2E_HUMAN	KMT2E	physical	26678539
UBP7_HUMAN	USP7	physical	26678539
KDM1B_HUMAN	KDM1B	physical	25773598
U119A_HUMAN	UNC119	physical	27173435

Drug and Disease Associations

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

Regulatory Network of OGT1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.	18669648 [Abstract]

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