KEGG   ENZYME: 2.4.1.255Help
Entry
EC 2.4.1.255                Enzyme                                 

Name
protein O-GlcNAc transferase;
O-GlcNAc transferase;
OGTase;
O-linked N-acetylglucosaminyltransferase;
uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase;
protein O-linked beta-N-acetylglucosamine transferase
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
BRITE hierarchy
Sysname
UDP-N-alpha-acetyl-D-glucosamine:[protein]-3-O-N-acetyl-beta-D-glucosaminyl transferase
Reaction(IUBMB)
(1) UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine [RN:R09676];
(2) UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine [RN:R09677]
Reaction(KEGG)
R09676 R09677;
(other) R09304(G)
Show
Substrate
UDP-N-acetyl-alpha-D-glucosamine [CPD:C00043];
[protein]-L-serine [CPD:C02189];
[protein]-L-threonine [CPD:C19803]
Product
UDP [CPD:C00015];
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine [CPD:C19802];
[protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine [CPD:C19804]
Comment
Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. EC 2.4.1.255 (protein O-GlcNAc transferase) transfers GlcNAc onto substrate proteins and EC 3.2.1.169 (protein O-GlcNAcase) cleaves GlcNAc from the modified proteins.
History
EC 2.4.1.255 created 2011
Pathway
Other types of O-glycan biosynthesis
Orthology
K09667  
protein O-GlcNAc transferase
K18134  
protein O-GlcNAc transferase
Genes
HSA: 
285203(EOGT) 8473(OGT)
PTR: 
465702(OGT) 494220(EOGT)
PPS: 
100970968(EOGT) 100989146(OGT)
GGO: 
101130943(EOGT) 101140533(OGT)
PON: 
100174354(OGT) 100440288(EOGT)
NLE: 
100591966(OGT) 100597324(EOGT)
MCC: 
696742(EOGT) 698268(OGT)
MCF: 
101866582(OGT) 102115709(EOGT)
RRO: 
104664903(OGT) 104677919(EOGT)
CJC: 
100386886(OGT) 100390811(EOGT)
MMU: 
101351(Eogt) 108155(Ogt)
RNO: 
26295(Ogt) 494219(Eogt)
CGE: 
100757071(Eogt) 100768670(Ogt)
NGI: 
HGL: 
OCU: 
100342123(EOGT) 100354727(OGT)
TUP: 
102479359(OGT) 102499112(EOGT)
CFA: 
480955(OGT) 494221(EOGT)
AML: 
100475282(OGT) 100479105(EOGT)
UMR: 
103674238(EOGT) 103682584(OGT)
FCA: 
101089680(EOGT) 101094162(OGT)
PTG: 
102959921(EOGT) 102964072(OGT)
BTA: 
508782(EOGT) 532053(OGT)
BOM: 
102279900(EOGT) 102286677(OGT)
PHD: 
102328809(EOGT) 102344387(OGT)
CHX: 
102176741(EOGT) 102187305(OGT)
OAS: 
101106996(OGT) 101117114(EOGT)
SSC: 
100155485(EOGT) 664652(OGT)
CFR: 
102516733(OGT) 102521209(EOGT)
BACU: 
LVE: 
103071794(EOGT) 103073601(OGT)
ECB: 
100053493(EOGT) 100056148(OGT)
MYB: 
102245549(OGT) 102247874(EOGT)
MYD: 
102751826(EOGT) 102773180(OGT)
PALE: 
102879009(EOGT) 102890872(OGT)
MDO: 
100011073(OGT) 100618477(EOGT)
SHR: 
100929019(OGT) 100931735(EOGT)
OAA: 
100078373(EOGT)
GGA: 
422203(OGT) 426961(EOGT)
MGP: 
100538830(OGT) 100550764(EOGT)
CJO: 
107312490(OGT) 107319994(EOGT)
APLA: 
101796788(EOGT) 101799851(OGT)
TGU: 
100224237(OGT) 100225538(EOGT)
GFR: 
102042181(EOGT) 102044727(OGT)
FAB: 
101808611(OGT) 101809614(EOGT)
PHI: 
102112943(OGT) 102113990(EOGT)
CCW: 
104683359(EOGT) 104691638(OGT)
FPG: 
101915918(OGT) 101923329(EOGT)
FCH: 
102050428(EOGT) 102052264(OGT)
CLV: 
102092523(OGT) 102092951(EOGT)
AAM: 
106482679(OGT) 106494570(EOGT)
ASN: 
102381905(EOGT) 102387350(OGT)
AMJ: 
PSS: 
102445994(OGT) 102448245(EOGT)
CMY: 
ACS: 
100554805(eogt) 100561277(ogt)
PBI: 
103048321(EOGT) 103059316(OGT)
GJA: 
107108561(OGT) 107121813(EOGT)
XLA: 
443983(eogt) 447694(ogt)
XTR: 
553157(ogt) 780148(eogt)
DRE: 
337685(ogt.1) 652952(ogt.2) 798087(eogt)
TRU: 
101076057(ogt) 777950(eogt)
MZE: 
101479094(ogt) 101484112(eogt)
OLA: 
101164571(ogt) 101170339(eogt)
XMA: 
102227742(ogt) 102236401(eogt)
LCM: 
102352761(EOGT) 102361281(OGT)
CMK: 
103179783(eogt) 103189357(ogt)
BFO: 
CIN: 
SPU: 
SKO: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD17889(Dsim_GD17889) Dsimw501_GD23152(Dsim_GD23152) Dsimw501_GD28381(Dsim_GD28381)
DWI: 
DYA: 
Dyak_GE11251(dyak_GLEANR_11370) Dyak_GE18152(dyak_GLEANR_1946)
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
408434(GB20085) 551425(sxc)
SOC: 
AEC: 
HST: 
CFO: 
NVI: 
TCA: 
BMOR: 
PXY: 
API: 
PHU: 
ISC: 
CEL: 
CELE_H12D21.10(H12D21.10) CELE_K04G7.3(ogt-1)
CBR: 
CBG16605(Cbr-ogt-1)
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
CRG: 
OBI: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
EGR: 
GMX: 
PVU: 
VRA: 
MTR: 
CAM: 
ADU: 
AIP: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
POPTR_0006s04710g(POPTRDRAFT_652692) POPTR_0008s09220g(POPTRDRAFT_564268) POPTR_0010s16950g(POPTRDRAFT_226224) POPTR_0010s16960g(POPTRDRAFT_226227) POPTR_0013s04820g(POPTRDRAFT_895082) POPTR_0016s05740g(POPTRDRAFT_576368) POPTR_0019s04230g(POPTRDRAFT_738316)
VVI: 
SLY: 
SPEN: 
SOT: 
SIND: 
BVG: 
NNU: 
DOSA: 
Os02t0489550-00(Os02g0489550)
OBR: 
BDI: 
SBI: 
SORBI_04g019560(SORBIDRAFT_04g019560)
ZMA: 
100381672(cl27878_1(278))
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
BPG: 
CSL: 
CVR: 
APRO: 
GSL: 
CCP: 
MAJ: 
ELA: 
TMS: 
ABP: 
AGABI1DRAFT78054(AGABI1DRAFT_78054)
MBR: 
SRE: 
ACAN: 
PTI: 
TPS: 
AAF: 
NGD: 
PIF: 
PSOJ: 
SPAR: 
EHX: 
GTT: 
NGR: 
GLA: 
 » show all
Taxonomy
Reference
1  [PMID:18948359]
  Authors
Banerjee S, Robbins PW, Samuelson J
  Title
Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum.
  Journal
Glycobiology. 19 (2009) 331-6.
  Sequence
Reference
2  [PMID:18818698]
  Authors
Clarke AJ, Hurtado-Guerrero R, Pathak S, Schuttelkopf AW, Borodkin V, Shepherd SM, Ibrahim AF, van Aalten DM
  Title
Structural insights into mechanism and specificity of O-GlcNAc transferase.
  Journal
EMBO. J. 27 (2008) 2780-8.
Reference
3  [PMID:16541109]
  Authors
Rao FV, Dorfmueller HC, Villa F, Allwood M, Eggleston IM, van Aalten DM
  Title
Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis.
  Journal
EMBO. J. 25 (2006) 1569-78.
Reference
4  [PMID:1533623]
  Authors
Haltiwanger RS, Blomberg MA, Hart GW
  Title
Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.
  Journal
J. Biol. Chem. 267 (1992) 9005-13.
Reference
5  [PMID:9083068]
  Authors
Lubas WA, Frank DW, Krause M, Hanover JA
  Title
O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats.
  Journal
J. Biol. Chem. 272 (1997) 9316-24.
  Sequence
[cel:CELE_K04G7.3] [hsa:8473]
Reference
6  [PMID:21240259]
  Authors
Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S
  Title
Structure of human O-GlcNAc transferase and its complex with a peptide substrate.
  Journal
Nature. 469 (2011) 564-7.
  Sequence
[hsa:8473]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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