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MGI:Ogt

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Contents

Species (Taxon ID) Mus musculus (house mouse) (taxon:10090)
Gene Name(s) Ogt ( synonyms: OGT, Ogtl )
Protein Name(s) O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase),
External Links
MGI MGI:1339639

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000123

histone acetyltransferase complex

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

C

From MGI

GO:0003824

catalytic activity

MGI:MGI:86854
PMID:9083067[1]

ISS: Inferred from Sequence or Structural Similarity

F

From MGI

GO:0005515

protein binding

MGI:MGI:3761912
PMID:17670746[2]

IPI: Inferred from Physical Interaction

UniProtKB:Q60520

F

From MGI

GO:0005547

phosphatidylinositol-3,4,5-trisphosphate binding

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

F

From MGI

GO:0005622

intracellular

MGI:MGI:1858670
PMID:10801981[3]

TAS: Traceable Author Statement

C

From MGI

GO:0005634

nucleus

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P56558

C

From MGI

GO:0005634

nucleus

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

C

From MGI

GO:0005634

nucleus

MGI:MGI:86854
PMID:9083067[1]

TAS: Traceable Author Statement

C

From MGI

GO:0005737

cytoplasm

MGI:MGI:86854
PMID:9083067[1]

TAS: Traceable Author Statement

C

From MGI

GO:0005813

centrosome

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

C

From MGI

GO:0005829

cytosol

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P56558

C

From MGI

GO:0005829

cytosol

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

C

From MGI

GO:0005886

plasma membrane

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

C

From MGI

GO:0006493

protein O-linked glycosylation

MGI:MGI:1858670
PMID:10801981[3]

TAS: Traceable Author Statement

P

From MGI

GO:0006493

protein O-linked glycosylation

MGI:MGI:3761912
PMID:17670746[2]

IDA: Inferred from Direct Assay

P

From MGI

GO:0006493

protein O-linked glycosylation

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P56558

P

From MGI

GO:0006493

protein O-linked glycosylation

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0006493

protein O-linked glycosylation

MGI:MGI:86854
PMID:9083067[1]

ISS: Inferred from Sequence or Structural Similarity

P

From MGI

GO:0006917

induction of apoptosis

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0008047

enzyme activator activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

F

From MGI

GO:0008080

N-acetyltransferase activity

MGI:MGI:1858670
PMID:10801981[3]

TAS: Traceable Author Statement

F

From MGI

GO:0008152

metabolic process

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0328

P

From MGI

GO:0008289

lipid binding

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0446

F

From MGI

GO:0016020

membrane

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0472

C

From MGI

GO:0016262

protein N-acetylglucosaminyltransferase activity

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P56558

F

From MGI

GO:0016262

protein N-acetylglucosaminyltransferase activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

F

From MGI

GO:0016568

chromatin modification

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0156

P

From MGI

GO:0016740

transferase activity

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0808

F

From MGI

GO:0016757

transferase activity, transferring glycosyl groups

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0328

F

From MGI

GO:0030854

positive regulation of granulocyte differentiation

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0032868

response to insulin stimulus

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0035020

regulation of Rac protein signal transduction

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0042277

peptide binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P56558

F

From MGI

GO:0043085

positive regulation of catalytic activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0043981

histone H4-K5 acetylation

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0043982

histone H4-K8 acetylation

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0043984

histone H4-K16 acetylation

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0045862

positive regulation of proteolysis

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0046626

regulation of insulin receptor signaling pathway

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0048015

phosphatidylinositol-mediated signaling

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0048029

monosaccharide binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P56558

F

From MGI

GO:0051571

positive regulation of histone H3-K4 methylation

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI

GO:0070207

protein homotrimerization

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:P56558

P

From MGI

GO:0070688

MLL5-L complex

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

C

From MGI

GO:0071300

cellular response to retinoic acid

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:O15294

P

From MGI


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 1.0 1.1 1.2 1.3 Kreppel LK et al. (1997) Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J Biol Chem 272: 9308-15 PubMed GONUTS page
  2. 2.0 2.1 Yao D et al. (2007) High glucose increases angiopoietin-2 transcription in microvascular endothelial cells through methylglyoxal modification of mSin3A. J Biol Chem 282: 31038-45 PubMed GONUTS page
  3. 3.0 3.1 3.2 Shafi R et al. (2000) The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc Natl Acad Sci U S A 97: 5735-9 PubMed GONUTS page
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