P56558 (OGT1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 93.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit EC=2.4.1.- Alternative name(s): O-GlcNAc transferase subunit p110 O-linked N-acetylglucosamine transferase 110 kDa subunit | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 1036 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Mediates the O-glycosylation of MLL5 and HCFC1. Promotes proteolytic maturation of HCFC1 By similarity. |
| Catalytic activity | UDP-N-acetyl-D-glucosamine + peptide = UDP + N-acetyl-beta-D-glucosaminyl-peptide. |
| Enzyme regulation | By tyrosine phosphorylation and O-GlcNAc modifications. |
| Pathway | |
| Subunit structure | Interacts directly with HCFC1. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT By similarity. Heterotrimer of two 110 kDa and one 78 kDa subunits. It is not known if the 78 kDa subunit is encoded by a separate gene or is the product of either of a proteolytic degradation or an alternative initiation of the 110 kDa subunit. Interacts with ATXN10. Ref.2 |
| Subcellular location | Cytoplasm. Nucleus By similarity. Note: Mostly in the nucleus By similarity. Ref.2 |
| Tissue specificity | Appears to be present in all tissues examined except kidney. |
| Domain | The TPR repeat domain mediates recognition of protein substrates By similarity. |
| Post-translational modification | O-glycosylated; contains O-GlcNAc. Ubiquitinated, leading to its proteasomal degradation By similarity. |
| Sequence similarities | Belongs to the O-GlcNAc transferase family. Contains 13 TPR repeats. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Domain | Repeat TPR repeat |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Acetylation Glycoprotein Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | positive regulation of proteolysis Inferred from sequence or structural similarity. Source: UniProtKB protein O-linked glycosylationInferred from direct assay Ref.1. Source: RGD protein homotrimerizationInferred from direct assay. Source: RGD |
| Cellular component | cytosol Inferred from direct assay Ref.1. Source: RGD |
| Molecular function | monosaccharide binding Inferred from direct assay. Source: RGD peptide bindingInferred from direct assay. Source: RGD protein N-acetylglucosaminyltransferase activityInferred from direct assay Ref.1. Source: RGD protein bindingInferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 1036 | 1035 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit | PRO_0000191774 | |||||
Regions | |||||||||
| Repeat | 11 – 44 | 34 | TPR 1 | ||||||
| Repeat | 79 – 112 | 34 | TPR 2 | ||||||
| Repeat | 113 – 146 | 34 | TPR 3 | ||||||
| Repeat | 147 – 180 | 34 | TPR 4 | ||||||
| Repeat | 181 – 214 | 34 | TPR 5 | ||||||
| Repeat | 215 – 248 | 34 | TPR 6 | ||||||
| Repeat | 249 – 282 | 34 | TPR 7 | ||||||
| Repeat | 283 – 316 | 34 | TPR 8 | ||||||
| Repeat | 317 – 350 | 34 | TPR 9 | ||||||
| Repeat | 351 – 384 | 34 | TPR 10 | ||||||
| Repeat | 385 – 418 | 34 | TPR 11 | ||||||
| Repeat | 419 – 452 | 34 | TPR 12 | ||||||
| Repeat | 453 – 463 | 11 | TPR 13; truncated | ||||||
| Nucleotide binding | 895 – 898 | 4 | UDP By similarity | ||||||
| Nucleotide binding | 901 – 904 | 4 | UDP By similarity | ||||||
| Nucleotide binding | 919 – 921 | 3 | UDP By similarity | ||||||
| Motif | 478 – 493 | 16 | Nuclear localization signal Potential | ||||||
Sites | |||||||||
| Active site | 498 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 839 | 1 | UDP By similarity | ||||||
| Binding site | 842 | 1 | UDP By similarity | ||||||
| Binding site | 925 | 1 | UDP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 979 | 1 | Phosphotyrosine Probable | ||||||
Sequences
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References
| [1] | "Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats." Kreppel L.K., Blomberg M.A., Hart G.W. J. Biol. Chem. 272:9308-9315(1997) [PubMed: 9083067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Sprague-Dawley. Tissue: Liver. |
| [2] | "Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain." Maerz P., Stetefeld J., Bendfeldt K., Nitsch C., Reinstein J., Shoeman R.L., Dimitriades-Schmutz B., Schwager M., Leiser D., Ozcan S., Otten U., Ozbek S. J. Biol. Chem. 281:20263-20270(2006) [PubMed: 16714295] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ATXN10. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U76557 mRNA. Translation: AAC53121.1. |
| IPI | IPI00231503. |
| PIR | T31673. |
| RefSeq | NP_058803.2. NM_017107.2. |
| UniGene | Rn.82705. |
3D structure databases | |
| ProteinModelPortal | P56558. |
| SMR | P56558. Positions 13-400. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P56558. |
Protein family/group databases | |
| CAZy | GT41. Glycosyltransferase Family 41. |
PTM databases | |
| PhosphoSite | P56558. |
Proteomic databases | |
| PRIDE | P56558. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 26295. |
| KEGG | rno:26295. |
| UCSC | NM_017107. rat. |
Organism-specific databases | |
| CTD | 8473. |
| RGD | 62060. Ogt. |
Phylogenomic databases | |
| eggNOG | roNOG07233. |
| GeneTree | ENSGT00550000074327. |
| HOVERGEN | HBG000351. |
| InParanoid | P56558. |
| OrthoDB | EOG4HQDHJ. |
| PhylomeDB | P56558. |
Enzyme and pathway databases | |
| BRENDA | 2.4.1.94. 5301. |
Gene expression databases | |
| ArrayExpress | P56558. |
| Genevestigator | P56558. |
| GermOnline | ENSRNOG00000003359. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR001440. TPR-1. IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view] |
| Gene3D | G3DSA:1.25.40.10. TPR-like_helical. 2 hits. |
| KO | K09667. |
| Pfam | PF00515. TPR_1. 10 hits. [Graphical view] |
| SMART | SM00028. TPR. 11 hits. [Graphical view] |
| PROSITE | PS50005. TPR. 12 hits. PS50293. TPR_REGION. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 608004. |
Entry information
| Entry name | OGT1_RAT | ||||||||
| Accession | Primary (citable) accession number: P56558 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with