Q6P5E4 (UGGG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 82.
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-glucose:glycoprotein glucosyltransferase 1 Short name=UGT1 EC=2.4.1.- Alternative name(s): UDP--Glc:glycoprotein glucosyltransferase UDP-glucose ceramide glucosyltransferase-like 1 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1551 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 | Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation By similarity. |
| Cofactor | Calcium By similarity. |
| Pathway | |
| Subunit structure | Monomer as well as in a tight complex with SEP15. Ref.3 |
| Subcellular location | Endoplasmic reticulum lumen By similarity. Endoplasmic reticulum-Golgi intermediate compartment By similarity UniProtKB Q9NYU2. |
| Domain | The N-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects By similarity. |
| Sequence similarities | Belongs to the glycosyltransferase 8 family. UniProtKB Q9JLA3 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Domain | Signal |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | endoplasmic reticulum lumen Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum-Golgi intermediate compartmentInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | UDP-glucose:glycoprotein glucosyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB unfolded protein bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 42 | 42 | By similarity | ||||||
| Chain | 43 – 1551 | 1509 | UDP-glucose:glycoprotein glucosyltransferase 1 | PRO_0000012272 | |||||
Regions | |||||||||
| Region | 1244 – 1551 | 308 | Glucosyltransferase By similarity | ||||||
| Motif | 1548 – 1551 | 4 | Prevents secretion from ER Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1277 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 269 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 536 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1228 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 319 | 1 | K → E in AAH68283. Ref.1 | ||||||
| Sequence conflict | 445 | 1 | S → F in AAH68283. Ref.1 | ||||||
| Sequence conflict | 824 | 1 | S → N in AAH68283. Ref.1 | ||||||
| Sequence conflict | 935 | 1 | Q → R in AAH68283. Ref.1 | ||||||
| Sequence conflict | 1015 | 1 | N → T in AAH68283. Ref.1 | ||||||
| Sequence conflict | 1058 | 1 | I → T in AAH68283. Ref.1 | ||||||
| Sequence conflict | 1083 | 1 | E → Q in AAH62936. Ref.2 | ||||||
| Sequence conflict | 1212 | 1 | K → R in AAH68283. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and ICR. Tissue: Brain and Trophoblast stem cell. |
| [3] | "Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells." Korotkov K.V., Kumaraswamy E., Zhou Y., Hatfield D.L., Gladyshev V.N. J. Biol. Chem. 276:15330-15336(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEP15. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC133102 Genomic DNA. No translation available. BC062936 mRNA. Translation: AAH62936.1. BC068283 mRNA. Translation: AAH68283.1. |
| IPI | IPI00762897. |
| RefSeq | NP_942602.2. NM_198899.2. |
| UniGene | Mm.261022. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-1863721. |
Protein family/group databases | |
| CAZy | GT24. Glycosyltransferase Family 24. |
PTM databases | |
| PhosphoSite | Q6P5E4. |
Proteomic databases | |
| PaxDb | Q6P5E4. |
| PRIDE | Q6P5E4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000046875; ENSMUSP00000037930; ENSMUSG00000037470. |
| GeneID | 320011. |
| KEGG | mmu:320011. |
| UCSC | uc007app.2. mouse. |
Organism-specific databases | |
| CTD | 56886. |
| MGI | MGI:2443162. Uggt1. |
Phylogenomic databases | |
| eggNOG | NOG320899. |
| GeneTree | ENSGT00390000004600. |
| HOGENOM | HOG000184622. |
| HOVERGEN | HBG079469. |
| InParanoid | Q6P5E4. |
| KO | K11718. |
| OMA | QNIGSSD. |
| OrthoDB | EOG46WZ7H. |
Enzyme and pathway databases | |
| UniPathway | UPA00378. |
Gene expression databases | |
| ArrayExpress | Q6P5E4. |
| Bgee | Q6P5E4. |
| CleanEx | MM_UGCGL1. |
| Genevestigator | Q6P5E4. |
| GermOnline | ENSMUSG00000037470. Mus musculus. |
Family and domain databases | |
| InterPro | IPR009448. UDP-g_GGtrans. [Graphical view] |
| PANTHER | PTHR11226. PTHR11226. 1 hit. |
| Pfam | PF06427. UDP-g_GGTase. 1 hit. [Graphical view] |
| PROSITE | PS00014. ER_TARGET. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | UGGT1. mouse. |
| NextBio | 395857. |
| SOURCE | Search... |
Entry information
| Entry name | UGGG1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q6P5E4 Secondary accession number(s): E9QQ49, Q6NV70 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
