Q9NYU2 (UGGG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 100.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: UDP-glucose:glycoprotein glucosyltransferase 1 Short name=UGT1 Short name=hUGT1 EC=2.4.1.- Alternative name(s): UDP--Glc:glycoprotein glucosyltransferase UDP-glucose ceramide glucosyltransferase-like 1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1555 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. Ref.1 |
| Cofactor | Calcium or manganese. Ref.1 |
| Pathway | |
| Subunit structure | Monomer as well as in a tight complex with SEP15 By similarity. UniProtKB Q9JLA3 |
| Subcellular location | Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment Ref.1. |
| Tissue specificity | Higher levels in pancreas, skeletal muscle, kidney, and brain. Low levels in lung and heart. Ref.1 |
| Induction | By tunicamycin and A23187. Induced 3-4 fold 10 hours after treatment. Ref.1 |
| 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. Ref.1 |
| Sequence caution | The sequence AAY14885.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAB14632.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Coding sequence diversity | Alternative splicing |
| Domain | Signal |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | 'de novo' posttranslational protein folding Traceable author statement Ref.1. Source: UniProtKB post-translational protein modificationTraceable author statement. Source: Reactome protein N-linked glycosylation via asparagineTraceable author statement. Source: Reactome |
| Cellular_component | endoplasmic reticulum lumen Traceable author statement. Source: Reactome endoplasmic reticulum-Golgi intermediate compartmentInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | UDP-glucose:glycoprotein glucosyltransferase activity Inferred from direct assay Ref.1. Source: UniProtKB unfolded protein bindingInferred from direct assay Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9NYU2-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q9NYU2-2) The sequence of this isoform differs from the canonical sequence as follows: 1-24: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 42 | 42 | By similarity | ||||||
| Chain | 43 – 1555 | 1513 | UDP-glucose:glycoprotein glucosyltransferase 1 | PRO_0000012271 | |||||
Regions | |||||||||
| Region | 1244 – 1555 | 312 | Glucosyltransferase By similarity | ||||||
| Motif | 1552 – 1555 | 4 | Prevents secretion from ER Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1277 | 1 | Phosphoserine Ref.6 | ||||||
| Glycosylation | 536 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1228 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 24 | 24 | Missing in isoform 2. | VSP_036508 | |||||
Experimental info | |||||||||
| Mutagenesis | 1452 – 1457 | 6 | Missing: Inactive. Ref.1 | ||||||
| Mutagenesis | 1452 | 1 | D → A: Inactive. Ref.1 | ||||||
| Mutagenesis | 1453 | 1 | Q → A: 4% active. Ref.1 | ||||||
| Mutagenesis | 1454 | 1 | D → A: Inactive. Ref.1 | ||||||
| Mutagenesis | 1455 | 1 | L → A: 2% active. Ref.1 | ||||||
| Mutagenesis | 1456 | 1 | P → A: 41% active. Ref.1 | ||||||
| Mutagenesis | 1457 | 1 | N → A: 7% active. Ref.1 | ||||||
| Sequence conflict | 1487 | 1 | A → T in BAB14632. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity." Arnold S.M., Fessler L.I., Fessler J.H., Kaufman R.J. Biochemistry 39:2149-2163(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-1452; GLN-1453; ASP-1454; LEU-1455; PRO-1456 AND ASN-1457. Tissue: Fetal liver. |
| [2] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "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] (ISOFORM 2). Tissue: Eye. |
| [4] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1555 (ISOFORMS 1/2). Tissue: Placenta. |
| [5] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [6] | "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1277, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Web resources
| GGDB GlycoGene database |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF227905 mRNA. Translation: AAF66232.1. AC017079 Genomic DNA. Translation: AAY14735.1. AC108059 Genomic DNA. Translation: AAY14885.1. Sequence problems. BC041098 mRNA. Translation: AAH41098.1. AK023671 mRNA. Translation: BAB14632.1. Different initiation. |
| IPI | IPI00024466. IPI00619903. |
| RefSeq | NP_064505.1. NM_020120.3. |
| UniGene | Hs.34180. |
3D structure databases | |
| ProteinModelPortal | Q9NYU2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9NYU2. 2 interactions. |
| STRING | 9606.ENSP00000259253. |
Protein family/group databases | |
| CAZy | GT24. Glycosyltransferase Family 24. |
PTM databases | |
| PhosphoSite | Q9NYU2. |
Polymorphism databases | |
| DMDM | 224471872. |
Proteomic databases | |
| PaxDb | Q9NYU2. |
| PRIDE | Q9NYU2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000259253; ENSP00000259253; ENSG00000136731. ENST00000375990; ENSP00000365158; ENSG00000136731. |
| GeneID | 56886. |
| KEGG | hsa:56886. |
| UCSC | uc002tpr.3. human. |
Organism-specific databases | |
| CTD | 56886. |
| GeneCards | GC02P128848. |
| H-InvDB | HIX0002447. |
| HGNC | HGNC:15663. UGGT1. |
| HPA | HPA012761. HPA015127. |
| MIM | 605897. gene. |
| neXtProt | NX_Q9NYU2. |
| PharmGKB | PA38014. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG320899. |
| HOGENOM | HOG000184622. |
| HOVERGEN | HBG079469. |
| InParanoid | Q9NYU2. |
| KO | K11718. |
| OMA | QNIGSSD. |
| OrthoDB | EOG46WZ7H. |
| PhylomeDB | Q9NYU2. |
Enzyme and pathway databases | |
| Reactome | REACT_17015. Metabolism of proteins. |
| UniPathway | UPA00378. |
Gene expression databases | |
| ArrayExpress | Q9NYU2. |
| Bgee | Q9NYU2. |
| CleanEx | HS_UGCGL1. |
| Genevestigator | Q9NYU2. |
| GermOnline | ENSG00000136731. Homo sapiens. |
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. human. |
| GenomeRNAi | 56886. |
| NextBio | 62283. |
| SOURCE | Search... |
Entry information
| Entry name | UGGG1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9NYU2 Secondary accession number(s): Q53QP2 Q9H8I4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
