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Details on Person UniProt:Q9NP73 ALG13
| Class:Id | ReferenceGeneProduct:218399 |
|---|---|
| _chainChangeLog | chain:1-1137 added on Fri February 6 2015 |
| _displayName | UniProt:Q9NP73 ALG13 |
| _timestamp | 2025-02-21 18:54:06 |
| chain | chain:1-1137 |
| checksum | 4E56437BA2609589 |
| comment | FUNCTION Catalytic subunit of the UDP-N-acetylglucosamine transferase complex that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. On the cytoplasmic face of the endoplasmic reticulum, the dimeric ALG13/ALG14 complex catalyzes the second step of dolichol pyrophosphate biosynthesis, transferring a beta1,4-linked N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to GlcNAc-pyrophosphatedolichol (Gn-PDol) to produce N,N'-diacetylchitobiosyl diphosphodolichol. N,N'-diacetylchitobiosyl diphosphodolichol is a substrate for ALG1, the following enzyme in the biosynthetic pathway.FUNCTION Catalytic subunit of the UDP-N-acetylglucosamine transferase complex that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. On the cytoplasmic face of the endoplasmic reticulum, the dimeric ALG13/ALG14 complex catalyzes the second step of dolichol pyrophosphate biosynthesis, transferring a beta1,4-linked N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to GlcNAc-pyrophosphatedolichol (Gn-PDol) to produce N,N'-diacetylchitobiosyl diphosphodolichol. N,N'-diacetylchitobiosyl diphosphodolichol is a substrate for ALG1, the following enzyme in the biosynthetic pathway.FUNCTION No glycosyltransferase or deubiquitinase activity is detected for this potential multifunctional enzyme.CATALYTIC ACTIVITY an N-acetyl-alpha-D-glucosaminyl-diphospho-di-trans,poly-cis-dolichol + UDP-N-acetyl-alpha-D-glucosamine = an N,N'-diacetylchitobiosyl-diphospho-di-trans,poly-cis-dolichol + UDP + H(+)BIOPHYSICOCHEMICAL PROPERTIES Optimum pH is 7.0 (at 37 degrees Celsius).PATHWAY Protein modification; protein glycosylation.SUBUNIT Forms with ALG14 the active heterodimeric UDP-N-acetylglucosamine transferase complex.SUBUNIT Not able to interact with ALG14 to form an active UDP-N-acetylglucosamine transferase complex.INTERACTION Recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14.ALTERNATIVE PRODUCTS The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the glycosyltransferase 28 family.CAUTION Contains 1 OTU domain with intact active sites. However, no deubiquitinase activity is detected in vitro with this domain compared to other isolated OTU domains.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Truncated C-terminus. |
| created | [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 |
| description | recommendedName: fullName evidence="19"UDP-N-acetylglucosamine transferase subunit ALG13 ecNumber evidence="6 13"2.4.1.141 alternativeName: fullName evidence="20"Asparagine-linked glycosylation 13 homolog alternativeName: fullName evidence="20"Glycosyltransferase 28 domain-containing protein 1 |
| geneName | ALG13 CXorf45 GLT28D1 MDS031 |
| identifier | Q9NP73 |
| isSequenceChanged | FALSE |
| keyword | Alternative splicing Congenital disorder of glycosylation Disease variant Endoplasmic reticulum Epilepsy Glycosyltransferase Hydrolase Membrane Multifunctional enzyme Protease Proteomics identification Reference proteome Thiol protease Transferase Ubl conjugation pathway |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | ALG13 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8996410] ENSEMBL:ENSG00000101901 ALG13 [Homo sapiens] |
| secondaryIdentifier | ALG13_HUMAN B1AKD6 B1AKM1 B2R5L5 B7Z6J0 B7Z804 B7Z847 B7Z9A8 B7ZAJ1 B7ZB57 Q17RC3 Q5JXY9 Q9H5U8 |
| sequenceLength | 1137 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:8970379] UniProt:Q9NP73-1 ALG13 [Homo sapiens] [ReferenceIsoform:8970380] UniProt:Q9NP73-2 ALG13 [Homo sapiens] [ReferenceIsoform:8970381] UniProt:Q9NP73-3 ALG13 [Homo sapiens] [ReferenceIsoform:8970382] UniProt:Q9NP73-4 ALG13 [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:449329] ALG13(1-1137) [endoplasmic reticulum membrane] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:Q9NP73 ALG13 (218399)
