Detail Information for IndEnz0002018620
IED ID IndEnz0002018620
Enzyme Type ID protease018620
Protein Name Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13
EC 2.4.1.141
EC 3.4.19.12
Asparagine-linked glycosylation 13 homolog
Glycosyltransferase 28 domain-containing protein 1
UDP-N-acetylglucosamine transferase subunit ALG13 homolog
Gene Name ALG13 CXorf45 GLT28D1 MDS031
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDVYRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYCTCRVLTCPGQAKSIASAPGKCQDSAALTSTAFSGLDFGLLSGYLHKQALVTATHPTCTLLFPSCHAFFPLPLTPTLYKMHKGWKNYCSQKSLNEASMDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYSKQFQSSAAVCQAVLYEILYKDVFVVDEEELKTAIKLFRSGSKKNRNNAVTGSEDAHTDYKSSNQNRMEEWGACYNAENIPEGYNKGTEETKSPENPSKMPFPYKVLKALDPEIYRNVEFDVWLDSRKELQKSDYMEYAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQKMPGGYVPEIVISEMDIKQQKKMFKKIRGKEVYMTMAYGKGDPLLPPRLQHSMHYGHDPPMHYSQTAGNVMSNEHFHPQHPSPRQGRGYGMPRNSSRFINRHNMPGPKVDFYPGPGKRCCQSYDNFSYRSRSFRRSHRQMSCVNKESQYGFTPGNGQMPRGLEETITFYEVEEGDETAYPTLPNHGGPSTMVPATSGYCVGRRGHSSGKQTLNLEEGNGQSENGRYHEEYLYRAEPDYETSGVYSTTASTANLSLQDRKSCSMSPQDTVTSYNYPQKMMGNIAAVAASCANNVPAPVLSNGAAANQAISTTSVSSQNAIQPLFVSPPTHGRPVIASPSYPCHSAIPHAGASLPPPPPPPPPPPPPPPPPPPPPPPPPPPALDVGETSNLQPPPPLPPPPYSCDPSGSDLPQDTKVLQYYFNLGLQCYYHSYWHSMVYVPQMQQQLHVENYPVYTEPPLVDQTVPQCYSEVRREDGIQAEASANDTFPNADSSSVPHGAVYYPVMSDPYGQPPLPGFDSCLPVVPDYSCVPPWHPVGTAYGGSSQIHGAINPGPIGCIAPSPPASHYVPQGM
Enzyme Length 1137
Uniprot Accession Number Q9NP73
Absorption
Active Site ACT_SITE 239; /note=For deubiquitinase activity; /evidence=ECO:0000250; ACT_SITE 242; /note=Nucleophile; for deubiquitinase activity; /evidence=ECO:0000250; ACT_SITE 345; /note=For deubiquitinase activity; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519, Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427; EC=2.4.1.141; CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
DNA Binding
EC Number 2.4.1.141; 3.4.19.12
Enzyme Function FUNCTION: [Isoform 1]: Possible multifunctional enzyme with both glycosyltransferase and deubiquitinase activities.; FUNCTION: [Isoform 2]: May be involved in protein N-glycosylation, second step of the dolichol-linked oligosaccharide pathway.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (6); Chain (1); Compositional bias (2); Domain (2); Erroneous initiation (5); Erroneous termination (1); Natural variant (2); Region (4); Sequence conflict (11)
Keywords Alternative splicing;Congenital disorder of glycosylation;Disease variant;Endoplasmic reticulum;Epilepsy;Glycosyltransferase;Hydrolase;Multifunctional enzyme;Protease;Reference proteome;Thiol protease;Transferase;Ubl conjugation pathway
Interact With O95429; P49639; O60336; Q01974
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000305}. Note=Could be recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 16713569; 18985028; 20711500; 23404334; 24255178;
Motif
Gene Encoded By
Mass 126,056
Kinetics
Metal Binding
Rhea ID RHEA:23380
Cross Reference Brenda