Q9NP73 · ALG13_HUMAN
- ProteinUDP-N-acetylglucosamine transferase subunit ALG13
- GeneALG13
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1137 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Isoform 2
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.
Isoform 1
No glycosyltransferase or deubiquitinase activity is detected for this potential multifunctional enzyme.
Catalytic activity
Isoform 2
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 + H+ + UDPThis reaction proceeds in the forward direction.an N-acetyl-α-D-glucosaminyl-diphospho-di-trans,poly-cis-dolichol RHEA-COMP:19507 + CHEBI:57705 = an N,N'-diacetylchitobiosyl-diphospho-di-trans,poly-cis-dolichol RHEA-COMP:19510 + CHEBI:15378 + CHEBI:58223
Kinetics
Isoform 2
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
94.1 μM | N-acetyl-alpha-D-glucosaminyl-diphosphodolichol | 7.5 | 37 |
pH Dependence
Optimum pH is 7.0 (at 37 degrees Celsius).
Pathway
Isoform 2
Protein modification; protein glycosylation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 239 | For deubiquitinase activity | ||||
Sequence: D | ||||||
Active site | 242 | Nucleophile; for deubiquitinase activity | ||||
Sequence: C | ||||||
Active site | 345 | For deubiquitinase activity | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic side of endoplasmic reticulum membrane | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | UDP-N-acetylglucosamine transferase complex | |
Molecular Function | cysteine-type deubiquitinase activity | |
Molecular Function | N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity | |
Biological Process | dolichol-linked oligosaccharide biosynthetic process | |
Biological Process | protein N-linked glycosylation | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUDP-N-acetylglucosamine transferase subunit ALG13
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NP73
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 2
Endoplasmic reticulum membrane ; Peripheral membrane protein
Note: Recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Developmental and epileptic encephalopathy 36 (DEE36)
- Note
- DescriptionA form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. Some DEE36 patients may present with an abnormal isoelectric focusing of serum transferrin, consistent with a diagnostic classification of congenital disorder of glycosylation type I. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
- See alsoMIM:300884
Natural variants in DEE36
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_069218 | 94 | K>E | in DEE36; disease features include abnormal isoelectric focusing of serum transferrin consistent with a glycosylation defect; enzyme activity at about 17% of wild-type; decreased N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; dbSNP:rs867599353 | |
VAR_069412 | 107 | N>S | in DEE36; de novo mutation detected in unrelated patients; decreased N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; dbSNP:rs398122394 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 17 | Decreased N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity. | ||||
Sequence: I → N | ||||||
Mutagenesis | 81 | Decreased N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity. | ||||
Sequence: A → T | ||||||
Natural variant | VAR_069218 | 94 | in DEE36; disease features include abnormal isoelectric focusing of serum transferrin consistent with a glycosylation defect; enzyme activity at about 17% of wild-type; decreased N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; dbSNP:rs867599353 | |||
Sequence: K → E | ||||||
Natural variant | VAR_069412 | 107 | in DEE36; de novo mutation detected in unrelated patients; decreased N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; dbSNP:rs398122394 | |||
Sequence: N → S | ||||||
Natural variant | VAR_089351 | 213 | ||||
Sequence: S → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,022 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000254573 | 1-1137 | UDP-N-acetylglucosamine transferase subunit ALG13 | |||
Sequence: MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDVYRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYCTCRVLTCPGQAKSIASAPGKCQDSAALTSTAFSGLDFGLLSGYLHKQALVTATHPTCTLLFPSCHAFFPLPLTPTLYKMHKGWKNYCSQKSLNEASMDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYSKQFQSSAAVCQAVLYEILYKDVFVVDEEELKTAIKLFRSGSKKNRNNAVTGSEDAHTDYKSSNQNRMEEWGACYNAENIPEGYNKGTEETKSPENPSKMPFPYKVLKALDPEIYRNVEFDVWLDSRKELQKSDYMEYAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQKMPGGYVPEIVISEMDIKQQKKMFKKIRGKEVYMTMAYGKGDPLLPPRLQHSMHYGHDPPMHYSQTAGNVMSNEHFHPQHPSPRQGRGYGMPRNSSRFINRHNMPGPKVDFYPGPGKRCCQSYDNFSYRSRSFRRSHRQMSCVNKESQYGFTPGNGQMPRGLEETITFYEVEEGDETAYPTLPNHGGPSTMVPATSGYCVGRRGHSSGKQTLNLEEGNGQSENGRYHEEYLYRAEPDYETSGVYSTTASTANLSLQDRKSCSMSPQDTVTSYNYPQKMMGNIAAVAASCANNVPAPVLSNGAAANQAISTTSVSSQNAIQPLFVSPPTHGRPVIASPSYPCHSAIPHAGASLPPPPPPPPPPPPPPPPPPPPPPPPPPPALDVGETSNLQPPPPLPPPPYSCDPSGSDLPQDTKVLQYYFNLGLQCYYHSYWHSMVYVPQMQQQLHVENYPVYTEPPLVDQTVPQCYSEVRREDGIQAEASANDTFPNADSSSVPHGAVYYPVMSDPYGQPPLPGFDSCLPVVPDYSCVPPWHPVGTAYGGSSQIHGAINPGPIGCIAPSPPASHYVPQGM |
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Isoform 2
Forms with ALG14 the active heterodimeric UDP-N-acetylglucosamine transferase complex.
Isoform 1
Not able to interact with ALG14 to form an active UDP-N-acetylglucosamine transferase complex.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NP73 | SLC2A4 P14672 | 2 | EBI-947892, EBI-367146 | |
BINARY | Q9NP73-4 | BAG4 O95429 | 3 | EBI-10186621, EBI-2949658 | |
BINARY | Q9NP73-4 | HOXA1 P49639 | 3 | EBI-10186621, EBI-740785 | |
BINARY | Q9NP73-4 | MAPKBP1 O60336 | 3 | EBI-10186621, EBI-947402 | |
BINARY | Q9NP73-4 | ROR2 Q01974 | 3 | EBI-10186621, EBI-6422642 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-125 | Glycosyltransferase activity | ||||
Sequence: MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDVYRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYC | ||||||
Region | 126-400 | Deubiquitinase activity | ||||
Sequence: TCRVLTCPGQAKSIASAPGKCQDSAALTSTAFSGLDFGLLSGYLHKQALVTATHPTCTLLFPSCHAFFPLPLTPTLYKMHKGWKNYCSQKSLNEASMDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYSKQFQSSAAVCQAVLYEILYKDVFVVDEEELKTAIKLFRSGSKKNRNNAV | ||||||
Domain | 231-352 | OTU | ||||
Sequence: LFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYSK | ||||||
Domain | 492-552 | Tudor | ||||
Sequence: QYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVP | ||||||
Region | 641-673 | Disordered | ||||
Sequence: HFHPQHPSPRQGRGYGMPRNSSRFINRHNMPGP | ||||||
Region | 911-974 | Disordered | ||||
Sequence: IPHAGASLPPPPPPPPPPPPPPPPPPPPPPPPPPPALDVGETSNLQPPPPLPPPPYSCDPSGSD | ||||||
Compositional bias | 915-948 | Pro residues | ||||
Sequence: GASLPPPPPPPPPPPPPPPPPPPPPPPPPPPALD | ||||||
Compositional bias | 955-970 | Pro residues | ||||
Sequence: LQPPPPLPPPPYSCDP |
Sequence similarities
Belongs to the glycosyltransferase 28 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q9NP73-1
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.
- Name1
- Length1,137
- Mass (Da)126,056
- Last updated2010-06-15 v2
- Checksum4E56437BA2609589
Q9NP73-2
- Name2
Q9NP73-3
- Name3
Q9NP73-4
- Name4
Computationally mapped potential isoform sequences
There are 15 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A096LNJ4 | A0A096LNJ4_HUMAN | ALG13 | 132 | ||
A0A096LNJ5 | A0A096LNJ5_HUMAN | ALG13 | 77 | ||
A0A096LNL2 | A0A096LNL2_HUMAN | ALG13 | 150 | ||
A0A096LP10 | A0A096LP10_HUMAN | ALG13 | 162 | ||
A0A096LP54 | A0A096LP54_HUMAN | ALG13 | 42 | ||
A0A096LPI3 | A0A096LPI3_HUMAN | ALG13 | 1000 | ||
A0A096LPK3 | A0A096LPK3_HUMAN | ALG13 | 35 | ||
D6RE84 | D6RE84_HUMAN | ALG13 | 159 | ||
A0A1B0GVW6 | A0A1B0GVW6_HUMAN | ALG13 | 296 | ||
A0A8V8TQ59 | A0A8V8TQ59_HUMAN | ALG13 | 192 | ||
A0A087WT15 | A0A087WT15_HUMAN | ALG13 | 61 | ||
A0A087WTT9 | A0A087WTT9_HUMAN | ALG13 | 171 | ||
A0A087WVG5 | A0A087WVG5_HUMAN | ALG13 | 43 | ||
A0A087WX01 | A0A087WX01_HUMAN | ALG13 | 51 | ||
A0A087WX43 | A0A087WX43_HUMAN | ALG13 | 133 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039299 | 1-78 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_039298 | 1-104 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_039300 | 79-81 | in isoform 3 | |||
Sequence: SHA → MFT | ||||||
Alternative sequence | VSP_039301 | 128-165 | in isoform 2 | |||
Sequence: RVLTCPGQAKSIASAPGKCQDSAALTSTAFSGLDFGLL → STLPGLLQSMDLSTLKCYPPGQPEKFSAFLDKVVGLQK | ||||||
Alternative sequence | VSP_039302 | 166-1137 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 493 | in Ref. 1; BAH14677 | ||||
Sequence: Y → N | ||||||
Sequence conflict | 564 | in Ref. 1; BAH13276 | ||||
Sequence: G → D | ||||||
Sequence conflict | 588 | in Ref. 1; BAH14677 | ||||
Sequence: K → R | ||||||
Sequence conflict | 624 | in Ref. 1; BAH13276 | ||||
Sequence: D → G | ||||||
Sequence conflict | 658 | in Ref. 1; BAH13790 | ||||
Sequence: P → L | ||||||
Sequence conflict | 746-748 | in Ref. 1; BAB15521 | ||||
Sequence: PTL → ATF | ||||||
Sequence conflict | 752 | in Ref. 1; BAB15521 | ||||
Sequence: G → E | ||||||
Sequence conflict | 866 | in Ref. 1; BAH14677 | ||||
Sequence: N → K | ||||||
Alternative sequence | VSP_039303 | 899-977 | in isoform 4 | |||
Sequence: Missing | ||||||
Compositional bias | 915-948 | Pro residues | ||||
Sequence: GASLPPPPPPPPPPPPPPPPPPPPPPPPPPPALD | ||||||
Sequence conflict | 926 | in Ref. 1; BAH14244 | ||||
Sequence: P → L | ||||||
Sequence conflict | 954 | in Ref. 1; BAH14244 | ||||
Sequence: N → S | ||||||
Compositional bias | 955-970 | Pro residues | ||||
Sequence: LQPPPPLPPPPYSCDP | ||||||
Sequence conflict | 1018 | in Ref. 1; BAH14244 | ||||
Sequence: V → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF220051 EMBL· GenBank· DDBJ | AAF67644.1 EMBL· GenBank· DDBJ | mRNA | ||
AK026671 EMBL· GenBank· DDBJ | BAB15521.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK300394 EMBL· GenBank· DDBJ | BAH13276.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302729 EMBL· GenBank· DDBJ | BAH13790.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302890 EMBL· GenBank· DDBJ | BAH13833.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304712 EMBL· GenBank· DDBJ | BAH14244.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK316306 EMBL· GenBank· DDBJ | BAH14677.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316522 EMBL· GenBank· DDBJ | BAH14893.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312229 EMBL· GenBank· DDBJ | BAG35162.1 EMBL· GenBank· DDBJ | mRNA | ||
AL049563 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL096764 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471120 EMBL· GenBank· DDBJ | EAX02635.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC005336 EMBL· GenBank· DDBJ | AAH05336.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117377 EMBL· GenBank· DDBJ | AAI17378.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC117379 EMBL· GenBank· DDBJ | AAI17380.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK223154 EMBL· GenBank· DDBJ | BAD96874.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |