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Literature summary for 2.5.1.87 extracted from

  • Park, E.J.; Grabinska, K.A.; Guan, Z.; Stranecky, V.; Hartmannova, H.; Hodanova, K.; Baresova, V.; Sovova, J.; Jozsef, L.; Ondruskova, N.; Hansikova, H.; Honzik, T.; Zeman, J.; Hulkova, H.; Wen, R.; Kmoch, S.; Sessa, W.C.
    Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation (2014), Cell Metab., 20, 448-457.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.87

Cloned(Commentary)

Cloned (Comment) Organism
functional expression in Saccaromyces cerevisiae nus1DELTA/rer2DELTA/srt1DELTA mutant strain Homo sapiens
gene nus1 Saccharomyces cerevisiae
gene nus1, recombinant expression in the Saccharomyces cerevisiae triple deletion strain, nus1DELTA/rer2DELTA/srt1DELTA, functional complementation by recombinant expression of active Schizosaccharomyces pombe enzyme Schizosaccharomyces pombe

Protein Variants

Protein Variants Comment Organism
additional information generation a triple deletion strain, nus1DELTA/rer2DELTA/srt1DELTA, expressing the homomeric cis-PTase from Giardia lamblia (GlcisPT), GlcisPT on a plasmid with a URA3 marker, to support growth, functional complementation by recombinant expression of active human and Schizosaccharomyces pombe enzymes Saccharomyces cerevisiae
additional information generation of NgBR knockout mice Mus musculus
R290H a naturally occuring NgBR R290H mutation leading to congenital disorder of glycosylation. cis-PTase activity and mannose incorporation into proteins is markedly lower in NgBR R290H fibroblasts compared to control, the NgBR R290H mutant is a loss of function mutation that affects cis-PTase function of NgBR without disrupting complex formation with hCIT or Nogo-B. The reduced cis-PTase activity in fibroblasts is manifested as altered dolichol profiles in the urine or serum as assessed by mass spectrometry of all carriers of the R290H mutation, phenotype, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane enzyme NgBR is a polytypic membrane protein Homo sapiens 16020
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membrane enzyme NgBR is a polytypic membrane protein Mus musculus 16020
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microsome
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 Saccharomyces cerevisiae
-
-
microsome
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 Schizosaccharomyces pombe
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q96E22
-
-
Mus musculus Q99LJ8
-
-
Saccharomyces cerevisiae Q12063 gene nus1
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Saccharomyces cerevisiae BY4742 Q12063 gene nus1
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Schizosaccharomyces pombe Q9Y7K8 gene nus1
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Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
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 Homo sapiens
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fibroblast
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 Mus musculus
-

Synonyms

Synonyms Comment Organism
cis-prenyltransferase
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 Homo sapiens
cis-prenyltransferase
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 Mus musculus
cis-PTase
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 Homo sapiens
cis-PTase
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 Mus musculus
cis-PTase
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 Saccharomyces cerevisiae
cis-PTase
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 Schizosaccharomyces pombe
NgBR
-
 Homo sapiens
NgBR
-
 Mus musculus
Nogo-B receptor
-
 Homo sapiens
Nogo-B receptor
-
 Mus musculus

General Information

General Information Comment Organism
evolution amino acid at 4th position from the C-terminus of NgBR is a functionally and evolutionary conserved residue Homo sapiens
malfunction unique congenital disorder of glycosylation caused by a mutation in NgBR, a conserved subunit of cis-PTase. The disorder of glycosylation is caused by a loss-of-function mutation R290H in the conserved C-terminus of NgBR protein, fibroblasts isolated from patients exhibit reduced dolichol profiles. Mutation of NgBR-R290H in humans show the importance of the evolutionarily conserved residue R290 for mammalian cis-PTase activity and function Mus musculus
malfunction unique congenital disorder of glycosylation caused by a mutation in NgBR, a conserved subunit of cis-PTase. The disorder of glycosylation is caused by a loss-of-function mutation R290H in the conserved C-terminus of NgBR protein, fibroblasts isolated from patients exhibit reduced dolichol profiles. Mutation of NgBR-R290H in humans show the importance of the evolutionarily conserved residue R290 for mammalian cis-PTase activity and function. SRD5A3-CDG affects the final step in dolichol synthesis. Its clinical features are typical for CDG type 1 glycosylation disorders including psychomotor retardation, ocular malformations, cerebellar hypoplasia, skin lesions, and facial dysmorphism Homo sapiens
metabolism necessity of both dehydrodolichol diphosphate synthase, DHDDS or hCIT, and Nogo-B receptor, NgBR, for dolichol biosynthesis Mus musculus
metabolism necessity of both dehydrodolichol diphosphate synthase, DHDDS or hCIT, and Nogo-B receptor, NgBR, for dolichol biosynthesis. Single subunit cis-PTases catalyze the condensation reactions of isopentenyl diphosphate (IPP) with farnesyl diphosphate (FPP) to synthesize linear polyprenyl diphosphate with specific chain lengths. Polyprenyl pyrophosphate is dephosphorylated into polyprenol and then reduced by a polyprenol reductase to produce dolichol Homo sapiens
physiological function cis-prenyltransferase is committed to the synthesis of dolichol, the Nogo-B receptor, NgBR, is a subunit required for dolichol synthesis in humans, essential role of NgBR in dolichol synthesis and protein glycosylation. NgBR as a protein interacts with reticulon 4B, also called Nogo-B Homo sapiens
physiological function cis-prenyltransferase is committed to the synthesis of dolichol, the Nogo-B receptor, NgBR, is a subunit required for dolichol synthesis in mice, essential role of NgBR in dolichol synthesis and protein glycosylation Mus musculus