NUS1
entrez
116150
canonical
uniprot
Q96E22
canonical
ensembl
ENSG00000153989
resolver
ensp
ENSP00000357480
resolver
enst
ENST00000368494
resolver
genesymbol
NUS1
resolver
genesymbol_syn
C6orf68
resolver
genesymbol_syn
NGBR
resolver
hgnc
HGNC:21042
resolver
uniprot
B2RWQ4
resolver
uniprot
O00251
resolver
uniprot_entry
NGBR_HUMAN
resolver
uniprot_sec
B2RWQ4
resolver
uniprot_sec
O00251
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phospholipids including cardiolipin, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol and phosphatidylserine. {ECO:0000269|PubMed:28842490, ECO:0000269|PubMed:32817466}.
uniprot
proteins
amino_acid_sequence
MTGLYELVWRVLHALLCLHRTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPPAVGRNRRHHRHPRGGSCLAAAHHRMRWRADGRSLEKLPVHMGLVITEVEQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGLDCSKYSPEFANSNDKDDQVLNCHLAVKVLSPEDGKADIVRAAQDFCQLVAQKQKRPTDLDVDTLASLLSSNGCPDPDLVLKFGPVDSTLGFLPWHIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK
uniprot
proteins
disease_involvement
DISEASE: Congenital disorder of glycosylation 1AA (CDG1AA) [MIM:617082]: A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. 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. CDG1AA inheritance is autosomal recessive. {ECO:0000269|PubMed:25066056}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Intellectual developmental disorder, autosomal dominant 55, with seizures (MRD55) [MIM:617831]: A form of intellectual disability, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD55 patients suffer from seizures appearing during the first years of life. {ECO:0000269|PubMed:29100083}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.5.1.87
uniprot
proteins
function
FUNCTION: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery (PubMed:21572394, PubMed:25066056, PubMed:28842490, PubMed:32817466, PubMed:33077723). Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER) (PubMed:21572394, PubMed:25066056, PubMed:28842490, PubMed:32817466, PubMed:33077723). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length (PubMed:32817466). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol (PubMed:21572394). Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator (PubMed:16835300). {ECO:0000269|PubMed:16835300, ECO:0000269|PubMed:21572394, ECO:0000269|PubMed:25066056, ECO:0000269|PubMed:28842490, ECO:0000269|PubMed:32817466, ECO:0000269|PubMed:33077723}.
uniprot
proteins
mass_dalton
33224
uniprot
proteins
mutagenesis
MUTAGEN 100; /note="H->A: 3.5-fold reduction in catalytic activity and no marked change in affinity for FPP and IPP."; /evidence="ECO:0000269|PubMed:28842490"; MUTAGEN 196; /note="G->A: Decreases binding to DHDDS."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 197; /note="K->A: Decreases binding to DHDDS."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 200; /note="I->A: Disrupts NUS1-DHDDS heterodimerization."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 226; /note="L->A: Disrupts NUS1-DHDDS heterodimerization."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 230; /note="L->A: Disrupts NUS1-DHDDS heterodimerization."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 252; /note="G->A: Disrupts NUS1-DHDDS heterodimerization."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 253; /note="F->A: Disrupts NUS1-DHDDS heterodimerization."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 255; /note="P->A: Disrupts NUS1-DHDDS heterodimerization."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 292; /note="G->A: Almost complete loss of catalytic activity."; /evidence="ECO:0000269|PubMed:28842490"; MUTAGEN 293; /note="K->KA: Almost complete loss of catalytic activity."; /evidence="ECO:0000269|PubMed:28842490"; MUTAGEN 293; /note="Missing: Almost complete loss of catalytic activity."; /evidence="ECO:0000269|PubMed:28842490
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:25066056, ECO:0000269|PubMed:33077723}.; PATHWAY: Lipid metabolism. {ECO:0000269|PubMed:25066056, ECO:0000269|PubMed:28842490}.
uniprot
proteins
protein_family
UPP synthase family
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16835300
uniprot
proteins
pubmed
19723497
uniprot
proteins
pubmed
21572394
uniprot
proteins
pubmed
25066056
uniprot
proteins
pubmed
28842490
uniprot
proteins
pubmed
29100083
uniprot
proteins
pubmed
32817466
uniprot
proteins
pubmed
33077723
uniprot
proteins
pubmed
33798445
uniprot
proteins
pubmed
35584224
uniprot
proteins
pubmed
9294218
uniprot
proteins
sequence_length
293
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19723497, ECO:0000269|PubMed:21572394}; Multi-pass membrane protein {ECO:0000303|PubMed:21572394}. Note=Colocalizes with Nogo-B during VEGF and wound healing angiogenesis. {ECO:0000269|PubMed:19723497}.
uniprot
proteins
transmembrane_region
TRANSMEM 1..23; /note="Helical; Name=1"; /evidence="ECO:0000303|PubMed:21572394"; TRANSMEM 35..56; /note="Helical; Name=2"; /evidence="ECO:0000303|PubMed:21572394"; TRANSMEM 117..135; /note="Helical; Name=3"; /evidence="ECO:0000303|PubMed:21572394
uniprot
proteins