DHDDS
entrez
79947
canonical
uniprot
Q86SQ9
canonical
ensembl
ENSG00000117682
resolver
ensp
ENSP00000236342
resolver
ensp
ENSP00000353104
resolver
ensp
ENSP00000434219
resolver
ensp
ENSP00000434984
resolver
ensp
ENSP00000515248
resolver
ensp
ENSP00000551524
resolver
ensp
ENSP00000551526
resolver
ensp
ENSP00000551528
resolver
ensp
ENSP00000551530
resolver
ensp
ENSP00000551531
resolver
ensp
ENSP00000551533
resolver
ensp
ENSP00000631165
resolver
genesymbol
DHDDS
resolver
genesymbol_syn
HDS
resolver
hgnc
HGNC:20603
resolver
uniprot
B7Z4B9
resolver
uniprot
B7ZB20
resolver
uniprot
D3DPK7
resolver
uniprot
D3DPK8
resolver
uniprot
D3DPK9
resolver
uniprot
E9KL43
resolver
uniprot
Q5T0A4
resolver
uniprot
Q8NE90
resolver
uniprot
Q9BTG5
resolver
uniprot
Q9BTK3
resolver
uniprot
Q9H905
resolver
uniprot_entry
DHDDS_HUMAN
resolver
uniprot_sec
B7Z4B9
resolver
uniprot_sec
B7ZB20
resolver
uniprot_sec
D3DPK7
resolver
uniprot_sec
D3DPK8
resolver
uniprot_sec
D3DPK9
resolver
uniprot_sec
E9KL43
resolver
uniprot_sec
Q5T0A4
resolver
uniprot_sec
Q8NE90
resolver
uniprot_sec
Q9BTG5
resolver
uniprot_sec
Q9BTK3
resolver
uniprot_sec
Q9H905
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phospholipids including cardiolipin, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol and phosphatidylserine. {ECO:0000269|PubMed:28842490}.
uniprot
proteins
amino_acid_sequence
MSWIKEGELSLWERFCANIIKAGPMPKHIAFIMDGNRRYAKKCQVERQEGHSQGFNKLAETLRWCLNLGILEVTVYAFSIENFKRSKSEVDGLMDLARQKFSRLMEEKEKLQKHGVCIRVLGDLHLLPLDLQELIAQAVQATKNYNKCFLNVCFAYTSRHEISNAVREMAWGVEQGLLDPSDISESLLDKCLYTNRSPHPDILIRTSGEVRLSDFLLWQTSHSCLVFQPVLWPEYTFWNLFEAILQFQMNHSVLQKARDMYAEERKRQQLERDQATVTEQLLREGLQASGDAQLRRTRLHKLSARREERVQGFLQALELKRADWLARLGTASA
uniprot
proteins
disease_involvement
DISEASE: Retinitis pigmentosa 59 (RP59) [MIM:613861]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:21295282, ECO:0000269|PubMed:21295283, ECO:0000269|PubMed:28842490}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental delay and seizures with or without movement abnormalities (DEDSM) [MIM:617836]: An autosomal dominant neurodevelopmental disorder characterized by global developmental delay, variable intellectual disability, and early-onset seizures with a myoclonic component. Most patients have delayed motor development and show abnormal movements, including ataxia, dystonia, and tremor. {ECO:0000269|PubMed:29100083, ECO:0000269|PubMed:33077723}. Note=The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Congenital disorder of glycosylation 1BB (CDG1BB) [MIM:621567]: 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. CDG1BB is an autosomal recessive form clinically characterized by axial hypotonia, peripheral hypertonia, enlarged liver, micropenis, cryptorchidism, sensorineural deafness, and seizures. {ECO:0000269|PubMed:27343064}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.5.1.87
uniprot
proteins
function
FUNCTION: With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery (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: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). {ECO:0000269|PubMed:21572394, ECO:0000269|PubMed:25066056, ECO:0000269|PubMed:28842490, ECO:0000269|PubMed:32817466, ECO:0000269|PubMed:33077723}.
uniprot
proteins
mass_dalton
38657
uniprot
proteins
mutagenesis
MUTAGEN 12; /note="W->A: Markedly decreases phosphatidylinositol-mediated activation of cis-prenyltransferase activity resulting in products with longer chain length; when associated with A-15 and A-19."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 15; /note="F->A: Markedly decreases phosphatidylinositol-mediated activation of cis-prenyltransferase activity resulting in products with longer chain length; when associated with A-12 and A-19."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 19; /note="I->A: Markedly decreases phosphatidylinositol-mediated activation of cis-prenyltransferase activity resulting in products with longer chain length; when associated with A-12 and A-15."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 34; /note="D->A,E,N: Strongly reduced cis-prenyltransferase activity."; /evidence="ECO:0000269|PubMed:33077723"; MUTAGEN 38; /note="R->H: Strongly reduced cis-prenyltransferase activity."; /evidence="ECO:0000269|PubMed:33077723"; MUTAGEN 106..109; /note="Missing: Affects chain elongation resulting in shorter products."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 306; /note="R->A: Delays cell growth; when associated with A-313 and A-317."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 313; /note="F->A: Delays cell growth; when associated with A-306 and A-317."; /evidence="ECO:0000269|PubMed:32817466"; MUTAGEN 317; /note="L->A: Delays cell growth; when associated with A-306 and A-313."; /evidence="ECO:0000269|PubMed:32817466
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:25066056}.; PATHWAY: Lipid metabolism. {ECO:0000269|PubMed:28842490}.
uniprot
proteins
protein_family
UPP synthase family
uniprot
proteins
pubmed
12591616
uniprot
proteins
pubmed
14652022
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
20736409
uniprot
proteins
pubmed
21295282
uniprot
proteins
pubmed
21295283
uniprot
proteins
pubmed
21572394
uniprot
proteins
pubmed
25066056
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27343064
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
sequence_length
333
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14652022}; Peripheral membrane protein {ECO:0000269|PubMed:14652022}. Note=colocalizes with calnexin.
uniprot
proteins