ID Q12063; PN Dehydrodolichyl diphosphate synthase complex subunit NUS1; GN NUS1; OS 559292; SL Nucleus Position: SL-0178; SL Nucleus Position: SL-0182; SL Comments: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:11086160, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14690591}. Nucleus membrane {ECO:0000269|PubMed:14690591}; Single-pass membrane protein {ECO:0000305}. DR UNIPROT: Q12063; DR UNIPROT: D6VRG0; DR PDB: 6JCN; DE Function: With SRT1 or RER2, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). {ECO:0000269|PubMed:25066056}. DE Reference Proteome: Yes; DE Interaction: P40069; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P15108; IntAct: EBI-708615; Score: 0.56 DE Interaction: P02829; IntAct: EBI-708618; Score: 0.40 DE Interaction: P32589; IntAct: EBI-3727462; Score: 0.35 DE Interaction: Q04432; IntAct: EBI-3830702; Score: 0.35 DE Interaction: P53239; IntAct: EBI-16256836; Score: 0.00 DE Interaction: P60010; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P05030; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P46970; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P15992; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P32836; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P32835; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P00950; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P33892; IntAct: EBI-16287555; Score: 0.35 DE Interaction: P00830; IntAct: EBI-16287555; Score: 0.35 GO GO:1904423; GO GO:0005783; GO GO:0005789; GO GO:0016021; GO GO:0005811; GO GO:0005635; GO GO:0031965; GO GO:0016765; GO GO:0019408; GO GO:0006486; TP Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255}; SQ MPTMIKKDDKAMEPPNEKPHRKIERDDVPESSNHIPPPESGVLKGGKVNSKTRALKAVTSIIADADENPQKKVNNETNGV SQ QKQKTEDLSKRIGKFEYLFYKFLLVLLYICFGLFRYGQYQYNKMKLRIFSIIYNHAYTPQLIRQDVIPLKKIPKRLAAIL SQ EVKPVGDVGGGVTGLLNDASEIVCWTVSAGIKHLMLYDYDGILQRNVPELRMEIHSNLAKYFGPAHVPNYAVKIPHSNKI SQ FYNLDGIETETDVGNEIEANQEKDKIAIEISLLSNRDGRETIVDLTKTMAELCAVNELSVSDITMDLVDSELKQLVGPEP SQ DLLLYFGPSLDLQGFPPWHIRLTEFYWEKDNNEVIYSVFIRGLRQYAGCKVNVGK //