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Protein

Dehydrodolichyl diphosphate synthase complex subunit NUS1

Gene

NUS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

With DHDDS, 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). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator.3 Publications

Miscellaneous

NUS1 seems to exist in two topological orientations, a minor glycosylated species with its C-terminus oriented towards the lumen regulating NPC2 stability, and a major fraction oriented with its C-terminus directed towards the cytosol where it regulates cis-IPTase activity.1 Publication

Catalytic activityi

(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55).1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cell differentiation Source: UniProtKB-KW
  • cholesterol homeostasis Source: Ensembl
  • dolichol biosynthetic process Source: MGI
  • dolichyl diphosphate biosynthetic process Source: Reactome
  • protein mannosylation Source: Ensembl
  • regulation of intracellular cholesterol transport Source: MGI

Keywordsi

Molecular functionDevelopmental protein, Receptor, Transferase
Biological processAngiogenesis, Differentiation

Enzyme and pathway databases

ReactomeiR-HSA-446199. Synthesis of Dolichyl-phosphate.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrodolichyl diphosphate synthase complex subunit NUS1Curated (EC:2.5.1.871 Publication)
Alternative name(s):
Di-trans,poly-cis-decaprenylcistransferaseCurated
Nogo-B receptor1 Publication
Short name:
NgBR1 Publication
Nuclear undecaprenyl pyrophosphate synthase 1 homologCurated
Gene namesi
Name:NUS1
Synonyms:C6orf68, NGBR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000153989.7.
HGNCiHGNC:21042. NUS1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei1 – 23Helical; Name=11 PublicationAdd BLAST23
Transmembranei35 – 56Helical; Name=21 PublicationAdd BLAST22
Transmembranei117 – 135Helical; Name=31 PublicationAdd BLAST19

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1AA (CDG1AA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:617082
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071210290R → H in CDG1AA; loss of function in protein glycosylation. 1 Publication1

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

DisGeNETi116150.
MIMi617082. phenotype.
OpenTargetsiENSG00000153989.
PharmGKBiPA162398248.

Polymorphism and mutation databases

BioMutaiNUS1.
DMDMi74762651.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002731671 – 293Dehydrodolichyl diphosphate synthase complex subunit NUS1Add BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi144N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi271N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ96E22.
MaxQBiQ96E22.
PaxDbiQ96E22.
PeptideAtlasiQ96E22.
PRIDEiQ96E22.

PTM databases

iPTMnetiQ96E22.
PhosphoSitePlusiQ96E22.

Expressioni

Gene expression databases

BgeeiENSG00000153989.
CleanExiHS_NUS1.
GenevisibleiQ96E22. HS.

Organism-specific databases

HPAiHPA027504.

Interactioni

Subunit structurei

Forms an active dehydrodolichyl diphosphate synthase complex with DHDDS. Interacts with NPC2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C10orf95Q9H7T33EBI-6949352,EBI-6949335

Protein-protein interaction databases

BioGridi125481. 26 interactors.
CORUMiQ96E22.
DIPiDIP-61225N.
IntActiQ96E22. 4 interactors.
MINTiMINT-3052208.
STRINGi9606.ENSP00000357480.

Structurei

3D structure databases

ProteinModelPortaliQ96E22.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the UPP synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2818. Eukaryota.
COG0020. LUCA.
GeneTreeiENSGT00390000003223.
HOGENOMiHOG000007321.
HOVERGENiHBG082024.
InParanoidiQ96E22.
KOiK19177.
OMAiHIRLTEF.
OrthoDBiEOG091G0YHE.
PhylomeDBiQ96E22.
TreeFamiTF332448.

Family and domain databases

Gene3Di3.40.1180.10. 2 hits.
InterProiView protein in InterPro
IPR001441. UPP_synth-like.
PfamiView protein in Pfam
PF01255. Prenyltransf. 1 hit.
SUPFAMiSSF64005. SSF64005. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96E22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGLYELVWR VLHALLCLHR TLTSWLRVRF GTWNWIWRRC CRAASAAVLA
60 70 80 90 100
PLGFTLRKPP AVGRNRRHHR HPRGGSCLAA AHHRMRWRAD GRSLEKLPVH
110 120 130 140 150
MGLVITEVEQ EPSFSDIASL VVWCMAVGIS YISVYDHQGI FKRNNSRLMD
160 170 180 190 200
EILKQQQELL GLDCSKYSPE FANSNDKDDQ VLNCHLAVKV LSPEDGKADI
210 220 230 240 250
VRAAQDFCQL VAQKQKRPTD LDVDTLASLL SSNGCPDPDL VLKFGPVDST
260 270 280 290
LGFLPWHIRL TEIVSLPSHL NISYEDFFSA LRQYAACEQR LGK
Length:293
Mass (Da):33,224
Last modified:December 1, 2001 - v1
Checksum:iE6A0C9D9B39D4BCA
GO

Sequence cautioni

The sequence AAB72234 differs from that shown. Reason: Frameshift at several positions.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030092175N → Y. Corresponds to variant dbSNP:rs28362518Ensembl.1
Natural variantiVAR_030093179D → E. Corresponds to variant dbSNP:rs28362519Ensembl.1
Natural variantiVAR_030094210Missing . Corresponds to variant dbSNP:rs1052237Ensembl.1
Natural variantiVAR_030095216K → R1 PublicationCorresponds to variant dbSNP:rs1052239Ensembl.1
Natural variantiVAR_030096219T → K1 PublicationCorresponds to variant dbSNP:rs1132147Ensembl.1
Natural variantiVAR_071210290R → H in CDG1AA; loss of function in protein glycosylation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98172, AL590303 Genomic DNA. Translation: CAI19895.1.
AL590303, Z98172 Genomic DNA. Translation: CAH71370.1.
CH471051 Genomic DNA. Translation: EAW48201.1.
BC013026 mRNA. Translation: AAH13026.1.
BC063794 mRNA. Translation: AAH63794.1.
BC066910 mRNA. Translation: AAH66910.1.
BC110325 mRNA. Translation: AAI10326.1.
BC150654 mRNA. Translation: AAI50655.1.
BC150655 mRNA. Translation: AAI50656.1.
U82319 mRNA. Translation: AAB72234.1. Frameshift.
CCDSiCCDS5118.1.
RefSeqiNP_612468.1. NM_138459.3.
UniGeneiHs.289008.
Hs.525826.

Genome annotation databases

EnsembliENST00000368494; ENSP00000357480; ENSG00000153989.
GeneIDi116150.
KEGGihsa:116150.
UCSCiuc003pxw.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiNGBR_HUMAN
AccessioniPrimary (citable) accession number: Q96E22
Secondary accession number(s): B2RWQ4, O00251
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: September 27, 2017
This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families