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Entry version 160 (25 May 2022)
Sequence version 1 (01 Dec 2001)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. 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).

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. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator (PubMed:16835300).

5 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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by phospholipids including cardiolipin, phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol and phosphatidylserine.2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Values were measured with the heterodimer. kcat is 0.58 sec(-1) with (2E,6E)-farnesyl diphosphate and isopentenyl diphosphate as substrates.1 Publication
  1. KM=11.1 µM for isopentenyl diphosphate1 Publication
  2. KM=0.68 µM for (2E,6E)-farnesyl diphosphate1 Publication

pH dependencei

Optimum pH is 8-9. Active from pH 5.5 to 9.3.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Pathwayi: Lipid metabolism

This protein is involved in Lipid metabolism.2 Publications
View all proteins of this organism that are known to be involved in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei291Isopentenyl diphosphate; via amide nitrogen1 Publication1
Binding sitei292Isopentenyl diphosphate; via amide nitrogen1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Receptor, Transferase
Biological processAngiogenesis, Differentiation, Lipid metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.5.1.87, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q96E22

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-446199, Synthesis of Dolichyl-phosphate
R-HSA-4755609, Defective DHDDS causes retinitis pigmentosa 59

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q96E22

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00378

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Dehydrodolichyl diphosphate synthase complex subunit NUS1Curated (EC:2.5.1.872 Publications)
Alternative name(s):
Cis-prenyltransferase subunit NgBR1 Publication
Nogo-B receptor1 Publication
Short name:
NgBR2 Publications
Nuclear undecaprenyl pyrophosphate synthase 1 homologCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NUS11 PublicationImported
Synonyms:C6orf68, NGBR
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:21042, NUS1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
610463, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q96E22

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000153989

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1 – 23Helical; Name=11 PublicationAdd BLAST23
Transmembranei35 – 56Helical; Name=21 PublicationAdd BLAST22
Transmembranei117 – 135Helical; Name=31 PublicationAdd BLAST19

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Congenital disorder of glycosylation 1AA (CDG1AA)1 Publication
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071210290R → H in CDG1AA; loss of function in protein glycosylation; 5-fold reduction in catalytic activity and reduced affinity for FPP and IPP.. 2 PublicationsCorresponds to variant dbSNP:rs886037858EnsemblClinVar.1
Intellectual developmental disorder, autosomal dominant 55, with seizures (MRD55)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, 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.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi100H → A: 3.5-fold reduction in catalytic activity and no marked change in affinity for FPP and IPP. 1 Publication1
Mutagenesisi196G → A: Decreases binding to DHDDS. 1 Publication1
Mutagenesisi197K → A: Decreases binding to DHDDS. 1 Publication1
Mutagenesisi200I → A: Disrupts NUS1-DHDDS heterodimerization. 1 Publication1
Mutagenesisi226L → A: Disrupts NUS1-DHDDS heterodimerization. 1 Publication1
Mutagenesisi230L → A: Disrupts NUS1-DHDDS heterodimerization. 1 Publication1
Mutagenesisi252G → A: Disrupts NUS1-DHDDS heterodimerization. 1 Publication1
Mutagenesisi253F → A: Disrupts NUS1-DHDDS heterodimerization. 1 Publication1
Mutagenesisi255P → A: Disrupts NUS1-DHDDS heterodimerization. 1 Publication1
Mutagenesisi292G → A: Almost complete loss of catalytic activity. 1 Publication1
Mutagenesisi293K → KA: Almost complete loss of catalytic activity. 1 Publication1
Mutagenesisi293Missing : Almost complete loss of catalytic activity. 1 Publication1

Keywords - Diseasei

Congenital disorder of glycosylation, Disease variant, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
116150

MalaCards human disease database

More...
MalaCardsi
NUS1
MIMi617082, phenotype
617831, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000153989

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
442835, Non-specific early-onset epileptic encephalopathy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162398248

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q96E22, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
NUS1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74762651

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002731671 – 293Dehydrodolichyl diphosphate synthase complex subunit NUS1Add BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi144N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi271N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q96E22

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q96E22

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q96E22

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q96E22

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q96E22

PeptideAtlas

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PeptideAtlasi
Q96E22

PRoteomics IDEntifications database

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PRIDEi
Q96E22

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
76366

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q96E22, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q96E22

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q96E22

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000153989, Expressed in endometrium and 217 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q96E22, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000153989, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms an active dehydrodolichyl diphosphate synthase complex with DHDDS (NUS1-DHDDS) (PubMed:28842490, PubMed:19723497, PubMed:25066056, PubMed:32817466).

Interacts with NPC2 (PubMed:21572394).

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
125481, 67 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-6701, Dehydrodolichyl diphosphate synthase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q96E22

Database of interacting proteins

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DIPi
DIP-61225N

Protein interaction database and analysis system

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IntActi
Q96E22, 24 interactors

Molecular INTeraction database

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MINTi
Q96E22

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000357480

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q96E22, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

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AlphaFoldDBi
Q96E22

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q96E22

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi290 – 292RXG motif; crucial for prenyltransferase activity1 Publication1 Publication3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains the RXG motif, which is important for substrate binding and prenyltransferase activity. The catalytic site at NUS1-DHDDS interface accomodates both the allylic and the homoallylic IPP substrates to the S1 and S2 pockets respectively. The beta-phosphate groups of IPP substrates form hydrogen bonds with the RXG motif of NUS1 and four conserved residues of DHDDS (Arg-85, Arg-205, Arg-211 and Ser-213), while the allylic isopentenyl group is pointed toward the hydrophobic tunnel of the S1 pocket where the product elongation occurs.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the UPP synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2818, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000003223

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_051870_2_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q96E22

Identification of Orthologs from Complete Genome Data

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OMAi
MPRVYEA

Database of Orthologous Groups

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OrthoDBi
1448374at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q96E22

TreeFam database of animal gene trees

More...
TreeFami
TF332448

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1180.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR038887, Nus1/NgBR
IPR001441, UPP_synth-like
IPR036424, UPP_synth-like_sf

The PANTHER Classification System

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PANTHERi
PTHR21528, PTHR21528, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01255, Prenyltransf, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF64005, SSF64005, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE6A0C9D9B39D4BCA
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08390091G → C Probable disease-associated variant found in a patient with Parkinson's disease; 40 % reduction in prenyltransferase activity. 1 Publication1
Natural variantiVAR_085036104 – 293Missing Probable disease-associated variant found in a patient with progressive myoclonus epilepsy. 1 PublicationAdd BLAST190
Natural variantiVAR_030092175N → Y. Corresponds to variant dbSNP:rs28362518Ensembl.1
Natural variantiVAR_030093179D → E. Corresponds to variant dbSNP:rs28362519EnsemblClinVar.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; 5-fold reduction in catalytic activity and reduced affinity for FPP and IPP.. 2 PublicationsCorresponds to variant dbSNP:rs886037858EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Z98172 Genomic DNA No translation available.
AL590303 Genomic DNA No translation available.
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.

The Consensus CDS (CCDS) project

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CCDSi
CCDS5118.1

NCBI Reference Sequences

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RefSeqi
NP_612468.1, NM_138459.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000368494.4; ENSP00000357480.3; ENSG00000153989.8

Database of genes from NCBI RefSeq genomes

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GeneIDi
116150

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:116150

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

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MANE-Selecti
ENST00000368494.4; ENSP00000357480.3; NM_138459.5; NP_612468.1

UCSC genome browser

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UCSCi
uc003pxw.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98172 Genomic DNA No translation available.
AL590303 Genomic DNA No translation available.
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6W2LX-ray2.31B80-293[»]
6Z1NX-ray2.30B73-293[»]
AlphaFoldDBiQ96E22
SMRiQ96E22
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi125481, 67 interactors
ComplexPortaliCPX-6701, Dehydrodolichyl diphosphate synthase complex
CORUMiQ96E22
DIPiDIP-61225N
IntActiQ96E22, 24 interactors
MINTiQ96E22
STRINGi9606.ENSP00000357480

PTM databases

GlyGeniQ96E22, 2 sites
iPTMnetiQ96E22
PhosphoSitePlusiQ96E22

Genetic variation databases

BioMutaiNUS1
DMDMi74762651

Proteomic databases

EPDiQ96E22
jPOSTiQ96E22
MassIVEiQ96E22
MaxQBiQ96E22
PaxDbiQ96E22
PeptideAtlasiQ96E22
PRIDEiQ96E22
ProteomicsDBi76366

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
32563, 111 antibodies from 22 providers

The DNASU plasmid repository

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DNASUi
116150

Genome annotation databases

EnsembliENST00000368494.4; ENSP00000357480.3; ENSG00000153989.8
GeneIDi116150
KEGGihsa:116150
MANE-SelectiENST00000368494.4; ENSP00000357480.3; NM_138459.5; NP_612468.1
UCSCiuc003pxw.4, human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
116150
DisGeNETi116150

GeneCards: human genes, protein and diseases

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GeneCardsi
NUS1
HGNCiHGNC:21042, NUS1
HPAiENSG00000153989, Low tissue specificity
MalaCardsiNUS1
MIMi610463, gene
617082, phenotype
617831, phenotype
neXtProtiNX_Q96E22
OpenTargetsiENSG00000153989
Orphaneti442835, Non-specific early-onset epileptic encephalopathy
PharmGKBiPA162398248
VEuPathDBiHostDB:ENSG00000153989

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2818, Eukaryota
GeneTreeiENSGT00390000003223
HOGENOMiCLU_051870_2_1_1
InParanoidiQ96E22
OMAiMPRVYEA
OrthoDBi1448374at2759
PhylomeDBiQ96E22
TreeFamiTF332448

Enzyme and pathway databases

UniPathwayiUPA00378
BRENDAi2.5.1.87, 2681
PathwayCommonsiQ96E22
ReactomeiR-HSA-446199, Synthesis of Dolichyl-phosphate
R-HSA-4755609, Defective DHDDS causes retinitis pigmentosa 59
SignaLinkiQ96E22

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
116150, 760 hits in 1041 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
NUS1, human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
116150
PharosiQ96E22, Tbio

Protein Ontology

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PROi
PR:Q96E22
RNActiQ96E22, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000153989, Expressed in endometrium and 217 other tissues
GenevisibleiQ96E22, HS

Family and domain databases

Gene3Di3.40.1180.10, 1 hit
InterProiView protein in InterPro
IPR038887, Nus1/NgBR
IPR001441, UPP_synth-like
IPR036424, UPP_synth-like_sf
PANTHERiPTHR21528, PTHR21528, 1 hit
PfamiView protein in Pfam
PF01255, Prenyltransf, 1 hit
SUPFAMiSSF64005, SSF64005, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNGBR_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q96E22
Secondary accession number(s): B2RWQ4, O00251
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: May 25, 2022
This is version 160 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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