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Entry version 147 (16 Oct 2019)
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). 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).4 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_section">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_section">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.1 Publication

<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_section">'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.

    <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

    • dehydrodolichyl diphosphate synthase activity Source: UniProtKB

    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

    Enzyme and pathway databases

    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

    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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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)

    More...
    MIMi
    610463 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q96E22

    <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

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

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 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.
    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
    Mental retardation, autosomal dominant 55, with seizures (MRD55)1 Publication
    The disease is caused by mutations 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_and_biotech_section">'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
    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 mutation, 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 Undetermined early-onset epileptic encephalopathy

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA162398248

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q96E22

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    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.<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_processing_section">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

    More...
    jPOSTi
    Q96E22

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q96E22

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q96E22

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

    More...
    PaxDbi
    Q96E22

    PeptideAtlas

    More...
    PeptideAtlasi
    Q96E22

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q96E22

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    76366

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    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

    More...
    Bgeei
    ENSG00000153989 Expressed in 200 organ(s), highest expression level in endometrium

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q96E22 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA027504

    <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_section">'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_section">'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 (PubMed:28842490, PubMed:19723497, PubMed:25066056).

    Interacts with NPC2 (PubMed:21572394).

    4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9H7T33EBI-6949352,EBI-6949335

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    125481, 27 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q96E22

    Database of interacting proteins

    More...
    DIPi
    DIP-61225N

    Protein interaction database and analysis system

    More...
    IntActi
    Q96E22, 24 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q96E22

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000357480

    <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 Publication3

    <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
    COG0020 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000003223

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000007321

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q96E22

    KEGG Orthology (KO)

    More...
    KOi
    K19177

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    TEIFCLQ

    Database of Orthologous Groups

    More...
    OrthoDBi
    1448374at2759

    Database for complete collections of gene phylogenies

    More...
    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

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

    The PANTHER Classification System

    More...
    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

    More...
    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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_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; 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

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    More...
    CCDSi
    CCDS5118.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_612468.1, NM_138459.3

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000368494; ENSP00000357480; ENSG00000153989

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    116150

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:116150

    UCSC genome browser

    More...
    UCSCi
    uc003pxw.4 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <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

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Protein-protein interaction databases

    BioGridi125481, 27 interactors
    CORUMiQ96E22
    DIPiDIP-61225N
    IntActiQ96E22, 24 interactors
    MINTiQ96E22
    STRINGi9606.ENSP00000357480

    PTM databases

    iPTMnetiQ96E22
    PhosphoSitePlusiQ96E22

    Polymorphism and mutation databases

    BioMutaiNUS1
    DMDMi74762651

    Proteomic databases

    EPDiQ96E22
    jPOSTiQ96E22
    MassIVEiQ96E22
    MaxQBiQ96E22
    PaxDbiQ96E22
    PeptideAtlasiQ96E22
    PRIDEiQ96E22
    ProteomicsDBi76366

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    116150
    DisGeNETi116150

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    NUS1
    HGNCiHGNC:21042 NUS1
    HPAiHPA027504
    MalaCardsiNUS1
    MIMi610463 gene
    617082 phenotype
    617831 phenotype
    neXtProtiNX_Q96E22
    OpenTargetsiENSG00000153989
    Orphaneti442835 Undetermined early-onset epileptic encephalopathy
    PharmGKBiPA162398248

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2818 Eukaryota
    COG0020 LUCA
    GeneTreeiENSGT00390000003223
    HOGENOMiHOG000007321
    InParanoidiQ96E22
    KOiK19177
    OMAiTEIFCLQ
    OrthoDBi1448374at2759
    PhylomeDBiQ96E22
    TreeFamiTF332448

    Enzyme and pathway databases

    UniPathwayiUPA00378
    ReactomeiR-HSA-446199 Synthesis of Dolichyl-phosphate
    R-HSA-4755609 Defective DHDDS causes retinitis pigmentosa 59

    Miscellaneous databases

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

    More...
    ChiTaRSi
    NUS1 human

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

    More...
    GenomeRNAii
    116150
    PharosiQ96E22

    Protein Ontology

    More...
    PROi
    PR:Q96E22

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000153989 Expressed in 200 organ(s), highest expression level in endometrium
    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    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_and_isoforms">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: October 16, 2019
    This is version 147 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

    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. SIMILARITY comments
      Index of protein domains and families
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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