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Q96E22

- NGBR_HUMAN

UniProt

Q96E22 - NGBR_HUMAN

Protein

Nogo-B receptor

Gene

NUS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator. Regulates the stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol.
    Essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery.

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. transferase activity, transferring alkyl or aryl (other than methyl) groups Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. intracellular cholesterol transport Source: MGI
    4. protein glycosylation Source: UniProtKB-UniPathway
    5. sterol homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nogo-B receptor
    Short name:
    NgBR
    Alternative name(s):
    Nuclear undecaprenyl pyrophosphate synthase 1 homolog
    Gene namesi
    Name:NUS1
    Synonyms:C6orf68, NGBR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21042. NUS1.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Single-pass type I membrane protein 2 Publications
    Note: Colocalizes with Nogo-B during VEGF and wound healing angiogenesis.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: MGI
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162398248.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 293270Nogo-B receptorPRO_0000273167Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi144 – 1441N-linked (GlcNAc...)1 Publication
    Glycosylationi271 – 2711N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ96E22.
    PaxDbiQ96E22.
    PRIDEiQ96E22.

    Expressioni

    Gene expression databases

    BgeeiQ96E22.
    CleanExiHS_NUS1.
    GenevestigatoriQ96E22.

    Organism-specific databases

    HPAiHPA027504.

    Interactioni

    Subunit structurei

    Interacts with DHDDS, promoting its isoprenyltransferase activity. Interacts with NPC2.2 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    IntActiQ96E22. 1 interaction.
    MINTiMINT-3052208.
    STRINGi9606.ENSP00000357480.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96E22.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 11693CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini136 – 293158LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei117 – 13519HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UPP synthase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0020.
    HOGENOMiHOG000007321.
    HOVERGENiHBG082024.
    InParanoidiQ96E22.
    OMAiYVSVYDH.
    OrthoDBiEOG773XGR.
    PhylomeDBiQ96E22.
    TreeFamiTF332448.

    Family and domain databases

    Gene3Di3.40.1180.10. 1 hit.
    InterProiIPR001441. UPP_synth-like.
    [Graphical view]
    PfamiPF01255. Prenyltransf. 1 hit.
    [Graphical view]
    SUPFAMiSSF64005. SSF64005. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q96E22-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGLYELVWR VLHALLCLHR TLTSWLRVRF GTWNWIWRRC CRAASAAVLA    50
    PLGFTLRKPP AVGRNRRHHR HPRGGSCLAA AHHRMRWRAD GRSLEKLPVH 100
    MGLVITEVEQ EPSFSDIASL VVWCMAVGIS YISVYDHQGI FKRNNSRLMD 150
    EILKQQQELL GLDCSKYSPE FANSNDKDDQ VLNCHLAVKV LSPEDGKADI 200
    VRAAQDFCQL VAQKQKRPTD LDVDTLASLL SSNGCPDPDL VLKFGPVDST 250
    LGFLPWHIRL TEIVSLPSHL NISYEDFFSA LRQYAACEQR LGK 293
    Length:293
    Mass (Da):33,224
    Last modified:December 1, 2001 - v1
    Checksum:iE6A0C9D9B39D4BCA
    GO

    Sequence cautioni

    The sequence AAB72234.1 differs from that shown. Reason: Frameshift at several positions.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751N → Y.
    Corresponds to variant rs28362518 [ dbSNP | Ensembl ].
    VAR_030092
    Natural varianti179 – 1791D → E.
    Corresponds to variant rs28362519 [ dbSNP | Ensembl ].
    VAR_030093
    Natural varianti210 – 2101Missing.
    Corresponds to variant rs1052237 [ dbSNP | Ensembl ].
    VAR_030094
    Natural varianti216 – 2161K → R.1 Publication
    Corresponds to variant rs1052239 [ dbSNP | Ensembl ].
    VAR_030095
    Natural varianti219 – 2191T → K.1 Publication
    Corresponds to variant rs1132147 [ dbSNP | Ensembl ].
    VAR_030096

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human.

    Polymorphism databases

    DMDMi74762651.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS5118.1.
    RefSeqi NP_612468.1. NM_138459.3.
    UniGenei Hs.289008.
    Hs.525826.

    3D structure databases

    ProteinModelPortali Q96E22.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q96E22. 1 interaction.
    MINTi MINT-3052208.
    STRINGi 9606.ENSP00000357480.

    Polymorphism databases

    DMDMi 74762651.

    Proteomic databases

    MaxQBi Q96E22.
    PaxDbi Q96E22.
    PRIDEi Q96E22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368494 ; ENSP00000357480 ; ENSG00000153989 .
    GeneIDi 116150.
    KEGGi hsa:116150.
    UCSCi uc003pxw.3. human.

    Organism-specific databases

    CTDi 116150.
    GeneCardsi GC06P117997.
    H-InvDB HIX0022536.
    HGNCi HGNC:21042. NUS1.
    HPAi HPA027504.
    MIMi 610463. gene.
    neXtProti NX_Q96E22.
    PharmGKBi PA162398248.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0020.
    HOGENOMi HOG000007321.
    HOVERGENi HBG082024.
    InParanoidi Q96E22.
    OMAi YVSVYDH.
    OrthoDBi EOG773XGR.
    PhylomeDBi Q96E22.
    TreeFami TF332448.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    GenomeRNAii 116150.
    NextBioi 79794.
    PROi Q96E22.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96E22.
    CleanExi HS_NUS1.
    Genevestigatori Q96E22.

    Family and domain databases

    Gene3Di 3.40.1180.10. 1 hit.
    InterProi IPR001441. UPP_synth-like.
    [Graphical view ]
    Pfami PF01255. Prenyltransf. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64005. SSF64005. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lymph, Muscle, Testis and Uterus.
    4. "Direct isolation of human transcribed sequences from yeast artificial chromosomes through the application of RNA fingerprinting."
      Still I.H., Vince P., Cowell J.K.
      Proc. Natl. Acad. Sci. U.S.A. 94:10373-10378(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 171-293, VARIANTS ARG-216 AND LYS-219.
    5. "Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells."
      Miao R.Q., Gao Y., Harrison K.D., Prendergast J., Acevedo L.M., Yu J., Hu F., Strittmatter S.M., Sessa W.C.
      Proc. Natl. Acad. Sci. U.S.A. 103:10997-11002(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, LACK OF TRANSFERASE ACTIVITY.
    6. "Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking."
      Harrison K.D., Miao R.Q., Fernandez-Hernando C., Suarez Y., Davalos A., Sessa W.C.
      Cell Metab. 10:208-218(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NPC2.
    7. "Nogo-B receptor is necessary for cellular dolichol biosynthesis and protein N-glycosylation."
      Harrison K.D., Park E.J., Gao N., Kuo A., Rush J.S., Waechter C.J., Lehrman M.A., Sessa W.C.
      EMBO J. 30:2490-2500(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DOLICHOL BIOSYNTHESIS, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-144 AND ASN-271, INTERACTION WITH DHDDS.

    Entry informationi

    Entry nameiNGBR_HUMAN
    AccessioniPrimary (citable) accession number: Q96E22
    Secondary accession number(s): B2RWQ4, O00251
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [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

    Miscellaneous

    Although strongly related to UPP synthase family proteins, it has no lipid transferase activity.
    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.

    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

    External Data

    Dasty 3