SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96E22

- NGBR_HUMAN

UniProt

Q96E22 - NGBR_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Nogo-B receptor
Gene
NUS1, C6orf68, NGBR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications
Essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery.2 Publications

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 11693Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei117 – 13519Helical; Reviewed prediction
Add
BLAST
Topological domaini136 – 293158Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162398248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 293270Nogo-B receptor
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the UPP synthase family.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 102 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

Similar proteinsi