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Q96E22 (NGBR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nogo-B receptor

Short name=NgBR
Alternative name(s):
Nuclear undecaprenyl pyrophosphate synthase 1 homolog
Gene names
Name:NUS1
Synonyms:C6orf68, NGBR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7

Essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Ref.5 Ref.7

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with DHDDS, promoting its isoprenyltransferase activity. Interacts with NPC2. Ref.6 Ref.7

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein. Note: Colocalizes with Nogo-B during VEGF and wound healing angiogenesis. Ref.6 Ref.7

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.

Sequence similarities

Belongs to the UPP synthase family.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

C10orf95Q9H7T33EBI-6949352,EBI-6949335

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 293270Nogo-B receptor
PRO_0000273167

Regions

Topological domain24 – 11693Cytoplasmic Potential
Transmembrane117 – 13519Helical; Potential
Topological domain136 – 293158Lumenal Potential

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...) Ref.7
Glycosylation2711N-linked (GlcNAc...) Ref.7

Natural variations

Natural variant1751N → Y.
Corresponds to variant rs28362518 [ dbSNP | Ensembl ].
VAR_030092
Natural variant1791D → E.
Corresponds to variant rs28362519 [ dbSNP | Ensembl ].
VAR_030093
Natural variant2101Missing.
Corresponds to variant rs1052237 [ dbSNP | Ensembl ].
VAR_030094
Natural variant2161K → R. Ref.4
Corresponds to variant rs1052239 [ dbSNP | Ensembl ].
VAR_030095
Natural variant2191T → K. Ref.4
Corresponds to variant rs1132147 [ dbSNP | Ensembl ].
VAR_030096

Sequences

Sequence LengthMass (Da)Tools
Q96E22 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E6A0C9D9B39D4BCA

FASTA29333,224
        10         20         30         40         50         60 
MTGLYELVWR VLHALLCLHR TLTSWLRVRF GTWNWIWRRC CRAASAAVLA PLGFTLRKPP 

        70         80         90        100        110        120 
AVGRNRRHHR HPRGGSCLAA AHHRMRWRAD GRSLEKLPVH MGLVITEVEQ EPSFSDIASL 

       130        140        150        160        170        180 
VVWCMAVGIS YISVYDHQGI FKRNNSRLMD EILKQQQELL GLDCSKYSPE FANSNDKDDQ 

       190        200        210        220        230        240 
VLNCHLAVKV LSPEDGKADI VRAAQDFCQL VAQKQKRPTD LDVDTLASLL SSNGCPDPDL 

       250        260        270        280        290 
VLKFGPVDST LGFLPWHIRL TEIVSLPSHL NISYEDFFSA LRQYAACEQR LGK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5118.1.
RefSeqNP_612468.1. NM_138459.3.
UniGeneHs.289008.
Hs.525826.

3D structure databases

ProteinModelPortalQ96E22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ96E22. 1 interaction.
MINTMINT-3052208.
STRING9606.ENSP00000357480.

Polymorphism databases

DMDM74762651.

Proteomic databases

MaxQBQ96E22.
PaxDbQ96E22.
PRIDEQ96E22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368494; ENSP00000357480; ENSG00000153989.
GeneID116150.
KEGGhsa:116150.
UCSCuc003pxw.3. human.

Organism-specific databases

CTD116150.
GeneCardsGC06P117997.
H-InvDBHIX0022536.
HGNCHGNC:21042. NUS1.
HPAHPA027504.
MIM610463. gene.
neXtProtNX_Q96E22.
PharmGKBPA162398248.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0020.
HOGENOMHOG000007321.
HOVERGENHBG082024.
InParanoidQ96E22.
OMAYVSVYDH.
OrthoDBEOG773XGR.
PhylomeDBQ96E22.
TreeFamTF332448.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ96E22.
CleanExHS_NUS1.
GenevestigatorQ96E22.

Family and domain databases

Gene3D3.40.1180.10. 1 hit.
InterProIPR001441. UPP_synth-like.
[Graphical view]
PfamPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMSSF64005. SSF64005. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi116150.
NextBio79794.
PROQ96E22.
SOURCESearch...

Entry information

Entry nameNGBR_HUMAN
AccessionPrimary (citable) accession number: Q96E22
Secondary accession number(s): B2RWQ4, O00251
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM