Q96E22 (NGBR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nogo-B receptor
Short name=NgBR

Alternative name(s):
Nuclear undecaprenyl pyrophosphate synthase 1 homolog

Gene names

Name:	NUS1
Synonyms:	C6orf68, NGBR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein Receptor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW intracellular cholesterol transport Inferred from genetic interaction Ref.6. Source: MGI protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway sterol homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum membrane Inferred from direct assay Ref.6. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 293	270	Nogo-B receptor		PRO_0000273167
Regions
	Topological domain	24 – 116	93	Cytoplasmic Potential
	Transmembrane	117 – 135	19	Helical; Potential
	Topological domain	136 – 293	158	Lumenal Potential
Amino acid modifications
	Glycosylation	144	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	271	1	N-linked (GlcNAc...) Ref.7
Natural variations
	Natural variant	175	1	N → Y. Corresponds to variant rs28362518 [ dbSNP | Ensembl ].		VAR_030092
	Natural variant	179	1	D → E. Corresponds to variant rs28362519 [ dbSNP | Ensembl ].		VAR_030093
	Natural variant	210	1	Missing. Corresponds to variant rs1052237 [ dbSNP | Ensembl ].		VAR_030094
	Natural variant	216	1	K → R. Ref.4 Corresponds to variant rs1052239 [ dbSNP | Ensembl ].		VAR_030095
	Natural variant	219	1	T → K. Ref.4 Corresponds to variant rs1132147 [ dbSNP | Ensembl ].		VAR_030096

Sequences

	Sequence		Length	Mass (Da)
	Q96E22 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E6A0C9D9B39D4BCA	FASTA	293	33,224
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00061142.
RefSeq	NP_612468.1. NM_138459.3.
UniGene	Hs.289008. Hs.525826.
3D structure databases
ProteinModelPortal	Q96E22.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000357480.
Polymorphism databases
DMDM	74762651.
Proteomic databases
PaxDb	Q96E22.
PRIDE	Q96E22.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000368494; ENSP00000357480; ENSG00000153989.
GeneID	116150.
KEGG	hsa:116150.
UCSC	uc003pxw.3. human.
Organism-specific databases
CTD	116150.
GeneCards	GC06P117997.
H-InvDB	HIX0022536.
HGNC	HGNC:21042. NUS1.
HPA	HPA027504.
MIM	610463. gene.
neXtProt	NX_Q96E22.
PharmGKB	PA162398248.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0020.
HOGENOM	HOG000007321.
HOVERGEN	HBG082024.
InParanoid	Q96E22.
OMA	TEEEQEP.
OrthoDB	EOG4K0QPK.
PhylomeDB	Q96E22.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q96E22.
CleanEx	HS_NUS1.
Genevestigator	Q96E22.
Family and domain databases
Gene3D	3.40.1180.10. 1 hit.
InterPro	IPR001441. UPP_synth-like. [Graphical view]
Pfam	PF01255. Prenyltransf. 1 hit. [Graphical view]
SUPFAM	SSF64005. UPP_synth. 1 hit.
PROSITE	PS01066. UPP_SYNTHASE. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	116150.
NextBio	79794.
SOURCE	Search...

Entry information

Entry name

NGBR_HUMAN

Accession

Primary (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:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.