Reviewed, UniProtKB/Swiss-Prot P04844 (RPN2_HUMAN)

Names and origin

Protein names

Recommended name:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
    EC=2.4.1.119
Alternative name(s):
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
    Ribophorin-2
    Ribophorin II
      Short name=RPN-II
    RIBIIR

Gene names

Name:

RPN2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	631 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	Essential subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains.
Catalytic activity	Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine.
Subunit structure	Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.
Tissue specificity	Expressed in all tissues tested.
Sequence similarities	Belongs to the SWP1 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane
Molecular function	Transferase
PTM	Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid N-linked glycosylation via asparagine Ref.8 Non-traceable author statement. Source: HGNC
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW oligosaccharyltransferase complex Ref.8 Traceable author statement. Source: HGNC
Molecular function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Ref.8 Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GSTK1	Q9Y2Q3	1	EBI-719731,EBI-1053767
NDRG1	Q92597	1	EBI-719731,EBI-716486
SAP18	O00422	1	EBI-719731,EBI-1044156
TMBIM4	Q9HC24	1	EBI-719731,EBI-1045545

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Ref.6
	Chain	23 – 631	609	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2		PRO_0000022244
Regions
	Topological domain	23 – 540	518	Lumenal Potential
	Transmembrane	541 – 561	21	Potential
	Transmembrane	572 – 592	21	Potential
	Transmembrane	597 – 617	21	Potential
	Topological domain	618 – 631	14	Cytoplasmic Potential
Amino acid modifications
	Modified residue	282	1	Phosphothreonine Ref.9
	Glycosylation	106	1	N-linked (GlcNAc...)
	Cross-link	154		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10
Natural variations
	Natural variant	597	1	L → F: dbSNP rs34951322.		VAR_054040
Experimental info
	Sequence conflict	197	1	V → L in CAA68393. Ref.1
	Sequence conflict	201	1	F → C in CAA68393. Ref.1
	Sequence conflict	260	1	A → S in CAA68393. Ref.1
	Sequence conflict	286	1	A → S in CAG33180. Ref.3
	Sequence conflict	423	1	V → M in CAA68393. Ref.1
	Sequence conflict	427	1	A → V in CAG33180. Ref.3
	Sequence conflict	571	1	T → I in AAH13028. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P04844-1 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: E24D7B3565141676	FASTA	631	69,284
	10 20 30 40 50 60 MAPPGSSTVF LLALTIIAST WALTPTHYLT KHDVERLKAS LDRPFTNLES AFYSIVGLSS 70 80 90 100 110 120 LGAQVPDAKK ACTYIRSNLD PSNVDSLFYA AQASQALSGC EISISNETKD LLLAAVSEDS 130 140 150 160 170 180 SVTQIYHAVA ALSGFGLPLA SQEALSALTA RLSKEETVLA TVQALQTASH LSQQADLRSI 190 200 210 220 230 240 VEEIEDLVAR LDELGGVYLQ FEEGLETTAL FVAATYKLMD HVGTEPSIKE DQVIQLMNAI 250 260 270 280 290 300 FSKKNFESLS EAFSVASAAA VLSHNRYHVP VVVVPEGSAS DTHEQAILRL QVTNVLSQPL 310 320 330 340 350 360 TQATVKLEHA KSVASRATVL QKTSFTPVGD VFELNFMNVK FSSGYYDFLV EVEGDNRYIA 370 380 390 400 410 420 NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA KAKGTFIADS HQNFALFFQL 430 440 450 460 470 480 VDVNTGAELT PHQTFVRLHN QKTGQEVVFV AEPDNKNVYK FELDTSERKI EFDSASGTYT 490 500 510 520 530 540 LYLIIGDATL KNPILWNVAD VVIKFPEEEA PSTVLSQNLF TPKQEIQHLF REPEKRPPTV 550 560 570 580 590 600 VSNTFTALIL SPLLLLFALW IRIGANVSNF TFAPSTIIFH LGHAAMLGLM YVYWTQLNMF 610 620 630 QTLKYLAILG SVTFLAGNRM LAQQAVKRTA H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins." Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I. EMBO J. 6:75-82(1987) [PubMed: 3034581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic structure of human ribophorin II gene." Iolascon A., Totaro A., Gasparini P. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle, Pancreas and Placenta.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-36. Tissue: Platelet.
[7]	"Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties." Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R. Mol. Cell 12:101-111(2003) [PubMed: 12887896] [Abstract] Cited for: COMPOSITION OF THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
[8]	"Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits." Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R. Biochemistry 44:5982-5992(2005) [PubMed: 15835887] [Abstract] Cited for: COMPOSITION OF THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
[9]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282, MASS SPECTROMETRY.
[10]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-154, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y00282 mRNA. Translation: CAA68393.1. AJ237734 , AJ237735, AJ237733, AJ237736, AJ237737, AJ237738, AJ237739, AJ237740, AJ237741, AJ237742, AJ237743, AJ237744, AJ237745, AJ237746, AJ237747, AJ237748, AJ237749 Genomic DNA. Translation: CAB54801.1. CR456899 mRNA. Translation: CAG33180.1. AL031659 Genomic DNA. Translation: CAB41763.1. BC002380 mRNA. Translation: AAH02380.2. BC003560 mRNA. Translation: AAH03560.1. BC013028 mRNA. Translation: AAH13028.2. BC020222 mRNA. Translation: AAH20222.1.
IPI	IPI00844076.
PIR	B26168.
RefSeq	NP_002942.2.
UniGene	Hs.370895
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P04844. 14 interactions.
PTM databases
PhosphoSite	P04844.
Proteomic databases
PRIDE	P04844.
Genome annotation databases
Ensembl	ENSG00000118705. Homo sapiens. [Contig view]
GeneID	6185.
UCSC	uc002xgp.1. human.
Organism-specific databases
GeneCards	GC20P035240.
H-InvDB	HIX0015791.
HGNC	HGNC:10382. RPN2.
HPA	HPA008297.
MIM	180490. gene.
PharmGKB	PA34778.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P04844.
Enzyme and pathway databases
BRENDA	2.4.1.119. 247.
Reactome	REACT_15380. Diabetes pathways.
Gene expression databases
ArrayExpress	P04844.
Bgee	P04844.
CleanEx	HS_RPN2.
GermOnline	ENSG00000118705. Homo sapiens.
Family and domain databases
InterPro	IPR008814. Ribophorin_II. [Graphical view]
PANTHER	PTHR12640. Ribophorin_II. 1 hit.
Pfam	PF05817. Ribophorin_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	24021.
SOURCE	Search...

Entry information

Entry name

RPN2_HUMAN

Accession

Primary (citable) accession number: P04844
Secondary accession number(s): Q6IBA5 , Q96E21, Q9BUQ3, Q9UBE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	December 1, 2000
Last modified:	July 7, 2009
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)