P04844 (RPN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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
RIBIIR
Ribophorin II
Short name=RPN-II
Ribophorin-2

Gene names

Name:

RPN2

Organism

Homo sapiens (Human)

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 Transmembrane helix
Molecular function	Transferase
PTM	Glycoprotein Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Non-traceable author statement Ref.8. Source: HGNC
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA oligosaccharyltransferase complex Traceable author statement Ref.8. Source: HGNC
Molecular function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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	Helical; Potential
	Transmembrane	572 – 592	21	Helical; Potential
	Transmembrane	597 – 617	21	Helical; Potential
	Topological domain	618 – 631	14	Cytoplasmic Potential
Amino acid modifications
	Modified residue	282	1	Phosphothreonine Ref.9
	Glycosylation	106	1	N-linked (GlcNAc...) Ref.11
	Cross-link	154		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10
Natural variations
	Natural variant	597	1	L → F. Corresponds to variant rs34951322 [ dbSNP | Ensembl ].		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 [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. Tissue: Cervix carcinoma.
[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]	"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.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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	IPI00028635.
PIR	B26168.
RefSeq	NP_001129243.1. NM_001135771.1. NP_002942.2. NM_002951.3.
UniGene	Hs.370895.
3D structure databases
ProteinModelPortal	P04844.
ModBase	Search...
Protein-protein interaction databases
IntAct	P04844. 10 interactions.
STRING	P04844.
PTM databases
PhosphoSite	P04844.
Polymorphism databases
DMDM	9297108.
Proteomic databases
PRIDE	P04844.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000237530; ENSP00000237530; ENSG00000118705.
GeneID	6185.
KEGG	hsa:6185.
UCSC	uc002xgp.1. human.
Organism-specific databases
CTD	6185.
GeneCards	GC20P035806.
H-InvDB	HIX0015791.
HGNC	HGNC:10382. RPN2.
HPA	CAB019277. HPA008297. HPA025922.
MIM	180490. gene.
neXtProt	NX_P04844.
PharmGKB	PA34778.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000002635.
HOGENOM	HBG283937.
HOVERGEN	HBG002365.
InParanoid	P04844.
OMA	TQLNMFQ.
OrthoDB	EOG4C87S7.
PhylomeDB	P04844.
Enzyme and pathway databases
Reactome	REACT_15380. Diabetes pathways. REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P04844.
Bgee	P04844.
CleanEx	HS_RPN2.
Genevestigator	P04844.
GermOnline	ENSG00000118705. Homo sapiens.
Family and domain databases
InterPro	IPR008814. Ribophorin_II. [Graphical view]
KO	K12667.
PANTHER	PTHR12640. Ribophorin_II. 1 hit.
Pfam	PF05817. Ribophorin_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 118 of the entry and version 3 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.