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P04844 (RPN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2

EC=2.4.99.18
Alternative name(s):
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
RIBIIR
Ribophorin II
Short name=RPN-II
Ribophorin-2
Gene names
Name:RPN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length631 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential subunit of the N-oligosaccharyl transferase (OST) complex 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-beta-D-glycosyl linkage to a protein L-asparagine.

Pathway

Protein modification; protein glycosylation.

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. Also identified as part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP. This contains known members of the OST complex and may be a form of this complex. Ref.9 Ref.10 Ref.13

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Expressed in all tissues tested.

Sequence similarities

Belongs to the SWP1 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processSRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

aging

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular protein modification process

Traceable author statement PubMed 10660554. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Non-traceable author statement Ref.10. Source: HGNC

response to drug

Inferred from electronic annotation. Source: Ensembl

translation

Traceable author statement. Source: Reactome

   Cellular_componentautophagic vacuole membrane

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay. Source: HPA

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay. Source: HPA

oligosaccharyltransferase complex

Traceable author statement Ref.10. Source: HGNC

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionribosome binding

Inferred from electronic annotation. Source: Ensembl

transferase activity, transferring glycosyl groups

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P04844-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P04844-2)

The sequence of this isoform differs from the canonical sequence as follows:
     70-101: Missing.
     627-627: K → KRIAAEQSSRLAKYRTL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.8
Chain23 – 631609Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
PRO_0000022244

Regions

Topological domain23 – 540518Lumenal Potential
Transmembrane541 – 56121Helical; Potential
Topological domain562 – 57110Cytoplasmic Potential
Transmembrane572 – 59221Helical; Potential
Topological domain593 – 5964Lumenal Potential
Transmembrane597 – 61721Helical; Potential
Topological domain618 – 63114Cytoplasmic Potential

Amino acid modifications

Glycosylation1061N-linked (GlcNAc...) Ref.11
Cross-link154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence70 – 10132Missing in isoform 2.
VSP_043051
Alternative sequence6271K → KRIAAEQSSRLAKYRTL in isoform 2.
VSP_043052
Natural variant5971L → F.
Corresponds to variant rs34951322 [ dbSNP | Ensembl ].
VAR_054040

Experimental info

Sequence conflict1971V → L in CAA68393. Ref.1
Sequence conflict2011F → C in CAA68393. Ref.1
Sequence conflict2601A → S in CAA68393. Ref.1
Sequence conflict2861A → S in CAG33180. Ref.4
Sequence conflict4231V → M in CAA68393. Ref.1
Sequence conflict4271A → V in CAG33180. Ref.4
Sequence conflict5711T → I in AAH13028. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2000. Version 3.
Checksum: E24D7B3565141676

FASTA63169,284
        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 

« Hide

Isoform 2 [UniParc].

Checksum: FC967C1FA17A011E
Show »

FASTA61567,723

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"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] (ISOFORM 1).
[5]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton 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].
[7]"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] (ISOFORM 1).
Tissue: Muscle, Pancreas and Placenta.
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-36.
Tissue: Platelet.
[9]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX.
[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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106.
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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CANX; DERL1; DERL2; DDOST; RPN1; SELK; STT3A; VCP AND VIMP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00282 mRNA. Translation: CAA68393.1.
AJ237734 expand/collapse EMBL AC list , AJ237735, AJ237733, AJ237736, AJ237737, AJ237738, AJ237739, AJ237740, AJ237741, AJ237742, AJ237743, AJ237744, AJ237745, AJ237746, AJ237747, AJ237748, AJ237749 Genomic DNA. Translation: CAB54801.1.
AK096243 mRNA. Translation: BAG53237.1.
CR456899 mRNA. Translation: CAG33180.1.
AL031659 Genomic DNA. Translation: CAB41763.1.
AL031659 Genomic DNA. Translation: CAI42668.1.
CH471077 Genomic DNA. Translation: EAW76073.1.
BC002380 mRNA. Translation: AAH02380.2.
BC003560 mRNA. Translation: AAH03560.1.
BC013028 mRNA. Translation: AAH13028.2.
BC020222 mRNA. Translation: AAH20222.1.
PIRB26168.
RefSeqNP_001129243.1. NM_001135771.1.
NP_002942.2. NM_002951.3.
UniGeneHs.370895.

3D structure databases

ProteinModelPortalP04844.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112100. 36 interactions.
IntActP04844. 15 interactions.
MINTMINT-8247596.
STRING9606.ENSP00000237530.

PTM databases

PhosphoSiteP04844.

Polymorphism databases

DMDM9297108.

Proteomic databases

PaxDbP04844.
PRIDEP04844.

Protocols and materials databases

DNASU6185.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000237530; ENSP00000237530; ENSG00000118705. [P04844-1]
ENST00000373622; ENSP00000362724; ENSG00000118705. [P04844-2]
GeneID6185.
KEGGhsa:6185.
UCSCuc002xgp.3. human. [P04844-1]
uc002xgq.3. human. [P04844-2]

Organism-specific databases

CTD6185.
GeneCardsGC20P035806.
HGNCHGNC:10382. RPN2.
HPACAB019277.
HPA008297.
HPA025922.
MIM180490. gene.
neXtProtNX_P04844.
PharmGKBPA34778.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258688.
HOGENOMHOG000231261.
HOVERGENHBG002365.
InParanoidP04844.
KOK12667.
OMAPTHYLTK.
OrthoDBEOG78SQHS.
PhylomeDBP04844.
TreeFamTF106146.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP04844.
BgeeP04844.
CleanExHS_RPN2.
GenevestigatorP04844.

Family and domain databases

InterProIPR008814. Swp1.
[Graphical view]
PANTHERPTHR12640:SF0. PTHR12640:SF0. 1 hit.
PfamPF05817. Ribophorin_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPN2. human.
GeneWikiRPN2.
GenomeRNAi6185.
NextBio24021.
PROP04844.
SOURCESearch...

Entry information

Entry nameRPN2_HUMAN
AccessionPrimary (citable) accession number: P04844
Secondary accession number(s): Q5JYR6 expand/collapse secondary AC list , Q6IBA5, Q96E21, Q9BUQ3, Q9UBE1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 142 of the entry and version 3 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 20

Human chromosome 20: entries, gene names and cross-references to MIM