Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P04844 (RPN2_HUMAN)

Last modified November 4, 2008. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

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

Hide | Top

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 oligosaccharyl transferase (OST) complex. OST seems to exist in different forms which contain at least RPN1/ribophorin-1, RPN2/ribophorin-2, OST48, DAD1, and either STT3A or STT3B.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane proteinPotential.

Tissue specificity

Expressed in all tissues tested.

Sequence similarities

Belongs to the SWP1 family.

Hide | Top

Ontologies

Keywords

   Cellular componentEndoplasmic reticulum
Membrane
   DomainSignal
Transmembrane
   Molecular functionTransferase
   PTMGlycoprotein
Phosphoprotein
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processprotein amino acid N-linked glycosylation via asparagine Ref.8

Non-traceable author statement. Source: HGNC

   Cellular componentoligosaccharyltransferase complex Ref.8

Traceable author statement. Source: HGNC

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Topological domain23 – 540518Lumenal Potential
Transmembrane541 – 56121 Potential
Transmembrane572 – 59221 Potential
Transmembrane597 – 61721 Potential
Topological domain618 – 63114Cytoplasmic Potential

Amino acid modifications

Modified residue2821Phosphothreonine
Glycosylation1061N-linked (GlcNAc...) Probable

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.3
Sequence conflict4231V → M in CAA68393. Ref.1
Sequence conflict4271A → V in CAG33180. Ref.3
Sequence conflict5711T → I in AAH13028. Ref.5

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P04844-1 [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

Hide | Top

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: 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. 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: 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 OLIGOSACCHARYL TRANSFERASE 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 OLIGOSACCHARYL TRANSFERASE 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.

Hide | Top

Cross-references

Sequence databases

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.
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.
PIRB26168.
RefSeqNP_002942.2.
UniGeneHs.370895

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP04844.

PTM databases

PhosphoSiteP04844.

Genome annotation databases

EnsemblENSG00000118705. Homo sapiens. [Contig view]
GeneID6185.
KEGGhsa:6185.

Organism-specific databases

H-InvDBHIX0015791.
HGNCHGNC:10382. RPN2.
HPAHPA008297.
MIM180490. gene.
PharmGKBPA34778.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP04844.

Gene expression databases

ArrayExpressP04844.
CleanExHS_RPN2.
GermOnlineENSG00000118705. Homo sapiens.

Family and domain databases

InterProIPR008814. Ribophorin_II.
[Graphical view]
PANTHERPTHR12640. Ribophorin_II. 1 hit.
PfamPF05817. Ribophorin_II. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio24021.
SOURCESearch...

Hide | Top

Entry information

Entry nameRPN2_HUMAN
AccessionPrimary (citable) accession number: P04844
Secondary accession number(s): Q6IBA5 expand/collapse secondary AC list , Q96E21, Q9BUQ3, Q9UBE1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 1, 2000
Last modified: November 4, 2008
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 20

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

MIM cross-references

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents