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UniProtKB/Swiss-Prot entry P04844


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RPN2_HUMAN
Primary accession number P04844
Secondary accession numbers Q6IBA5 Q96E21 Q9BUQ3 Q9UBE1
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on December 1, 2000 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 [Precursor]
Synonyms EC 2.4.1.119
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
Ribophorin-2
Ribophorin II
RPN-II
RIBIIR
Gene name
Name: RPN2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3034581 [NCBI, ExPASy, EBI, Israel, Japan]
Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I.;
"Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins.";
EMBO J. 6:75-82(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Iolascon A., Totaro A., Gasparini P.;
"Genomic structure of human ribophorin II gene.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, Pancreas, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 23-36.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
COMPOSITION OF THE OLIGOSACCHARYL TRANSFERASE COMPLEX.
DOI=10.1016/S1097-2765(03)00243-0; PubMed=12887896 [NCBI, ExPASy, EBI, Israel, Japan]
Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
"Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties.";
Mol. Cell 12:101-111(2003).
[8]
COMPOSITION OF THE OLIGOSACCHARYL TRANSFERASE COMPLEX.
DOI=10.1021/bi047328f; PubMed=15835887 [NCBI, ExPASy, EBI, Israel, Japan]
Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.;
"Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits.";
Biochemistry 44:5982-5992(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00282; CAA68393.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237734; CAB54801.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237735; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237733; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237736; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237737; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237738; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237739; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237740; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237741; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237742; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237743; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237744; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237745; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237746; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237747; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237748; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ237749; CAB54801.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456899; CAG33180.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031659; CAB41763.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002380; AAH02380.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003560; AAH03560.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013028; AAH13028.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020222; AAH20222.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B26168; B26168.
RefSeq NP_002942.2; -.
UniGene Hs.370895
3D structure databases
ModBase P04844.
Protein-protein interaction databases
IntAct P04844; -.
PTM databases
PhosphoSite P04844; -.
Organism-specific databases
H-InvDB HIX0015791; -.
HGNC HGNC:10382; RPN2.
GenAtlas RPN2.
HPA HPA008297; -.
MIM 180490; gene. [NCBI / EBI]
PharmGKB PA34778; -.
GeneCards P04844.
Gene expression databases
ArrayExpress P04844; -.
CleanEx HS_RPN2; -.
GermOnline ENSG00000118705; Homo sapiens.
Ontologies
GO
GO:0008250; Cellular component: oligosaccharyltransferase complex (traceable author statement from HGNC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0018279; Biological process: protein amino acid N-linked glycosylation via asparagine (non-traceable author statement from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR008814; Ribophorin_II.
Graphical view of domain structure.
PANTHER PTHR12640; Ribophorin_II; 1.
Pfam PF05817; Ribophorin_II; 1.
Pfam graphical view of domain structure.
BLOCKS P04844.
ProtoNet P04844.
Genome annotation databases
Ensembl ENSG00000118705; Homo sapiens. [Contig view]
GeneID 6185; -.
KEGG hsa:6185; -.
Phylogenomic databases
HOVERGEN P04844; -.
Other
NextBio 24021; -.
SOURCE RPN2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein; Signal; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    22  22      
CHAIN   23   631  609     Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2. PRO_0000022244
TOPO_DOM   23   540  518     Lumenal (Potential). 
TRANSMEM   541   561  21     Potential. 
TRANSMEM   572   592  21     Potential. 
TRANSMEM   597   617  21     Potential. 
TOPO_DOM   618   631  14     Cytoplasmic (Potential). 
MOD_RES   282   282        Phosphothreonine. 
CARBOHYD   106   106        N-linked (GlcNAc...) (Probable). 
CONFLICT   197   197        V -> L (in Ref. 1; CAA68393). 
CONFLICT   201   201        F -> C (in Ref. 1; CAA68393). 
CONFLICT   260   260        A -> S (in Ref. 1; CAA68393). 
CONFLICT   286   286        A -> S (in Ref. 3; CAG33180). 
CONFLICT   423   423        V -> M (in Ref. 1; CAA68393). 
CONFLICT   427   427        A -> V (in Ref. 3; CAG33180). 
CONFLICT   571   571        T -> I (in Ref. 5; AAH13028). 
Sequence information
Length: 631 AA [This is the length of the unprocessed precursor] Molecular weight: 69284 Da [This is the MW of the unprocessed precursor] CRC64: E24D7B3565141676 [This is a checksum on the sequence]
        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 

P04844 in FASTA format

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