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Identification
HMDB Protein ID HMDBP01592
Secondary Accession Numbers
  • 6888
  • HMDBP10098
Name Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Synonyms
  1. Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit
  2. RIBIIR
  3. RPN-II
  4. Ribophorin II
  5. Ribophorin-2
  6. SubName: Ribophorin II, isoform CRA_a
  7. SubName: cDNA FLJ38924 fis, clone NT2NE2011896, highly similar to Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit (EC 2.4.1.119)
Gene Name RPN2
Protein Type Enzyme
Biological Properties
General Function Involved in dolichyl-diphosphooligosaccharide-protein glycotransferase activity
Specific 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.
Pathways
  • N-Glycan biosynthesis
  • protein glycosylation
  • Protein processing in endoplasmic reticulum
Reactions
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 details
GO Classification
Biological Process
translation
SRP-dependent cotranslational protein targeting to membrane
post-translational protein modification
protein N-linked glycosylation via asparagine
Cellular Component
nucleus
oligosaccharyltransferase complex
integral to membrane
Component
membrane
cell part
endoplasmic reticulum membrane
organelle membrane
macromolecular complex
protein complex
oligosaccharyltransferase complex
Function
catalytic activity
transferase activity
transferase activity, transferring hexosyl groups
transferase activity, transferring glycosyl groups
oligosaccharyl transferase activity
dolichyl-diphosphooligosaccharide-protein glycotransferase activity
Molecular Function
dolichyl-diphosphooligosaccharide-protein glycotransferase activity
Process
metabolic process
macromolecule metabolic process
macromolecule modification
protein modification process
protein amino acid glycosylation
protein amino acid n-linked glycosylation
protein amino acid n-linked glycosylation via asparagine
Cellular Location
  1. Multi-pass membrane protein (Potential)
  2. Endoplasmic reticulum membrane
Gene Properties
Chromosome Location 20
Locus 20q12-q13.1
SNPs RPN2
Gene Sequence
>1896 bp
ATGGCGCCGCCGGGTTCAAGCACTGTCTTCCTGTTGGCCCTGACAATCATAGCCAGCACC
TGGGCTCTGACGCCCACTCACTACCTCACCAAGCATGACGTGGAGAGACTAAAAGCCTCG
CTGGATCGCCCTTTCACAAATTTGGAATCTGCCTTCTACTCCATCGTGGGACTCAGCAGC
CTTGGTGCTCAGGTGCCAGATGCAAAGAAAGCATGTACCTACATCAGATCTAACCTTGAT
CCCAGCAATGTGGATTCCCTCTTCTACGCTGCCCAGGCCAGCCAGGCCCTCTCAGGATGT
GAGATCTCTATTTCAAATGAGACCAAAGATCTGCTTCTGGCAGCTGTCAGTGAGGACTCA
TCAGTTACCCAGATCTACCATGCAGTTGCAGCTCTAAGTGGCTTTGGCCTTCCCTTGGCA
TCCCAAGAAGCACTCAGTGCCCTTACTGCTCGTCTCAGCAAGGAGGAGACTGTGCTGGCA
ACAGTCCAGGCTCTGCAGACAGCATCCCACCTGTCCCAGCAGGCTGACCTGAGGAGCATC
GTGGAGGAGATTGAGGACCTTGTTGCTCGCCTGGATGAACTCGGGGGCGTGTATCTCCAG
TTTGAAGAAGGACTGGAAACAACAGCGTTATTTGTGGCTGCCACCTACAAGCTCATGGAT
CATGTGGGGACTGAGCCATCCATTAAGGAGGATCAGGTCATCCAGCTGATGAACGCGATC
TTCAGCAAGAAGAACTTTGAGTCCCTCTCCGAAGCCTTCAGCGTGGCCTCTGCAGCTGCT
GTGCTCTCGCATAATCGCTACCACGTGCCAGTTGTGGTTGTGCCTGAGGGCTCTGCTTCC
GACACTCATGAACAGGCTATCTTGCGGTTGCAAGTCACCAATGTTCTGTCTCAGCCTCTG
ACTCAGGCCACTGTTAAACTAGAACATGCTAAATCTGTTGCTTCCAGAGCCACTGTCCTC
CAGAAGACATCCTTCACCCCTGTAGGGGATGTTTTTGAACTAAATTTCATGAACGTCAAA
TTTTCCAGTGGTTATTATGACTTCCTTGTCGAAGTTGAAGGTGACAACCGGTATATTGCA
AATACCGTAGAGCTCAGAGTCAAGATCTCCACTGAAGTTGGCATCACAAATGTTGATCTT
TCCACCGTGGATAAGGATCAGAGCATTGCACCCAAAACTACCCGGGTGACATACCCAGCC
AAAGCCAAGGGCACATTCATCGCAGACAGCCACCAGAACTTCGCCTTGTTCTTCCAGCTG
GTAGATGTGAACACTGGTGCTGAACTCACTCCTCACCAGACATTTGTCCGACTCCATAAC
CAGAAGACTGGCCAGGAAGTGGTGTTTGTTGCCGAGCCAGACAACAAGAACGTGTACAAG
TTTGAACTGGATACCTCTGAAAGAAAGATTGAATTTGACTCTGCCTCTGGCACCTACACT
CTCTACTTAATCATTGGAGATGCCACTTTGAAGAACCCAATCCTCTGGAATGTGGCTGAT
GTGGTCATCAAGTTCCCTGAGGAAGAAGCTCCCTCGACTGTCTTGTCCCAGAACCTTTTC
ACTCCAAAACAGGAAATTCAGCACCTGTTCCGCGAGCCTGAGAAGAGGCCCCCCACCGTG
GTGTCCAATACATTCACTGCCCTGATCCTCTCGCCGTTGCTTCTGCTCTTCGCTCTGTGG
ATCCGGATTGGTGCCAATGTCTCCAACTTCACTTTTGCTCCTAGCACGATTATATTTCAC
CTGGGACATGCTGCTATGCTGGGACTCATGTATGTCTACTGGACTCAGCTCAACATGTTC
CAGACCTTGAAGTACCTGGCCATCTTGGGCAGTGTGACGTTTCTGGCTGGCAATCGGATG
CTGGCCCAGCAGGCAGTCAAGAGAACAGCACATTAG
Protein Properties
Number of Residues 631
Molecular Weight 67722.73
Theoretical pI 6.067
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
MAPPGSSTVFLLALTIIASTWALTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSS
LGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDS
SVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSI
VEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAI
FSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPL
TQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIA
NTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQL
VDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYT
LYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTV
VSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMF
QTLKYLAILGSVTFLAGNRMLAQQAVKRTAH
GenBank ID Protein 5834424
UniProtKB/Swiss-Prot ID P04844
UniProtKB/Swiss-Prot Entry Name RPN2_HUMAN
PDB IDs Not Available
GenBank Gene ID AJ237734
GeneCard ID RPN2
GenAtlas ID RPN2
HGNC ID HGNC:10382
References
General References
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  4. 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. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  5. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed:11780052 ]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  7. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. doi: 10.1021/pr800468j. Epub 2008 Sep 10. [PubMed:18781797 ]
  8. Crimaudo C, Hortsch M, Gausepohl H, Meyer DI: Human ribophorins I and II: the primary structure and membrane topology of two highly conserved rough endoplasmic reticulum-specific glycoproteins. EMBO J. 1987 Jan;6(1):75-82. [PubMed:3034581 ]
  9. Kelleher DJ, Karaoglu D, Mandon EC, Gilmore R: Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol Cell. 2003 Jul;12(1):101-11. [PubMed:12887896 ]
  10. Shibatani T, David LL, McCormack AL, Frueh K, Skach WR: Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry. 2005 Apr 26;44(16):5982-92. [PubMed:15835887 ]