UniProt Accession

 RPN2_HUMAN; P04844; Q5JYR6; Q6IBA5; Q96E21; Q9BUQ3; Q9UBE1 

Genbank Protein ID

 Y00282; AJ237734; AJ237735; AJ237733; AJ237736; AJ237737; AJ237738; AJ237739; AJ237740; AJ237741; AJ237742; AJ237743; AJ237744; AJ237745; AJ237746; AJ237747; AJ237748; AJ237749; AK096243; CR456899; AL031659; AL031659; CH471077; BC002380; BC003560; BC013028; BC020222 

Genbank Nucleotide ID

 CAA68393.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; CAB54801.1; BAG53237.1; CAG33180.1; CAB41763.1; CAI42668.1; EAW76073.1; AAH02380.2; AAH03560.1; AAH13028.2; AAH20222.1 

Protein Name

 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 

Protein Synonyms/Alias

 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit; RIBIIR; Ribophorin II; RPN-II; Ribophorin-2 

Gene Name

 RPN2 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
69	GAQVPDAKKACTYIR	ubiquitination	[1]
70	AQVPDAKKACTYIRS	ubiquitination	[1]
154	ALTARLSKEETVLAT	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
243	LMNAIFSKKNFESLS	ubiquitination	[8]
244	MNAIFSKKNFESLSE	ubiquitination	[7]
306	PLTQATVKLEHAKSV	ubiquitination	[1, 4, 7]
311	TVKLEHAKSVASRAT	ubiquitination	[1, 4, 5]
322	SRATVLQKTSFTPVG	ubiquitination	[1, 4, 5, 7, 8]
368	NTVELRVKISTEVGI	ubiquitination	[7]
401	TRVTYPAKAKGTFIA	ubiquitination	[4]
442	FVRLHNQKTGQEVVF	ubiquitination	[1, 4, 5, 7, 8]
456	FVAEPDNKNVYKFEL	ubiquitination	[1, 4, 8]
460	PDNKNVYKFELDTSE	ubiquitination	[1, 4, 5, 7, 8]
491	IIGDATLKNPILWNV	ubiquitination	[1]
523	SQNLFTPKQEIQHLF	ubiquitination	[1, 8]
627	MLAQQAVKRTAH***	ubiquitination	[1, 4, 5, 6, 7]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 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. 

Sequence Annotation

 CARBOHYD 106 106 N-linked (GlcNAc...).
 CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 Alternative splicing; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Isopeptide bond; Membrane; Polymorphism; Reference proteome; Signal; Transferase; Transmembrane; Transmembrane helix; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 631 AA 

Protein Sequence

Gene Ontology

 GO:0000421; C:autophagic vacuole membrane; IEA:Compara.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0008250; C:oligosaccharyltransferase complex; TAS:HGNC.
 GO:0005791; C:rough endoplasmic reticulum; IEA:Compara.
 GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:InterPro.
 GO:0043022; F:ribosome binding; IEA:Compara.
 GO:0007568; P:aging; IEA:Compara.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0018279; P:protein N-linked glycosylation via asparagine; NAS:HGNC.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
 GO:0006412; P:translation; TAS:Reactome. 

Interpro

 IPR008814; Ribophorin_II. 

Pfam

 PF05817; Ribophorin_II 

SMART

  

PROSITE

  

PRINTS