CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002174
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 
Protein Synonyms/Alias
 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit; Ribophorin I; RPN-I; Ribophorin-1 
Gene Name
 RPN1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
48DLSSHLAKVTAEVVLubiquitination[1]
116SGRFFTVKLPVALDPubiquitination[1, 2, 3, 4]
187RNVESYTKLGNPTRSacetylation[5]
187RNVESYTKLGNPTRSubiquitination[1, 2, 4, 6, 7]
215AYSQDTFKVHYENNSubiquitination[2]
258KHTGAVLKGPFSRYDubiquitination[2, 3, 4]
281ISSIRSFKTILPAAAubiquitination[2, 6, 7]
352LGDQYALKMRFVDHVubiquitination[2]
371VIDSLTVKIILPEGAubiquitination[2]
379IILPEGAKNIEIDSPubiquitination[1, 2, 4]
413RPVIVAYKKNLVEQHubiquitination[2]
488QVLTLVNKRIGLYRHubiquitination[1, 2, 8]
504DETVNRYKQSRDISTubiquitination[2]
516ISTLNSGKKSLETEHubiquitination[2]
538ALLQSRLKTEGSDLCubiquitination[1, 2, 8, 9]
553DRVSEMQKLDAQVKEubiquitination[1, 4, 7]
559QKLDAQVKELVLKSAubiquitination[1, 2, 3, 4, 6, 7]
578RLVAGKLKKDTYIENubiquitination[1]
579LVAGKLKKDTYIENEubiquitination[4]
592NEKLISGKRQELVTKubiquitination[2, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
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
 MOD_RES 187 187 N6-acetyllysine.
 CARBOHYD 299 299 N-linked (GlcNAc...).  
Keyword
 Acetylation; Complete proteome; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 607 AA 
Protein Sequence
MEAPAAGLFL LLLLGTWAPA PGSASSEAPP LINEDVKRTV DLSSHLAKVT AEVVLAHLGG 60
GSTSRATSFL LALEPELEAR LAHLGVQVKG EDEEENNLEV RETKIKGKSG RFFTVKLPVA 120
LDPGAKISVI VETVYTHVLH PYPTQITQSE KQFVVFEGNH YFYSPYPTKT QTMRVKLASR 180
NVESYTKLGN PTRSEDLLDY GPFRDVPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG 240
NIAVEENVDL KHTGAVLKGP FSRYDYQRQP DSGISSIRSF KTILPAAAQD VYYRDEIGNV 300
STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA LKMRFVDHVF 360
DEQVIDSLTV KIILPEGAKN IEIDSPYEIS RAPDELHYTY LDTFGRPVIV AYKKNLVEQH 420
IQDIVVHYTF NKVLMLQEPL LVVAAFYILF FTVIIYVRLD FSITKDPAAE ARMKVACITE 480
QVLTLVNKRI GLYRHFDETV NRYKQSRDIS TLNSGKKSLE TEHKALTSEI ALLQSRLKTE 540
GSDLCDRVSE MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI 600
DHILDAL 607 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0008250; C:oligosaccharyltransferase complex; TAS:HGNC.
 GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
 GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:InterPro.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:HGNC.
 GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
 GO:0006412; P:translation; TAS:Reactome. 
Interpro
 IPR007676; Ribophorin_I. 
Pfam
 PF04597; Ribophorin_I 
SMART
  
PROSITE
  
PRINTS