CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002444
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
114SGRFFTVKLPVALDPacetylation[1]
185RNVESHTKLGNPSRSacetylation[1]
202ILDYGPFKDIPAYSQacetylation[1]
514ISTLNSGKKSLETEHacetylation[1]
536AVLQSRLKTEGSDLCacetylation[1]
551DRVSEMQKLDAQVKEacetylation[1]
557QKLDAQVKELVLKSAacetylation[1]
597KRQELVTKIDHILDAacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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 185 185 N6-acetyllysine (By similarity).
 CARBOHYD 297 297 N-linked (GlcNAc...) (Potential).  
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
 605 AA 
Protein Sequence
MEAPIVLLLL LWLALAPTPG SASSEAPPLV NEDVKRTVDL SSHLAKVTAE VVLAHPGGGS 60
TARASSFVLA LEPELESRLA HLGVQVKGED EEDNNLEVRE TKMKGKSGRF FTVKLPVALD 120
PGSKISIVVE TVYTHVLHPY PTQITQSEKQ FVVFEGNHYF YSPYPTKTQT MRVRLASRNV 180
ESHTKLGNPS RSEDILDYGP FKDIPAYSQD TFKVHYENNS PFLTITSMTR VIEVSHWGNI 240
AVEENVDLKH TGAVLKGPFS RYDYQRQPDS GISSIRSFKT ILPAAAQDVY YRDEIGNVST 300
SHLLILDDSV EMEIRPRFGL FGGWKTHYIV GYNLPSYEYL YNLGDQYALK MRFVDHVFDE 360
QVIDSLTVKI ILPEGAKNIQ VDSPYDISRA PDELHYTYLD TFGRPVIVAY KKNLVEQHIQ 420
DIVVHYTFNK VLMLQEPLLV VAAFYILFFT VIIYVRLDFS ITKDPAAEAR MKVACITEQV 480
LTLVNKRLGL YRHFDETVNR YKQSRDISTL NSGKKSLETE HKAVTSEIAV LQSRLKTEGS 540
DLCDRVSEMQ KLDAQVKELV LKSAVEAERL VAGKLKKDTY IENEKLSSGK RQELVTKIDH 600
ILDAL 605 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
 GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:InterPro.
 GO:0015833; P:peptide transport; NAS:RGD.
 GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. 
Interpro
 IPR007676; Ribophorin_I. 
Pfam
 PF04597; Ribophorin_I 
SMART
  
PROSITE
  
PRINTS