Tag | Content |
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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 |
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114 | SGRFFTVKLPVALDP | acetylation | [1] | 185 | RNVESHTKLGNPSRS | acetylation | [1] | 202 | ILDYGPFKDIPAYSQ | acetylation | [1] | 514 | ISTLNSGKKSLETEH | acetylation | [1] | 536 | AVLQSRLKTEGSDLC | acetylation | [1] | 551 | DRVSEMQKLDAQVKE | acetylation | [1] | 557 | QKLDAQVKELVLKSA | acetylation | [1] | 597 | KRQELVTKIDHILDA | acetylation | [1] |
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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. |
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PROSITE | |
PRINTS | |