| Tag | Content |
|---|
| CPLM ID | CPLM-005355 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 |
Protein Synonyms/Alias | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit; Ribophorin II; RPN-II; Ribophorin-2 |
Gene Name | Rpn2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 306 | PLAQAAVKLEHAKSV | acetylation | [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 (By similarity). |
Sequence Annotation | CARBOHYD 106 106 N-linked (GlcNAc...) (Probable).
CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly) |
Keyword | Complete proteome; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Isopeptide bond; Membrane; Reference proteome; Signal; Transferase; Transmembrane; Transmembrane helix; Ubl conjugation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 631 AA |
Protein Sequence | MAPPGSSAVF LLALTITAST QALTPTHYLT KHDVERLKAS LDRPFTSLES AFYSIVGLNS 60
LGAQVPDVKK ACAFIKSNLD PSNVDSLFYA AQSSQVLSGC EISVSNETRD LLLAAVSEDS 120
SVAQIYHAVA ALSGFGLPLA SHEALGALTA RLSKEETVLA TVQALHTASH LSQQADLRNI 180
VEEIEDLVAR LDELGGVYLQ FEEGLELTAL FVAATYKLMD HVGTEPSIKE DQVIQLMNTI 240
FSKKNFESLS EAFSVASAAA ALSQNRYHVP VVVVPEGSAS DTQEQAILRL QVSSVLSQPL 300
AQAAVKLEHA KSVASRATVL QKMPFSLVGD VFELNFKNVK LPSGYYDFSV RVEGDNRYIA 360
NTVELRVKIS TEVGITNVDL STVDKDQSIA PKTTRVTYPA KAKGTFIADS HQNFALFFQL 420
VDVNTGAELT PHQTFVRLHN QKTGQEVVFV AEPDNKNVYK FELDTSERKI EFDSASGTYT 480
LYLIIGDATL KNPILWNVAD VVIKFPEEEA PSTVLSQNLF TPKQEIQHLF REPEKRPPTV 540
VSNTFTALIL SPLLLLFALW IRIGANVSNF TFAPSTVIFH LGHAAMLGLM YVYWTQLNMF 600
QTLKYLAVLG TVTFLAGNRM LAQQAVKRTA H 631 |
Gene Ontology | GO:0000421; C:autophagic vacuole membrane; IDA:RGD. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005634; C:nucleus; IEA:Compara. GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro. GO:0005791; C:rough endoplasmic reticulum; IDA:RGD. GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:InterPro. GO:0043022; F:ribosome binding; IDA:RGD. GO:0007568; P:aging; IEP:RGD. GO:0018279; P:protein N-linked glycosylation via asparagine; IEA:InterPro. GO:0042493; P:response to drug; IEP:RGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |