CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005091
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 rRNA 2'-O-methyltransferase fibrillarin 
Protein Synonyms/Alias
 Nucleolar protein 1 
Gene Name
 Fbl 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
108GVFICRGKEDALVTKacetylation[1]
127GESVYGEKRVSISEGacetylation[1]
211RDLINLAKKRTNIIPacetylation[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
 Involved in pre-rRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'- hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity). 
Sequence Annotation
 REGION 178 179 S-adenosyl-L-methionine binding (By
 REGION 197 198 S-adenosyl-L-methionine binding (By
 REGION 222 223 S-adenosyl-L-methionine binding (By
 BINDING 149 149 S-adenosyl-L-methionine (By similarity).
 BINDING 242 242 S-adenosyl-L-methionine (By similarity).
 MOD_RES 8 8 Asymmetric dimethylarginine.
 MOD_RES 15 15 Asymmetric dimethylarginine.
 MOD_RES 21 21 Asymmetric dimethylarginine.
 MOD_RES 24 24 Asymmetric dimethylarginine.
 MOD_RES 28 28 Asymmetric dimethylarginine.
 MOD_RES 31 31 Asymmetric dimethylarginine.
 MOD_RES 130 130 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Direct protein sequencing; Methylation; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 327 AA 
Protein Sequence
MKPGFSPRGG GFGGRGGFGD RGGRGGGRGG RGGFGGGRGG FGGGGRGRGG GGGGFRGRGG 60
GGGRGGGFQS GGGRGRGGGR GGKRGNQSGK NVMVEPHRHE GVFICRGKED ALVTKNLVPG 120
ESVYGEKRVS ISEGDDKIEY RAWNPFRSKL AAAILGGVDQ IHIKPGAKVL YLGAASGTTV 180
SHVSDIVGPD GLVYAVEFSH RSGRDLINLA KKRTNIIPVI EDARHPHKYR MLIAMVDVIF 240
ADVAQPDQTR IVALNAHTFL RNGGHFVISI KANCIDSTAS AEAVFASEVK KMQQENMKPQ 300
EQLTLEPYER DHAVVVGVYR PPPKAKN 327 
Gene Ontology
 GO:0015030; C:Cajal body; IEA:Compara.
 GO:0001651; C:dense fibrillar component; IDA:UniProtKB.
 GO:0001652; C:granular component; IEA:Compara.
 GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
 GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0006396; P:RNA processing; IDA:UniProtKB.
 GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
 GO:0016074; P:snoRNA metabolic process; IEA:Compara.
 GO:0008033; P:tRNA processing; IEA:InterPro. 
Interpro
 IPR000692; Fibrillarin.
 IPR020813; Fibrillarin_CS. 
Pfam
 PF01269; Fibrillarin 
SMART
  
PROSITE
 PS00566; FIBRILLARIN 
PRINTS
 PR00052; FIBRILLARIN.