CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005043
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 rRNA 2'-O-methyltransferase fibrillarin 
Protein Synonyms/Alias
 34 kDa nucleolar scleroderma antigen 
Gene Name
 FBL 
Gene Synonyms/Alias
 FIB1; FLRN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
102GVFICRGKEDALVTKubiquitination[1, 2, 3]
109KEDALVTKNLVPGESubiquitination[1, 3, 4, 5, 6, 7]
121GESVYGEKRVSISEGubiquitination[1, 2, 3, 6]
131SISEGDDKIEYRAWNubiquitination[1, 3]
143AWNPFRSKLAAAILGubiquitination[3]
158GVDQIHIKPGAKVLYubiquitination[1, 3, 4, 7]
205RDLINLAKKRTNIIPacetylation[8]
205RDLINLAKKRTNIIPubiquitination[1, 3]
206DLINLAKKRTNIIPVubiquitination[3]
222EDARHPHKYRMLIAMubiquitination[3]
284AVFASEVKKMQQENMubiquitination[2, 3]
285VFASEVKKMQQENMKubiquitination[3]
292KMQQENMKPQEQLTLubiquitination[1, 3, 6]
318GVYRPPPKVKN****ubiquitination[4, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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
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. 
Sequence Annotation
 REGION 172 173 S-adenosyl-L-methionine binding (By
 REGION 191 192 S-adenosyl-L-methionine binding (By
 REGION 216 217 S-adenosyl-L-methionine binding (By
 REGION 274 306 Helical (Potential).
 BINDING 143 143 S-adenosyl-L-methionine (By similarity).
 BINDING 236 236 S-adenosyl-L-methionine (By similarity).
 MOD_RES 8 8 Asymmetric dimethylarginine (By
 MOD_RES 15 15 Asymmetric dimethylarginine (By
 MOD_RES 21 21 Asymmetric dimethylarginine (By
 MOD_RES 24 24 Asymmetric dimethylarginine (By
 MOD_RES 27 27 Asymmetric dimethylarginine (By
 MOD_RES 124 124 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Methylation; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding; rRNA processing; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 321 AA 
Protein Sequence
MKPGFSPRGG GFGGRGGFGD RGGRGGRGGF GGGRGRGGGF RGRGRGGGGG GGGGGGGGRG 60
GGGFHSGGNR GRGRGGKRGN QSGKNVMVEP HRHEGVFICR GKEDALVTKN LVPGESVYGE 120
KRVSISEGDD KIEYRAWNPF RSKLAAAILG GVDQIHIKPG AKVLYLGAAS GTTVSHVSDI 180
VGPDGLVYAV EFSHRSGRDL INLAKKRTNI IPVIEDARHP HKYRMLIAMV DVIFADVAQP 240
DQTRIVALNA HTFLRNGGHF VISIKANCID STASAEAVFA SEVKKMQQEN MKPQEQLTLE 300
PYERDHAVVV GVYRPPPKVK N 321 
Gene Ontology
 GO:0031428; C:box C/D snoRNP complex; NAS:BHF-UCL.
 GO:0015030; C:Cajal body; IDA:BHF-UCL.
 GO:0001651; C:dense fibrillar component; IEA:Compara.
 GO:0001652; C:granular component; IEA:Compara.
 GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0006364; P:rRNA processing; TAS:ProtInc.
 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.