CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007441
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative ribosomal RNA methyltransferase Nop2 
Protein Synonyms/Alias
 Nucleolar protein 2 
Gene Name
 NOP2 
Gene Synonyms/Alias
 YNA1; YNL061W; N2428; YNL2428W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
35NRKLEKGKRPSTTQGacetylation[1]
215VKVLENFKTLGAEGRubiquitination[2]
380VFANDANKSRTKSLIubiquitination[2]
510DTGLAIGKEAFTSYRubiquitination[2]
548FFVAKFQKIGPSSFDubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Required for 60S ribosomal subunit synthesis. May act as ribosomal RNA methyltransferase. 
Sequence Annotation
 REGION 353 359 S-adenosyl-L-methionine binding (By
 ACT_SITE 478 478 Nucleophile (Potential).
 BINDING 377 377 S-adenosyl-L-methionine (By similarity).
 BINDING 404 404 S-adenosyl-L-methionine (By similarity).
 BINDING 421 421 S-adenosyl-L-methionine (By similarity).
 MOD_RES 580 580 Phosphoserine.  
Keyword
 Complete proteome; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 618 AA 
Protein Sequence
MGSRRHKNKQ AAPPTLEEFQ ARKEKKANRK LEKGKRPSTT QGDEVSDRKK KKSKPFKKSR 60
KEEEEVVEED KDLPEVDLEE LSKARKSLFD DEEDDDEAGL VDEELKDEFD LEQEYDYDED 120
EDNDAHPIFS DDDDEADLEE LNAQNMEALS KKLDEEEAEE AEEAEMELVE AENMQPRADI 180
LPTEEQEEMM AQETPNLTST RTRMIEIVKV LENFKTLGAE GRSRGEYVDR LLKDICEYFG 240
YTPFLAEKLF NLFSPAEAME FFEANEIARP ITIRTNTLKT RRRDLAQTLV NRGVNLQPIG 300
SWTKVGLQIF DSQVPIGATP EYLAGHYILQ AASSFLPVIA LDPHENERIL DMAAAPGGKT 360
TYISAMMKNT GCVFANDANK SRTKSLIANI HRLGCTNTIV CNYDAREFPK VIGGFDRILL 420
DAPCSGTGVI GKDQSVKVSR TEKDFIQIPH LQKQLLLSAI DSVDCNSKHG GVIVYSTCSV 480
AVEEDEAVID YALRKRPNVK LVDTGLAIGK EAFTSYRGKK FHPSVKLARR YYPHTYNVDG 540
FFVAKFQKIG PSSFDDNQAS AKEKETAARK EALEEGIIHS DFATFEDEED DKYIEKSVKN 600
NLLKKGVNPK AKRPSNEK 618 
Gene Ontology
 GO:0005730; C:nucleolus; TAS:SGD.
 GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008173; F:RNA methyltransferase activity; TAS:SGD.
 GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:SGD.
 GO:0006364; P:rRNA processing; TAS:SGD. 
Interpro
 IPR001678; Fmu/NOL1/Nop2p.
 IPR018314; Fmu/NOL1/Nop2p_CS.
 IPR011023; Nop2p.
 IPR023267; RCMT.
 IPR023273; RCMT_NOP2. 
Pfam
 PF01189; Nol1_Nop2_Fmu 
SMART
  
PROSITE
 PS01153; NOL1_NOP2_SUN 
PRINTS
 PR02008; RCMTFAMILY.
 PR02012; RCMTNOP2.