CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007775
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative ribosomal RNA methyltransferase NOP2 
Protein Synonyms/Alias
 Nucleolar protein 1; Nucleolar protein 2 homolog; Proliferating-cell nucleolar antigen p120; Proliferation-associated nucleolar protein p120 
Gene Name
 NOP2 
Gene Synonyms/Alias
 NOL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
340VNLDPLGKWSKTGLVubiquitination[1, 2]
398MCCAPGGKTSYMAQLubiquitination[2, 3]
407SYMAQLMKNTGVILAubiquitination[4]
471SGTGVISKDPAVKTNubiquitination[2, 4]
482VKTNKDEKDILRCAHacetylation[3]
649PKKASFQKLNGISKGacetylation[5]
772FEKAAFQKQNDTPKGacetylation[6]
Reference
 [1] 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]
 [2] 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]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 
Functional Description
 May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation. May act as ribosomal RNA methyltransferase. 
Sequence Annotation
 REGION 392 398 S-adenosyl-L-methionine binding
 ACT_SITE 517 517 Nucleophile (Potential).
 BINDING 416 416 S-adenosyl-L-methionine (Potential).
 BINDING 443 443 S-adenosyl-L-methionine (Potential).
 BINDING 460 460 S-adenosyl-L-methionine (Potential).
 MOD_RES 36 36 Phosphoserine.
 MOD_RES 58 58 Phosphoserine.
 MOD_RES 67 67 Phosphoserine.
 MOD_RES 181 181 Phosphoserine.
 MOD_RES 185 185 Phosphothreonine.
 MOD_RES 195 195 Phosphothreonine.
 MOD_RES 649 649 N6-acetyllysine.
 MOD_RES 666 666 Phosphoserine.
 MOD_RES 675 675 Phosphoserine.
 MOD_RES 732 732 Phosphoserine.
 MOD_RES 734 734 Phosphoserine.
 MOD_RES 739 739 Phosphothreonine.
 MOD_RES 776 776 Phosphothreonine.
 MOD_RES 786 786 Phosphoserine.
 MOD_RES 801 801 Phosphoserine.
 MOD_RES 812 812 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 812 AA 
Protein Sequence
MGRKLDPTKE KRGPGRKARK QKGAETELVR FLPAVSDENS KRLSSRARKR AAKRRLGSVE 60
APKTNKSPEA KPLPGKLPKG ISAGAVQTAG KKGPQSLFNA PRGKKRPAPG SDEEEEEEDS 120
EEDGMVNHGD LWGSEDDADT VDDYGADSNS EDEEEGEALL PIERAARKQK AREAAAGIQW 180
SEEETEDEEE EKEVTPESGP PKVEEADGGL QINVDEEPFV LPPAGEMEQD AQAPDLQRVH 240
KRIQDIVGIL RDFGAQREEG RSRSEYLNRL KKDLAIYYSY GDFLLGKLMD LFPLSELVEF 300
LEANEVPRPV TLRTNTLKTR RRDLAQALIN RGVNLDPLGK WSKTGLVVYD SSVPIGATPE 360
YLAGHYMLQG ASSMLPVMAL APQEHERILD MCCAPGGKTS YMAQLMKNTG VILANDANAE 420
RLKSVVGNLH RLGVTNTIIS HYDGRQFPKV VGGFDRVLLD APCSGTGVIS KDPAVKTNKD 480
EKDILRCAHL QKELLLSAID SVNATSKTGG YLVYCTCSIT VEENEWVVDY ALKKRNVRLV 540
PTGLDFGQEG FTRFRERRFH PSLRSTRRFY PHTHNMDGFF IAKFKKFSNS IPQSQTGNSE 600
TATPTNVDLP QVIPKSENSS QPAKKAKGAA KTKQQLQKQQ HPKKASFQKL NGISKGADSE 660
LSTVPSVTKT QASSSFQDSS QPAGKAEGIR EPKVTGKLKQ RSPKLQSSKK VAFLRQNAPP 720
KGTDTQTPAV LSPSKTQATL KPKDHHQPLG RAKGVEKQQL PEQPFEKAAF QKQNDTPKGP 780
QPPTVSPIRS SRPPPAKRKK SQSRGNSQLL LS 812 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0006364; P:rRNA processing; IEA:InterPro. 
Interpro
 IPR001678; Fmu/NOL1/Nop2p.
 IPR018314; Fmu/NOL1/Nop2p_CS.
 IPR011023; Nop2p.
 IPR012586; P120R.
 IPR023267; RCMT.
 IPR023273; RCMT_NOP2. 
Pfam
 PF01189; Nol1_Nop2_Fmu
 PF08062; P120R 
SMART
  
PROSITE
 PS01153; NOL1_NOP2_SUN 
PRINTS
 PR02008; RCMTFAMILY.
 PR02012; RCMTNOP2.