CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011666
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 tRNA (cytosine(34)-C(5))-methyltransferase 
Protein Synonyms/Alias
 Myc-induced SUN domain-containing protein; Misu; NOL1/NOP2/Sun domain family member 2; Substrate of AIM1/Aurora kinase B; tRNA (cytosine-5-)-methyltransferase; tRNA methyltransferase 4 homolog; hTrm4 
Gene Name
 NSUN2 
Gene Synonyms/Alias
 SAKI; TRM4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
28DGAEGGGKRGEAGWEubiquitination[1, 2]
46PEIVKENKLFEHYYQubiquitination[3, 4]
88TGYKSHAKEILHCLKubiquitination[2]
95KEILHCLKNKYFKELubiquitination[1, 2]
144RKSPHLEKFHQFLVSubiquitination[2, 3, 4]
229YLLVHQAKRLSSPCIubiquitination[2]
257QIDVDGRKEILFYDRubiquitination[2]
279SGDGTMRKNIDVWKKubiquitination[2]
286KNIDVWKKWTTLNSLubiquitination[2]
356SNELPGLKWMPGITQubiquitination[1, 5]
365MPGITQWKVMTKDGQubiquitination[2, 3, 4, 5]
369TQWKVMTKDGQWFTDubiquitination[5]
437KSSMPWNKRQPKLQGubiquitination[2]
509CGPPPSKKMKLFGFKubiquitination[2]
511PPPSKKMKLFGFKEDubiquitination[3, 4]
565RQLYMVSKELRNVLLubiquitination[2]
577VLLNNSEKMKVINTGubiquitination[1, 2, 5]
579LNNSEKMKVINTGIKubiquitination[1, 2]
586KVINTGIKVWCRNNSmalonylation[6]
586KVINTGIKVWCRNNSubiquitination[2]
628TVSMEDVKILLTQENubiquitination[1]
640QENPFFRKLSSETYSubiquitination[1, 2]
650SETYSQAKDLAKGSIubiquitination[1, 2, 3, 4, 5]
654SQAKDLAKGSIVLKYubiquitination[1, 2, 3, 4, 5]
660AKGSIVLKYEPDSANubiquitination[5, 7]
692SIRTFVPKNERLHYLubiquitination[2, 3, 4]
711LEVLGEKKKEGVILTubiquitination[2, 5]
712EVLGEKKKEGVILTNubiquitination[2, 5]
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] 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] 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]
 [4] 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]
 [5] 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]
 [6] The first identification of lysine malonylation substrates and its regulatory enzyme.
 Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
 Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
Functional Description
 RNA methyltransferase that methylates tRNAs, and possibly RNA polymerase III transcripts. Methylates cytosine to 5- methylcytosine (m5C) at position 34 of intron-containing tRNA(Leu)(CAA) precursors. Not able to modify tRNAs at positions 48 or 49. May act downstream of Myc to regulate epidermal cell growth and proliferation. Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity. 
Sequence Annotation
 REGION 184 190 S-adenosyl-L-methionine binding (By
 ACT_SITE 321 321 Nucleophile (Potential).
 BINDING 215 215 S-adenosyl-L-methionine (By similarity).
 BINDING 242 242 S-adenosyl-L-methionine (By similarity).
 BINDING 268 268 S-adenosyl-L-methionine (By similarity).
 MOD_RES 139 139 Phosphoserine; by AURKB.
 MOD_RES 456 456 Phosphoserine.
 MOD_RES 473 473 Phosphoserine.
 MOD_RES 586 586 N6-malonyllysine.
 MOD_RES 593 593 Phosphoserine.
 MOD_RES 724 724 Phosphoserine (By similarity).
 MOD_RES 743 743 Phosphoserine.
 MOD_RES 751 751 Phosphoserine.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Mental retardation; Methyltransferase; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 767 AA 
Protein Sequence
MGRRSRGRRL QQQQRPEDAE DGAEGGGKRG EAGWEGGYPE IVKENKLFEH YYQELKIVPE 60
GEWGQFMDAL REPLPATLRI TGYKSHAKEI LHCLKNKYFK ELEDLEVDGQ KVEVPQPLSW 120
YPEELAWHTN LSRKILRKSP HLEKFHQFLV SETESGNISR QEAVSMIPPL LLNVRPHHKI 180
LDMCAAPGSK TTQLIEMLHA DMNVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN 240
HDASSIPRLQ IDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL 300
RIATRGAEQL AEGGRMVYST CSLNPIEDEA VIASLLEKSE GALELADVSN ELPGLKWMPG 360
ITQWKVMTKD GQWFTDWDAV PHSRHTQIRP TMFPPKDPEK LQAMHLERCL RILPHHQNTG 420
GFFVAVLVKK SSMPWNKRQP KLQGKSAETR ESTQLSPADL TEGKPTDPSK LESPSFTGTG 480
DTEIAHATED LENNGSKKDG VCGPPPSKKM KLFGFKEDPF VFIPEDDPLF PPIEKFYALD 540
PSFPRMNLLT RTTEGKKRQL YMVSKELRNV LLNNSEKMKV INTGIKVWCR NNSGEEFDCA 600
FRLAQEGIYT LYPFINSRII TVSMEDVKIL LTQENPFFRK LSSETYSQAK DLAKGSIVLK 660
YEPDSANPDA LQCPIVLCGW RGKASIRTFV PKNERLHYLR MMGLEVLGEK KKEGVILTNE 720
SAASTGQPDN DVTEGQRAGE PNSPDAEEAN SPDVTAGCDP AGVHPPR 767 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW. 
Interpro
 IPR001678; Fmu/NOL1/Nop2p.
 IPR023267; RCMT.
 IPR023270; RCMT_NCL1. 
Pfam
 PF01189; Nol1_Nop2_Fmu 
SMART
  
PROSITE
 PS01153; NOL1_NOP2_SUN 
PRINTS
 PR02008; RCMTFAMILY.
 PR02011; RCMTNCL1.