UniProt Accession

 NSUN2_HUMAN; Q08J23; B2RNR4; B4DQW2; Q9BVN4; Q9H858; Q9NXD9 

Genbank Protein ID

 AB255451; AK000310; AK023994; AK298980; AC010366; AC027334; CH471102; BC001041; BC137083 

Genbank Nucleotide ID

 BAF34150.1; BAA91075.1; BAB14762.1; BAG61074.1; EAX08105.1; AAH01041.3; AAI37084.1 

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
28	DGAEGGGKRGEAGWE	ubiquitination	[1, 2]
46	PEIVKENKLFEHYYQ	ubiquitination	[3, 4]
88	TGYKSHAKEILHCLK	ubiquitination	[2]
95	KEILHCLKNKYFKEL	ubiquitination	[1, 2]
144	RKSPHLEKFHQFLVS	ubiquitination	[2, 3, 4]
229	YLLVHQAKRLSSPCI	ubiquitination	[2]
257	QIDVDGRKEILFYDR	ubiquitination	[2]
279	SGDGTMRKNIDVWKK	ubiquitination	[2]
286	KNIDVWKKWTTLNSL	ubiquitination	[2]
356	SNELPGLKWMPGITQ	ubiquitination	[1, 5]
365	MPGITQWKVMTKDGQ	ubiquitination	[2, 3, 4, 5]
369	TQWKVMTKDGQWFTD	ubiquitination	[5]
437	KSSMPWNKRQPKLQG	ubiquitination	[2]
509	CGPPPSKKMKLFGFK	ubiquitination	[2]
511	PPPSKKMKLFGFKED	ubiquitination	[3, 4]
565	RQLYMVSKELRNVLL	ubiquitination	[2]
577	VLLNNSEKMKVINTG	ubiquitination	[1, 2, 5]
579	LNNSEKMKVINTGIK	ubiquitination	[1, 2]
586	KVINTGIKVWCRNNS	malonylation	[6]
586	KVINTGIKVWCRNNS	ubiquitination	[2]
628	TVSMEDVKILLTQEN	ubiquitination	[1]
640	QENPFFRKLSSETYS	ubiquitination	[1, 2]
650	SETYSQAKDLAKGSI	ubiquitination	[1, 2, 3, 4, 5]
654	SQAKDLAKGSIVLKY	ubiquitination	[1, 2, 3, 4, 5]
660	AKGSIVLKYEPDSAN	ubiquitination	[5, 7]
692	SIRTFVPKNERLHYL	ubiquitination	[2, 3, 4]
711	LEVLGEKKKEGVILT	ubiquitination	[2, 5]
712	EVLGEKKKEGVILTN	ubiquitination	[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

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.