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Protein

tRNA (cytosine(34)-C(5))-methyltransferase

Gene

Nsun2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA methyltransferase that methylates tRNAs, and possibly RNA polymerase III transcripts. Methylates cytosine to 5-methylcytosine (m5C) at positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors (By similarity). 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.By similarity2 Publications

Catalytic activityi

S-adenosyl-L-methionine + cytosine(34) in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine(34) in tRNA precursor.

Enzyme regulationi

Inhibited by magnesium ions.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei242 – 2421S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei268 – 2681S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei321 – 3211NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • meiotic cell cycle checkpoint Source: CACAO
  • mitotic nuclear division Source: UniProtKB-KW
  • pachytene Source: CACAO
  • spermatid development Source: CACAO
  • tRNA methylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, tRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (cytosine(34)-C(5))-methyltransferase (EC:2.1.1.203)
Alternative name(s):
Myc-induced SUN domain-containing protein
Short name:
Misu
NOL1/NOP2/Sun domain family member 2
Gene namesi
Name:Nsun2
Synonyms:D13Wsu123e, Misu
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:107252. Nsun2.

Subcellular locationi

GO - Cellular componenti

  • chromatoid body Source: CACAO
  • cytoplasm Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: MGI
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 757757tRNA (cytosine(34)-C(5))-methyltransferasePRO_0000289224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei139 – 1391Phosphoserine; by AURKBBy similarity
Modified residuei456 – 4561PhosphoserineBy similarity
Modified residuei473 – 4731PhosphoserineBy similarity
Modified residuei585 – 5851N6-acetyllysine; alternate1 Publication
Modified residuei585 – 5851N6-malonyllysine; alternateBy similarity
Modified residuei592 – 5921PhosphoserineBy similarity
Modified residuei723 – 7231Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated at Ser-139 by AURKB during mitosis, leading to abolish methyltransferase activity and the interaction with NPM1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ1HFZ0.
PaxDbiQ1HFZ0.
PRIDEiQ1HFZ0.

PTM databases

PhosphoSiteiQ1HFZ0.

Expressioni

Tissue specificityi

Ubiquitously expressed at low level. Up-regulated in tumors.1 Publication

Developmental stagei

In G1, it is predominantly found in the nucleol. During S phase, it is present at its highest level and is distributed more uniformly throughout the nucleus (at protein level).1 Publication

Inductioni

By Myc (at protein level).1 Publication

Gene expression databases

BgeeiQ1HFZ0.
CleanExiMM_NSUN2.
ExpressionAtlasiQ1HFZ0. baseline and differential.
GenevisibleiQ1HFZ0. MM.

Interactioni

Subunit structurei

Interacts with NPM1 and NCL during interphase; interaction is disrupted following phosphorylation at Ser-139.By similarity

Protein-protein interaction databases

BioGridi205771. 3 interactions.
STRINGi10090.ENSMUSP00000105321.

Structurei

3D structure databases

ProteinModelPortaliQ1HFZ0.
SMRiQ1HFZ0. Positions 68-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 1907S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. TRM4 subfamily.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0144.
GeneTreeiENSGT00660000095589.
HOGENOMiHOG000205147.
HOVERGENiHBG106711.
InParanoidiQ1HFZ0.
KOiK15335.
OMAiPLFPPIX.
OrthoDBiEOG72VH5D.
PhylomeDBiQ1HFZ0.
TreeFamiTF300702.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR001678. MeTrfase_RsmB/NOP2.
IPR023267. RCMT.
IPR023270. RCMT_NCL1.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view]
PRINTSiPR02008. RCMTFAMILY.
PR02011. RCMTNCL1.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q1HFZ0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRRARGRRF QQPPQPEGEE DASDGGRKRG QAGWEGGYPE IVKENKLFEH
60 70 80 90 100
YYQELKIVPE GEWDQFMESL REPLPATLRI TGYKSHAKEI LHCLKNKYFK
110 120 130 140 150
ELEDLEVDGQ KVEVPQPLSW YPEELAWHTN LSRKILRKSP LLAKFHQFLV
160 170 180 190 200
SETESGNISR QEAVSMIPPL LLNVEPHHKI LDMCAAPGSK TTQLIEMLHA
210 220 230 240 250
DMSVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN HDASSIPRLT
260 270 280 290 300
VDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL
310 320 330 340 350
RIATRGAEQL AEGGRMVYST CSLNPVEDEA VIAALLEKSE GALELADVSA
360 370 380 390 400
ELPGLKWMPG VSQWKVMTRD GQWFADWHEV PQGRHTQIRP TMFPPTDLEK
410 420 430 440 450
LQAMHLERCL RILPHHQNTG GFFVAVLVKK APMPWNKRQP KVQNKSAEAR
460 470 480 490 500
EPRVSSHVAA TEGNPSDQSE LESQMITGAG DSETAHNTEN TESNEKKDGV
510 520 530 540 550
CGPPPSKKMK LFGFKEDPFV FIPEDDPLFP PIEKFYALDP SFPRMNLLTR
560 570 580 590 600
TTEGKKRQLY MVSKELRNVL LNNSEKMKVI NTGIKVWCRN NSGEEFDCAF
610 620 630 640 650
RLAQEGIYTL YPFINSRIIT VSMEDVKTLL TQENPFFRKL SSEAYSQVKD
660 670 680 690 700
LAKGSVVLKY EPDSANPDTL QCPIVLCGWR GKASIRTFVP KNERLHYLRM
710 720 730 740 750
MGLEVLGEKK KEGVILTNEN AASPEQPGDE DAKQTAQDPC VPDSVPGCDA

AAAEPSR
Length:757
Mass (Da):85,452
Last modified:May 29, 2007 - v2
Checksum:i73B06947DEC50298
GO
Isoform 2 (identifier: Q1HFZ0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Note: No experimental confirmation available.
Show »
Length:691
Mass (Da):77,747
Checksum:iCA8B554730D496E6
GO

Sequence cautioni

The sequence AAH13625.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC36110.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061F → L in BAE30795 (PubMed:16141072).Curated
Sequence conflicti206 – 2061F → L in BAE29720 (PubMed:16141072).Curated
Sequence conflicti253 – 2531V → L in BAE30795 (PubMed:16141072).Curated
Sequence conflicti253 – 2531V → L in BAE29720 (PubMed:16141072).Curated
Sequence conflicti482 – 4821S → L in ABF29536 (PubMed:16713953).Curated
Sequence conflicti482 – 4821S → L in AAH25549 (PubMed:15489334).Curated
Sequence conflicti490 – 4901N → I in ABF29536 (PubMed:16713953).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform 2. 1 PublicationVSP_025969Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490066 mRNA. Translation: ABF29536.1.
AK030124 mRNA. Translation: BAC26795.1.
AK075999 mRNA. Translation: BAC36110.1. Different initiation.
AK150631 mRNA. Translation: BAE29720.1.
AK151917 mRNA. Translation: BAE30795.1.
BC013625 mRNA. Translation: AAH13625.1. Different initiation.
BC025549 mRNA. Translation: AAH25549.1. Different termination.
CCDSiCCDS36722.2. [Q1HFZ0-1]
RefSeqiNP_663329.3. NM_145354.5. [Q1HFZ0-1]
UniGeneiMm.260009.

Genome annotation databases

EnsembliENSMUST00000022087; ENSMUSP00000022087; ENSMUSG00000021595. [Q1HFZ0-2]
ENSMUST00000109699; ENSMUSP00000105321; ENSMUSG00000021595. [Q1HFZ0-1]
GeneIDi28114.
KEGGimmu:28114.
UCSCiuc007rcm.3. mouse. [Q1HFZ0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490066 mRNA. Translation: ABF29536.1.
AK030124 mRNA. Translation: BAC26795.1.
AK075999 mRNA. Translation: BAC36110.1. Different initiation.
AK150631 mRNA. Translation: BAE29720.1.
AK151917 mRNA. Translation: BAE30795.1.
BC013625 mRNA. Translation: AAH13625.1. Different initiation.
BC025549 mRNA. Translation: AAH25549.1. Different termination.
CCDSiCCDS36722.2. [Q1HFZ0-1]
RefSeqiNP_663329.3. NM_145354.5. [Q1HFZ0-1]
UniGeneiMm.260009.

3D structure databases

ProteinModelPortaliQ1HFZ0.
SMRiQ1HFZ0. Positions 68-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205771. 3 interactions.
STRINGi10090.ENSMUSP00000105321.

PTM databases

PhosphoSiteiQ1HFZ0.

Proteomic databases

MaxQBiQ1HFZ0.
PaxDbiQ1HFZ0.
PRIDEiQ1HFZ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022087; ENSMUSP00000022087; ENSMUSG00000021595. [Q1HFZ0-2]
ENSMUST00000109699; ENSMUSP00000105321; ENSMUSG00000021595. [Q1HFZ0-1]
GeneIDi28114.
KEGGimmu:28114.
UCSCiuc007rcm.3. mouse. [Q1HFZ0-1]

Organism-specific databases

CTDi54888.
MGIiMGI:107252. Nsun2.

Phylogenomic databases

eggNOGiCOG0144.
GeneTreeiENSGT00660000095589.
HOGENOMiHOG000205147.
HOVERGENiHBG106711.
InParanoidiQ1HFZ0.
KOiK15335.
OMAiPLFPPIX.
OrthoDBiEOG72VH5D.
PhylomeDBiQ1HFZ0.
TreeFamiTF300702.

Miscellaneous databases

ChiTaRSiNsun2. mouse.
NextBioi306674.
PROiQ1HFZ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ1HFZ0.
CleanExiMM_NSUN2.
ExpressionAtlasiQ1HFZ0. baseline and differential.
GenevisibleiQ1HFZ0. MM.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR001678. MeTrfase_RsmB/NOP2.
IPR023267. RCMT.
IPR023270. RCMT_NCL1.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view]
PRINTSiPR02008. RCMTFAMILY.
PR02011. RCMTNCL1.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The RNA methyltransferase Misu (NSun2) mediates Myc-induced proliferation and is upregulated in tumors."
    Frye M., Watt F.M.
    Curr. Biol. 16:971-981(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Bone marrow and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: Czech II and FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The nucleolar RNA methyltransferase Misu (NSun2) is required for mitotic spindle stability."
    Hussain S., Benavente S.B., Nascimento E., Dragoni I., Kurowski A., Gillich A., Humphreys P., Frye M.
    J. Cell Biol. 186:27-40(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-585, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNSUN2_MOUSE
AccessioniPrimary (citable) accession number: Q1HFZ0
Secondary accession number(s): A0PJD6
, Q3U972, Q8BPG9, Q8CDF9, Q91YX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 22, 2015
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.