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Q1HFZ0 (NSUN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Nsun2
Synonyms:D13Wsu123e, Misu
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7

Catalytic activity

S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor.

Enzyme regulation

Inhibited by magnesium ions By similarity.

Subunit structure

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

Subcellular location

Nucleusnucleolus. Cytoplasmcytoskeletonspindle. Note: Concentrated in the nucleolus during interphase and translocates to the spindle during mitosis as an RNA-protein complex that includes 18S ribosomal RNA. Ref.1 Ref.7

Tissue specificity

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

Developmental stage

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). Ref.1

Induction

By Myc (at protein level). Ref.1

Post-translational modification

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

Sequence similarities

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

Sequence caution

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

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
tRNA processing
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
S-adenosyl-L-methionine
tRNA-binding
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontRNA (cytosine-5-)-methyltransferase activity

Inferred from electronic annotation. Source: InterPro

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q1HFZ0-1)

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.
Isoform 2 (identifier: Q1HFZ0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 757757tRNA (cytosine(34)-C(5))-methyltransferase
PRO_0000289224

Regions

Region184 – 1907S-adenosyl-L-methionine binding By similarity

Sites

Active site3211Nucleophile By similarity
Binding site2151S-adenosyl-L-methionine By similarity
Binding site2421S-adenosyl-L-methionine By similarity
Binding site2681S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue231Phosphoserine Ref.5
Modified residue1391Phosphoserine; by AURKB By similarity
Modified residue4561Phosphoserine By similarity
Modified residue4731Phosphoserine By similarity
Modified residue5851N6-acetyllysine; alternate Ref.8
Modified residue5851N6-malonyllysine; alternate By similarity
Modified residue5921Phosphoserine By similarity
Modified residue7231Phosphoserine Ref.4 Ref.6

Natural variations

Alternative sequence1 – 6666Missing in isoform 2.
VSP_025969

Experimental info

Sequence conflict2061F → L in BAE30795. Ref.2
Sequence conflict2061F → L in BAE29720. Ref.2
Sequence conflict2531V → L in BAE30795. Ref.2
Sequence conflict2531V → L in BAE29720. Ref.2
Sequence conflict4821S → L in ABF29536. Ref.1
Sequence conflict4821S → L in AAH25549. Ref.3
Sequence conflict4901N → I in ABF29536. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: 73B06947DEC50298

FASTA75785,452
        10         20         30         40         50         60 
MGRRARGRRF QQPPQPEGEE DASDGGRKRG QAGWEGGYPE IVKENKLFEH YYQELKIVPE 

        70         80         90        100        110        120 
GEWDQFMESL REPLPATLRI TGYKSHAKEI LHCLKNKYFK ELEDLEVDGQ KVEVPQPLSW 

       130        140        150        160        170        180 
YPEELAWHTN LSRKILRKSP LLAKFHQFLV SETESGNISR QEAVSMIPPL LLNVEPHHKI 

       190        200        210        220        230        240 
LDMCAAPGSK TTQLIEMLHA DMSVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN 

       250        260        270        280        290        300 
HDASSIPRLT VDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL 

       310        320        330        340        350        360 
RIATRGAEQL AEGGRMVYST CSLNPVEDEA VIAALLEKSE GALELADVSA ELPGLKWMPG 

       370        380        390        400        410        420 
VSQWKVMTRD GQWFADWHEV PQGRHTQIRP TMFPPTDLEK LQAMHLERCL RILPHHQNTG 

       430        440        450        460        470        480 
GFFVAVLVKK APMPWNKRQP KVQNKSAEAR EPRVSSHVAA TEGNPSDQSE LESQMITGAG 

       490        500        510        520        530        540 
DSETAHNTEN TESNEKKDGV CGPPPSKKMK LFGFKEDPFV FIPEDDPLFP PIEKFYALDP 

       550        560        570        580        590        600 
SFPRMNLLTR TTEGKKRQLY MVSKELRNVL LNNSEKMKVI NTGIKVWCRN NSGEEFDCAF 

       610        620        630        640        650        660 
RLAQEGIYTL YPFINSRIIT VSMEDVKTLL TQENPFFRKL SSEAYSQVKD LAKGSVVLKY 

       670        680        690        700        710        720 
EPDSANPDTL QCPIVLCGWR GKASIRTFVP KNERLHYLRM MGLEVLGEKK KEGVILTNEN 

       730        740        750 
AASPEQPGDE DAKQTAQDPC VPDSVPGCDA AAAEPSR 

« Hide

Isoform 2 [UniParc].

Checksum: CA8B554730D496E6
Show »

FASTA69177,747

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_663329.3. NM_145354.5.
UniGeneMm.260009.

3D structure databases

ProteinModelPortalQ1HFZ0.
SMRQ1HFZ0. Positions 48-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205771. 9 interactions.

PTM databases

PhosphoSiteQ1HFZ0.

Proteomic databases

PaxDbQ1HFZ0.
PRIDEQ1HFZ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022087; ENSMUSP00000022087; ENSMUSG00000021595. [Q1HFZ0-2]
ENSMUST00000109699; ENSMUSP00000105321; ENSMUSG00000021595. [Q1HFZ0-1]
GeneID28114.
KEGGmmu:28114.
UCSCuc007rcm.2. mouse. [Q1HFZ0-1]

Organism-specific databases

CTD54888.
MGIMGI:107252. Nsun2.

Phylogenomic databases

eggNOGCOG0144.
GeneTreeENSGT00660000095589.
HOGENOMHOG000205147.
HOVERGENHBG106711.
InParanoidQ1HFZ0.
KOK15335.
OMAKMKVINT.
OrthoDBEOG72VH5D.
PhylomeDBQ1HFZ0.
TreeFamTF300702.

Gene expression databases

ArrayExpressQ1HFZ0.
BgeeQ1HFZ0.
CleanExMM_NSUN2.
GenevestigatorQ1HFZ0.

Family and domain databases

InterProIPR001678. Fmu/NOL1/Nop2p.
IPR023267. RCMT.
IPR023270. RCMT_NCL1.
[Graphical view]
PfamPF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view]
PRINTSPR02008. RCMTFAMILY.
PR02011. RCMTNCL1.
PROSITEPS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNSUN2. mouse.
NextBio306674.
PROQ1HFZ0.
SOURCESearch...

Entry information

Entry nameNSUN2_MOUSE
AccessionPrimary (citable) accession number: Q1HFZ0
Secondary accession number(s): A0PJD6 expand/collapse secondary AC list , Q3U972, Q8BPG9, Q8CDF9, Q91YX9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: April 16, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot