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tRNA (cytosine(34)-C(5))-methyltransferase (EC 2.1.1.203) (Myc-induced SUN domain-containing protein) (Misu) (NOL1/NOP2/Sun domain family member 2)

 NSUN2_MOUSE             Reviewed;         757 AA.
Q1HFZ0; A0PJD6; Q3U972; Q8BPG9; Q8CDF9; Q91YX9;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 2.
23-MAY-2018, entry version 106.
RecName: Full=tRNA (cytosine(34)-C(5))-methyltransferase;
EC=2.1.1.203;
AltName: Full=Myc-induced SUN domain-containing protein;
Short=Misu;
AltName: Full=NOL1/NOP2/Sun domain family member 2;
Name=Nsun2; Synonyms=D13Wsu123e, Misu;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=16713953; DOI=10.1016/j.cub.2006.04.027;
Frye M., Watt F.M.;
"The RNA methyltransferase Misu (NSun2) mediates Myc-induced
proliferation and is upregulated in tumors.";
Curr. Biol. 16:971-981(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19596847; DOI=10.1083/jcb.200810180;
Hussain S., Benavente S.B., Nascimento E., Dragoni I., Kurowski A.,
Gillich A., Humphreys P., Frye M.;
"The nucleolar RNA methyltransferase Misu (NSun2) is required for
mitotic spindle stability.";
J. Cell Biol. 186:27-40(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; THR-717 AND SER-723,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-585, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
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.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- 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. {ECO:0000250,
ECO:0000269|PubMed:16713953, ECO:0000269|PubMed:19596847}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(34) in tRNA
precursor = S-adenosyl-L-homocysteine + 5-methylcytosine(34) in
tRNA precursor.
-!- ENZYME REGULATION: Inhibited by magnesium ions. {ECO:0000250}.
-!- SUBUNIT: Interacts with NPM1 and NCL during interphase;
interaction is disrupted following phosphorylation at Ser-139.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm, cytoskeleton,
spindle. Note=Concentrated in the nucleolus during interphase and
translocates to the spindle during mitosis as an RNA-protein
complex that includes 18S ribosomal RNA.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q1HFZ0-1; Sequence=Displayed;
Name=2;
IsoId=Q1HFZ0-2; Sequence=VSP_025969;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed at low level. Up-
regulated in tumors. {ECO:0000269|PubMed:16713953}.
-!- 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). {ECO:0000269|PubMed:16713953}.
-!- INDUCTION: By Myc (at protein level).
{ECO:0000269|PubMed:16713953}.
-!- PTM: Phosphorylated at Ser-139 by AURKB during mitosis, leading to
abolish methyltransferase activity and the interaction with NPM1.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. RsmB/NOP family. TRM4 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU01023}.
-!- SEQUENCE CAUTION:
Sequence=AAH13625.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC36110.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; DQ490066; ABF29536.1; -; mRNA.
EMBL; AK030124; BAC26795.1; -; mRNA.
EMBL; AK075999; BAC36110.1; ALT_INIT; mRNA.
EMBL; AK150631; BAE29720.1; -; mRNA.
EMBL; AK151917; BAE30795.1; -; mRNA.
EMBL; BC013625; AAH13625.1; ALT_INIT; mRNA.
EMBL; BC025549; AAH25549.1; ALT_TERM; mRNA.
CCDS; CCDS36722.2; -. [Q1HFZ0-1]
RefSeq; NP_663329.3; NM_145354.5. [Q1HFZ0-1]
UniGene; Mm.260009; -.
ProteinModelPortal; Q1HFZ0; -.
SMR; Q1HFZ0; -.
BioGrid; 205771; 4.
IntAct; Q1HFZ0; 1.
STRING; 10090.ENSMUSP00000105321; -.
iPTMnet; Q1HFZ0; -.
PhosphoSitePlus; Q1HFZ0; -.
SwissPalm; Q1HFZ0; -.
EPD; Q1HFZ0; -.
MaxQB; Q1HFZ0; -.
PaxDb; Q1HFZ0; -.
PeptideAtlas; Q1HFZ0; -.
PRIDE; Q1HFZ0; -.
Ensembl; ENSMUST00000022087; ENSMUSP00000022087; ENSMUSG00000021595. [Q1HFZ0-2]
Ensembl; ENSMUST00000109699; ENSMUSP00000105321; ENSMUSG00000021595. [Q1HFZ0-1]
GeneID; 28114; -.
KEGG; mmu:28114; -.
UCSC; uc007rcm.3; mouse. [Q1HFZ0-1]
CTD; 54888; -.
MGI; MGI:107252; Nsun2.
eggNOG; KOG2198; Eukaryota.
eggNOG; COG0144; LUCA.
GeneTree; ENSGT00660000095589; -.
HOGENOM; HOG000205147; -.
HOVERGEN; HBG106711; -.
InParanoid; Q1HFZ0; -.
KO; K15335; -.
OMA; TFVRCEN; -.
OrthoDB; EOG091G04FO; -.
PhylomeDB; Q1HFZ0; -.
TreeFam; TF300702; -.
ChiTaRS; Nsun2; mouse.
PRO; PR:Q1HFZ0; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021595; -.
CleanEx; MM_NSUN2; -.
ExpressionAtlas; Q1HFZ0; baseline and differential.
Genevisible; Q1HFZ0; MM.
GO; GO:0033391; C:chromatoid body; IDA:CACAO.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; ISO:MGI.
GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0048820; P:hair follicle maturation; IMP:MGI.
GO; GO:0033313; P:meiotic cell cycle checkpoint; IMP:CACAO.
GO; GO:0007286; P:spermatid development; IMP:CACAO.
GO; GO:0030488; P:tRNA methylation; ISO:MGI.
InterPro; IPR001678; MeTrfase_RsmB/NOP2.
InterPro; IPR023267; RCMT.
InterPro; IPR023270; RCMT_NCL1.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01189; Methyltr_RsmB-F; 1.
PRINTS; PR02008; RCMTFAMILY.
PRINTS; PR02011; RCMTNCL1.
SUPFAM; SSF53335; SSF53335; 2.
PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Cytoskeleton; Isopeptide bond;
Methyltransferase; Mitosis; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase;
tRNA processing; tRNA-binding; Ubl conjugation.
CHAIN 1 757 tRNA (cytosine(34)-C(5))-
methyltransferase.
/FTId=PRO_0000289224.
REGION 184 190 S-adenosyl-L-methionine binding.
{ECO:0000255|PROSITE-ProRule:PRU01023}.
ACT_SITE 321 321 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01023}.
BINDING 215 215 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01023}.
BINDING 242 242 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01023}.
BINDING 268 268 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01023}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 139 139 Phosphoserine; by AURKB.
{ECO:0000250|UniProtKB:Q08J23}.
MOD_RES 456 456 Phosphoserine.
{ECO:0000250|UniProtKB:Q08J23}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000250|UniProtKB:Q08J23}.
MOD_RES 585 585 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 585 585 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 592 592 Phosphoserine.
{ECO:0000250|UniProtKB:Q08J23}.
MOD_RES 717 717 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 723 723 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CROSSLNK 46 46 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q08J23}.
CROSSLNK 510 510 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q08J23}.
CROSSLNK 515 515 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q08J23}.
CROSSLNK 585 585 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q08J23}.
CROSSLNK 639 639 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q08J23}.
CROSSLNK 653 653 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q08J23}.
CROSSLNK 659 659 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q08J23}.
VAR_SEQ 1 66 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_025969.
CONFLICT 206 206 F -> L (in Ref. 2; BAE30795/BAE29720).
{ECO:0000305}.
CONFLICT 253 253 V -> L (in Ref. 2; BAE30795/BAE29720).
{ECO:0000305}.
CONFLICT 482 482 S -> L (in Ref. 1; ABF29536 and 3;
AAH25549). {ECO:0000305}.
CONFLICT 490 490 N -> I (in Ref. 1; ABF29536).
{ECO:0000305}.
SEQUENCE 757 AA; 85452 MW; 73B06947DEC50298 CRC64;
MGRRARGRRF QQPPQPEGEE DASDGGRKRG QAGWEGGYPE IVKENKLFEH YYQELKIVPE
GEWDQFMESL REPLPATLRI TGYKSHAKEI LHCLKNKYFK ELEDLEVDGQ KVEVPQPLSW
YPEELAWHTN LSRKILRKSP LLAKFHQFLV SETESGNISR QEAVSMIPPL LLNVEPHHKI
LDMCAAPGSK TTQLIEMLHA DMSVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN
HDASSIPRLT VDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL
RIATRGAEQL AEGGRMVYST CSLNPVEDEA VIAALLEKSE GALELADVSA ELPGLKWMPG
VSQWKVMTRD GQWFADWHEV PQGRHTQIRP TMFPPTDLEK LQAMHLERCL RILPHHQNTG
GFFVAVLVKK APMPWNKRQP KVQNKSAEAR EPRVSSHVAA TEGNPSDQSE LESQMITGAG
DSETAHNTEN TESNEKKDGV CGPPPSKKMK LFGFKEDPFV FIPEDDPLFP PIEKFYALDP
SFPRMNLLTR TTEGKKRQLY MVSKELRNVL LNNSEKMKVI NTGIKVWCRN NSGEEFDCAF
RLAQEGIYTL YPFINSRIIT VSMEDVKTLL TQENPFFRKL SSEAYSQVKD LAKGSVVLKY
EPDSANPDTL QCPIVLCGWR GKASIRTFVP KNERLHYLRM MGLEVLGEKK KEGVILTNEN
AASPEQPGDE DAKQTAQDPC VPDSVPGCDA AAAEPSR


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