Q1HFZ0 (NSUN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA (cytosine(34)-C(5))-methyltransferase
EC=2.1.1.203

Alternative name(s):
Myc-induced SUN domain-containing protein
NOL1/NOP2/Sun domain family member 2

Gene names

Name:	Nsun2
Synonyms:	D13Wsu123e, Misu

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	757 AA.
Sequence status	Complete.
Protein existence	Evidence 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 position 34 of intron-containing tRNA(Leu)(CAA) precursors. Not able to modify tRNAs at positions 48 or 49 By similarity. May act downstream of Myc to regulate epidermal cell growth and proliferation. Ref.1
Catalytic activity	S-adenosyl-L-methionine + cytosine(34) in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine(34) in tRNA precursor.
Subunit structure	Interacts with NPM1 and NCL during interphase; interaction is disrupted following phosphorylation at Ser-139 By similarity.
Subcellular location	Nucleus › nucleolus. Cytoplasm. Note: Concentrated in the nucleolus during interphase and distributed in the perichromosome and cytoplasm during mitosis. Ref.1
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. Ref.4 Ref.5
Sequence similarities	Belongs to the 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 process	tRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding S-adenosyl-L-methionine tRNA-binding
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 757	757	tRNA (cytosine(34)-C(5))-methyltransferase		PRO_0000289224
Regions
	Region	184 – 190	7	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	321	1	Nucleophile Potential
	Binding site	215	1	S-adenosyl-L-methionine By similarity
	Binding site	242	1	S-adenosyl-L-methionine By similarity
	Binding site	268	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	23	1	Phosphoserine Ref.5
	Modified residue	139	1	Phosphoserine; by AURKB By similarity
	Modified residue	456	1	Phosphoserine By similarity
	Modified residue	461	1	Phosphothreonine By similarity
	Modified residue	473	1	Phosphoserine By similarity
	Modified residue	592	1	Phosphoserine By similarity
	Modified residue	723	1	Phosphoserine Ref.4
Natural variations
	Alternative sequence	1 – 66	66	Missing in isoform 2.		VSP_025969
Experimental info
	Sequence conflict	206	1	F → L in BAE30795. Ref.2
	Sequence conflict	206	1	F → L in BAE29720. Ref.2
	Sequence conflict	253	1	V → L in BAE30795. Ref.2
	Sequence conflict	253	1	V → L in BAE29720. Ref.2
	Sequence conflict	482	1	S → L in ABF29536. Ref.1
	Sequence conflict	482	1	S → L in AAH25549. Ref.3
	Sequence conflict	490	1	N → I in ABF29536. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: 73B06947DEC50298	FASTA	757	85,452
	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
	Isoform 2 [UniParc]. Checksum: CA8B554730D496E6	FASTA	691	77,747
	10 20 30 40 50 60 MESLREPLPA TLRITGYKSH AKEILHCLKN KYFKELEDLE VDGQKVEVPQ PLSWYPEELA 70 80 90 100 110 120 WHTNLSRKIL RKSPLLAKFH QFLVSETESG NISRQEAVSM IPPLLLNVEP HHKILDMCAA 130 140 150 160 170 180 PGSKTTQLIE MLHADMSVPF PEGFVIANDV DNKRCYLLVH QAKRLSSPCI MVVNHDASSI 190 200 210 220 230 240 PRLTVDVDGR KEILFYDRIL CDVPCSGDGT MRKNIDVWKK WTTLNSLQLH GLQLRIATRG 250 260 270 280 290 300 AEQLAEGGRM VYSTCSLNPV EDEAVIAALL EKSEGALELA DVSAELPGLK WMPGVSQWKV 310 320 330 340 350 360 MTRDGQWFAD WHEVPQGRHT QIRPTMFPPT DLEKLQAMHL ERCLRILPHH QNTGGFFVAV 370 380 390 400 410 420 LVKKAPMPWN KRQPKVQNKS AEAREPRVSS HVAATEGNPS DQSELESQMI TGAGDSETAH 430 440 450 460 470 480 NTENTESNEK KDGVCGPPPS KKMKLFGFKE DPFVFIPEDD PLFPPIEKFY ALDPSFPRMN 490 500 510 520 530 540 LLTRTTEGKK RQLYMVSKEL RNVLLNNSEK MKVINTGIKV WCRNNSGEEF DCAFRLAQEG 550 560 570 580 590 600 IYTLYPFINS RIITVSMEDV KTLLTQENPF FRKLSSEAYS QVKDLAKGSV VLKYEPDSAN 610 620 630 640 650 660 PDTLQCPIVL CGWRGKASIR TFVPKNERLH YLRMMGLEVL GEKKKEGVIL TNENAASPEQ 670 680 690 PGDEDAKQTA QDPCVPDSVP GCDAAAAEPS R

References

	« Hide 'large scale' referencesShow '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: 16713953] [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: 16141072] [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: 15489334] [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: 15345747] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, MASS SPECTROMETRY. Tissue: Embryonic brain.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY. Tissue: Melanoma.
+	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.
IPI	IPI00850580. IPI00894870.
RefSeq	NP_663329.3. NM_145354.4.
UniGene	Mm.260009.
3D structure databases
ProteinModelPortal	Q1HFZ0.
SMR	Q1HFZ0. Positions 48-430.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1HFZ0.
PTM databases
PhosphoSite	Q1HFZ0.
Proteomic databases
PRIDE	Q1HFZ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000022087; ENSMUSP00000022087; ENSMUSG00000021595. ENSMUST00000109699; ENSMUSP00000105321; ENSMUSG00000021595.
GeneID	28114.
KEGG	mmu:28114.
NMPDR	fig|10090.3.peg.28089.
UCSC	uc007rcm.2. mouse. uc007rcn.2. mouse.
Organism-specific databases
CTD	54888.
MGI	MGI:107252. Nsun2.
Phylogenomic databases
eggNOG	roNOG05017.
GeneTree	ENSGT00550000074937.
HOGENOM	HBG315458.
HOVERGEN	HBG106711.
InParanoid	Q1HFZ0.
OrthoDB	EOG4K9BBQ.
PhylomeDB	Q1HFZ0.
Gene expression databases
ArrayExpress	Q1HFZ0.
Bgee	Q1HFZ0.
CleanEx	MM_NSUN2.
Genevestigator	Q1HFZ0.
Family and domain databases
InterPro	IPR001678. Fmu/NOL1/Nop2p. IPR023267. RCMT. IPR023270. RCMT_NCL1. [Graphical view]
KO	K15335.
Pfam	PF01189. Nol1_Nop2_Fmu. 1 hit. [Graphical view]
PRINTS	PR02008. RCMTFAMILY. PR02011. RCMTNCL1.
PROSITE	PS01153. NOL1_NOP2_SUN. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	306674.
SOURCE	Search...

Entry information

Entry name

NSUN2_MOUSE

Accession

Primary (citable) accession number: Q1HFZ0
Secondary accession number(s): A0PJD6 , Q3U972, Q8BPG9, Q8CDF9, Q91YX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 29, 2007
Last modified:	November 16, 2011
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program