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Q1HFZ0

- NSUN2_MOUSE

UniProt

Q1HFZ0 - NSUN2_MOUSE

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Protein
tRNA (cytosine(34)-C(5))-methyltransferase
Gene
Nsun2, D13Wsu123e, Misu
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.2 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-methionine By similarity
Binding sitei242 – 2421S-adenosyl-L-methionine By similarity
Binding sitei268 – 2681S-adenosyl-L-methionine By similarity
Active sitei321 – 3211Nucleophile By similarity

GO - Molecular functioni

  1. tRNA (cytosine-5-)-methyltransferase activity Source: InterPro
  2. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
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: Chromosome 13

Organism-specific databases

MGIiMGI:107252. Nsun2.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleolus Source: UniProtKB-SubCell
  3. 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))-methyltransferase
PRO_0000289224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphoserine1 Publication
Modified residuei139 – 1391Phosphoserine; by AURKB By similarity
Modified residuei456 – 4561Phosphoserine By similarity
Modified residuei473 – 4731Phosphoserine By similarity
Modified residuei585 – 5851N6-acetyllysine; alternate1 Publication
Modified residuei585 – 5851N6-malonyllysine; alternate By similarity
Modified residuei592 – 5921Phosphoserine By 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

ArrayExpressiQ1HFZ0.
BgeeiQ1HFZ0.
CleanExiMM_NSUN2.
GenevestigatoriQ1HFZ0.

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. 10 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ1HFZ0.
SMRiQ1HFZ0. Positions 68-429.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 1907S-adenosyl-L-methionine binding By similarity

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR001678. Fmu/NOL1/Nop2p.
IPR023267. RCMT.
IPR023270. RCMT_NCL1.
IPR029063. SAM-dependent_MTases-like.
[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. Align

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

MGRRARGRRF QQPPQPEGEE DASDGGRKRG QAGWEGGYPE IVKENKLFEH    50
YYQELKIVPE GEWDQFMESL REPLPATLRI TGYKSHAKEI LHCLKNKYFK 100
ELEDLEVDGQ KVEVPQPLSW YPEELAWHTN LSRKILRKSP LLAKFHQFLV 150
SETESGNISR QEAVSMIPPL LLNVEPHHKI LDMCAAPGSK TTQLIEMLHA 200
DMSVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN HDASSIPRLT 250
VDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL 300
RIATRGAEQL AEGGRMVYST CSLNPVEDEA VIAALLEKSE GALELADVSA 350
ELPGLKWMPG VSQWKVMTRD GQWFADWHEV PQGRHTQIRP TMFPPTDLEK 400
LQAMHLERCL RILPHHQNTG GFFVAVLVKK APMPWNKRQP KVQNKSAEAR 450
EPRVSSHVAA TEGNPSDQSE LESQMITGAG DSETAHNTEN TESNEKKDGV 500
CGPPPSKKMK LFGFKEDPFV FIPEDDPLFP PIEKFYALDP SFPRMNLLTR 550
TTEGKKRQLY MVSKELRNVL LNNSEKMKVI NTGIKVWCRN NSGEEFDCAF 600
RLAQEGIYTL YPFINSRIIT VSMEDVKTLL TQENPFFRKL SSEAYSQVKD 650
LAKGSVVLKY EPDSANPDTL QCPIVLCGWR GKASIRTFVP KNERLHYLRM 700
MGLEVLGEKK KEGVILTNEN AASPEQPGDE DAKQTAQDPC VPDSVPGCDA 750
AAAEPSR 757
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.
The sequence BAC36110.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform 2.
VSP_025969Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061F → L in BAE30795. 1 Publication
Sequence conflicti206 – 2061F → L in BAE29720. 1 Publication
Sequence conflicti253 – 2531V → L in BAE30795. 1 Publication
Sequence conflicti253 – 2531V → L in BAE29720. 1 Publication
Sequence conflicti482 – 4821S → L in ABF29536. 1 Publication
Sequence conflicti482 – 4821S → L in AAH25549. 1 Publication
Sequence conflicti490 – 4901N → I in ABF29536. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.2. mouse. [Q1HFZ0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS36722.2. [Q1HFZ0-1 ]
RefSeqi NP_663329.3. NM_145354.5. [Q1HFZ0-1 ]
UniGenei Mm.260009.

3D structure databases

ProteinModelPortali Q1HFZ0.
SMRi Q1HFZ0. Positions 68-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205771. 10 interactions.

PTM databases

PhosphoSitei Q1HFZ0.

Proteomic databases

MaxQBi Q1HFZ0.
PaxDbi Q1HFZ0.
PRIDEi Q1HFZ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022087 ; ENSMUSP00000022087 ; ENSMUSG00000021595 . [Q1HFZ0-2 ]
ENSMUST00000109699 ; ENSMUSP00000105321 ; ENSMUSG00000021595 . [Q1HFZ0-1 ]
GeneIDi 28114.
KEGGi mmu:28114.
UCSCi uc007rcm.2. mouse. [Q1HFZ0-1 ]

Organism-specific databases

CTDi 54888.
MGIi MGI:107252. Nsun2.

Phylogenomic databases

eggNOGi COG0144.
GeneTreei ENSGT00660000095589.
HOGENOMi HOG000205147.
HOVERGENi HBG106711.
InParanoidi Q1HFZ0.
KOi K15335.
OMAi PIEKFYA.
OrthoDBi EOG72VH5D.
PhylomeDBi Q1HFZ0.
TreeFami TF300702.

Miscellaneous databases

ChiTaRSi NSUN2. mouse.
NextBioi 306674.
PROi Q1HFZ0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q1HFZ0.
Bgeei Q1HFZ0.
CleanExi MM_NSUN2.
Genevestigatori Q1HFZ0.

Family and domain databases

Gene3Di 3.40.50.150. 2 hits.
InterProi IPR001678. Fmu/NOL1/Nop2p.
IPR023267. RCMT.
IPR023270. RCMT_NCL1.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view ]
PRINTSi PR02008. RCMTFAMILY.
PR02011. RCMTNCL1.
SUPFAMi SSF53335. SSF53335. 2 hits.
PROSITEi PS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 76 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

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