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Q1HFZ0

- NSUN2_MOUSE

UniProt

Q1HFZ0 - NSUN2_MOUSE

Protein

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

Gene

Nsun2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      Previous versions | rss
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    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

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

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW

    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. nucleolus Source: UniProtKB-SubCell
    3. spindle Source: UniProtKB-SubCell

    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

    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.
    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 77 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