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Q08J23

- NSUN2_HUMAN

UniProt

Q08J23 - NSUN2_HUMAN

Protein

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

Gene

NSUN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (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. 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.3 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + cytosine(34) in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine(34) in tRNA precursor.1 Publication

    Enzyme regulationi

    Inhibited by magnesium ions.1 Publication

    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. poly(A) RNA binding Source: UniProtKB
    2. tRNA (cytosine-5-)-methyltransferase activity Source: UniProtKB
    3. tRNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW
    2. tRNA methylation Source: UniProtKB

    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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS12087-MONOMER.

    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
    Substrate of AIM1/Aurora kinase B
    tRNA (cytosine-5-)-methyltransferase
    tRNA methyltransferase 4 homolog
    Short name:
    hTrm4
    Gene namesi
    Name:NSUN2
    Synonyms:SAKI, TRM4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:25994. 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
    2. nucleolus Source: UniProtKB
    3. nucleus Source: HPA
    4. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal recessive 5 (MRT5) [MIM:611091]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti679 – 6791G → R in MRT5; impairs proper intracellular localization. 1 Publication
    VAR_068530

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi139 – 1391S → A: Induces a constitutive association with NPM1. 1 Publication
    Mutagenesisi139 – 1391S → E: Mimicks constitutive phosphorylation and abolishes methyltransferase activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi611091. phenotype.
    Orphaneti88616. Autosomal recessive nonsyndromic intellectual disability.
    235. Dubowitz syndrome.
    PharmGKBiPA134953940.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 767767tRNA (cytosine(34)-C(5))-methyltransferasePRO_0000289223Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei139 – 1391Phosphoserine; by AURKB1 Publication
    Modified residuei456 – 4561Phosphoserine2 Publications
    Modified residuei473 – 4731Phosphoserine2 Publications
    Modified residuei586 – 5861N6-acetyllysine; alternateBy similarity
    Modified residuei586 – 5861N6-malonyllysine; alternate1 Publication
    Modified residuei593 – 5931Phosphoserine2 Publications
    Modified residuei724 – 7241PhosphoserineBy similarity
    Modified residuei743 – 7431Phosphoserine6 Publications
    Modified residuei751 – 7511Phosphoserine5 Publications

    Post-translational modificationi

    Phosphorylated at Ser-139 by AURKB during mitosis, leading to abolish methyltransferase activity and the interaction with NPM1.8 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ08J23.
    PaxDbiQ08J23.
    PeptideAtlasiQ08J23.
    PRIDEiQ08J23.

    PTM databases

    PhosphoSiteiQ08J23.

    Expressioni

    Tissue specificityi

    Expressed in adult and fetal brain and in lymphoblastoid cells.1 Publication

    Gene expression databases

    ArrayExpressiQ08J23.
    BgeeiQ08J23.
    CleanExiHS_NSUN2.
    GenevestigatoriQ08J23.

    Organism-specific databases

    HPAiHPA037896.

    Interactioni

    Subunit structurei

    Interacts with NPM1 and NCL during interphase; interaction is disrupted following phosphorylation at Ser-139.1 Publication

    Protein-protein interaction databases

    BioGridi120236. 59 interactions.
    DIPiDIP-52456N.
    IntActiQ08J23. 8 interactions.
    MINTiMINT-4851220.
    STRINGi9606.ENSP00000264670.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08J23.
    SMRiQ08J23. Positions 45-427.
    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.
    HOGENOMiHOG000205147.
    HOVERGENiHBG106711.
    InParanoidiQ08J23.
    KOiK15335.
    OMAiPIEKFYA.
    OrthoDBiEOG72VH5D.
    PhylomeDBiQ08J23.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q08J23-1) [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

    MGRRSRGRRL QQQQRPEDAE DGAEGGGKRG EAGWEGGYPE IVKENKLFEH    50
    YYQELKIVPE GEWGQFMDAL REPLPATLRI TGYKSHAKEI LHCLKNKYFK 100
    ELEDLEVDGQ KVEVPQPLSW YPEELAWHTN LSRKILRKSP HLEKFHQFLV 150
    SETESGNISR QEAVSMIPPL LLNVRPHHKI LDMCAAPGSK TTQLIEMLHA 200
    DMNVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN HDASSIPRLQ 250
    IDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL 300
    RIATRGAEQL AEGGRMVYST CSLNPIEDEA VIASLLEKSE GALELADVSN 350
    ELPGLKWMPG ITQWKVMTKD GQWFTDWDAV PHSRHTQIRP TMFPPKDPEK 400
    LQAMHLERCL RILPHHQNTG GFFVAVLVKK SSMPWNKRQP KLQGKSAETR 450
    ESTQLSPADL TEGKPTDPSK LESPSFTGTG DTEIAHATED LENNGSKKDG 500
    VCGPPPSKKM KLFGFKEDPF VFIPEDDPLF PPIEKFYALD PSFPRMNLLT 550
    RTTEGKKRQL YMVSKELRNV LLNNSEKMKV INTGIKVWCR NNSGEEFDCA 600
    FRLAQEGIYT LYPFINSRII TVSMEDVKIL LTQENPFFRK LSSETYSQAK 650
    DLAKGSIVLK YEPDSANPDA LQCPIVLCGW RGKASIRTFV PKNERLHYLR 700
    MMGLEVLGEK KKEGVILTNE SAASTGQPDN DVTEGQRAGE PNSPDAEEAN 750
    SPDVTAGCDP AGVHPPR 767
    Length:767
    Mass (Da):86,471
    Last modified:May 29, 2007 - v2
    Checksum:iFE4B34309978A8D2
    GO
    Isoform 2 (identifier: Q08J23-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-120: SHAKEILHCLKNKYFKELEDLEVDGQKVEVPQPLSW → R

    Note: No experimental confirmation available.

    Show »
    Length:732
    Mass (Da):82,393
    Checksum:i3C092217D0A3A22B
    GO
    Isoform 3 (identifier: Q08J23-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-236: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:531
    Mass (Da):59,384
    Checksum:i69211E04631124B4
    GO

    Sequence cautioni

    The sequence BAA91075.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB14762.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti316 – 3161M → V in BAA91075. (PubMed:14702039)Curated
    Sequence conflicti327 – 3271E → G in BAF83833. (PubMed:14702039)Curated
    Sequence conflicti484 – 4841I → V in BAG51521. (PubMed:14702039)Curated
    Sequence conflicti594 – 5941G → D in BAB14762. (PubMed:14702039)Curated
    Sequence conflicti605 – 6051Q → R in BAF34150. (PubMed:17215513)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti627 – 6271V → I.
    Corresponds to variant rs2303708 [ dbSNP | Ensembl ].
    VAR_032604
    Natural varianti679 – 6791G → R in MRT5; impairs proper intracellular localization. 1 Publication
    VAR_068530

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 236236Missing in isoform 3. 1 PublicationVSP_053598Add
    BLAST
    Alternative sequencei85 – 12036SHAKE…QPLSW → R in isoform 2. 1 PublicationVSP_042621Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB255451 mRNA. Translation: BAF34150.1.
    AK000310 mRNA. Translation: BAA91075.1. Different initiation.
    AK023994 mRNA. Translation: BAB14762.1. Different initiation.
    AK055456 mRNA. Translation: BAG51521.1.
    AK291144 mRNA. Translation: BAF83833.1.
    AK298980 mRNA. Translation: BAG61074.1.
    AC010366 Genomic DNA. No translation available.
    AC027334 Genomic DNA. No translation available.
    CH471102 Genomic DNA. Translation: EAX08105.1.
    CH471102 Genomic DNA. Translation: EAX08106.1.
    BC001041 mRNA. Translation: AAH01041.3.
    BC137083 mRNA. Translation: AAI37084.1.
    CCDSiCCDS3869.1. [Q08J23-1]
    CCDS54832.1. [Q08J23-2]
    RefSeqiNP_001180384.1. NM_001193455.1. [Q08J23-2]
    NP_060225.4. NM_017755.5. [Q08J23-1]
    UniGeneiHs.481526.

    Genome annotation databases

    EnsembliENST00000264670; ENSP00000264670; ENSG00000037474. [Q08J23-1]
    ENST00000506139; ENSP00000420957; ENSG00000037474. [Q08J23-2]
    GeneIDi54888.
    KEGGihsa:54888.
    UCSCiuc003jdt.3. human. [Q08J23-1]
    uc011cmk.2. human. [Q08J23-2]

    Polymorphism databases

    DMDMi148887180.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB255451 mRNA. Translation: BAF34150.1 .
    AK000310 mRNA. Translation: BAA91075.1 . Different initiation.
    AK023994 mRNA. Translation: BAB14762.1 . Different initiation.
    AK055456 mRNA. Translation: BAG51521.1 .
    AK291144 mRNA. Translation: BAF83833.1 .
    AK298980 mRNA. Translation: BAG61074.1 .
    AC010366 Genomic DNA. No translation available.
    AC027334 Genomic DNA. No translation available.
    CH471102 Genomic DNA. Translation: EAX08105.1 .
    CH471102 Genomic DNA. Translation: EAX08106.1 .
    BC001041 mRNA. Translation: AAH01041.3 .
    BC137083 mRNA. Translation: AAI37084.1 .
    CCDSi CCDS3869.1. [Q08J23-1 ]
    CCDS54832.1. [Q08J23-2 ]
    RefSeqi NP_001180384.1. NM_001193455.1. [Q08J23-2 ]
    NP_060225.4. NM_017755.5. [Q08J23-1 ]
    UniGenei Hs.481526.

    3D structure databases

    ProteinModelPortali Q08J23.
    SMRi Q08J23. Positions 45-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120236. 59 interactions.
    DIPi DIP-52456N.
    IntActi Q08J23. 8 interactions.
    MINTi MINT-4851220.
    STRINGi 9606.ENSP00000264670.

    PTM databases

    PhosphoSitei Q08J23.

    Polymorphism databases

    DMDMi 148887180.

    Proteomic databases

    MaxQBi Q08J23.
    PaxDbi Q08J23.
    PeptideAtlasi Q08J23.
    PRIDEi Q08J23.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264670 ; ENSP00000264670 ; ENSG00000037474 . [Q08J23-1 ]
    ENST00000506139 ; ENSP00000420957 ; ENSG00000037474 . [Q08J23-2 ]
    GeneIDi 54888.
    KEGGi hsa:54888.
    UCSCi uc003jdt.3. human. [Q08J23-1 ]
    uc011cmk.2. human. [Q08J23-2 ]

    Organism-specific databases

    CTDi 54888.
    GeneCardsi GC05M006654.
    H-InvDB HIX0004733.
    HGNCi HGNC:25994. NSUN2.
    HPAi HPA037896.
    MIMi 610916. gene.
    611091. phenotype.
    neXtProti NX_Q08J23.
    Orphaneti 88616. Autosomal recessive nonsyndromic intellectual disability.
    235. Dubowitz syndrome.
    PharmGKBi PA134953940.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0144.
    HOGENOMi HOG000205147.
    HOVERGENi HBG106711.
    InParanoidi Q08J23.
    KOi K15335.
    OMAi PIEKFYA.
    OrthoDBi EOG72VH5D.
    PhylomeDBi Q08J23.
    TreeFami TF300702.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS12087-MONOMER.

    Miscellaneous databases

    ChiTaRSi NSUN2. human.
    GeneWikii NSUN2.
    GenomeRNAii 54888.
    NextBioi 27034002.
    PROi Q08J23.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08J23.
    Bgeei Q08J23.
    CleanExi HS_NSUN2.
    Genevestigatori Q08J23.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-139, INTERACTION WITH NPM1 AND NCL, MUTAGENESIS OF SER-139.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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).
      Tissue: Lung and Placenta.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Identification of human tRNA:m5C methyltransferase catalysing intron-dependent m5C formation in the first position of the anticodon of the pre-tRNA Leu (CAA)."
      Brzezicha B., Schmidt M., Makalowska I., Jarmolowski A., Pienkowska J., Szweykowska-Kulinska Z.
      Nucleic Acids Res. 34:6034-6043(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-473; SER-743 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-593 AND SER-743, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: MALONYLATION AT LYS-586.
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-593, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: INVOLVEMENT IN MRT5, TISSUE SPECIFICITY.
    19. "The human tRNA m (5) C methyltransferase Misu is multisite-specific."
      Auxilien S., Guerineau V., Szweykowska-Kulinska Z., Golinelli-Pimpaneau B.
      RNA Biol. 9:1331-1338(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    20. Cited for: VARIANT MRT5 ARG-679, CHARACTERIZATION OF VARIANT MRT5 ARG-679.

    Entry informationi

    Entry nameiNSUN2_HUMAN
    AccessioniPrimary (citable) accession number: Q08J23
    Secondary accession number(s): A8K529
    , B2RNR4, B3KP09, B4DQW2, G3V1R4, Q9BVN4, Q9H858, Q9NXD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3