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Q6P7W5

- SEN2_MOUSE

UniProt

Q6P7W5 - SEN2_MOUSE

Protein

tRNA-splicing endonuclease subunit Sen2

Gene

Tsen2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. Probably carries the active site for 5'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events By similarity.By similarity

    Catalytic activityi

    PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei364 – 3641By similarity
    Active sitei372 – 3721By similarity
    Active sitei411 – 4111By similarity

    GO - Molecular functioni

    1. lyase activity Source: UniProtKB-KW
    2. nucleic acid binding Source: InterPro
    3. tRNA-intron endonuclease activity Source: InterPro

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. tRNA splicing, via endonucleolytic cleavage and ligation Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    mRNA processing, tRNA processing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA-splicing endonuclease subunit Sen2 (EC:4.6.1.16)
    Alternative name(s):
    tRNA-intron endonuclease Sen2
    Gene namesi
    Name:Tsen2
    Synonyms:Sen2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:2141599. Tsen2.

    Subcellular locationi

    Nucleus By similarity. Nucleusnucleolus By similarity
    Note: May be transiently localized in the nucleolus.By similarity

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. cytoplasm Source: Ensembl
    3. nucleolus Source: UniProtKB-SubCell
    4. tRNA-intron endonuclease complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 460460tRNA-splicing endonuclease subunit Sen2PRO_0000109453Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei403 – 4031Phosphoserine1 Publication
    Modified residuei406 – 4061Phosphoserine1 Publication
    Modified residuei410 – 4101Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ6P7W5.

    PTM databases

    PhosphoSiteiQ6P7W5.

    Expressioni

    Gene expression databases

    BgeeiQ6P7W5.
    GenevestigatoriQ6P7W5.

    Interactioni

    Subunit structurei

    tRNA splicing endonuclease is a heterotetramer composed of SEN2, SEN15, SEN34/LENG5 and SEN54. tRNA splicing endonuclease complex also contains proteins of the pre-mRNA 3'-end processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ6P7W5.
    SMRiQ6P7W5. Positions 292-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tRNA-intron endonuclease family.Curated

    Phylogenomic databases

    eggNOGiCOG1676.
    GeneTreeiENSGT00390000013266.
    HOGENOMiHOG000154285.
    HOVERGENiHBG056610.
    InParanoidiQ6P7W5.
    KOiK15322.
    OMAiKLVCRRN.
    OrthoDBiEOG76X623.
    PhylomeDBiQ6P7W5.
    TreeFamiTF314679.

    Family and domain databases

    Gene3Di3.40.1350.10. 1 hit.
    InterProiIPR011856. tRNA_endonuc-like_dom.
    IPR006677. tRNA_intron_Endonuc_cat-like.
    IPR006678. tRNA_intron_Endonuc_N.
    IPR016589. tRNA_splic_SEN2.
    [Graphical view]
    PfamiPF01974. tRNA_int_endo. 1 hit.
    PF02778. tRNA_int_endo_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF011789. tRNA_splic_SEN2. 1 hit.
    SUPFAMiSSF53032. SSF53032. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6P7W5-1 [UniParc]FASTAAdd to Basket

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    MAEAVFRAPK RKRRVYESYE SPLPIPFGQD QGPRKEFRIF QAEMISNNVV    50
    VRGTEDMEQL YGKGYFGKGI LSRSRPNFTI ANPTLAARWK GVQTDMPIIT 100
    SEKYQHRVEW ARDFLRRQGH DESTVQKILT DYTEPLELPC REEKEETPQH 150
    EPLSSKADSS LEGRVEKDEL PVTPGGAGQS DDLPGLGTHS DCLQEGPGHA 200
    TLAAASPSSH NGHVAEDPEV LPQETLVPQG GLWPEASSQA AGEKRAAHEY 250
    VLIEEELCGA QEEEAAAASD EKLLKRKKLV CRRNPYRIFE YLQLSLEEAF 300
    FLAYALGCLS IYYEKEPLTI VKLWQAFTAV QPTFRTTYMA YHYFRSKGWV 350
    PKVGLKYGTD LLLYRKGPPF YHASYSVIIE LLDDNYEGSL RRPFSWKSLA 400
    ALSRVSGNVS KELMLCYLIK PSTMTAEDME TPECMKRIQV QEVILSRWVS 450
    SRERSDQDEL 460
    Length:460
    Mass (Da):52,214
    Last modified:July 5, 2004 - v1
    Checksum:i1FC32E811F488184
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK134697 mRNA. Translation: BAE22246.1.
    BC061473 mRNA. Translation: AAH61473.1.
    CCDSiCCDS20440.1.
    RefSeqiNP_950198.1. NM_199033.1.
    UniGeneiMm.291208.

    Genome annotation databases

    EnsembliENSMUST00000040234; ENSMUSP00000038211; ENSMUSG00000042389.
    GeneIDi381802.
    KEGGimmu:381802.
    UCSCiuc009diu.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK134697 mRNA. Translation: BAE22246.1 .
    BC061473 mRNA. Translation: AAH61473.1 .
    CCDSi CCDS20440.1.
    RefSeqi NP_950198.1. NM_199033.1.
    UniGenei Mm.291208.

    3D structure databases

    ProteinModelPortali Q6P7W5.
    SMRi Q6P7W5. Positions 292-415.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q6P7W5.

    Proteomic databases

    PRIDEi Q6P7W5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040234 ; ENSMUSP00000038211 ; ENSMUSG00000042389 .
    GeneIDi 381802.
    KEGGi mmu:381802.
    UCSCi uc009diu.1. mouse.

    Organism-specific databases

    CTDi 80746.
    MGIi MGI:2141599. Tsen2.

    Phylogenomic databases

    eggNOGi COG1676.
    GeneTreei ENSGT00390000013266.
    HOGENOMi HOG000154285.
    HOVERGENi HBG056610.
    InParanoidi Q6P7W5.
    KOi K15322.
    OMAi KLVCRRN.
    OrthoDBi EOG76X623.
    PhylomeDBi Q6P7W5.
    TreeFami TF314679.

    Miscellaneous databases

    NextBioi 402575.
    PROi Q6P7W5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6P7W5.
    Genevestigatori Q6P7W5.

    Family and domain databases

    Gene3Di 3.40.1350.10. 1 hit.
    InterProi IPR011856. tRNA_endonuc-like_dom.
    IPR006677. tRNA_intron_Endonuc_cat-like.
    IPR006678. tRNA_intron_Endonuc_N.
    IPR016589. tRNA_splic_SEN2.
    [Graphical view ]
    Pfami PF01974. tRNA_int_endo. 1 hit.
    PF02778. tRNA_int_endo_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF011789. tRNA_splic_SEN2. 1 hit.
    SUPFAMi SSF53032. SSF53032. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: C57BL/6J.
      Tissue: Medulla oblongata.
    2. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-406 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.

    Entry informationi

    Entry nameiSEN2_MOUSE
    AccessioniPrimary (citable) accession number: Q6P7W5
    Secondary accession number(s): Q3UYG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 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