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Q8WW01

- SEN15_HUMAN

UniProt

Q8WW01 - SEN15_HUMAN

Protein

tRNA-splicing endonuclease subunit Sen15

Gene

TSEN15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Non-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. 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.1 Publication

    GO - Molecular functioni

    1. 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 - Biological processi

    mRNA processing, tRNA processing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA-splicing endonuclease subunit Sen15
    Alternative name(s):
    SEN15 homolog
    Short name:
    HsSEN15
    tRNA-intron endonuclease Sen15
    Gene namesi
    Name:TSEN15
    Synonyms:C1orf19, SEN15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16791. TSEN15.

    Subcellular locationi

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

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162407135.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 171171tRNA-splicing endonuclease subunit Sen15PRO_0000194023Add
    BLAST

    Proteomic databases

    MaxQBiQ8WW01.
    PaxDbiQ8WW01.
    PRIDEiQ8WW01.

    PTM databases

    PhosphoSiteiQ8WW01.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in testis and uterus.1 Publication

    Gene expression databases

    ArrayExpressiQ8WW01.
    BgeeiQ8WW01.
    CleanExiHS_TSEN15.
    GenevestigatoriQ8WW01.

    Organism-specific databases

    HPAiHPA029237.

    Interactioni

    Subunit structurei

    Homodimer. 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 CSTF2.1 Publication

    Protein-protein interaction databases

    BioGridi125513. 9 interactions.
    IntActiQ8WW01. 4 interactions.
    MINTiMINT-1193061.
    STRINGi9606.ENSP00000355299.

    Structurei

    Secondary structure

    1
    171
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 507
    Beta strandi52 – 543
    Helixi57 – 7216
    Beta strandi77 – 848
    Turni85 – 884
    Beta strandi89 – 979
    Beta strandi104 – 1096
    Beta strandi113 – 1153
    Helixi116 – 12914
    Beta strandi138 – 1447
    Beta strandi150 – 1567

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GW6NMR-A/B36-157[»]
    ProteinModelPortaliQ8WW01.
    SMRiQ8WW01. Positions 36-157.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8WW01.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SEN15 family.Curated

    Phylogenomic databases

    eggNOGiNOG44101.
    HOGENOMiHOG000290172.
    HOVERGENiHBG058504.
    InParanoidiQ8WW01.
    KOiK15324.
    OMAiDASQVYI.
    OrthoDBiEOG757D0M.
    PhylomeDBiQ8WW01.
    TreeFamiTF336144.

    Family and domain databases

    InterProiIPR018593. tRNA-endonuc_su_Sen15.
    IPR006677. tRNA_intron_Endonuc_cat-like.
    [Graphical view]
    PfamiPF09631. Sen15. 1 hit.
    [Graphical view]
    SUPFAMiSSF53032. SSF53032. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WW01-1) [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

    MEERGDSEPT PGCSGLGPGG VRGFGDGGGA PSWAPEDAWM GTHPKYLEMM    50
    ELDIGDATQV YVAFLVYLDL MESKSWHEVN CVGLPELQLI CLVGTEIEGE 100
    GLQTVVPTPI TASLSHNRIR EILKASRKLQ GDPDLPMSFT LAIVESDSTI 150
    VYYKLTDGFM LPDPQNISLR R 171
    Length:171
    Mass (Da):18,641
    Last modified:March 1, 2002 - v1
    Checksum:iE728BF39A89DD1FB
    GO
    Isoform 2 (identifier: Q8WW01-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         120-171: REILKASRKLQGDPDLPMSFTLAIVESDSTIVYYKLTDGFMLPDPQNISLRR → FLLEDDIHVS

    Note: No experimental confirmation available.

    Show »
    Length:129
    Mass (Da):13,888
    Checksum:i681214969EA67A76
    GO

    Sequence cautioni

    The sequence AAG60614.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191G → D.
    Corresponds to variant rs2274432 [ dbSNP | Ensembl ].
    VAR_019457
    Natural varianti59 – 591Q → H.
    Corresponds to variant rs1046934 [ dbSNP | Ensembl ].
    VAR_019458

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei120 – 17152REILK…ISLRR → FLLEDDIHVS in isoform 2. 1 PublicationVSP_042723Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF288394 mRNA. Translation: AAG60614.1. Different initiation.
    AK296655 mRNA. Translation: BAG59252.1.
    AL157943 Genomic DNA. No translation available.
    AL158011 Genomic DNA. No translation available.
    CH471067 Genomic DNA. Translation: EAW91174.1.
    BC022030 mRNA. Translation: AAH22030.1.
    CCDSiCCDS1361.1. [Q8WW01-1]
    CCDS44286.1. [Q8WW01-2]
    RefSeqiNP_001120866.1. NM_001127394.2. [Q8WW01-2]
    NP_443197.1. NM_052965.2. [Q8WW01-1]
    UniGeneiHs.548197.

    Genome annotation databases

    EnsembliENST00000361641; ENSP00000355299; ENSG00000198860. [Q8WW01-1]
    ENST00000423085; ENSP00000402002; ENSG00000198860. [Q8WW01-2]
    GeneIDi116461.
    KEGGihsa:116461.
    UCSCiuc001gqt.4. human. [Q8WW01-1]
    uc001gqu.4. human. [Q8WW01-2]

    Polymorphism databases

    DMDMi50401628.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF288394 mRNA. Translation: AAG60614.1 . Different initiation.
    AK296655 mRNA. Translation: BAG59252.1 .
    AL157943 Genomic DNA. No translation available.
    AL158011 Genomic DNA. No translation available.
    CH471067 Genomic DNA. Translation: EAW91174.1 .
    BC022030 mRNA. Translation: AAH22030.1 .
    CCDSi CCDS1361.1. [Q8WW01-1 ]
    CCDS44286.1. [Q8WW01-2 ]
    RefSeqi NP_001120866.1. NM_001127394.2. [Q8WW01-2 ]
    NP_443197.1. NM_052965.2. [Q8WW01-1 ]
    UniGenei Hs.548197.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GW6 NMR - A/B 36-157 [» ]
    ProteinModelPortali Q8WW01.
    SMRi Q8WW01. Positions 36-157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125513. 9 interactions.
    IntActi Q8WW01. 4 interactions.
    MINTi MINT-1193061.
    STRINGi 9606.ENSP00000355299.

    PTM databases

    PhosphoSitei Q8WW01.

    Polymorphism databases

    DMDMi 50401628.

    Proteomic databases

    MaxQBi Q8WW01.
    PaxDbi Q8WW01.
    PRIDEi Q8WW01.

    Protocols and materials databases

    DNASUi 116461.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361641 ; ENSP00000355299 ; ENSG00000198860 . [Q8WW01-1 ]
    ENST00000423085 ; ENSP00000402002 ; ENSG00000198860 . [Q8WW01-2 ]
    GeneIDi 116461.
    KEGGi hsa:116461.
    UCSCi uc001gqt.4. human. [Q8WW01-1 ]
    uc001gqu.4. human. [Q8WW01-2 ]

    Organism-specific databases

    CTDi 116461.
    GeneCardsi GC01P184020.
    HGNCi HGNC:16791. TSEN15.
    HPAi HPA029237.
    MIMi 608756. gene.
    neXtProti NX_Q8WW01.
    PharmGKBi PA162407135.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44101.
    HOGENOMi HOG000290172.
    HOVERGENi HBG058504.
    InParanoidi Q8WW01.
    KOi K15324.
    OMAi DASQVYI.
    OrthoDBi EOG757D0M.
    PhylomeDBi Q8WW01.
    TreeFami TF336144.

    Miscellaneous databases

    EvolutionaryTracei Q8WW01.
    GeneWikii C1orf19.
    GenomeRNAii 116461.
    NextBioi 79944.
    PROi Q8WW01.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WW01.
    Bgeei Q8WW01.
    CleanExi HS_TSEN15.
    Genevestigatori Q8WW01.

    Family and domain databases

    InterProi IPR018593. tRNA-endonuc_su_Sen15.
    IPR006677. tRNA_intron_Endonuc_cat-like.
    [Graphical view ]
    Pfami PF09631. Sen15. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53032. SSF53032. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus."
      Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M., Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H., Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M., Carpten J.D.
      Genomics 73:211-222(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    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] (ISOFORM 2).
      Tissue: Colon.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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: Testis.
    6. "Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3' end formation."
      Paushkin S.V., Patel M., Furia B.S., Peltz S.W., Trotta C.R.
      Cell 117:311-321(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, COMPONENT OF A COMPLEX WITH SEN2; SEN54; SEN34 AND CLP1.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Three-dimensional structure determined for a subunit of human tRNA splicing endonuclease (Sen15) reveals a novel dimeric fold."
      Song J., Markley J.L.
      J. Mol. Biol. 366:155-164(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 36-157, SUBUNIT.

    Entry informationi

    Entry nameiSEN15_HUMAN
    AccessioniPrimary (citable) accession number: Q8WW01
    Secondary accession number(s): B4DKP0, Q9BZQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3