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Protein

tRNA-splicing endonuclease subunit Sen15

Gene

Tsen15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

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 (By similarity).By similarity

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
Complete GO annotation...

Keywords - Biological processi

mRNA processing, tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-splicing endonuclease subunit Sen15
Alternative name(s):
tRNA-intron endonuclease Sen15
Gene namesi
Name:Tsen15
Synonyms:Sen15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1913887. Tsen15.

Subcellular locationi

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

GO - Cellular componenti

  1. nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168tRNA-splicing endonuclease subunit Sen15PRO_0000194024Add
BLAST

Proteomic databases

MaxQBiQ8R3W5.
PaxDbiQ8R3W5.
PRIDEiQ8R3W5.

Expressioni

Gene expression databases

GenevestigatoriQ8R3W5.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi211612. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8R3W5.
SMRiQ8R3W5. Positions 33-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SEN15 family.Curated

Phylogenomic databases

eggNOGiNOG44101.
HOGENOMiHOG000290172.
HOVERGENiHBG058504.
InParanoidiQ8R3W5.
KOiK15324.
PhylomeDBiQ8R3W5.

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.

Sequencei

Sequence statusi: Complete.

Q8R3W5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEERSDSEPT PGCSGPGPAP VRDGGGAHTW APEDAWMGTH PKYLEMMELD
60 70 80 90 100
IGDATQVYIA FLVYLDLMES KSWHEVNCVG IPELQLICLL GTEIEGEGLQ
110 120 130 140 150
TVVPTPISAS LSHNRIREIL KASRKLQGDP ELPMSFTLAI VESDSTIVYY
160
KLTDGFMLPD PQNISLRR
Length:168
Mass (Da):18,530
Last modified:June 1, 2002 - v1
Checksum:i99D8E6E14C2FCAA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 84SDSE → TSSK in BAB30855. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK017650 mRNA. Translation: BAB30855.1.
BC024342 mRNA. Translation: AAH24342.1.
BC145701 mRNA. Translation: AAI45702.1.
CCDSiCCDS15363.1.
RefSeqiNP_079953.2. NM_025677.3.
UniGeneiMm.379120.

Genome annotation databases

GeneIDi66637.
KEGGimmu:66637.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK017650 mRNA. Translation: BAB30855.1.
BC024342 mRNA. Translation: AAH24342.1.
BC145701 mRNA. Translation: AAI45702.1.
CCDSiCCDS15363.1.
RefSeqiNP_079953.2. NM_025677.3.
UniGeneiMm.379120.

3D structure databases

ProteinModelPortaliQ8R3W5.
SMRiQ8R3W5. Positions 33-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211612. 1 interaction.

Proteomic databases

MaxQBiQ8R3W5.
PaxDbiQ8R3W5.
PRIDEiQ8R3W5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi66637.
KEGGimmu:66637.

Organism-specific databases

CTDi116461.
MGIiMGI:1913887. Tsen15.

Phylogenomic databases

eggNOGiNOG44101.
HOGENOMiHOG000290172.
HOVERGENiHBG058504.
InParanoidiQ8R3W5.
KOiK15324.
PhylomeDBiQ8R3W5.

Miscellaneous databases

NextBioi322238.
PROiQ8R3W5.
SOURCEiSearch...

Gene expression databases

GenevestigatoriQ8R3W5.

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.
ProtoNetiSearch...

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: Embryo.
  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: FVB/N-3.
    Tissue: Brain and Mammary gland.

Entry informationi

Entry nameiSEN15_MOUSE
AccessioniPrimary (citable) accession number: Q8R3W5
Secondary accession number(s): A6H601, Q9CQW8, Q9CYI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2002
Last modified: January 7, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Although only weakly related to the S.cerevisiae SEN15 protein, it probably displays the same function within the tRNA splicing endonuclease complex.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.