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Q8R3W5 (SEN15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA-splicing endonuclease subunit Sen15
Alternative name(s):
tRNA-intron endonuclease Sen15
Gene names
Name:Tsen15
Synonyms:Sen15
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

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

Sequence similarities

Belongs to the SEN15 family.

Caution

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

Ontologies

Keywords
   Biological processmRNA processing
tRNA processing
   Cellular componentNucleus
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA splicing, via endonucleolytic cleavage and ligation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontRNA-intron endonuclease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168tRNA-splicing endonuclease subunit Sen15
PRO_0000194024

Experimental info

Sequence conflict5 – 84SDSE → TSSK in BAB30855. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8R3W5 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 99D8E6E14C2FCAA0

FASTA16818,530
        10         20         30         40         50         60 
MEERSDSEPT PGCSGPGPAP VRDGGGAHTW APEDAWMGTH PKYLEMMELD IGDATQVYIA 

        70         80         90        100        110        120 
FLVYLDLMES KSWHEVNCVG IPELQLICLL GTEIEGEGLQ TVVPTPISAS LSHNRIREIL 

       130        140        150        160 
KASRKLQGDP ELPMSFTLAI VESDSTIVYY KLTDGFMLPD PQNISLRR 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK017650 mRNA. Translation: BAB30855.1.
BC024342 mRNA. Translation: AAH24342.1.
BC145701 mRNA. Translation: AAI45702.1.
RefSeqNP_079953.2. NM_025677.3.
UniGeneMm.379120.

3D structure databases

ProteinModelPortalQ8R3W5.
SMRQ8R3W5. Positions 33-154.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ8R3W5.
PRIDEQ8R3W5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID66637.
KEGGmmu:66637.

Organism-specific databases

CTD116461.
MGIMGI:1913887. Tsen15.

Phylogenomic databases

eggNOGNOG44101.
HOGENOMHOG000290172.
HOVERGENHBG058504.
InParanoidA6H601.
KOK15324.
PhylomeDBQ8R3W5.

Gene expression databases

GenevestigatorQ8R3W5.

Family and domain databases

InterProIPR018593. tRNA-endonuc_su_Sen15.
IPR006677. tRNA_intron_Endonuc_cat-like.
[Graphical view]
PfamPF09631. Sen15. 1 hit.
[Graphical view]
SUPFAMSSF53032. SSF53032. 1 hit.
ProtoNetSearch...

Other

NextBio322238.
PROQ8R3W5.
SOURCESearch...

Entry information

Entry nameSEN15_MOUSE
AccessionPrimary (citable) accession number: Q8R3W5
Secondary accession number(s): A6H601, Q9CQW8, Q9CYI5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot