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Q6P7W5 (SEN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. 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
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 Sen2
EC=3.1.27.9
Alternative name(s):
tRNA-intron endonuclease Sen2
Gene names
Name:Tsen2
Synonyms:Sen2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Endonucleolytic cleavage of pre-tRNA, producing 5'-hydroxy and 2',3'-cyclic phosphate termini, and specifically removing the intron.

Subunit structure

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

Sequence similarities

Belongs to the tRNA-intron endonuclease family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460tRNA-splicing endonuclease subunit Sen2
PRO_0000109453

Sites

Active site3641 By similarity
Active site3721 By similarity
Active site4111 By similarity

Amino acid modifications

Modified residue4031Phosphoserine Ref.3
Modified residue4061Phosphoserine Ref.3
Modified residue4101Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q6P7W5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 1FC32E811F488184

FASTA46052,214
        10         20         30         40         50         60 
MAEAVFRAPK RKRRVYESYE SPLPIPFGQD QGPRKEFRIF QAEMISNNVV VRGTEDMEQL 

        70         80         90        100        110        120 
YGKGYFGKGI LSRSRPNFTI ANPTLAARWK GVQTDMPIIT SEKYQHRVEW ARDFLRRQGH 

       130        140        150        160        170        180 
DESTVQKILT DYTEPLELPC REEKEETPQH EPLSSKADSS LEGRVEKDEL PVTPGGAGQS 

       190        200        210        220        230        240 
DDLPGLGTHS DCLQEGPGHA TLAAASPSSH NGHVAEDPEV LPQETLVPQG GLWPEASSQA 

       250        260        270        280        290        300 
AGEKRAAHEY VLIEEELCGA QEEEAAAASD EKLLKRKKLV CRRNPYRIFE YLQLSLEEAF 

       310        320        330        340        350        360 
FLAYALGCLS IYYEKEPLTI VKLWQAFTAV QPTFRTTYMA YHYFRSKGWV PKVGLKYGTD 

       370        380        390        400        410        420 
LLLYRKGPPF YHASYSVIIE LLDDNYEGSL RRPFSWKSLA ALSRVSGNVS KELMLCYLIK 

       430        440        450        460 
PSTMTAEDME TPECMKRIQV QEVILSRWVS SRERSDQDEL

« 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: 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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-406 AND SER-410, MASS SPECTROMETRY.
Tissue: Embryonic brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK134697 mRNA. Translation: BAE22246.1.
BC061473 mRNA. Translation: AAH61473.1.
IPIIPI00125172.
RefSeqNP_950198.1. NM_199033.1.
UniGeneMm.291208.

3D structure databases

ProteinModelPortalQ6P7W5.
SMRQ6P7W5. Positions 292-415.
ModBaseSearch...

PTM databases

PhosphoSiteQ6P7W5.

Proteomic databases

PRIDEQ6P7W5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040234; ENSMUSP00000038211; ENSMUSG00000042389.
GeneID381802.
KEGGmmu:381802.
UCSCuc009diu.1. mouse.

Organism-specific databases

CTD80746.
MGIMGI:2141599. Tsen2.

Phylogenomic databases

eggNOGCOG1676.
GeneTreeENSGT00390000013266.
HOGENOMHOG000154285.
HOVERGENHBG056610.
InParanoidQ6P7W5.
KOK15322.
OMAERSDQDE.
OrthoDBEOG4Z36DM.

Gene expression databases

BgeeQ6P7W5.
GenevestigatorQ6P7W5.
GermOnlineENSMUSG00000042389. Mus musculus.

Family and domain databases

Gene3D3.40.1350.10. 1 hit.
InterProIPR011856. tRNA_endonuc-like_dom.
IPR006677. tRNA_intron_Endonuc_cat-like.
IPR006678. tRNA_intron_Endonuc_N.
IPR016589. tRNA_splic_SEN2.
[Graphical view]
PfamPF01974. tRNA_int_endo. 1 hit.
PF02778. tRNA_int_endo_N. 1 hit.
[Graphical view]
PIRSFPIRSF011789. tRNA_splic_SEN2. 1 hit.
SUPFAMSSF53032. tRNA_int_endo_C. 1 hit.
ProtoNetSearch...

Other

NextBio402575.
SOURCESearch...

Entry information

Entry nameSEN2_MOUSE
AccessionPrimary (citable) accession number: Q6P7W5
Secondary accession number(s): Q3UYG6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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