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Protein

tRNA-splicing endonuclease subunit Sen54

Gene

Tsen54

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-splicing endonuclease subunit Sen54
Alternative name(s):
tRNA-intron endonuclease Sen54
Gene namesi
Name:Tsen54
Synonyms:Sen54
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1923515. Tsen54.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 525525tRNA-splicing endonuclease subunit Sen54PRO_0000194030Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei178 – 1781PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8C2A2.
MaxQBiQ8C2A2.
PaxDbiQ8C2A2.
PRIDEiQ8C2A2.

PTM databases

PhosphoSiteiQ8C2A2.

Expressioni

Gene expression databases

BgeeiQ8C2A2.
ExpressionAtlasiQ8C2A2. baseline and differential.
GenevisibleiQ8C2A2. MM.

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021134.

Structurei

3D structure databases

ProteinModelPortaliQ8C2A2.
SMRiQ8C2A2. Positions 102-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SEN54 family.Curated

Phylogenomic databases

eggNOGiKOG4772. Eukaryota.
ENOG4111KNC. LUCA.
GeneTreeiENSGT00390000004214.
HOGENOMiHOG000049169.
HOVERGENiHBG061211.
InParanoidiQ8C2A2.
KOiK15326.
OMAiAGKFWQT.
OrthoDBiEOG73V6P9.
PhylomeDBiQ8C2A2.
TreeFamiTF314691.

Family and domain databases

InterProiIPR024337. tRNA_splic_suSen54.
IPR024336. tRNA_splic_suSen54_N.
[Graphical view]
PANTHERiPTHR21027. PTHR21027. 3 hits.
PfamiPF12928. tRNA_int_end_N2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8C2A2-1) [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

        10         20         30         40         50
MEPEPEPGSV EVPAGRVLSA SELRAARSRS QKLPQRSHGP KDFLPDGSEA
60 70 80 90 100
QAERLRLCRQ ELWQLLAEER VERLGSLVAA EWKPEEGFVE LTSPAGKFWQ
110 120 130 140 150
TMGYSEEGRQ RLHPEEALYL LECGSIQLFY QDLPLSIQEA YQLLLTEDTL
160 170 180 190 200
SFLQYQVFSH LKRLGYVVRR FQLSSVVSPY ERQLNLDGYA QCLEDGSGKR
210 220 230 240 250
KRSSSCRSVN KKPKVLQNSL PPVSLAASSS PACDQSSQYP EEKSQDSSPR
260 270 280 290 300
QGSELPLQFL GSSEPCSDLA REDVGCDRES HKIENGAKGT PKLRWNFEQI
310 320 330 340 350
SFPNMASDSR HTFLPAPAPE LLPANVIGRG TDAESWCQKL NQRREKLSRR
360 370 380 390 400
DREQQAVVQQ FREDVNADPE VRGCSSWQEY KELLQRRQTQ KSQPRPPHLW
410 420 430 440 450
GQSVTPLLDP DKADCPAAVL QHISVLQTTH LADGGYRLLE KSGGLQISFD
460 470 480 490 500
VYQADAVATF RKNSPGKPYV RMCISGFDDP VPDLCSLKCL TYQSGDVPLI
510 520
FALVDHGDIS FYSFRDFTLP RDLGH
Length:525
Mass (Da):59,083
Last modified:July 19, 2004 - v2
Checksum:iEBC3D92CFA647BF7
GO
Isoform 2 (identifier: Q8C2A2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     438-476: Missing.

Note: No experimental confirmation available.
Show »
Length:486
Mass (Da):54,854
Checksum:iEE255B3D43473402
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441S → P in BAC40696 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei438 – 47639Missing in isoform 2. 1 PublicationVSP_010990Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002758 mRNA. Translation: BAB22335.1.
AK089005 mRNA. Translation: BAC40696.1.
AL645852 Genomic DNA. Translation: CAM21979.1.
AL645852 Genomic DNA. Translation: CAM21980.1.
CCDSiCCDS25648.1. [Q8C2A2-1]
RefSeqiNP_083833.1. NM_029557.1. [Q8C2A2-1]
UniGeneiMm.275438.

Genome annotation databases

EnsembliENSMUST00000021134; ENSMUSP00000021134; ENSMUSG00000020781. [Q8C2A2-1]
ENSMUST00000106481; ENSMUSP00000102090; ENSMUSG00000020781. [Q8C2A2-2]
GeneIDi76265.
KEGGimmu:76265.
UCSCiuc007miq.1. mouse. [Q8C2A2-1]
uc011yhp.1. mouse. [Q8C2A2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002758 mRNA. Translation: BAB22335.1.
AK089005 mRNA. Translation: BAC40696.1.
AL645852 Genomic DNA. Translation: CAM21979.1.
AL645852 Genomic DNA. Translation: CAM21980.1.
CCDSiCCDS25648.1. [Q8C2A2-1]
RefSeqiNP_083833.1. NM_029557.1. [Q8C2A2-1]
UniGeneiMm.275438.

3D structure databases

ProteinModelPortaliQ8C2A2.
SMRiQ8C2A2. Positions 102-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000021134.

PTM databases

PhosphoSiteiQ8C2A2.

Proteomic databases

EPDiQ8C2A2.
MaxQBiQ8C2A2.
PaxDbiQ8C2A2.
PRIDEiQ8C2A2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021134; ENSMUSP00000021134; ENSMUSG00000020781. [Q8C2A2-1]
ENSMUST00000106481; ENSMUSP00000102090; ENSMUSG00000020781. [Q8C2A2-2]
GeneIDi76265.
KEGGimmu:76265.
UCSCiuc007miq.1. mouse. [Q8C2A2-1]
uc011yhp.1. mouse. [Q8C2A2-2]

Organism-specific databases

CTDi283989.
MGIiMGI:1923515. Tsen54.

Phylogenomic databases

eggNOGiKOG4772. Eukaryota.
ENOG4111KNC. LUCA.
GeneTreeiENSGT00390000004214.
HOGENOMiHOG000049169.
HOVERGENiHBG061211.
InParanoidiQ8C2A2.
KOiK15326.
OMAiAGKFWQT.
OrthoDBiEOG73V6P9.
PhylomeDBiQ8C2A2.
TreeFamiTF314691.

Miscellaneous databases

ChiTaRSiTsen54. mouse.
NextBioi344883.
PROiQ8C2A2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C2A2.
ExpressionAtlasiQ8C2A2. baseline and differential.
GenevisibleiQ8C2A2. MM.

Family and domain databases

InterProiIPR024337. tRNA_splic_suSen54.
IPR024336. tRNA_splic_suSen54_N.
[Graphical view]
PANTHERiPTHR21027. PTHR21027. 3 hits.
PfamiPF12928. tRNA_int_end_N2. 1 hit.
[Graphical view]
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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-525 (ISOFORM 2).
    Strain: C57BL/6J and NOD.
    Tissue: Kidney and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiSEN54_MOUSE
AccessioniPrimary (citable) accession number: Q8C2A2
Secondary accession number(s): B1ATA4, B1ATA5, Q9DCI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: May 11, 2016
This is version 91 of the entry and version 2 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

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 one 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.