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Q9BSV6 (SEN34_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 Sen34

EC=4.6.1.16
Alternative name(s):
Leukocyte receptor cluster member 5
tRNA-intron endonuclease Sen34
Short name=HsSen34
Gene names
Name:TSEN34
Synonyms:LENG5, SEN34
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length310 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. It probably carries the active site for 3'-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. Ref.1

Catalytic activity

PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.

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. Ref.6

Subcellular location

Nucleus. Nucleusnucleolus. Note: May be transiently localized in the nucleolus. Ref.1

Involvement in disease

Pontocerebellar hypoplasia 2C (PCH2C) [MIM:612390]: A disorder characterized by an abnormally small cerebellum and brainstem, and progressive microcephaly from birth combined with extrapyramidal dyskinesia. Severe chorea occurs and epilepsy is frequent. There are no signs of spinal cord anterior horn cells degeneration.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Miscellaneous

Belongs to the leukocyte receptor cluster (LRC) present on 19q13.4.

Sequence similarities

Belongs to the tRNA-intron endonuclease family.

Sequence caution

The sequence BAB15284.1 differs from that shown. Reason: Erroneous termination at position 311. Translated as stop.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310tRNA-splicing endonuclease subunit Sen34
PRO_0000109463

Sites

Active site2471 By similarity
Active site2551 By similarity
Active site2861 By similarity

Natural variations

Natural variant581R → W in PCH2C. Ref.11
VAR_054811
Natural variant1121L → V. Ref.2
Corresponds to variant rs17849378 [ dbSNP | Ensembl ].
VAR_061149

Sequences

Sequence LengthMass (Da)Tools
Q9BSV6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1C1522D030148EC3

FASTA31033,652
        10         20         30         40         50         60 
MLVVEVANGR SLVWGAEAVQ ALRERLGVGG RTVGALPRGP RQNSRLGLPL LLMPEEARLL 

        70         80         90        100        110        120 
AEIGAVTLVS APRPDSRHHS LALTSFKRQQ EESFQEQSAL AAEARETRRQ ELLEKITEGQ 

       130        140        150        160        170        180 
AAKKQKLEQA SGASSSQEAG SSQAAKEDET SDGQASGEQE EAGPSSSQAG PSNGVAPLPR 

       190        200        210        220        230        240 
SALLVQLATA RPRPVKARPL DWRVQSKDWP HAGRPAHELR YSIYRDLWER GFFLSAAGKF 

       250        260        270        280        290        300 
GGDFLVYPGD PLRFHAHYIA QCWAPEDTIP LQDLVAAGRL GTSVRKTLLL CSPQPDGKVV 

       310 
YTSLQWASLQ 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, COMPONENT OF A COMPLEX WITH SEN2; SEN15; SEN54 AND CLP1.
[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. expand/collapse author list , 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], VARIANT VAL-112.
Tissue: Kidney epithelium.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Brain and Eye.
[6]"Extensive gene duplications and a large inversion characterize the human leukocyte receptor cluster."
Wende H., Volz A., Ziegler A.
Immunogenetics 51:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE LRC.
[7]Erratum
Wende H., Volz A., Ziegler A.
Immunogenetics 52:3-4(2001)
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"tRNA splicing endonuclease mutations cause pontocerebellar hypoplasia."
Budde B.S., Namavar Y., Barth P.G., Poll-The B.T., Nuernberg G., Becker C., van Ruissen F., Weterman M.A.J., Fluiter K., te Beek E.T., Aronica E., van der Knaap M.S., Hoehne W., Toliat M.R., Crow Y.J., Steinling M., Voit T., Roelenso F. expand/collapse author list , Brussel W., Brockmann K., Kyllerman M., Boltshauser E., Hammersen G., Willemsen M., Basel-Vanagaite L., Kraegeloh-Mann I., de Vries L.S., Sztriha L., Muntoni F., Ferrie C.D., Battini R., Hennekam R.C.M., Grillo E., Beemer F.A., Stoets L.M.E., Wollnik B., Nuernberg P., Baas F.
Nat. Genet. 40:1113-1118(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PCH2C TRP-58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK025929 mRNA. Translation: BAB15284.1. Sequence problems.
CU457734 Genomic DNA. Translation: CAP19124.1.
CU151838 Genomic DNA. Translation: CAQ09596.1.
CH471135 Genomic DNA. Translation: EAW72203.1.
BC004530 mRNA. Translation: AAH04530.1.
BC020805 mRNA. Translation: AAH20805.1.
CCDSCCDS42609.1.
RefSeqNP_001070914.1. NM_001077446.3.
NP_001269261.1. NM_001282332.1.
NP_076980.2. NM_024075.4.
UniGeneHs.15580.

3D structure databases

ProteinModelPortalQ9BSV6.
SMRQ9BSV6. Positions 213-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122505. 14 interactions.
STRING9606.ENSP00000305524.

PTM databases

PhosphoSiteQ9BSV6.

Polymorphism databases

DMDM50401668.

Proteomic databases

MaxQBQ9BSV6.
PaxDbQ9BSV6.
PeptideAtlasQ9BSV6.
PRIDEQ9BSV6.

Protocols and materials databases

DNASU79042.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302937; ENSP00000305524; ENSG00000170892.
ENST00000396383; ENSP00000379667; ENSG00000170892.
ENST00000396388; ENSP00000379671; ENSG00000170892.
ENST00000571364; ENSP00000460819; ENSG00000273235.
ENST00000571677; ENSP00000460904; ENSG00000262716.
ENST00000572746; ENSP00000459858; ENSG00000273235.
ENST00000572922; ENSP00000458776; ENSG00000262868.
ENST00000573330; ENSP00000458839; ENSG00000262868.
ENST00000573700; ENSP00000458617; ENSG00000262716.
ENST00000574141; ENSP00000458732; ENSG00000262868.
ENST00000575240; ENSP00000460175; ENSG00000273235.
ENST00000575967; ENSP00000461803; ENSG00000262716.
ENST00000604966; ENSP00000475123; ENSG00000270502.
ENST00000605174; ENSP00000475117; ENSG00000270502.
ENST00000605624; ENSP00000474517; ENSG00000270502.
ENST00000607908; ENSP00000477363; ENSG00000273053.
ENST00000608211; ENSP00000477288; ENSG00000272561.
ENST00000608445; ENSP00000477336; ENSG00000272739.
ENST00000608656; ENSP00000477302; ENSG00000272561.
ENST00000609057; ENSP00000476430; ENSG00000272705.
ENST00000609180; ENSP00000477414; ENSG00000272705.
ENST00000609466; ENSP00000477459; ENSG00000273053.
ENST00000609559; ENSP00000477061; ENSG00000273490.
ENST00000609614; ENSP00000476947; ENSG00000272739.
ENST00000609633; ENSP00000477098; ENSG00000273053.
ENST00000609822; ENSP00000476350; ENSG00000272739.
ENST00000609869; ENSP00000476939; ENSG00000272705.
ENST00000610006; ENSP00000477364; ENSG00000272561.
ENST00000610082; ENSP00000477383; ENSG00000273490.
ENST00000610118; ENSP00000477116; ENSG00000273490.
GeneID79042.
KEGGhsa:79042.
UCSCuc002qdu.3. human.

Organism-specific databases

CTD79042.
GeneCardsGC19P054863.
HGNCHGNC:15506. TSEN34.
HPAHPA041111.
MIM608754. gene.
612390. phenotype.
neXtProtNX_Q9BSV6.
Orphanet2524. Pontocerebellar hypoplasia type 2.
PharmGKBPA134871088.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1676.
HOGENOMHOG000232197.
HOVERGENHBG054846.
InParanoidQ9BSV6.
KOK15323.
PhylomeDBQ9BSV6.
TreeFamTF314631.

Gene expression databases

ArrayExpressQ9BSV6.
BgeeQ9BSV6.
CleanExHS_TSEN34.
GenevestigatorQ9BSV6.

Family and domain databases

Gene3D3.40.1350.10. 1 hit.
InterProIPR011856. tRNA_endonuc-like_dom.
IPR006677. tRNA_intron_Endonuc_cat-like.
IPR006676. tRNA_splic.
IPR016690. tRNA_splic_SEN34.
[Graphical view]
PfamPF01974. tRNA_int_endo. 1 hit.
[Graphical view]
PIRSFPIRSF017250. tRNA_splic_SEN34. 1 hit.
SUPFAMSSF53032. SSF53032. 1 hit.
TIGRFAMsTIGR00324. endA. 1 hit.
ProtoNetSearch...

Other

GeneWikiTSEN34.
GenomeRNAi79042.
NextBio67781.
PROQ9BSV6.
SOURCESearch...

Entry information

Entry nameSEN34_HUMAN
AccessionPrimary (citable) accession number: Q9BSV6
Secondary accession number(s): A6NNB1 expand/collapse secondary AC list , B0V3J1, Q9BVT1, Q9H6H5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM