SEN1/YLR430W Protein Information Help

Standard Name Sen1p 1
Systematic Name Ylr430wp
Alias Cik3p , Nrd2p
ORF Classification Verified
Description Presumed helicase and subunit of the Nrd1 complex (Nrd1p-Nab3p-Sen1p); complex interacts with the exosome to mediate 3' end formation of some mRNAs, snRNAs, snoRNAs, and CUTs; has a separate role in coordinating DNA replication with transcription, by associating with moving replication forks and preventing errors that occur when forks encounter transcribed regions; homolog of Senataxin, which is implicated in Ataxia-Oculomotor Apraxia 2 and a dominant form of ALS (2, 3, 4, 5, 6, 7)
Name Description Splicing ENdonuclease 1
Experimental Data
Molecules/cell 125 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 2,231
Molecular Weight (Da) 252,495
Isoelectric Point (pI) 8.83

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Sen1p (InterPro)
Physical Interactions There are 78 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000135849 | Q00416
MIPS: YLR430W
NCBI: 172574 | 2340994 | 3123282 | 398366241 | 664872 | NP_013534.3 | NM_001182318.3
GenBank/EMBL/DDBJ: DAA09731.1 | M74589 | U20939 | U21094
External Classifications EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]
EC: 3.6.4.-
Amino Acid Sequence (or in FASTA format)
       1  MNSNNPDNNN SNNINNNNKD KDIAPNSDVQ LATVYTKAKS YIPQIEQVYQ
      51  GTNPNIQEAK LLGELLQVLA EVPKGTHLFC DPILEPISIF SLTIFSFNEE
     101  ATATWLKNHF NPILSVCDKC ILNFARGKCK MLQHFAIQRH VPHEHVAKFN
     151  DIVCQWRVEA VFPILRNISV NDNTGINITN EIETAMYECL CNPHMLRLNK
     201  QLKATFEAIF KFFYDTKHRL LDVTNPLSIK TFISGVIFCW CEGSKEENEW
     251  SRAFLKDLYS RNFHINLSNL TPDIIEEVYI HILFLQNPAN WTEIVVSQFW
     301  SRLLPVFNLF DKDVFIEYFQ VPKNVESLKK TFKFPLEPIF KMWYNHLSKS
     351  YHDKPLDFLL RGLTMFLNKF GSEFWSKIEP FTFHSILDII FNRDSFPIKL
     401  IKIQDNPIVE HQTEVYFQLT GSVTDLLSWT LPFYHALSPS KRIQMVRKVS
     451  MAFLRIIANY PSLKSIPKAC LMNSATALLR AVLTIKENER AMLYKNDEFE
     501  TVLLTKTDSR ALLNNPLIQD IIIRSASNPN DFYPGLGAAS ASVATSTMMV
     551  LAECIDFDIL LLCHRTFKLY SGKPISEIPI STNVLENVTN KIDLRSFHDG
     601  PLLAKQLLVS LKNINGLLIV PSNTAVAEAH NALNQKFLLL STRLMEKFAD
     651  ILPGQLSKIL ADEDASQGFW SCIFSSDKHL YQAATNILYN TFDVEGRLEG
     701  ILAILNSNLT VNLKNINVML QRLINCEFYE PCPRAVRVLM DVVSAFVDPI
     751  SGVFANFQTL KSQNTEKEFL KFWESCWLFL DTIYKFTLKW ASKYDYSELE
     801  NFTKDTLDLS RSLVDSFREF SDILHDQTKN LLLNVLETFK NMLYWLRLSD
     851  EVLLESCVRL IISTSDLAHE KHVKVDDSLV EMMAKYASKA KRFSNKLTEQ
     901  QASEILQKAK IFNKALTEEV ATEAENYRKE KELSRLGKVI DLTDSVPASP
     951  SLSPSLSSTI ASSSAESRAD YLQRKALSSS ITGRPRVAQP KITSFGTFQS
    1001  SANAKLHRTK PVKPLSKMEL ARMQLLNNRV VHPPSAPAFH TKSRGLSNKN
    1051  DDSSSEESDN DIESARELFA IAKAKGKGIQ TVDINGKVVK RQTAAELAKQ
    1101  ELEHMRKRLN VDMNPLYEII LQWDYTRNSE YPDDEPIGNY SDVKDFFNSP
    1151  ADYQKVMKPL LLLESWQGLC SSRDREDYKP FSIIVGNRTA VSDFYDVYAS
    1201  VAKQVIQDCG ISESDLIVMA YLPDFRPDKR LSSDDFKKAQ HTCLAKVRTL
    1251  KNTKGGNVDV TLRIHRNHSF SKFLTLRSEI YCVKVMQMTT IEREYSTLEG
    1301  LEYYDLVGQI LQAKPSPPVN VDAAEIETVK KSYKLNTSQA EAIVNSVSKE
    1351  GFSLIQGPPG TGKTKTILGI IGYFLSTKNA SSSNVIKVPL EKNSSNTEQL
    1401  LKKQKILICA PSNAAVDEIC LRLKSGVYDK QGHQFKPQLV RVGRSDVVNV
    1451  AIKDLTLEEL VDKRIGERNY EIRTDPELER KFNNAVTKRR ELRGKLDSES
    1501  GNPESPMSTE DISKLQLKIR ELSKIINELG RDRDEMREKN SVNYRNRDLD
    1551  RRNAQAHILA VSDIICSTLS GSAHDVLATM GIKFDTVIID EACQCTELSS
    1601  IIPLRYGGKR CIMVGDPNQL PPTVLSGAAS NFKYNQSLFV RMEKNSSPYL
    1651  LDVQYRMHPS ISKFPSSEFY QGRLKDGPGM DILNKRPWHQ LEPLAPYKFF
    1701  DIISGRQEQN AKTMSYTNME EIRVAIELVD YLFRKFDNKI DFTGKIGIIS
    1751  PYREQMQKMR KEFARYFGGM INKSIDFNTI DGFQGQEKEI ILISCVRADD
    1801  TKSSVGFLKD FRRMNVALTR AKTSIWVLGH QRSLAKSKLW RDLIEDAKDR
    1851  SCLAYACSGF LDPRNNRAQS ILRKFNVPVP SEQEDDYKLP MEYITQGPDE
    1901  VKSNKDTKKR RVVDEGEEAD KAVKKKKKEK KKEKKKSKAD DKKKNNKKAE
    1951  SPSTSSGTKK KSSIFGGMSV PSAVVPKTFP DVDSNKKAAA VVGKKKNNKH
    2001  VCFSDDVSFI PRNDEPEIKV TRSLSSVLKE KQLGLKETRT ISPPEISNNE
    2051  DDDDEDDYTP SISDSSLMKS EANGRNNRVA SHNQNFSASI YDDPQVSQAK
    2101  QTQVPAAITK HRSSNSVLSG GSSRILTASD YGEPNQNGQN GANRTLSQHV
    2151  GNANQYSTAP VGTGELHETL PAHPQDSYPA EAEDPYDLNP HPQPQSSAFK
    2201  GPGSGPTGTR NSSRRNASSS PFIPKKRKPR S*                   

external links for Sen1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CGD) CYC2008 (complexes) Pfam domains
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Sen1p
1) Winey M and Culbertson MR  (1988) Mutations affecting the tRNA-splicing endonuclease activity of Saccharomyces cerevisiae. Genetics 118(4):609-17
2) Ursic D, et al.  (1997) The yeast SEN1 gene is required for the processing of diverse RNA classes. Nucleic Acids Res 25(23):4778-85
3) Rasmussen TP and Culbertson MR  (1998) The putative nucleic acid helicase Sen1p is required for formation and stability of termini and for maximal rates of synthesis and levels of accumulation of small nucleolar RNAs in Saccharomyces cerevisiae. Mol Cell Biol 18(12):6885-96
4) Steinmetz EJ, et al.  (2001) RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of RNA polymerase II transcripts. Nature 413(6853):327-31
5) Chen YZ, et al.  (2006) Senataxin, the yeast Sen1p orthologue: characterization of a unique protein in which recessive mutations cause ataxia and dominant mutations cause motor neuron disease. Neurobiol Dis 23(1):97-108
6) Steinmetz EJ, et al.  (2006) Genome-wide distribution of yeast RNA polymerase II and its control by Sen1 helicase. Mol Cell 24(5):735-46
7) Alzu A, et al.  (2012) Senataxin associates with replication forks to protect fork integrity across RNA-polymerase-II-transcribed genes. Cell 151(4):835-46
8) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41