ID SETX_MOUSE Reviewed; 2646 AA. AC A2AKX3; A2AKX4; A2AR33; Q6IMG6; Q6PED8; Q6ZQ81; Q80V90; Q8C5P1; Q8C859; AC Q8C8P6; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Probable helicase senataxin {ECO:0000305}; DE EC=3.6.4.-; DE AltName: Full=Amyotrophic lateral sclerosis 4 protein homolog; DE AltName: Full=SEN1 homolog; GN Name=Setx {ECO:0000312|MGI:MGI:2443480}; Synonyms=Als4, Kiaa0625; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1050 (ISOFORM 2), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-858 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 2464-2646. RC STRAIN=C57BL/6J; TISSUE=Head, Retina, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1745-2646 (ISOFORM 1). RC STRAIN=129, and C57BL/6J; TISSUE=Brain, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1915-2646 (ISOFORM 1). RC TISSUE=Embryonic tail; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [5] RP IDENTIFICATION (ISOFORM 1). RC STRAIN=C57BL/6J; RX PubMed=14770181; DOI=10.1038/ng1303; RA Moreira M.-C., Klur S., Watanabe M., Nemeth A.H., Le Ber I., Moniz J.-C., RA Tranchant C., Aubourg P., Tazir M., Schoels L., Pandolfo M., Schulz J.B., RA Pouget J., Calvas P., Shizuka-Ikeda M., Shoji M., Tanaka M., Izatt L., RA Shaw C.E., M'Zahem A., Dunne E., Bomont P., Benhassine T., Bouslam N., RA Stevanin G., Brice A., Guimaraes J., Mendonca P., Barbot C., Coutinho P., RA Sequeiros J., Duerr A., Warter J.-M., Koenig M.; RT "Senataxin, the ortholog of a yeast RNA helicase, is mutant in ataxia- RT ocular apraxia 2."; RL Nat. Genet. 36:225-227(2004). RN [6] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16644229; DOI=10.1016/j.nbd.2006.02.007; RA Chen Y.-Z., Hashemi S.H., Anderson S.K., Huang Y., Moreira M.-C., RA Lynch D.R., Glass I.A., Chance P.F., Bennett C.L.; RT "Senataxin, the yeast Sen1p orthologue: characterization of a unique RT protein in which recessive mutations cause ataxia and dominant mutations RT cause motor neuron disease."; RL Neurobiol. Dis. 23:97-108(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-870; SER-871; RP SER-872; SER-1002; SER-1004; SER-1472 AND THR-1474, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP FUNCTION IN CIRCADIAN RHYTHMS, AND INTERACTION WITH PER2. RX PubMed=22767893; DOI=10.1126/science.1221592; RA Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.; RT "Feedback regulation of transcriptional termination by the mammalian RT circadian clock PERIOD complex."; RL Science 337:599-602(2012). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=23593030; DOI=10.1371/journal.pgen.1003435; RA Becherel O.J., Yeo A.J., Stellati A., Heng E.Y., Luff J., Suraweera A.M., RA Woods R., Fleming J., Carrie D., McKinney K., Xu X., Deng C., Lavin M.F.; RT "Senataxin plays an essential role with DNA damage response proteins in RT meiotic recombination and gene silencing."; RL PLoS Genet. 9:E1003435-E1003435(2013). CC -!- FUNCTION: Probable RNA/DNA helicase involved in diverse aspects of RNA CC metabolism and genomic integrity. Plays a role in transcription CC regulation by its ability to modulate RNA Polymerase II (Pol II) CC binding to chromatin and through its interaction with proteins involved CC in transcription. Contributes to the mRNA splicing efficiency and CC splice site selection. Required for the resolution of R-loop RNA-DNA CC hybrid formation at G-rich pause sites located downstream of the CC poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation CC of the downstream cleaved RNA and hence efficient RNA polymerase II CC (RNAp II) transcription termination (By similarity). Required for the CC 3' transcriptional termination of PER1 and CRY2, thus playing an CC important role in the circadian rhythm regulation (PubMed:22767893). CC Involved in DNA double-strand breaks damage response generated by CC oxidative stress. In association with RRP45, targets the RNA exosome CC complex to sites of transcription-induced DNA damage (By similarity). CC Plays a role in the development and maturation of germ cells: essential CC for male meiosis, acting at the interface of transcription and meiotic CC recombination, and in the process of gene silencing during meiotic sex CC chromosome inactivation (MSCI) (PubMed:23593030). Plays a role in CC neurite outgrowth in hippocampal cells through FGF8-activated signaling CC pathways. Inhibits retinoic acid-induced apoptosis. May be involved in CC telomeric stability through the regulation of telomere repeat- CC containing RNA (TERRA) transcription (By similarity). CC {ECO:0000250|UniProtKB:Q7Z333, ECO:0000269|PubMed:22767893, CC ECO:0000269|PubMed:23593030}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PER2; the CC interaction inhibits termination of circadian target genes CC (PubMed:22767893). Interacts with CHD4, POLR2A, PRKDC and TRIM28. Does CC not interact with C14orf178. Interacts with UBE2I. Interacts (via N- CC terminus domain) with EXOSC9 (via C-terminus region); the interaction CC enhances SETX sumoylation. Interacts with NCL (via N-terminus domain). CC Interacts with PABPN1, PABPC1 and SF3B1. Interacts with SMN1/SMN2 and CC POLR2A; SMN1/SMN2 recruits SETX to POLR2A (By similarity). CC {ECO:0000250|UniProtKB:Q7Z333, ECO:0000269|PubMed:22767893}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z333}. Nucleus, CC nucleoplasm {ECO:0000269|PubMed:16644229}. Nucleus, nucleolus CC {ECO:0000269|PubMed:16644229}. Cytoplasm {ECO:0000269|PubMed:16644229}. CC Chromosome {ECO:0000269|PubMed:23593030}. Chromosome, telomere CC {ECO:0000250|UniProtKB:Q7Z333}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q7Z333}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:Q7Z333}. Note=Most abundant in the nucleus (By CC similarity). Detected in granules (By similarity). Colocalized in CC cycling cells with FBL in the nucleolus. Localizes with telomeric DNA CC in a transcription-dependent manner. Under replication stress, CC colocalizes with a variety of DNA damage signaling and repair response CC proteins at distinct nuclear foci in mitotic S/G2- and G1-phase cells CC in a transcription- and RNA/DNA hybrid-dependent manner. Localizes at CC limited number of nuclear foci. Colocalizes with EXOSC9 in nuclear foci CC upon induction of transcription-related DNA damage at the S phase (By CC similarity). At pachytene stage, colocalizes predominantly to the CC heterochromatic XY-body of sex chromosomes with DNA damage response CC proteins in a BRCA1-dependent manner (PubMed:23593030). May be detected CC in the nucleolus only in cycling cells (PubMed:16644229). CC {ECO:0000250|UniProtKB:Q7Z333, ECO:0000269|PubMed:16644229, CC ECO:0000269|PubMed:23593030}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=A2AKX3-1; Sequence=Displayed; CC Name=2; CC IsoId=A2AKX3-2; Sequence=VSP_028827; CC -!- TISSUE SPECIFICITY: Expressed in cerebellum, hippocampus, olfactory CC bulb, Bergmann glial fibers, stellate cells and Purkinje cells. CC Expressed in the epithelial cells of the lens but not in mature lens CC fiber cells. Expressed in the retina (highly expressed in inner and CC outer segments of photoreceptors and outer plexiform layer cells but CC weakly expressed in the inner plexiform and ganglion cell layers). CC Expressed in the kidney. {ECO:0000269|PubMed:16644229}. CC -!- DOMAIN: The N-terminus domain is necessary for S/G2 nuclear foci CC localization. {ECO:0000250|UniProtKB:Q7Z333}. CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q7Z333}. CC -!- PTM: Sumoylated preferentially with SUMO2 or SUMO3. CC {ECO:0000250|UniProtKB:Q7Z333}. CC -!- DISRUPTION PHENOTYPE: Mice are viable. Male germ cells proceed normally CC from spermatogonia up to the meiotic pachytene stage but fail to enter CC into spermiogenesis and form mature spermatids (PubMed:23593030), CC resulting in male infertility. In particular, during spermatogenesis, CC male germ cells accumulated DNA:RNA hybrids (R-loops), meiotic DNA CC double-strand breaks, and fails to produce crossovers and meiotic sex CC chromosome inactivation (MSCI) (PubMed:23593030). CC {ECO:0000269|PubMed:23593030}. CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC32054.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAC97987.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it is derived from pre-RNA.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL772379; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL845267; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK044730; BAC32054.1; ALT_FRAME; mRNA. DR EMBL; AK048354; BAC33309.2; -; mRNA. DR EMBL; AK077911; BAC37058.1; -; mRNA. DR EMBL; BC046382; AAH46382.1; -; mRNA. DR EMBL; BC058109; AAH58109.2; -; mRNA. DR EMBL; BC079604; AAH79604.2; -; mRNA. DR EMBL; AK129177; BAC97987.1; ALT_SEQ; Transcribed_RNA. DR EMBL; BK001523; DAA01946.1; -; mRNA. DR CCDS; CCDS38090.1; -. [A2AKX3-1] DR RefSeq; NP_932150.2; NM_198033.2. [A2AKX3-1] DR AlphaFoldDB; A2AKX3; -. DR SMR; A2AKX3; -. DR BioGRID; 234629; 11. DR DIP; DIP-56995N; -. DR IntAct; A2AKX3; 6. DR MINT; A2AKX3; -. DR STRING; 10090.ENSMUSP00000051492; -. DR GlyGen; A2AKX3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; A2AKX3; -. DR PhosphoSitePlus; A2AKX3; -. DR SwissPalm; A2AKX3; -. DR EPD; A2AKX3; -. DR MaxQB; A2AKX3; -. DR PaxDb; 10090-ENSMUSP00000051492; -. DR PeptideAtlas; A2AKX3; -. DR ProteomicsDB; 257128; -. [A2AKX3-1] DR ProteomicsDB; 257129; -. [A2AKX3-2] DR Pumba; A2AKX3; -. DR Antibodypedia; 31672; 379 antibodies from 22 providers. DR DNASU; 269254; -. DR Ensembl; ENSMUST00000061578.9; ENSMUSP00000051492.3; ENSMUSG00000043535.14. [A2AKX3-1] DR GeneID; 269254; -. DR KEGG; mmu:269254; -. DR UCSC; uc008izm.1; mouse. [A2AKX3-1] DR AGR; MGI:2443480; -. DR CTD; 23064; -. DR MGI; MGI:2443480; Setx. DR VEuPathDB; HostDB:ENSMUSG00000043535; -. DR eggNOG; KOG1801; Eukaryota. DR GeneTree; ENSGT00940000160918; -. DR HOGENOM; CLU_000967_0_0_1; -. DR InParanoid; A2AKX3; -. DR OMA; HTMEREA; -. DR OrthoDB; 170190at2759; -. DR PhylomeDB; A2AKX3; -. DR TreeFam; TF324634; -. DR BioGRID-ORCS; 269254; 2 hits in 115 CRISPR screens. DR ChiTaRS; Setx; mouse. DR PRO; PR:A2AKX3; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; A2AKX3; Protein. DR Bgee; ENSMUSG00000043535; Expressed in spermatocyte and 224 other cell types or tissues. DR ExpressionAtlas; A2AKX3; baseline and differential. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0030426; C:growth cone; ISS:UniProtKB. DR GO; GO:0045171; C:intercellular bridge; ISO:MGI. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0001147; F:transcription termination site sequence-specific DNA binding; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB. DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB. DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; IMP:MGI. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006353; P:DNA-templated transcription termination; ISS:UniProtKB. DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB. DR GO; GO:0006376; P:mRNA splice site recognition; ISS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB. DR GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; ISS:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB. DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB. DR GO; GO:0060566; P:positive regulation of termination of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:2000806; P:positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:MGI. DR CDD; cd18042; DEXXQc_SETX; 1. DR CDD; cd18808; SF1_C_Upf1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR045055; DNA2/NAM7-like. DR InterPro; IPR041679; DNA2/NAM7-like_C. DR InterPro; IPR041677; DNA2/NAM7_AAA_11. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR047187; SF1_C_Upf1. DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1. DR PANTHER; PTHR10887:SF525; HELICASE SENATAXIN-RELATED; 1. DR Pfam; PF13086; AAA_11; 1. DR Pfam; PF13087; AAA_12; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; A2AKX3; MM. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Biological rhythms; Cell projection; KW Chromosome; Coiled coil; Cytoplasm; Differentiation; DNA damage; KW DNA recombination; DNA repair; Helicase; Hydrolase; Isopeptide bond; KW Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Spermatogenesis; Telomere; Ubl conjugation. FT CHAIN 1..2646 FT /note="Probable helicase senataxin" FT /id="PRO_0000307777" FT REGION 705..734 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 825..876 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1001..1023 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1122..1245 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1591..1627 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2450..2472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2486..2506 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2569..2624 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2632..2646 FT /note="Necessary for nuclear localization" FT /evidence="ECO:0000250" FT MOTIF 2046..2063 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 705..729 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 840..867 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1192..1214 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2596..2612 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1939..1946 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 640 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT MOD_RES 870 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 871 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 872 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 938 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT MOD_RES 1002 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1004 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1318 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT MOD_RES 1472 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1474 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2450 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT CROSSLNK 339 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT CROSSLNK 1051 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT CROSSLNK 1328 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT CROSSLNK 1329 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT CROSSLNK 1398 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q7Z333" FT VAR_SEQ 1..381 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_028827" FT CONFLICT 644 FT /note="S -> C (in Ref. 2; BAC32054)" FT /evidence="ECO:0000305" FT CONFLICT 1048 FT /note="Q -> R (in Ref. 2; BAC33309)" FT /evidence="ECO:0000305" SQ SEQUENCE 2646 AA; 297589 MW; 3036F84EFED4A098 CRC64; MSTCCWCTPG GSSTIDVLKR YASSTGSSEF QTADEDLCYC LECVAEYHRA RDEVPFLHEV LWELETLRLV SHFEKSMKAE AEDDDDLYIV DNNGEEQLFD CSGQDFENKL RVPLFEILKY PYLLLHERVN ELCVEALCRM EQNNCSFQVF DKYPGIYLFL VHPNEMVRRW AILTARNLGK VDRDDYYDLQ EVLTCLFKVI ELGLLESPDI YTSSVLEKGK LILLPAHMYD TTNYKNYWLG ICMLLTILEE QAMDSLLLGS DKQNDFMQSI LHTMEKQSDD DSMDPFWPAL HCFMVILDRL GSKVWGQLID PIEAFQTIIN NESYNREIQN IRNSSIRTKL EPEPHFDDMV TCSQIVYNFN PEKTKKDSGW RSAICPDYCP NMYEEMETLA NVLQSDIGQD MRVHNSTFLW FIPFVQSLMD LKDLGVAYIV EVIHHLYSEV KDVLNQTDAV CDKVTEFFIL ILISVIELHR NKKCLHLLWV SSQQWVEAVV KCAKLPTTAF VRSCEKSPGS TSRGAAIMSS LALHSVQSNS VQLACVQLIR GLLKEGYQLG QQTLCKRFWD KLNLFLRGNL SLGWQLTGQE THELQMCLKQ IIRNIKFKMP QYSTFGDSTS TFKTPPSFKE ESDKIDRKHK KNIYCLENCS PVSSKEPMKA DTHRVLMKVN TTEEENFKQH YIDLNEEEQE PLPAELCLKQ KSEALFSESA QEQVKISAEK SGKESSSYAP SNSTSRNGPE WGCDRGVIMS AHSLTDSSSD FMEQVSTSNE DVSLKDGSVG KTSKPSFKLQ KDEICAKLSH VIKKQIRKST LVDNIIDLEE NTAISDLENC SGTDGGALKE DSIGHNVPSD PVLDDKHEEQ KSQNSSLFKK EIKSEELDNS SSDDEDKLQI QEGRADDDLV SFTEVTDTLV KAPCEGHVKM VVESRDKEMR ESTALTSNLV EGQVPHDSSK PLVAGRQIDL CNITLISQTT VIQFPSGLSK QNSFQLQKGD KRCLTANQNS AATCRGQVIV ISDSDEEEDE DEDERSSSEE NIKQSKACIG KDCSEHRSLA VNASVEKQLV KEEERYPVEF EDSESQVFEF ESSSEVFSVW QDHKIDSKNS LQGEQKSYVT HVADSTNNNL GCGDSVSEEV VRNKAEGVKE HAGPHSSVSA EEFCKTGVKK PKRKRYDKVT AEDPQRPSSS VGTDQLPDRR DLTESDLKSA DMGMATPSSS VERDSTILQK STKSRTHSKP VRKVPASKAT KKTHSDTRRG QSKSSCYISC RTSPAIVPPK KLRQCPEPTS TVEKLGLKKA PRKAFELSQR SLECIVQLRD HGKTVGVVDA PKKAKLISPQ TLSIKNNKKL LTSQDLQFQR LMRSRSHKKR DFDYKNTDTV RVSRIVQGSD VLEADSDEPD DHRVSEPLAI SNEKQLAKCM LSKTEVAEAS SDPWVTGITC LVNQCESRVL SGGVPTDVVM VSASEDPVDG GAVTVQVGEV ASVKAAEPAS SSDTDDDDNL FLTQHDPQDM DLCSQLENKT IIVAHKKDTV QREDSLSRPQ LESLSITKCK YKDCVETTKN QGEYCPRHSE AKAADDGLFR KPGLPLSVAR PLRPTTTKIF SSSSASRTAN LSKSLESTTL QQSALKNKSS GAQPNLKVTP PSSMGSQKPV AEVKSLCNIF HFQTPSSSSK QSCKLTFSEN RPTSAASPVN ILLPSQSIFD TFIKEVLKWK YQMFLNFDKC GAPTSLCQSI SRPVPVRFQD CAEYFNVFLP LIILNAFETV AQEWLSSPNK ENFYQLQLRK FPADYKKYWE FLIYLNESEL AKQLHPKEND LVFLAPEKSY MDRHGMQDCS HYYCGYVHKF RRTSVMRSGK AECSLCIQTQ DTLPASVKNL TRCIVISSLV TTQRKLKAMS LLSSRNQLAR AVLNPNPMDF CTKDLLTTTS ERIVAYLKDF NEDQKKAIET AYAMVKHSPS VAKICLIHGP PGTGKSKTIV GLLYRLLTEN QRKGHSDENF NAKIKQNRVL VCAPSNAAVD ELMKKIILEF KEKCKDKKNP LGNCGDINLV RLGPEKSINT EVLKFSLDSQ VNHRMKKDLP SHIQEMLRRK EILDAQLDEL SRQRALCRGG REMQRQELDE HIAIVSKERQ ELASKIKEVQ GRPQRAQNTI ILESHVICCT LSTSGGLLLE SAFRGQGGVP FSCVIVDEAG QSCEVETLSP LIHRCNKLIL VGDPKQLPPT VISMKAQEYG YDQSMMARFC KLLEENVEQN MIGRLPVLQL TIQYRMHPDI CLFPSNYVYN KNLKTNRLTE SIRCSSEWPF QPYLVFDVGD GSERRDNDSY INVQEIKLVM EIIKLIKEKR KDISFRNIGI ITHYKAQKTM IQKDLEKEFD KKGPAEVDTV DAFQGRQKDC IIVTCVRASA VQGSIGFLAS LQRLNVTITR AKYSLFILGH LRTLMENQHW YELIQDAQKR GAIIKTSDPN YRHDAMKILK LKPVLQRSLT HPPATAPEAP RPQGGLPSNR LDSGLATTSF AASLYHTPSD TVTSKGPERP LLQDRLRDPR LLRRLDAEAK GTFLKDPQPV SPQLPGVVHL LGEPGFPVVF QDLGFVVPPS TAIVAPLGSH RSPMQAEPPP AHPAAAASTS KRKYSDPDAG LSHKREPRAF SGEQGRHGSV THHVLRSTDW DRRRLDDSSA KRRQFL //