SETX_MOUSE
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 03-AUG-2022, entry version 112.
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; 5.
DR MINT; A2AKX3; -.
DR STRING; 10090.ENSMUSP00000051492; -.
DR iPTMnet; A2AKX3; -.
DR PhosphoSitePlus; A2AKX3; -.
DR EPD; A2AKX3; -.
DR MaxQB; A2AKX3; -.
DR PaxDb; A2AKX3; -.
DR PeptideAtlas; A2AKX3; -.
DR PRIDE; A2AKX3; -.
DR ProteomicsDB; 257128; -. [A2AKX3-1]
DR ProteomicsDB; 257129; -. [A2AKX3-2]
DR Antibodypedia; 31672; 367 antibodies from 22 providers.
DR DNASU; 269254; -.
DR Ensembl; ENSMUST00000061578; ENSMUSP00000051492; ENSMUSG00000043535. [A2AKX3-1]
DR GeneID; 269254; -.
DR KEGG; mmu:269254; -.
DR UCSC; uc008izm.1; mouse. [A2AKX3-1]
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; KQEPLGN; -.
DR OrthoDB; 62494at2759; -.
DR PhylomeDB; A2AKX3; -.
DR TreeFam; TF324634; -.
DR BioGRID-ORCS; 269254; 1 hit in 110 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 221 other tissues.
DR ExpressionAtlas; A2AKX3; baseline and differential.
DR Genevisible; A2AKX3; MM.
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
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: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 selection; 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:2000144; P:positive regulation of DNA-templated transcription, initiation; ISS:UniProtKB.
DR GO; GO:0060566; P:positive regulation of DNA-templated transcription, termination; 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: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:0043491; P:protein kinase B signaling; 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; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR10887; PTHR10887; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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
