Associated with
Other Information
Genular Protein ID: 2598350977
Symbol: SETX_HUMAN
Name: Amyotrophic lateral sclerosis 4 protein
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 14770181
Title: Senataxin, the ortholog of a yeast RNA helicase, is mutant in ataxia-ocular apraxia 2.
PubMed ID: 14770181
DOI: 10.1038/ng1303
PubMed ID: 17974005
Title: The full-ORF clone resource of the German cDNA consortium.
PubMed ID: 17974005
PubMed ID: 15164053
Title: DNA sequence and analysis of human chromosome 9.
PubMed ID: 15164053
DOI: 10.1038/nature02465
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 9734811
Title: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.
PubMed ID: 9734811
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 17562789
Title: Senataxin, defective in ataxia oculomotor apraxia type 2, is involved in the defense against oxidative DNA damage.
PubMed ID: 17562789
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19515850
Title: Functional role for senataxin, defective in ataxia oculomotor apraxia type 2, in transcriptional regulation.
PubMed ID: 19515850
DOI: 10.1093/hmg/ddp278
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21576111
Title: Senataxin modulates neurite growth through fibroblast growth factor 8 signalling.
PubMed ID: 21576111
DOI: 10.1093/brain/awr084
PubMed ID: 21112256
Title: Role of senataxin in DNA damage and telomeric stability.
PubMed ID: 21112256
PubMed ID: 21700224
Title: Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination.
PubMed ID: 21700224
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 24105744
Title: A SUMO-dependent interaction between Senataxin and the exosome, disrupted in the neurodegenerative disease AOA2, targets the exosome to sites of transcription-induced DNA damage.
PubMed ID: 24105744
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23149945
Title: Senataxin, defective in the neurodegenerative disorder ataxia with oculomotor apraxia 2, lies at the interface of transcription and the DNA damage response.
PubMed ID: 23149945
DOI: 10.1128/mcb.01195-12
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 26700805
Title: SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination.
PubMed ID: 26700805
DOI: 10.1038/nature16469
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 15106121
Title: DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4).
PubMed ID: 15106121
DOI: 10.1086/421054
PubMed ID: 16644229
Title: Senataxin, the yeast Sen1p orthologue: characterization of a unique protein in which recessive mutations cause ataxia and dominant mutations cause motor neuron disease.
PubMed ID: 16644229
PubMed ID: 16717225
Title: Autosomal recessive ataxia with peripheral neuropathy and elevated AFP: novel mutations in SETX.
PubMed ID: 16717225
PubMed ID: 17096168
Title: In cis autosomal dominant mutation of Senataxin associated with tremor/ataxia syndrome.
PubMed ID: 17096168
PubMed ID: 21190393
Title: Senataxin mutations and amyotrophic lateral sclerosis.
PubMed ID: 21190393
PubMed ID: 23566282
Title: A new SETX mutation producing AOA2 in two siblings.
PubMed ID: 23566282
PubMed ID: 23786967
Title: Exome analysis reveals a Japanese family with spinocerebellar ataxia, autosomal recessive 1.
PubMed ID: 23786967
PubMed ID: 23941260
Title: SETX mutations are a frequent genetic cause of juvenile and adult onset cerebellar ataxia with neuropathy and elevated serum alpha-fetoprotein.
PubMed ID: 23941260
PubMed ID: 24244371
Title: Protein interaction analysis of senataxin and the ALS4 L389S mutant yields insights into senataxin post-translational modification and uncovers mutant-specific binding with a brain cytoplasmic RNA-encoded peptide.
PubMed ID: 24244371
Sequence Information:
- Length: 2677
- Mass: 302880
- Checksum: 552FFE4A23A83868
- Sequence:
MSTCCWCTPG GASTIDFLKR YASNTPSGEF QTADEDLCYC LECVAEYHKA RDELPFLHEV LWELETLRLI NHFEKSMKAE IGDDDELYIV DNNGEMPLFD ITGQDFENKL RVPLLEILKY PYLLLHERVN ELCVEALCRM EQANCSFQVF DKHPGIYLFL VHPNEMVRRW AILTARNLGK VDRDDYYDLQ EVLLCLFKVI ELGLLESPDI YTSSVLEKGK LILLPSHMYD TTNYKSYWLG ICMLLTILEE QAMDSLLLGS DKQNDFMQSI LHTMEREADD DSVDPFWPAL HCFMVILDRL GSKVWGQLMD PIVAFQTIIN NASYNREIRH IRNSSVRTKL EPESYLDDMV TCSQIVYNYN PEKTKKDSGW RTAICPDYCP NMYEEMETLA SVLQSDIGQD MRVHNSTFLW FIPFVQSLMD LKDLGVAYIA QVVNHLYSEV KEVLNQTDAV CDKVTEFFLL ILVSVIELHR NKKCLHLLWV SSQQWVEAVV KCAKLPTTAF TRSSEKSSGN CSKGTAMISS LSLHSMPSNS VQLAYVQLIR SLLKEGYQLG QQSLCKRFWD KLNLFLRGNL SLGWQLTSQE THELQSCLKQ IIRNIKFKAP PCNTFVDLTS ACKISPASYN KEESEQMGKT SRKDMHCLEA SSPTFSKEPM KVQDSVLIKA DNTIEGDNNE QNYIKDVKLE DHLLAGSCLK QSSKNIFTER AEDQIKISTR KQKSVKEISS YTPKDCTSRN GPERGCDRGI IVSTRLLTDS STDALEKVST SNEDFSLKDD ALAKTSKRKT KVQKDEICAK LSHVIKKQHR KSTLVDNTIN LDENLTVSNI ESFYSRKDTG VQKGDGFIHN LSLDPSGVLD DKNGEQKSQN NVLPKEKQLK NEELVIFSFH ENNCKIQEFH VDGKELIPFT EMTNASEKKS SPFKDLMTVP ESRDEEMSNS TSVIYSNLTR EQAPDISPKS DTLTDSQIDR DLHKLSLLAQ ASVITFPSDS PQNSSQLQRK VKEDKRCFTA NQNNVGDTSR GQVIIISDSD DDDDERILSL EKLTKQDKIC LEREHPEQHV STVNSKEEKN PVKEEKTETL FQFEESDSQC FEFESSSEVF SVWQDHPDDN NSVQDGEKKC LAPIANTTNG QGCTDYVSEV VKKGAEGIEE HTRPRSISVE EFCEIEVKKP KRKRSEKPMA EDPVRPSSSV RNEGQSDTNK RDLVGNDFKS IDRRTSTPNS RIQRATTVSQ KKSSKLCTCT EPIRKVPVSK TPKKTHSDAK KGQNRSSNYL SCRTTPAIVP PKKFRQCPEP TSTAEKLGLK KGPRKAYELS QRSLDYVAQL RDHGKTVGVV DTRKKTKLIS PQNLSVRNNK KLLTSQELQM QRQIRPKSQK NRRRLSDCES TDVKRAGSHT AQNSDIFVPE SDRSDYNCTG GTEVLANSNR KQLIKCMPSE PETIKAKHGS PATDDACPLN QCDSVVLNGT VPTNEVIVST SEDPLGGGDP TARHIEMAAL KEGEPDSSSD AEEDNLFLTQ NDPEDMDLCS QMENDNYKLI ELIHGKDTVE VEEDSVSRPQ LESLSGTKCK YKDCLETTKN QGEYCPKHSE VKAADEDVFR KPGLPPPASK PLRPTTKIFS SKSTSRIAGL SKSLETSSAL SPSLKNKSKG IQSILKVPQP VPLIAQKPVG EMKNSCNVLH PQSPNNSNRQ GCKVPFGESK YFPSSSPVNI LLSSQSVSDT FVKEVLKWKY EMFLNFGQCG PPASLCQSIS RPVPVRFHNY GDYFNVFFPL MVLNTFETVA QEWLNSPNRE NFYQLQVRKF PADYIKYWEF AVYLEECELA KQLYPKENDL VFLAPERINE EKKDTERNDI QDLHEYHSGY VHKFRRTSVM RNGKTECYLS IQTQENFPAN LNELVNCIVI SSLVTTQRKL KAMSLLGSRN QLARAVLNPN PMDFCTKDLL TTTSERIIAY LRDFNEDQKK AIETAYAMVK HSPSVAKICL IHGPPGTGKS KTIVGLLYRL LTENQRKGHS DENSNAKIKQ NRVLVCAPSN AAVDELMKKI ILEFKEKCKD KKNPLGNCGD INLVRLGPEK SINSEVLKFS LDSQVNHRMK KELPSHVQAM HKRKEFLDYQ LDELSRQRAL CRGGREIQRQ ELDENISKVS KERQELASKI KEVQGRPQKT QSIIILESHI ICCTLSTSGG LLLESAFRGQ GGVPFSCVIV DEAGQSCEIE TLTPLIHRCN KLILVGDPKQ LPPTVISMKA QEYGYDQSMM ARFCRLLEEN VEHNMISRLP ILQLTVQYRM HPDICLFPSN YVYNRNLKTN RQTEAIRCSS DWPFQPYLVF DVGDGSERRD NDSYINVQEI KLVMEIIKLI KDKRKDVSFR NIGIITHYKA QKTMIQKDLD KEFDRKGPAE VDTVDAFQGR QKDCVIVTCV RANSIQGSIG FLASLQRLNV TITRAKYSLF ILGHLRTLME NQHWNQLIQD AQKRGAIIKT CDKNYRHDAV KILKLKPVLQ RSLTHPPTIA PEGSRPQGGL PSSKLDSGFA KTSVAASLYH TPSDSKEITL TVTSKDPERP PVHDQLQDPR LLKRMGIEVK GGIFLWDPQP SSPQHPGATP PTGEPGFPVV HQDLSHIQQP AAVVAALSSH KPPVRGEPPA ASPEASTCQS KCDDPEEELC HRREARAFSE GEQEKCGSET HHTRRNSRWD KRTLEQEDSS SKKRKLL
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.