Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable helicase senataxin

Gene

SETX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription (PubMed:19515850, PubMed:21700224). Contributes to the mRNA splicing efficiency and splice site selection (PubMed:19515850). Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (PubMed:19515850, PubMed:21700224, PubMed:26700805). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (By similarity). Involved in DNA double-strand breaks damage response generated by oxidative stress (PubMed:17562789). In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (PubMed:24105744). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (By similarity). May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (PubMed:21112256). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis (PubMed:21576111).By similarity7 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1963 – 1970ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB
  • DNA helicase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • transcription termination site sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to fibroblast growth factor stimulus Source: UniProtKB
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular response to oxidative stress Source: UniProtKB
  • cellular response to retinoic acid Source: UniProtKB
  • circadian rhythm Source: Ensembl
  • DNA recombination Source: UniProtKB-KW
  • DNA-templated transcription, termination Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • mRNA splice site selection Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • positive regulation of DNA-templated transcription, initiation Source: UniProtKB
  • positive regulation of DNA-templated transcription, termination Source: UniProtKB
  • positive regulation of neuron projection development Source: UniProtKB
  • positive regulation of RNA splicing Source: UniProtKB
  • positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein kinase B signaling Source: UniProtKB
  • RNA processing Source: UniProtKB
  • spermatogenesis Source: UniProtKB-KW
  • termination of RNA polymerase II transcription Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Biological rhythms, Differentiation, DNA damage, DNA recombination, DNA repair, Neurogenesis, Spermatogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable helicase senataxinCurated (EC:3.6.4.-)
Alternative name(s):
Amyotrophic lateral sclerosis 4 protein
SEN1 homologCurated
Senataxin1 PublicationImported
Gene namesi
Name:SETX1 PublicationImported
Synonyms:ALS4, KIAA0625, SCAR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:445. SETX.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • chromosome, telomeric region Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • growth cone Source: UniProtKB
  • nuclear chromosome Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia, autosomal recessive, 1 (SCAR1)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSpinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR1 is an autosomal recessive form associated with peripheral neuropathy and elevated serum alpha-fetoprotein, immunoglobulins and, less commonly, creatine kinase levels. Some SCAR1 patients manifest oculomotor apraxia.
See also OMIM:606002
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036646274M → I in SCAR1. 1 Publication1
Natural variantiVAR_072587274M → V in SCAR1. 1 PublicationCorresponds to variant rs753713810dbSNPEnsembl.1
Natural variantiVAR_018777305W → C in SCAR1; abolishes interaction with EXOSC9; does not abolish interaction with UBE2I; decreases sumoylation. 2 Publications1
Natural variantiVAR_071682331I → K in SCAR1. 1 Publication1
Natural variantiVAR_018778332R → W in SCAR1. 1 PublicationCorresponds to variant rs29001665dbSNPEnsembl.1
Natural variantiVAR_018780413P → L in SCAR1; abolishes interaction with EXOSC9; does not abolish interaction with UBE2I; decreases sumoylation. 2 Publications1
Natural variantiVAR_071683496P → L in SCAR1. 1 Publication1
Natural variantiVAR_036647603N → D in SCAR1; atypical; associated with K-653. 1 PublicationCorresponds to variant rs116205032dbSNPEnsembl.1
Natural variantiVAR_036648653Q → K in SCAR1; atypical; associated with D-603. 1 PublicationCorresponds to variant rs116333061dbSNPEnsembl.1
Natural variantiVAR_0366491294R → C in SCAR1. 1 PublicationCorresponds to variant rs267607044dbSNPEnsembl.1
Natural variantiVAR_0187881756F → S in SCAR1; heterozygous in a British family. 1 PublicationCorresponds to variant rs762175796dbSNPEnsembl.1
Natural variantiVAR_0725881976L → R in SCAR1. 1 PublicationCorresponds to variant rs121434379dbSNPEnsembl.1
Natural variantiVAR_0187912213P → L in SCAR1. 1 PublicationCorresponds to variant rs28940290dbSNPEnsembl.1
Natural variantiVAR_0716872229M → T in SCAR1. 1 Publication1
Natural variantiVAR_0366502368P → R in SCAR1. 1 Publication1
Amyotrophic lateral sclerosis 4 (ALS4)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of amyotrophic lateral sclerosis with childhood- or adolescent-onset, and characterized by slow disease progression and the sparing of bulbar and respiratory muscles. Amyotrophic lateral sclerosis is a neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
See also OMIM:602433
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0187763T → I in ALS4; heterozygous; does not affect the interaction with EXOSC9 and UBE2I; does not decrease sumoylation. 1 PublicationCorresponds to variant rs28941475dbSNPEnsembl.1
Natural variantiVAR_018779389L → S in ALS4; does not affect the interaction with EXOSC9 and UBE2I; does not decrease sumoylation and ubiquitination; does not inhibit homodimerization; unlike the wild-type protein the mutant induces interaction with C14orf178. 3 PublicationsCorresponds to variant rs29001584dbSNPEnsembl.1
Natural variantiVAR_0716851554C → G in ALS4. 1 PublicationCorresponds to variant rs112089123dbSNPEnsembl.1
Natural variantiVAR_0716862029K → E in ALS4. 1 PublicationCorresponds to variant rs746525639dbSNPEnsembl.1
Natural variantiVAR_0187902136R → H in ALS4. 1 PublicationCorresponds to variant rs121434378dbSNPEnsembl.1
Natural variantiVAR_0716882547I → T in ALS4. 1 PublicationCorresponds to variant rs151117904dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65E → K: Abolishes interaction with EXOSC9 and UBE2I and decreases sumoylation. 1 Publication1

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi23064.
MalaCardsiSETX.
MIMi602433. phenotype.
606002. phenotype.
OpenTargetsiENSG00000107290.
Orphaneti357043. Amyotrophic lateral sclerosis type 4.
64753. Spinocerebellar ataxia with axonal neuropathy type 2.
PharmGKBiPA24751.

Polymorphism and mutation databases

BioMutaiSETX.
DMDMi296453021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000807241 – 2677Probable helicase senataxinAdd BLAST2677

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki339Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei615PhosphoserineCombined sources1
Modified residuei642PhosphoserineCombined sources1
Modified residuei878PhosphoserineBy similarity1
Modified residuei911PhosphoserineCombined sources1
Modified residuei947PhosphoserineCombined sources1
Modified residuei956PhosphoserineCombined sources1
Modified residuei1017PhosphoserineCombined sources1
Modified residuei1019PhosphoserineCombined sources1
Cross-linki1063Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1330PhosphoserineCombined sources1
Modified residuei1366PhosphoserineCombined sources1
Modified residuei1489PhosphoserineBy similarity1
Modified residuei1621PhosphoserineCombined sources1
Modified residuei1623PhosphoserineCombined sources1
Modified residuei1663PhosphoserineCombined sources1
Modified residuei2474PhosphothreonineCombined sources1

Post-translational modificationi

Ubiquitinated.1 Publication
Sumoylated preferentially with SUMO2 or SUMO3 (PubMed:24105744, PubMed:24244371).2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ7Z333.
MaxQBiQ7Z333.
PaxDbiQ7Z333.
PeptideAtlasiQ7Z333.
PRIDEiQ7Z333.

PTM databases

iPTMnetiQ7Z333.
PhosphoSitePlusiQ7Z333.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle. Expressed in heart, fibroblast, placenta and liver. Weakly expressed in brain and lung. Expressed in the cortex of the kidney (highly expressed in tubular epithelial cells but low expression in the glomerulus).4 Publications

Gene expression databases

BgeeiENSG00000107290.
ExpressionAtlasiQ7Z333. baseline and differential.
GenevisibleiQ7Z333. HS.

Organism-specific databases

HPAiHPA024105.
HPA057269.

Interactioni

Subunit structurei

Homodimer (PubMed:24244371). Interacts with PER2; the interaction inhibits termination of circadian target genes (By similarity). Interacts with CHD4, POLR2A, PRKDC and TRIM28 (PubMed:23149945). Does not interact with C14orf178 (PubMed:24244371). Interacts with UBE2I (PubMed:24105744). Interacts (via N-terminus domain) with EXOSC9 (via C-terminus region); the interaction enhances SETX sumoylation (PubMed:24105744). Interacts with NCL (via N-terminus domain) (PubMed:19515850). Interacts with PABPN1, PABPC1 and SF3B1 (PubMed:19515850). Interacts with SMN1/SMN2 and POLR2A; SMN1/SMN2 recruits SETX to POLR2A (PubMed:19515850, PubMed:26700805).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-1220123,EBI-1220123
UBE2IP632793EBI-1220123,EBI-80168

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi116699. 41 interactors.
DIPiDIP-38360N.
IntActiQ7Z333. 29 interactors.
MINTiMINT-4649968.
STRINGi9606.ENSP00000224140.

Structurei

3D structure databases

ProteinModelPortaliQ7Z333.
SMRiQ7Z333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2661 – 2677Necessary for nuclear localizationAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2105 – 2136Sequence analysisAdd BLAST32

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2070 – 2087Bipartite nuclear localization signalSequence analysisAdd BLAST18

Domaini

The N-terminus domain is necessary for S/G2 nuclear foci localization (PubMed:23149945).1 Publication

Sequence similaritiesi

Belongs to the DNA2/NAM7 helicase family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1801. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00810000125415.
HOVERGENiHBG108476.
InParanoidiQ7Z333.
KOiK10706.
OMAiPEDMDLC.
OrthoDBiEOG091G01EA.
PhylomeDBiQ7Z333.
TreeFamiTF324634.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR026121. Senataxin.
[Graphical view]
PANTHERiPTHR10887:SF377. PTHR10887:SF377. 3 hits.
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7Z333-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSTCCWCTPG GASTIDFLKR YASNTPSGEF QTADEDLCYC LECVAEYHKA
60 70 80 90 100
RDELPFLHEV LWELETLRLI NHFEKSMKAE IGDDDELYIV DNNGEMPLFD
110 120 130 140 150
ITGQDFENKL RVPLLEILKY PYLLLHERVN ELCVEALCRM EQANCSFQVF
160 170 180 190 200
DKHPGIYLFL VHPNEMVRRW AILTARNLGK VDRDDYYDLQ EVLLCLFKVI
210 220 230 240 250
ELGLLESPDI YTSSVLEKGK LILLPSHMYD TTNYKSYWLG ICMLLTILEE
260 270 280 290 300
QAMDSLLLGS DKQNDFMQSI LHTMEREADD DSVDPFWPAL HCFMVILDRL
310 320 330 340 350
GSKVWGQLMD PIVAFQTIIN NASYNREIRH IRNSSVRTKL EPESYLDDMV
360 370 380 390 400
TCSQIVYNYN PEKTKKDSGW RTAICPDYCP NMYEEMETLA SVLQSDIGQD
410 420 430 440 450
MRVHNSTFLW FIPFVQSLMD LKDLGVAYIA QVVNHLYSEV KEVLNQTDAV
460 470 480 490 500
CDKVTEFFLL ILVSVIELHR NKKCLHLLWV SSQQWVEAVV KCAKLPTTAF
510 520 530 540 550
TRSSEKSSGN CSKGTAMISS LSLHSMPSNS VQLAYVQLIR SLLKEGYQLG
560 570 580 590 600
QQSLCKRFWD KLNLFLRGNL SLGWQLTSQE THELQSCLKQ IIRNIKFKAP
610 620 630 640 650
PCNTFVDLTS ACKISPASYN KEESEQMGKT SRKDMHCLEA SSPTFSKEPM
660 670 680 690 700
KVQDSVLIKA DNTIEGDNNE QNYIKDVKLE DHLLAGSCLK QSSKNIFTER
710 720 730 740 750
AEDQIKISTR KQKSVKEISS YTPKDCTSRN GPERGCDRGI IVSTRLLTDS
760 770 780 790 800
STDALEKVST SNEDFSLKDD ALAKTSKRKT KVQKDEICAK LSHVIKKQHR
810 820 830 840 850
KSTLVDNTIN LDENLTVSNI ESFYSRKDTG VQKGDGFIHN LSLDPSGVLD
860 870 880 890 900
DKNGEQKSQN NVLPKEKQLK NEELVIFSFH ENNCKIQEFH VDGKELIPFT
910 920 930 940 950
EMTNASEKKS SPFKDLMTVP ESRDEEMSNS TSVIYSNLTR EQAPDISPKS
960 970 980 990 1000
DTLTDSQIDR DLHKLSLLAQ ASVITFPSDS PQNSSQLQRK VKEDKRCFTA
1010 1020 1030 1040 1050
NQNNVGDTSR GQVIIISDSD DDDDERILSL EKLTKQDKIC LEREHPEQHV
1060 1070 1080 1090 1100
STVNSKEEKN PVKEEKTETL FQFEESDSQC FEFESSSEVF SVWQDHPDDN
1110 1120 1130 1140 1150
NSVQDGEKKC LAPIANTTNG QGCTDYVSEV VKKGAEGIEE HTRPRSISVE
1160 1170 1180 1190 1200
EFCEIEVKKP KRKRSEKPMA EDPVRPSSSV RNEGQSDTNK RDLVGNDFKS
1210 1220 1230 1240 1250
IDRRTSTPNS RIQRATTVSQ KKSSKLCTCT EPIRKVPVSK TPKKTHSDAK
1260 1270 1280 1290 1300
KGQNRSSNYL SCRTTPAIVP PKKFRQCPEP TSTAEKLGLK KGPRKAYELS
1310 1320 1330 1340 1350
QRSLDYVAQL RDHGKTVGVV DTRKKTKLIS PQNLSVRNNK KLLTSQELQM
1360 1370 1380 1390 1400
QRQIRPKSQK NRRRLSDCES TDVKRAGSHT AQNSDIFVPE SDRSDYNCTG
1410 1420 1430 1440 1450
GTEVLANSNR KQLIKCMPSE PETIKAKHGS PATDDACPLN QCDSVVLNGT
1460 1470 1480 1490 1500
VPTNEVIVST SEDPLGGGDP TARHIEMAAL KEGEPDSSSD AEEDNLFLTQ
1510 1520 1530 1540 1550
NDPEDMDLCS QMENDNYKLI ELIHGKDTVE VEEDSVSRPQ LESLSGTKCK
1560 1570 1580 1590 1600
YKDCLETTKN QGEYCPKHSE VKAADEDVFR KPGLPPPASK PLRPTTKIFS
1610 1620 1630 1640 1650
SKSTSRIAGL SKSLETSSAL SPSLKNKSKG IQSILKVPQP VPLIAQKPVG
1660 1670 1680 1690 1700
EMKNSCNVLH PQSPNNSNRQ GCKVPFGESK YFPSSSPVNI LLSSQSVSDT
1710 1720 1730 1740 1750
FVKEVLKWKY EMFLNFGQCG PPASLCQSIS RPVPVRFHNY GDYFNVFFPL
1760 1770 1780 1790 1800
MVLNTFETVA QEWLNSPNRE NFYQLQVRKF PADYIKYWEF AVYLEECELA
1810 1820 1830 1840 1850
KQLYPKENDL VFLAPERINE EKKDTERNDI QDLHEYHSGY VHKFRRTSVM
1860 1870 1880 1890 1900
RNGKTECYLS IQTQENFPAN LNELVNCIVI SSLVTTQRKL KAMSLLGSRN
1910 1920 1930 1940 1950
QLARAVLNPN PMDFCTKDLL TTTSERIIAY LRDFNEDQKK AIETAYAMVK
1960 1970 1980 1990 2000
HSPSVAKICL IHGPPGTGKS KTIVGLLYRL LTENQRKGHS DENSNAKIKQ
2010 2020 2030 2040 2050
NRVLVCAPSN AAVDELMKKI ILEFKEKCKD KKNPLGNCGD INLVRLGPEK
2060 2070 2080 2090 2100
SINSEVLKFS LDSQVNHRMK KELPSHVQAM HKRKEFLDYQ LDELSRQRAL
2110 2120 2130 2140 2150
CRGGREIQRQ ELDENISKVS KERQELASKI KEVQGRPQKT QSIIILESHI
2160 2170 2180 2190 2200
ICCTLSTSGG LLLESAFRGQ GGVPFSCVIV DEAGQSCEIE TLTPLIHRCN
2210 2220 2230 2240 2250
KLILVGDPKQ LPPTVISMKA QEYGYDQSMM ARFCRLLEEN VEHNMISRLP
2260 2270 2280 2290 2300
ILQLTVQYRM HPDICLFPSN YVYNRNLKTN RQTEAIRCSS DWPFQPYLVF
2310 2320 2330 2340 2350
DVGDGSERRD NDSYINVQEI KLVMEIIKLI KDKRKDVSFR NIGIITHYKA
2360 2370 2380 2390 2400
QKTMIQKDLD KEFDRKGPAE VDTVDAFQGR QKDCVIVTCV RANSIQGSIG
2410 2420 2430 2440 2450
FLASLQRLNV TITRAKYSLF ILGHLRTLME NQHWNQLIQD AQKRGAIIKT
2460 2470 2480 2490 2500
CDKNYRHDAV KILKLKPVLQ RSLTHPPTIA PEGSRPQGGL PSSKLDSGFA
2510 2520 2530 2540 2550
KTSVAASLYH TPSDSKEITL TVTSKDPERP PVHDQLQDPR LLKRMGIEVK
2560 2570 2580 2590 2600
GGIFLWDPQP SSPQHPGATP PTGEPGFPVV HQDLSHIQQP AAVVAALSSH
2610 2620 2630 2640 2650
KPPVRGEPPA ASPEASTCQS KCDDPEEELC HRREARAFSE GEQEKCGSET
2660 2670
HHTRRNSRWD KRTLEQEDSS SKKRKLL
Length:2,677
Mass (Da):302,880
Last modified:May 18, 2010 - v4
Checksum:i552FFE4A23A83868
GO
Isoform 3 (identifier: Q7Z333-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2367-2399: Missing.

Note: No experimental confirmation available.
Show »
Length:2,644
Mass (Da):299,420
Checksum:i6FBDACF73E59C50A
GO
Isoform 4 (identifier: Q7Z333-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2429-2429: M → MQLLPRSFCVHVNHSPFFSPEPKYLHWALK

Note: No experimental confirmation available.
Show »
Length:2,706
Mass (Da):306,341
Checksum:i8CEE9E4BE6CB0526
GO

Sequence cautioni

The sequence BAA91701 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14299 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAD97857 differs from that shown. Reason: Frameshift at position 1626.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti657L → S in CAD98045 (PubMed:17974005).Curated1
Sequence conflicti866E → G in CAD97857 (PubMed:17974005).Curated1
Sequence conflicti894K → E in CAH18105 (PubMed:17974005).Curated1
Sequence conflicti895E → G in CAD98045 (PubMed:17974005).Curated1
Sequence conflicti895E → G in BAA31600 (PubMed:9734811).Curated1
Sequence conflicti977P → T in CAD97857 (PubMed:17974005).Curated1
Sequence conflicti1073F → C in CAD97857 (PubMed:17974005).Curated1
Sequence conflicti1276Q → E in BAA31600 (PubMed:9734811).Curated1
Sequence conflicti1593R → G in CAH18105 (PubMed:17974005).Curated1
Sequence conflicti1626N → K in CAD97857 (PubMed:17974005).Curated1
Sequence conflicti1634I → V in CAH18105 (PubMed:17974005).Curated1
Sequence conflicti1648 – 1650PVG → TRP in AAH32622 (PubMed:15489334).Curated3
Sequence conflicti1725L → P in CAD97857 (PubMed:17974005).Curated1
Sequence conflicti1826E → K in CAD98045 (PubMed:17974005).Curated1
Sequence conflicti1826E → K in AAH32600 (PubMed:15489334).Curated1
Sequence conflicti1826E → K in AAH32622 (PubMed:15489334).Curated1
Sequence conflicti1867F → L in AAR13367 (PubMed:14770181).Curated1
Sequence conflicti1867F → L in AAH32622 (PubMed:15489334).Curated1
Sequence conflicti2078Q → L in CAD97857 (PubMed:17974005).Curated1
Sequence conflicti2324M → E in BAB14299 (PubMed:14702039).Curated1
Sequence conflicti2423G → E in CAH18105 (PubMed:17974005).Curated1
Sequence conflicti2458D → G in CAH18105 (PubMed:17974005).Curated1
Sequence conflicti2539P → S in CAD97857 (PubMed:17974005).Curated1
Sequence conflicti2565H → R in CAD97857 (PubMed:17974005).Curated1
Sequence conflicti2577F → L in BAB14299 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0187763T → I in ALS4; heterozygous; does not affect the interaction with EXOSC9 and UBE2I; does not decrease sumoylation. 1 PublicationCorresponds to variant rs28941475dbSNPEnsembl.1
Natural variantiVAR_036646274M → I in SCAR1. 1 Publication1
Natural variantiVAR_072587274M → V in SCAR1. 1 PublicationCorresponds to variant rs753713810dbSNPEnsembl.1
Natural variantiVAR_018777305W → C in SCAR1; abolishes interaction with EXOSC9; does not abolish interaction with UBE2I; decreases sumoylation. 2 Publications1
Natural variantiVAR_071682331I → K in SCAR1. 1 Publication1
Natural variantiVAR_018778332R → W in SCAR1. 1 PublicationCorresponds to variant rs29001665dbSNPEnsembl.1
Natural variantiVAR_018779389L → S in ALS4; does not affect the interaction with EXOSC9 and UBE2I; does not decrease sumoylation and ubiquitination; does not inhibit homodimerization; unlike the wild-type protein the mutant induces interaction with C14orf178. 3 PublicationsCorresponds to variant rs29001584dbSNPEnsembl.1
Natural variantiVAR_018780413P → L in SCAR1; abolishes interaction with EXOSC9; does not abolish interaction with UBE2I; decreases sumoylation. 2 Publications1
Natural variantiVAR_071683496P → L in SCAR1. 1 Publication1
Natural variantiVAR_036647603N → D in SCAR1; atypical; associated with K-653. 1 PublicationCorresponds to variant rs116205032dbSNPEnsembl.1
Natural variantiVAR_036648653Q → K in SCAR1; atypical; associated with D-603. 1 PublicationCorresponds to variant rs116333061dbSNPEnsembl.1
Natural variantiVAR_018781660A → G.Corresponds to variant rs882709dbSNPEnsembl.1
Natural variantiVAR_071684992K → R.1 PublicationCorresponds to variant rs61742937dbSNPEnsembl.1
Natural variantiVAR_0187821061P → L.Corresponds to variant rs12352982dbSNPEnsembl.1
Natural variantiVAR_0187831152F → C.1 PublicationCorresponds to variant rs3739922dbSNPEnsembl.1
Natural variantiVAR_0187841192D → E.2 PublicationsCorresponds to variant rs1185193dbSNPEnsembl.1
Natural variantiVAR_0562081221K → N.Corresponds to variant rs12344006dbSNPEnsembl.1
Natural variantiVAR_0187851252G → R.2 PublicationsCorresponds to variant rs1183768dbSNPEnsembl.1
Natural variantiVAR_0366491294R → C in SCAR1. 1 PublicationCorresponds to variant rs267607044dbSNPEnsembl.1
Natural variantiVAR_0187861331P → L.Corresponds to variant rs11243731dbSNPEnsembl.1
Natural variantiVAR_0187871386I → V.2 PublicationsCorresponds to variant rs543573dbSNPEnsembl.1
Natural variantiVAR_0716851554C → G in ALS4. 1 PublicationCorresponds to variant rs112089123dbSNPEnsembl.1
Natural variantiVAR_0187881756F → S in SCAR1; heterozygous in a British family. 1 PublicationCorresponds to variant rs762175796dbSNPEnsembl.1
Natural variantiVAR_0187891855T → A.1 PublicationCorresponds to variant rs2296871dbSNPEnsembl.1
Natural variantiVAR_0594581855T → P.Corresponds to variant rs2296871dbSNPEnsembl.1
Natural variantiVAR_0725881976L → R in SCAR1. 1 PublicationCorresponds to variant rs121434379dbSNPEnsembl.1
Natural variantiVAR_0716862029K → E in ALS4. 1 PublicationCorresponds to variant rs746525639dbSNPEnsembl.1
Natural variantiVAR_0187902136R → H in ALS4. 1 PublicationCorresponds to variant rs121434378dbSNPEnsembl.1
Natural variantiVAR_0187912213P → L in SCAR1. 1 PublicationCorresponds to variant rs28940290dbSNPEnsembl.1
Natural variantiVAR_0716872229M → T in SCAR1. 1 Publication1
Natural variantiVAR_0366502368P → R in SCAR1. 1 Publication1
Natural variantiVAR_0716882547I → T in ALS4. 1 PublicationCorresponds to variant rs151117904dbSNPEnsembl.1
Natural variantiVAR_0187922587I → V.3 PublicationsCorresponds to variant rs1056899dbSNPEnsembl.1
Natural variantiVAR_0187932612S → G.1 PublicationCorresponds to variant rs3739927dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0171242367 – 2399Missing in isoform 3. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_0288262429M → MQLLPRSFCVHVNHSPFFSP EPKYLHWALK in isoform 4. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY362728 mRNA. Translation: AAR13367.1.
BX537849 mRNA. Translation: CAD97857.1. Frameshift.
BX538166 mRNA. Translation: CAD98045.1.
CR749249 mRNA. Translation: CAH18105.1.
AL159997, AL353701 Genomic DNA. Translation: CAI40854.1.
AL159997 Genomic DNA. Translation: CAI40857.1.
AL353701, AL159997 Genomic DNA. Translation: CAM14151.1.
BC032600 mRNA. Translation: AAH32600.2.
BC032622 mRNA. Translation: AAH32622.2.
BC078166 mRNA. Translation: AAH78166.1.
BC106017 mRNA. Translation: AAI06018.1.
BC137350 mRNA. Translation: AAI37351.1.
AB014525 mRNA. Translation: BAA31600.2.
AK001456 mRNA. Translation: BAA91701.1. Different initiation.
AK022902 mRNA. Translation: BAB14299.1. Different initiation.
CCDSiCCDS6947.1. [Q7Z333-1]
RefSeqiNP_055861.3. NM_015046.5. [Q7Z333-1]
XP_005272228.1. XM_005272171.1. [Q7Z333-4]
XP_005272229.1. XM_005272172.2. [Q7Z333-4]
XP_005272230.1. XM_005272173.2. [Q7Z333-4]
XP_011516706.1. XM_011518404.2. [Q7Z333-4]
XP_011516707.1. XM_011518405.2. [Q7Z333-4]
XP_016869984.1. XM_017014495.1. [Q7Z333-1]
XP_016869986.1. XM_017014497.1.
UniGeneiHs.460317.

Genome annotation databases

EnsembliENST00000224140; ENSP00000224140; ENSG00000107290. [Q7Z333-1]
GeneIDi23064.
KEGGihsa:23064.
UCSCiuc004cbk.4. human. [Q7Z333-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY362728 mRNA. Translation: AAR13367.1.
BX537849 mRNA. Translation: CAD97857.1. Frameshift.
BX538166 mRNA. Translation: CAD98045.1.
CR749249 mRNA. Translation: CAH18105.1.
AL159997, AL353701 Genomic DNA. Translation: CAI40854.1.
AL159997 Genomic DNA. Translation: CAI40857.1.
AL353701, AL159997 Genomic DNA. Translation: CAM14151.1.
BC032600 mRNA. Translation: AAH32600.2.
BC032622 mRNA. Translation: AAH32622.2.
BC078166 mRNA. Translation: AAH78166.1.
BC106017 mRNA. Translation: AAI06018.1.
BC137350 mRNA. Translation: AAI37351.1.
AB014525 mRNA. Translation: BAA31600.2.
AK001456 mRNA. Translation: BAA91701.1. Different initiation.
AK022902 mRNA. Translation: BAB14299.1. Different initiation.
CCDSiCCDS6947.1. [Q7Z333-1]
RefSeqiNP_055861.3. NM_015046.5. [Q7Z333-1]
XP_005272228.1. XM_005272171.1. [Q7Z333-4]
XP_005272229.1. XM_005272172.2. [Q7Z333-4]
XP_005272230.1. XM_005272173.2. [Q7Z333-4]
XP_011516706.1. XM_011518404.2. [Q7Z333-4]
XP_011516707.1. XM_011518405.2. [Q7Z333-4]
XP_016869984.1. XM_017014495.1. [Q7Z333-1]
XP_016869986.1. XM_017014497.1.
UniGeneiHs.460317.

3D structure databases

ProteinModelPortaliQ7Z333.
SMRiQ7Z333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116699. 41 interactors.
DIPiDIP-38360N.
IntActiQ7Z333. 29 interactors.
MINTiMINT-4649968.
STRINGi9606.ENSP00000224140.

PTM databases

iPTMnetiQ7Z333.
PhosphoSitePlusiQ7Z333.

Polymorphism and mutation databases

BioMutaiSETX.
DMDMi296453021.

Proteomic databases

EPDiQ7Z333.
MaxQBiQ7Z333.
PaxDbiQ7Z333.
PeptideAtlasiQ7Z333.
PRIDEiQ7Z333.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000224140; ENSP00000224140; ENSG00000107290. [Q7Z333-1]
GeneIDi23064.
KEGGihsa:23064.
UCSCiuc004cbk.4. human. [Q7Z333-1]

Organism-specific databases

CTDi23064.
DisGeNETi23064.
GeneCardsiSETX.
GeneReviewsiSETX.
HGNCiHGNC:445. SETX.
HPAiHPA024105.
HPA057269.
MalaCardsiSETX.
MIMi602433. phenotype.
606002. phenotype.
608465. gene.
neXtProtiNX_Q7Z333.
OpenTargetsiENSG00000107290.
Orphaneti357043. Amyotrophic lateral sclerosis type 4.
64753. Spinocerebellar ataxia with axonal neuropathy type 2.
PharmGKBiPA24751.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1801. Eukaryota.
COG1112. LUCA.
GeneTreeiENSGT00810000125415.
HOVERGENiHBG108476.
InParanoidiQ7Z333.
KOiK10706.
OMAiPEDMDLC.
OrthoDBiEOG091G01EA.
PhylomeDBiQ7Z333.
TreeFamiTF324634.

Miscellaneous databases

ChiTaRSiSETX. human.
GeneWikiiSETX.
GenomeRNAii23064.
PROiQ7Z333.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107290.
ExpressionAtlasiQ7Z333. baseline and differential.
GenevisibleiQ7Z333. HS.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR026121. Senataxin.
[Graphical view]
PANTHERiPTHR10887:SF377. PTHR10887:SF377. 3 hits.
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiSETX_HUMAN
AccessioniPrimary (citable) accession number: Q7Z333
Secondary accession number(s): A2A396
, B2RPB2, B5ME16, C9JQ10, O75120, Q3KQX4, Q5JUJ1, Q68DW5, Q6AZD7, Q7Z3J6, Q8WX33, Q9H9D1, Q9NVP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.