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Q7Z333

- SETX_HUMAN

UniProt

Q7Z333 - SETX_HUMAN

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Protein

Probable helicase senataxin

Gene

SETX

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

Functioni

Probable helicase involved in RNA maturation. Required for the 3' transcriptional termination of PER1 and CRY2, plays an important role in the circadian rhythm regulation. Involved in DNA double-strand breaks damage response generated by oxidative stress.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1963 – 19708ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB
  3. DNA helicase activity Source: UniProtKB

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. circadian rhythm Source: Ensembl
  3. DNA duplex unwinding Source: GOC
  4. double-strand break repair Source: UniProtKB
  5. RNA processing Source: UniProtKB
  6. termination of RNA polymerase II transcription Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Biological rhythms, DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable helicase senataxin (EC:3.6.4.-)
Alternative name(s):
Amyotrophic lateral sclerosis 4 protein
SEN1 homolog
Gene namesi
Name:SETX
Synonyms:ALS4, KIAA0625, SCAR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:445. SETX.

Subcellular locationi

Nucleusnucleoplasm. Nucleusnucleolus. Cytoplasm
Note: May be detected in the nucleolus only in cycling cells (By similarity). Most abundant in the nucleus. Detected in granules. Colocalized in cycling cells with FBL in the nucleolus.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia, autosomal recessive, 1 (SCAR1) [MIM:606002]: Spinocerebellar 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.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti274 – 2741M → I in SCAR1. 1 Publication
VAR_036646
Natural varianti305 – 3051W → C in SCAR1. 1 Publication
VAR_018777
Natural varianti331 – 3311I → K in SCAR1. 1 Publication
VAR_071682
Natural varianti332 – 3321R → W in SCAR1. 1 Publication
Corresponds to variant rs29001665 [ dbSNP | Ensembl ].
VAR_018778
Natural varianti413 – 4131P → L in SCAR1. 1 Publication
VAR_018780
Natural varianti496 – 4961P → L in SCAR1. 1 Publication
VAR_071683
Natural varianti603 – 6031N → D in SCAR1; atypical; associated with K-653. 1 Publication
Corresponds to variant rs116205032 [ dbSNP | Ensembl ].
VAR_036647
Natural varianti653 – 6531Q → K in SCAR1; atypical; associated with D-603. 1 Publication
Corresponds to variant rs116333061 [ dbSNP | Ensembl ].
VAR_036648
Natural varianti1294 – 12941R → C in SCAR1. 1 Publication
VAR_036649
Natural varianti1756 – 17561F → S in SCAR1; heterozygous in a British family. 1 Publication
VAR_018788
Natural varianti2213 – 22131P → L in SCAR1. 1 Publication
Corresponds to variant rs28940290 [ dbSNP | Ensembl ].
VAR_018791
Natural varianti2229 – 22291M → T in SCAR1. 1 Publication
VAR_071687
Natural varianti2368 – 23681P → R in SCAR1. 1 Publication
VAR_036650
Amyotrophic lateral sclerosis 4 (ALS4) [MIM:602433]: A 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31T → I in ALS4; heterozygous.
Corresponds to variant rs28941475 [ dbSNP | Ensembl ].
VAR_018776
Natural varianti389 – 3891L → S in ALS4. 1 Publication
Corresponds to variant rs29001584 [ dbSNP | Ensembl ].
VAR_018779
Natural varianti1554 – 15541C → G in ALS4. 1 Publication
VAR_071685
Natural varianti2029 – 20291K → E in ALS4. 1 Publication
VAR_071686
Natural varianti2136 – 21361R → H in ALS4. 1 Publication
VAR_018790
Natural varianti2547 – 25471I → T in ALS4. 1 Publication
VAR_071688

Keywords - Diseasei

Amyotrophic lateral sclerosis, Disease mutation, Neurodegeneration

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26772677Probable helicase senataxinPRO_0000080724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei615 – 6151Phosphoserine1 Publication
Modified residuei1017 – 10171Phosphoserine5 Publications
Modified residuei1019 – 10191Phosphoserine5 Publications
Modified residuei1621 – 16211Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7Z333.
PaxDbiQ7Z333.
PRIDEiQ7Z333.

PTM databases

PhosphoSiteiQ7Z333.

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

BgeeiQ7Z333.
ExpressionAtlasiQ7Z333. baseline and differential.
GenevestigatoriQ7Z333.

Organism-specific databases

HPAiHPA024105.

Interactioni

Subunit structurei

Interacts with PER2; the interaction inhibits termination of circadian target genes.By similarity

Protein-protein interaction databases

BioGridi116699. 13 interactions.
IntActiQ7Z333. 8 interactions.
MINTiMINT-4649968.

Structurei

3D structure databases

ProteinModelPortaliQ7Z333.
SMRiQ7Z333. Positions 1958-2449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2661 – 267717Necessary for nuclear localizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2105 – 213632Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2070 – 208718Bipartite nuclear localization signalSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the DNA2/NAM7 helicase family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1112.
GeneTreeiENSGT00730000110642.
HOVERGENiHBG108476.
InParanoidiQ7Z333.
KOiK10706.
OMAiDMDLCSQ.
OrthoDBiEOG7JX33B.
PhylomeDBiQ7Z333.
TreeFamiTF324634.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR026121. Senataxin.
[Graphical view]
PANTHERiPTHR10887:SF336. PTHR10887:SF336. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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 CAD97857.1 differs from that shown. Reason: Frameshift at position 1626.
The sequence BAA91701.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAB14299.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti657 – 6571L → S in CAD98045. (PubMed:17974005)Curated
Sequence conflicti866 – 8661E → G in CAD97857. (PubMed:17974005)Curated
Sequence conflicti894 – 8941K → E in CAH18105. (PubMed:17974005)Curated
Sequence conflicti895 – 8951E → G in CAD98045. (PubMed:17974005)Curated
Sequence conflicti895 – 8951E → G in BAA31600. (PubMed:9734811)Curated
Sequence conflicti977 – 9771P → T in CAD97857. (PubMed:17974005)Curated
Sequence conflicti1073 – 10731F → C in CAD97857. (PubMed:17974005)Curated
Sequence conflicti1276 – 12761Q → E in BAA31600. (PubMed:9734811)Curated
Sequence conflicti1593 – 15931R → G in CAH18105. (PubMed:17974005)Curated
Sequence conflicti1626 – 16261N → K in CAD97857. (PubMed:17974005)Curated
Sequence conflicti1634 – 16341I → V in CAH18105. (PubMed:17974005)Curated
Sequence conflicti1648 – 16503PVG → TRP in AAH32622. (PubMed:15489334)Curated
Sequence conflicti1725 – 17251L → P in CAD97857. (PubMed:17974005)Curated
Sequence conflicti1826 – 18261E → K in CAD98045. (PubMed:17974005)Curated
Sequence conflicti1826 – 18261E → K in AAH32600. (PubMed:15489334)Curated
Sequence conflicti1826 – 18261E → K in AAH32622. (PubMed:15489334)Curated
Sequence conflicti1867 – 18671F → L in AAR13367. (PubMed:14770181)Curated
Sequence conflicti1867 – 18671F → L in AAH32622. (PubMed:15489334)Curated
Sequence conflicti2078 – 20781Q → L in CAD97857. (PubMed:17974005)Curated
Sequence conflicti2324 – 23241M → E in BAB14299. (PubMed:14702039)Curated
Sequence conflicti2423 – 24231G → E in CAH18105. (PubMed:17974005)Curated
Sequence conflicti2458 – 24581D → G in CAH18105. (PubMed:17974005)Curated
Sequence conflicti2539 – 25391P → S in CAD97857. (PubMed:17974005)Curated
Sequence conflicti2565 – 25651H → R in CAD97857. (PubMed:17974005)Curated
Sequence conflicti2577 – 25771F → L in BAB14299. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31T → I in ALS4; heterozygous.
Corresponds to variant rs28941475 [ dbSNP | Ensembl ].
VAR_018776
Natural varianti274 – 2741M → I in SCAR1. 1 Publication
VAR_036646
Natural varianti305 – 3051W → C in SCAR1. 1 Publication
VAR_018777
Natural varianti331 – 3311I → K in SCAR1. 1 Publication
VAR_071682
Natural varianti332 – 3321R → W in SCAR1. 1 Publication
Corresponds to variant rs29001665 [ dbSNP | Ensembl ].
VAR_018778
Natural varianti389 – 3891L → S in ALS4. 1 Publication
Corresponds to variant rs29001584 [ dbSNP | Ensembl ].
VAR_018779
Natural varianti413 – 4131P → L in SCAR1. 1 Publication
VAR_018780
Natural varianti496 – 4961P → L in SCAR1. 1 Publication
VAR_071683
Natural varianti603 – 6031N → D in SCAR1; atypical; associated with K-653. 1 Publication
Corresponds to variant rs116205032 [ dbSNP | Ensembl ].
VAR_036647
Natural varianti653 – 6531Q → K in SCAR1; atypical; associated with D-603. 1 Publication
Corresponds to variant rs116333061 [ dbSNP | Ensembl ].
VAR_036648
Natural varianti660 – 6601A → G.
Corresponds to variant rs882709 [ dbSNP | Ensembl ].
VAR_018781
Natural varianti992 – 9921K → R.1 Publication
VAR_071684
Natural varianti1061 – 10611P → L.
Corresponds to variant rs12352982 [ dbSNP | Ensembl ].
VAR_018782
Natural varianti1152 – 11521F → C.1 Publication
Corresponds to variant rs3739922 [ dbSNP | Ensembl ].
VAR_018783
Natural varianti1192 – 11921D → E.2 Publications
Corresponds to variant rs1185193 [ dbSNP | Ensembl ].
VAR_018784
Natural varianti1221 – 12211K → N.
Corresponds to variant rs12344006 [ dbSNP | Ensembl ].
VAR_056208
Natural varianti1252 – 12521G → R.2 Publications
Corresponds to variant rs1183768 [ dbSNP | Ensembl ].
VAR_018785
Natural varianti1294 – 12941R → C in SCAR1. 1 Publication
VAR_036649
Natural varianti1331 – 13311P → L.
Corresponds to variant rs11243731 [ dbSNP | Ensembl ].
VAR_018786
Natural varianti1386 – 13861I → V.2 Publications
Corresponds to variant rs543573 [ dbSNP | Ensembl ].
VAR_018787
Natural varianti1554 – 15541C → G in ALS4. 1 Publication
VAR_071685
Natural varianti1756 – 17561F → S in SCAR1; heterozygous in a British family. 1 Publication
VAR_018788
Natural varianti1855 – 18551T → A.1 Publication
Corresponds to variant rs2296871 [ dbSNP | Ensembl ].
VAR_018789
Natural varianti1855 – 18551T → P.
Corresponds to variant rs2296871 [ dbSNP | Ensembl ].
VAR_059458
Natural varianti2029 – 20291K → E in ALS4. 1 Publication
VAR_071686
Natural varianti2136 – 21361R → H in ALS4. 1 Publication
VAR_018790
Natural varianti2213 – 22131P → L in SCAR1. 1 Publication
Corresponds to variant rs28940290 [ dbSNP | Ensembl ].
VAR_018791
Natural varianti2229 – 22291M → T in SCAR1. 1 Publication
VAR_071687
Natural varianti2368 – 23681P → R in SCAR1. 1 Publication
VAR_036650
Natural varianti2547 – 25471I → T in ALS4. 1 Publication
VAR_071688
Natural varianti2587 – 25871I → V.3 Publications
Corresponds to variant rs1056899 [ dbSNP | Ensembl ].
VAR_018792
Natural varianti2612 – 26121S → G.1 Publication
Corresponds to variant rs3739927 [ dbSNP | Ensembl ].
VAR_018793

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2367 – 239933Missing in isoform 3. 1 PublicationVSP_017124Add
BLAST
Alternative sequencei2429 – 24291M → MQLLPRSFCVHVNHSPFFSP EPKYLHWALK in isoform 4. CuratedVSP_028826

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005272172.1. [Q7Z333-4]
XP_005272230.1. XM_005272173.1. [Q7Z333-4]
UniGeneiHs.460317.

Genome annotation databases

EnsembliENST00000224140; ENSP00000224140; ENSG00000107290. [Q7Z333-1]
GeneIDi23064.
KEGGihsa:23064.
UCSCiuc004cbj.3. human. [Q7Z333-4]
uc004cbk.3. human. [Q7Z333-1]
uc010mzt.3. human. [Q7Z333-3]

Polymorphism databases

DMDMi296453021.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS6947.1. [Q7Z333-1 ]
RefSeqi NP_055861.3. NM_015046.5. [Q7Z333-1 ]
XP_005272228.1. XM_005272171.1. [Q7Z333-4 ]
XP_005272229.1. XM_005272172.1. [Q7Z333-4 ]
XP_005272230.1. XM_005272173.1. [Q7Z333-4 ]
UniGenei Hs.460317.

3D structure databases

ProteinModelPortali Q7Z333.
SMRi Q7Z333. Positions 1958-2449.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116699. 13 interactions.
IntActi Q7Z333. 8 interactions.
MINTi MINT-4649968.

PTM databases

PhosphoSitei Q7Z333.

Polymorphism databases

DMDMi 296453021.

Proteomic databases

MaxQBi Q7Z333.
PaxDbi Q7Z333.
PRIDEi Q7Z333.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000224140 ; ENSP00000224140 ; ENSG00000107290 . [Q7Z333-1 ]
GeneIDi 23064.
KEGGi hsa:23064.
UCSCi uc004cbj.3. human. [Q7Z333-4 ]
uc004cbk.3. human. [Q7Z333-1 ]
uc010mzt.3. human. [Q7Z333-3 ]

Organism-specific databases

CTDi 23064.
GeneCardsi GC09M135136.
GeneReviewsi SETX.
HGNCi HGNC:445. SETX.
HPAi HPA024105.
MIMi 602433. phenotype.
606002. phenotype.
608465. gene.
neXtProti NX_Q7Z333.
Orphaneti 357043. Amyotrophic lateral sclerosis type 4.
64753. Spinocerebellar ataxia with axonal neuropathy type 2.
PharmGKBi PA24751.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1112.
GeneTreei ENSGT00730000110642.
HOVERGENi HBG108476.
InParanoidi Q7Z333.
KOi K10706.
OMAi DMDLCSQ.
OrthoDBi EOG7JX33B.
PhylomeDBi Q7Z333.
TreeFami TF324634.

Miscellaneous databases

ChiTaRSi SETX. human.
GeneWikii SETX.
GenomeRNAii 23064.
NextBioi 44145.
PROi Q7Z333.
SOURCEi Search...

Gene expression databases

Bgeei Q7Z333.
ExpressionAtlasi Q7Z333. baseline and differential.
Genevestigatori Q7Z333.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR027417. P-loop_NTPase.
IPR026121. Senataxin.
[Graphical view ]
PANTHERi PTHR10887:SF336. PTHR10887:SF336. 1 hit.
SUPFAMi SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT CYS-1152, VARIANTS SCAR1 CYS-305; TRP-332; LEU-413; SER-1756 AND LEU-2213.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 447-2677 (ISOFORM 3), VARIANTS GLU-1192; ARG-1252; VAL-1386 AND VAL-2587.
    Tissue: Amygdala, Fetal kidney and Retina.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLU-1192; ARG-1252; VAL-1386; ALA-1855; VAL-2587 AND GLY-2612.
    Tissue: Peripheral nerve, Retinoblastoma, Testis and Uterus.
  5. "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."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-2677 (ISOFORM 1).
    Tissue: Brain.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1762-2677 (ISOFORM 1), VARIANT VAL-2587.
    Tissue: Teratocarcinoma.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017 AND SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Senataxin, defective in ataxia oculomotor apraxia type 2, is involved in the defense against oxidative DNA damage."
    Suraweera A., Becherel O.J., Chen P., Rundle N., Woods R., Nakamura J., Gatei M., Criscuolo C., Filla A., Chessa L., Fusser M., Epe B., Gueven N., Lavin M.F.
    J. Cell Biol. 177:969-979(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615; SER-1017 AND SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017 AND SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017 AND SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017 AND SER-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: VARIANTS ALS4 SER-389 AND HIS-2136, TISSUE SPECIFICITY.
  16. "Senataxin, the yeast Sen1p orthologue: characterization of a unique protein in which recessive mutations cause ataxia and dominant mutations cause motor neuron disease."
    Chen Y.-Z., Hashemi S.H., Anderson S.K., Huang Y., Moreira M.-C., Lynch D.R., Glass I.A., Chance P.F., Bennett C.L.
    Neurobiol. Dis. 23:97-108(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCAR1 ARG-2368, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  17. "Autosomal recessive ataxia with peripheral neuropathy and elevated AFP: novel mutations in SETX."
    Asaka T., Yokoji H., Ito J., Yamaguchi K., Matsushima A.
    Neurology 66:1580-1581(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCAR1 ILE-274 AND CYS-1294.
  18. "In cis autosomal dominant mutation of Senataxin associated with tremor/ataxia syndrome."
    Bassuk A.G., Chen Y.Z., Batish S.D., Nagan N., Opal P., Chance P.F., Bennett C.L.
    Neurogenetics 8:45-49(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCAR1 ASP-603 AND LYS-653.
  19. Cited for: VARIANTS ALS4 GLY-1554; GLU-2029 AND THR-2547.
  20. "SETX mutations are a frequent genetic cause of juvenile and adult onset cerebellar ataxia with neuropathy and elevated serum alpha-fetoprotein."
    Nanetti L., Cavalieri S., Pensato V., Erbetta A., Pareyson D., Panzeri M., Zorzi G., Antozzi C., Moroni I., Gellera C., Brusco A., Mariotti C.
    Orphanet J. Rare Dis. 8:123-123(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SCAR1 LYS-331; LEU-496 AND THR-2229, VARIANT ARG-992.

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: October 29, 2014
This is version 119 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

External Data

Dasty 3