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Protein

Probable helicase senataxin

Gene

Setx

Organism
Mus musculus (Mouse)
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. Contributes to the mRNA splicing efficiency and splice site selection. 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 (By similarity). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (PubMed:22767893). Involved in DNA double-strand breaks damage response generated by oxidative stress. In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (By similarity). 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) (PubMed:23593030). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis. May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (By similarity).By similarity2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1939 – 19468ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. helicase activity Source: UniProtKB-KW
  3. transcription termination site sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. cellular response to fibroblast growth factor stimulus Source: UniProtKB
  3. cellular response to hydrogen peroxide Source: UniProtKB
  4. cellular response to oxidative stress Source: UniProtKB
  5. cellular response to retinoic acid Source: UniProtKB
  6. circadian rhythm Source: MGI
  7. DNA recombination Source: UniProtKB-KW
  8. double-strand break repair Source: UniProtKB
  9. fibroblast growth factor receptor signaling pathway Source: UniProtKB
  10. MAPK cascade Source: UniProtKB
  11. mRNA splice site selection Source: UniProtKB
  12. negative regulation of apoptotic process Source: UniProtKB
  13. positive regulation of DNA-templated transcription, initiation Source: UniProtKB
  14. positive regulation of DNA-templated transcription, termination Source: UniProtKB
  15. positive regulation of neuron projection development Source: UniProtKB
  16. positive regulation of RNA splicing Source: UniProtKB
  17. positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled Source: UniProtKB
  18. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  19. protein kinase B signaling Source: UniProtKB
  20. spermatogenesis Source: UniProtKB-KW
  21. termination of RNA polymerase II transcription Source: MGI
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 homolog
SEN1 homolog
Gene namesi
Name:SetxImported
Synonyms:Als4, Kiaa0625
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2443480. Setx.

Subcellular locationi

  1. Nucleus By similarity
  2. Nucleusnucleoplasm 1 Publication
  3. Nucleusnucleolus 1 Publication
  4. Cytoplasm 1 Publication
  5. Chromosome 1 Publication
  6. Chromosometelomere By similarity
  7. Cell projectionaxon By similarity
  8. Cell projectiongrowth cone By similarity

  9. Note: Most abundant in the nucleus (By similarity). Detected in granules (By similarity). Colocalized in cycling cells with FBL in the nucleolus. Localizes with telomeric DNA in a transcription-dependent manner. Under replication stress, colocalizes with a variety of DNA damage signaling and repair response proteins at distinct nuclear foci in mitotic S/G2- and G1-phase cells in a transcription- and RNA/DNA hybrid-dependent manner. Localizes at limited number of nuclear foci. Colocalizes with EXOSC9 in nuclear foci upon induction of transcription-related DNA damage at the S phase (By similarity). At pachytene stage, colocalizes predominantly to the heterochromatic XY-body of sex chromosomes with DNA damage response proteins in a BRCA1-dependent manner (PubMed:23593030). May be detected in the nucleolus only in cycling cells (PubMed:16644229).By similarity2 Publications

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. chromosome, telomeric region Source: UniProtKB-SubCell
  3. cytoplasm Source: UniProtKB
  4. growth cone Source: UniProtKB
  5. nuclear chromosome Source: UniProtKB
  6. nucleolus Source: UniProtKB-SubCell
  7. nucleoplasm Source: UniProtKB
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Disruption phenotypei

Mice are viable. Male germ cells proceed normally from spermatogonia up to the meiotic pachytene stage but fail to enter into spermiogenesis and form mature spermatids (PubMed:23593030), resulting in male infertility. In particular, during spermatogenesis, male germ cells accumulated DNA:RNA hybrids (R-loops), meiotic DNA double-strand breaks, and fails to produce crossovers and meiotic sex chromosome inactivation (MSCI) (PubMed:23593030).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26462646Probable helicase senataxinPRO_0000307777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1002 – 10021PhosphoserineBy similarity
Modified residuei1004 – 10041PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated.By similarity
Sumoylated preferentially with SUMO2 or SUMO3.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiA2AKX3.
PaxDbiA2AKX3.
PRIDEiA2AKX3.

PTM databases

PhosphoSiteiA2AKX3.

Expressioni

Tissue specificityi

Expressed in cerebellum, hippocampus, olfactory bulb, Bergmann glial fibers, stellate cells and Purkinje cells. Expressed in the epithelial cells of the lens but not in mature lens fiber cells. Expressed in the retina (highly expressed in inner and outer segments of photoreceptors and outer plexiform layer cells but weakly expressed in the inner plexiform and ganglion cell layers). Expressed in the kidney.1 Publication

Gene expression databases

BgeeiA2AKX3.
CleanExiMM_SETX.
GenevestigatoriA2AKX3.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with PER2; the interaction inhibits termination of circadian target genes (PubMed:22767893). Interacts with CHD4, POLR2A, PRKDC and TRIM28. Does not interact with C14orf178. Interacts with UBE2I. Interacts (via N-terminus domain) with EXOSC9 (via C-terminus region); the interaction enhances SETX sumoylation. Interacts with NCL (via N-terminus domain). Interacts with PABPN1, PABPC1, SF3B1 and SMN1. Interacts with the RNA polymerase II large subunit (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi234629. 4 interactions.
DIPiDIP-56995N.
IntActiA2AKX3. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliA2AKX3.
SMRiA2AKX3. Positions 1907-2437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2632 – 264615Necessary for nuclear localizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2046 – 206318Bipartite nuclear localization signalBy similarityAdd
BLAST

Domaini

The N-terminus domain is necessary for S/G2 nuclear foci localization.By similarity

Sequence similaritiesi

Belongs to the DNA2/NAM7 helicase family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1112.
GeneTreeiENSGT00770000120665.
HOVERGENiHBG108476.
InParanoidiA2AKX3.
KOiK10706.
OrthoDBiEOG7JX33B.
PhylomeDBiA2AKX3.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A2AKX3-1) [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 GSSTIDVLKR YASSTGSSEF QTADEDLCYC LECVAEYHRA
60 70 80 90 100
RDEVPFLHEV LWELETLRLV SHFEKSMKAE AEDDDDLYIV DNNGEEQLFD
110 120 130 140 150
CSGQDFENKL RVPLFEILKY PYLLLHERVN ELCVEALCRM EQNNCSFQVF
160 170 180 190 200
DKYPGIYLFL VHPNEMVRRW AILTARNLGK VDRDDYYDLQ EVLTCLFKVI
210 220 230 240 250
ELGLLESPDI YTSSVLEKGK LILLPAHMYD TTNYKNYWLG ICMLLTILEE
260 270 280 290 300
QAMDSLLLGS DKQNDFMQSI LHTMEKQSDD DSMDPFWPAL HCFMVILDRL
310 320 330 340 350
GSKVWGQLID PIEAFQTIIN NESYNREIQN IRNSSIRTKL EPEPHFDDMV
360 370 380 390 400
TCSQIVYNFN PEKTKKDSGW RSAICPDYCP NMYEEMETLA NVLQSDIGQD
410 420 430 440 450
MRVHNSTFLW FIPFVQSLMD LKDLGVAYIV EVIHHLYSEV KDVLNQTDAV
460 470 480 490 500
CDKVTEFFIL ILISVIELHR NKKCLHLLWV SSQQWVEAVV KCAKLPTTAF
510 520 530 540 550
VRSCEKSPGS TSRGAAIMSS LALHSVQSNS VQLACVQLIR GLLKEGYQLG
560 570 580 590 600
QQTLCKRFWD KLNLFLRGNL SLGWQLTGQE THELQMCLKQ IIRNIKFKMP
610 620 630 640 650
QYSTFGDSTS TFKTPPSFKE ESDKIDRKHK KNIYCLENCS PVSSKEPMKA
660 670 680 690 700
DTHRVLMKVN TTEEENFKQH YIDLNEEEQE PLPAELCLKQ KSEALFSESA
710 720 730 740 750
QEQVKISAEK SGKESSSYAP SNSTSRNGPE WGCDRGVIMS AHSLTDSSSD
760 770 780 790 800
FMEQVSTSNE DVSLKDGSVG KTSKPSFKLQ KDEICAKLSH VIKKQIRKST
810 820 830 840 850
LVDNIIDLEE NTAISDLENC SGTDGGALKE DSIGHNVPSD PVLDDKHEEQ
860 870 880 890 900
KSQNSSLFKK EIKSEELDNS SSDDEDKLQI QEGRADDDLV SFTEVTDTLV
910 920 930 940 950
KAPCEGHVKM VVESRDKEMR ESTALTSNLV EGQVPHDSSK PLVAGRQIDL
960 970 980 990 1000
CNITLISQTT VIQFPSGLSK QNSFQLQKGD KRCLTANQNS AATCRGQVIV
1010 1020 1030 1040 1050
ISDSDEEEDE DEDERSSSEE NIKQSKACIG KDCSEHRSLA VNASVEKQLV
1060 1070 1080 1090 1100
KEEERYPVEF EDSESQVFEF ESSSEVFSVW QDHKIDSKNS LQGEQKSYVT
1110 1120 1130 1140 1150
HVADSTNNNL GCGDSVSEEV VRNKAEGVKE HAGPHSSVSA EEFCKTGVKK
1160 1170 1180 1190 1200
PKRKRYDKVT AEDPQRPSSS VGTDQLPDRR DLTESDLKSA DMGMATPSSS
1210 1220 1230 1240 1250
VERDSTILQK STKSRTHSKP VRKVPASKAT KKTHSDTRRG QSKSSCYISC
1260 1270 1280 1290 1300
RTSPAIVPPK KLRQCPEPTS TVEKLGLKKA PRKAFELSQR SLECIVQLRD
1310 1320 1330 1340 1350
HGKTVGVVDA PKKAKLISPQ TLSIKNNKKL LTSQDLQFQR LMRSRSHKKR
1360 1370 1380 1390 1400
DFDYKNTDTV RVSRIVQGSD VLEADSDEPD DHRVSEPLAI SNEKQLAKCM
1410 1420 1430 1440 1450
LSKTEVAEAS SDPWVTGITC LVNQCESRVL SGGVPTDVVM VSASEDPVDG
1460 1470 1480 1490 1500
GAVTVQVGEV ASVKAAEPAS SSDTDDDDNL FLTQHDPQDM DLCSQLENKT
1510 1520 1530 1540 1550
IIVAHKKDTV QREDSLSRPQ LESLSITKCK YKDCVETTKN QGEYCPRHSE
1560 1570 1580 1590 1600
AKAADDGLFR KPGLPLSVAR PLRPTTTKIF SSSSASRTAN LSKSLESTTL
1610 1620 1630 1640 1650
QQSALKNKSS GAQPNLKVTP PSSMGSQKPV AEVKSLCNIF HFQTPSSSSK
1660 1670 1680 1690 1700
QSCKLTFSEN RPTSAASPVN ILLPSQSIFD TFIKEVLKWK YQMFLNFDKC
1710 1720 1730 1740 1750
GAPTSLCQSI SRPVPVRFQD CAEYFNVFLP LIILNAFETV AQEWLSSPNK
1760 1770 1780 1790 1800
ENFYQLQLRK FPADYKKYWE FLIYLNESEL AKQLHPKEND LVFLAPEKSY
1810 1820 1830 1840 1850
MDRHGMQDCS HYYCGYVHKF RRTSVMRSGK AECSLCIQTQ DTLPASVKNL
1860 1870 1880 1890 1900
TRCIVISSLV TTQRKLKAMS LLSSRNQLAR AVLNPNPMDF CTKDLLTTTS
1910 1920 1930 1940 1950
ERIVAYLKDF NEDQKKAIET AYAMVKHSPS VAKICLIHGP PGTGKSKTIV
1960 1970 1980 1990 2000
GLLYRLLTEN QRKGHSDENF NAKIKQNRVL VCAPSNAAVD ELMKKIILEF
2010 2020 2030 2040 2050
KEKCKDKKNP LGNCGDINLV RLGPEKSINT EVLKFSLDSQ VNHRMKKDLP
2060 2070 2080 2090 2100
SHIQEMLRRK EILDAQLDEL SRQRALCRGG REMQRQELDE HIAIVSKERQ
2110 2120 2130 2140 2150
ELASKIKEVQ GRPQRAQNTI ILESHVICCT LSTSGGLLLE SAFRGQGGVP
2160 2170 2180 2190 2200
FSCVIVDEAG QSCEVETLSP LIHRCNKLIL VGDPKQLPPT VISMKAQEYG
2210 2220 2230 2240 2250
YDQSMMARFC KLLEENVEQN MIGRLPVLQL TIQYRMHPDI CLFPSNYVYN
2260 2270 2280 2290 2300
KNLKTNRLTE SIRCSSEWPF QPYLVFDVGD GSERRDNDSY INVQEIKLVM
2310 2320 2330 2340 2350
EIIKLIKEKR KDISFRNIGI ITHYKAQKTM IQKDLEKEFD KKGPAEVDTV
2360 2370 2380 2390 2400
DAFQGRQKDC IIVTCVRASA VQGSIGFLAS LQRLNVTITR AKYSLFILGH
2410 2420 2430 2440 2450
LRTLMENQHW YELIQDAQKR GAIIKTSDPN YRHDAMKILK LKPVLQRSLT
2460 2470 2480 2490 2500
HPPATAPEAP RPQGGLPSNR LDSGLATTSF AASLYHTPSD TVTSKGPERP
2510 2520 2530 2540 2550
LLQDRLRDPR LLRRLDAEAK GTFLKDPQPV SPQLPGVVHL LGEPGFPVVF
2560 2570 2580 2590 2600
QDLGFVVPPS TAIVAPLGSH RSPMQAEPPP AHPAAAASTS KRKYSDPDAG
2610 2620 2630 2640
LSHKREPRAF SGEQGRHGSV THHVLRSTDW DRRRLDDSSA KRRQFL
Length:2,646
Mass (Da):297,589
Last modified:February 20, 2007 - v1
Checksum:i3036F84EFED4A098
GO
Isoform 2 (identifier: A2AKX3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: Missing.

Note: No experimental confirmation available.

Show »
Length:2,265
Mass (Da):253,320
Checksum:iAA0DCF08E90FAEED
GO

Sequence cautioni

The sequence BAC32054.1 differs from that shown. Reason: Frameshift at position 699. Curated
The sequence BAC97987.1 differs from that shown.The sequence differs from that shown because it is derived from pre-RNA.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti644 – 6441S → C in BAC32054 (PubMed:16141072).Curated
Sequence conflicti1048 – 10481Q → R in BAC33309 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 381381Missing in isoform 2. 1 PublicationVSP_028827Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL772379, AL845267 Genomic DNA. Translation: CAM16246.1.
AL845267, AL772379 Genomic DNA. Translation: CAM23971.1.
AL845267 Genomic DNA. Translation: CAM23973.2.
AK044730 mRNA. Translation: BAC32054.1. Frameshift.
AK048354 mRNA. Translation: BAC33309.2.
AK077911 mRNA. Translation: BAC37058.1.
BC046382 mRNA. Translation: AAH46382.1.
BC058109 mRNA. Translation: AAH58109.2.
BC079604 mRNA. Translation: AAH79604.2.
AK129177 Transcribed RNA. Translation: BAC97987.1. Sequence problems.
BK001523 mRNA. Translation: DAA01946.1.
CCDSiCCDS38090.1. [A2AKX3-1]
RefSeqiNP_932150.2. NM_198033.2. [A2AKX3-1]
UniGeneiMm.41867.

Genome annotation databases

EnsembliENSMUST00000061578; ENSMUSP00000051492; ENSMUSG00000043535. [A2AKX3-1]
GeneIDi269254.
KEGGimmu:269254.
UCSCiuc008izm.1. mouse. [A2AKX3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL772379, AL845267 Genomic DNA. Translation: CAM16246.1.
AL845267, AL772379 Genomic DNA. Translation: CAM23971.1.
AL845267 Genomic DNA. Translation: CAM23973.2.
AK044730 mRNA. Translation: BAC32054.1. Frameshift.
AK048354 mRNA. Translation: BAC33309.2.
AK077911 mRNA. Translation: BAC37058.1.
BC046382 mRNA. Translation: AAH46382.1.
BC058109 mRNA. Translation: AAH58109.2.
BC079604 mRNA. Translation: AAH79604.2.
AK129177 Transcribed RNA. Translation: BAC97987.1. Sequence problems.
BK001523 mRNA. Translation: DAA01946.1.
CCDSiCCDS38090.1. [A2AKX3-1]
RefSeqiNP_932150.2. NM_198033.2. [A2AKX3-1]
UniGeneiMm.41867.

3D structure databases

ProteinModelPortaliA2AKX3.
SMRiA2AKX3. Positions 1907-2437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234629. 4 interactions.
DIPiDIP-56995N.
IntActiA2AKX3. 3 interactions.

PTM databases

PhosphoSiteiA2AKX3.

Proteomic databases

MaxQBiA2AKX3.
PaxDbiA2AKX3.
PRIDEiA2AKX3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061578; ENSMUSP00000051492; ENSMUSG00000043535. [A2AKX3-1]
GeneIDi269254.
KEGGimmu:269254.
UCSCiuc008izm.1. mouse. [A2AKX3-1]

Organism-specific databases

CTDi23064.
MGIiMGI:2443480. Setx.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG1112.
GeneTreeiENSGT00770000120665.
HOVERGENiHBG108476.
InParanoidiA2AKX3.
KOiK10706.
OrthoDBiEOG7JX33B.
PhylomeDBiA2AKX3.
TreeFamiTF324634.

Miscellaneous databases

NextBioi392760.
PROiA2AKX3.
SOURCEiSearch...

Gene expression databases

BgeeiA2AKX3.
CleanExiMM_SETX.
GenevestigatoriA2AKX3.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1050 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-858 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2464-2646.
    Strain: C57BL/6J.
    Tissue: Head, Retina and Testis.
  3. "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] OF 1745-2646 (ISOFORM 1).
    Strain: 129 and C57BL/6.
    Tissue: Brain and Mammary tumor.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1915-2646 (ISOFORM 1).
    Tissue: Embryonic tail.
  5. Cited for: IDENTIFICATION (ISOFORM 1).
    Strain: C57BL/6J.
  6. "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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Feedback regulation of transcriptional termination by the mammalian circadian clock PERIOD complex."
    Padmanabhan K., Robles M.S., Westerling T., Weitz C.J.
    Science 337:599-602(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN RHYTHMS, INTERACTION WITH PER2.
  8. "Senataxin plays an essential role with DNA damage response proteins in meiotic recombination and gene silencing."
    Becherel O.J., Yeo A.J., Stellati A., Heng E.Y., Luff J., Suraweera A.M., Woods R., Fleming J., Carrie D., McKinney K., Xu X., Deng C., Lavin M.F.
    PLoS Genet. 9:E1003435-E1003435(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSETX_MOUSE
AccessioniPrimary (citable) accession number: A2AKX3
Secondary accession number(s): A2AKX4
, A2AR33, Q6IMG6, Q6PED8, Q6ZQ81, Q80V90, Q8C5P1, Q8C859, Q8C8P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: February 20, 2007
Last modified: April 29, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.