SETX
entrez
23064
canonical
uniprot
Q7Z333
canonical
ensembl
ENSG00000107290
resolver
ensp
ENSP00000224140
resolver
ensp
ENSP00000575365
resolver
ensp
ENSP00000593274
resolver
ensp
ENSP00000593275
resolver
ensp
ENSP00000744487
resolver
genesymbol
SETX
resolver
genesymbol_syn
ALS4
resolver
genesymbol_syn
KIAA0625
resolver
genesymbol_syn
SCAR1
resolver
hgnc
HGNC:445
resolver
uniprot
A2A396
resolver
uniprot
B2RPB2
resolver
uniprot
B5ME16
resolver
uniprot
C9JQ10
resolver
uniprot
O75120
resolver
uniprot
Q3KQX4
resolver
uniprot
Q5JUJ1
resolver
uniprot
Q68DW5
resolver
uniprot
Q6AZD7
resolver
uniprot
Q7Z3J6
resolver
uniprot
Q8WX33
resolver
uniprot
Q9H9D1
resolver
uniprot
Q9NVP9
resolver
uniprot_entry
SETX_HUMAN
resolver
uniprot_sec
A2A396
resolver
uniprot_sec
B2RPB2
resolver
uniprot_sec
B5ME16
resolver
uniprot_sec
C9JQ10
resolver
uniprot_sec
O75120
resolver
uniprot_sec
Q3KQX4
resolver
uniprot_sec
Q5JUJ1
resolver
uniprot_sec
Q68DW5
resolver
uniprot_sec
Q6AZD7
resolver
uniprot_sec
Q7Z3J6
resolver
uniprot_sec
Q8WX33
resolver
uniprot_sec
Q9H9D1
resolver
uniprot_sec
Q9NVP9
resolver
amino_acid_sequence
MSTCCWCTPGGASTIDFLKRYASNTPSGEFQTADEDLCYCLECVAEYHKARDELPFLHEVLWELETLRLINHFEKSMKAEIGDDDELYIVDNNGEMPLFDITGQDFENKLRVPLLEILKYPYLLLHERVNELCVEALCRMEQANCSFQVFDKHPGIYLFLVHPNEMVRRWAILTARNLGKVDRDDYYDLQEVLLCLFKVIELGLLESPDIYTSSVLEKGKLILLPSHMYDTTNYKSYWLGICMLLTILEEQAMDSLLLGSDKQNDFMQSILHTMEREADDDSVDPFWPALHCFMVILDRLGSKVWGQLMDPIVAFQTIINNASYNREIRHIRNSSVRTKLEPESYLDDMVTCSQIVYNYNPEKTKKDSGWRTAICPDYCPNMYEEMETLASVLQSDIGQDMRVHNSTFLWFIPFVQSLMDLKDLGVAYIAQVVNHLYSEVKEVLNQTDAVCDKVTEFFLLILVSVIELHRNKKCLHLLWVSSQQWVEAVVKCAKLPTTAFTRSSEKSSGNCSKGTAMISSLSLHSMPSNSVQLAYVQLIRSLLKEGYQLGQQSLCKRFWDKLNLFLRGNLSLGWQLTSQETHELQSCLKQIIRNIKFKAPPCNTFVDLTSACKISPASYNKEESEQMGKTSRKDMHCLEASSPTFSKEPMKVQDSVLIKADNTIEGDNNEQNYIKDVKLEDHLLAGSCLKQSSKNIFTERAEDQIKISTRKQKSVKEISSYTPKDCTSRNGPERGCDRGIIVSTRLLTDSSTDALEKVSTSNEDFSLKDDALAKTSKRKTKVQKDEICAKLSHVIKKQHRKSTLVDNTINLDENLTVSNIESFYSRKDTGVQKGDGFIHNLSLDPSGVLDDKNGEQKSQNNVLPKEKQLKNEELVIFSFHENNCKIQEFHVDGKELIPFTEMTNASEKKSSPFKDLMTVPESRDEEMSNSTSVIYSNLTREQAPDISPKSDTLTDSQIDRDLHKLSLLAQASVITFPSDSPQNSSQLQRKVKEDKRCFTANQNNVGDTSRGQVIIISDSDDDDDERILSLEKLTKQDKICLEREHPEQHVSTVNSKEEKNPVKEEKTETLFQFEESDSQCFEFESSSEVFSVWQDHPDDNNSVQDGEKKCLAPIANTTNGQGCTDYVSEVVKKGAEGIEEHTRPRSISVEEFCEIEVKKPKRKRSEKPMAEDPVRPSSSVRNEGQSDTNKRDLVGNDFKSIDRRTSTPNSRIQRATTVSQKKSSKLCTCTEPIRKVPVSKTPKKTHSDAKKGQNRSSNYLSCRTTPAIVPPKKFRQCPEPTSTAEKLGLKKGPRKAYELSQRSLDYVAQLRDHGKTVGVVDTRKKTKLISPQNLSVRNNKKLLTSQELQMQRQIRPKSQKNRRRLSDCESTDVKRAGSHTAQNSDIFVPESDRSDYNCTGGTEVLANSNRKQLIKCMPSEPETIKAKHGSPATDDACPLNQCDSVVLNGTVPTNEVIVSTSEDPLGGGDPTARHIEMAALKEGEPDSSSDAEEDNLFLTQNDPEDMDLCSQMENDNYKLIELIHGKDTVEVEEDSVSRPQLESLSGTKCKYKDCLETTKNQGEYCPKHSEVKAADEDVFRKPGLPPPASKPLRPTTKIFSSKSTSRIAGLSKSLETSSALSPSLKNKSKGIQSILKVPQPVPLIAQKPVGEMKNSCNVLHPQSPNNSNRQGCKVPFGESKYFPSSSPVNILLSSQSVSDTFVKEVLKWKYEMFLNFGQCGPPASLCQSISRPVPVRFHNYGDYFNVFFPLMVLNTFETVAQEWLNSPNRENFYQLQVRKFPADYIKYWEFAVYLEECELAKQLYPKENDLVFLAPERINEEKKDTERNDIQDLHEYHSGYVHKFRRTSVMRNGKTECYLSIQTQENFPANLNELVNCIVISSLVTTQRKLKAMSLLGSRNQLARAVLNPNPMDFCTKDLLTTTSERIIAYLRDFNEDQKKAIETAYAMVKHSPSVAKICLIHGPPGTGKSKTIVGLLYRLLTENQRKGHSDENSNAKIKQNRVLVCAPSNAAVDELMKKIILEFKEKCKDKKNPLGNCGDINLVRLGPEKSINSEVLKFSLDSQVNHRMKKELPSHVQAMHKRKEFLDYQLDELSRQRALCRGGREIQRQELDENISKVSKERQELASKIKEVQGRPQKTQSIIILESHIICCTLSTSGGLLLESAFRGQGGVPFSCVIVDEAGQSCEIETLTPLIHRCNKLILVGDPKQLPPTVISMKAQEYGYDQSMMARFCRLLEENVEHNMISRLPILQLTVQYRMHPDICLFPSNYVYNRNLKTNRQTEAIRCSSDWPFQPYLVFDVGDGSERRDNDSYINVQEIKLVMEIIKLIKDKRKDVSFRNIGIITHYKAQKTMIQKDLDKEFDRKGPAEVDTVDAFQGRQKDCVIVTCVRANSIQGSIGFLASLQRLNVTITRAKYSLFILGHLRTLMENQHWNQLIQDAQKRGAIIKTCDKNYRHDAVKILKLKPVLQRSLTHPPTIAPEGSRPQGGLPSSKLDSGFAKTSVAASLYHTPSDSKEITLTVTSKDPERPPVHDQLQDPRLLKRMGIEVKGGIFLWDPQPSSPQHPGATPPTGEPGFPVVHQDLSHIQQPAAVVAALSSHKPPVRGEPPAASPEASTCQSKCDDPEEELCHRREARAFSEGEQEKCGSETHHTRRNSRWDKRTLEQEDSSSKKRKLL
uniprot
proteins
disease_involvement
DISEASE: Spinocerebellar ataxia, autosomal recessive, with axonal neuropathy 2 (SCAN2) [MIM:606002]: A form of spinocerebellar ataxia, 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. SCAN2 is an autosomal recessive form associated with peripheral neuropathy and elevated serum alpha-fetoprotein, immunoglobulins and, less commonly, creatine kinase levels. Some SCAN2 patients manifest oculomotor apraxia. {ECO:0000269|PubMed:14770181, ECO:0000269|PubMed:16644229, ECO:0000269|PubMed:16717225, ECO:0000269|PubMed:17096168, ECO:0000269|PubMed:23566282, ECO:0000269|PubMed:23786967, ECO:0000269|PubMed:23941260, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:36864660}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: 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. {ECO:0000269|PubMed:14770181, ECO:0000269|PubMed:15106121, ECO:0000269|PubMed:21190393, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:24244371, ECO:0000269|PubMed:36864660}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
5.6.2.3
uniprot
proteins
function
FUNCTION: ATP-dependent 5'-3' helicase that preferentially unwinds RNA:DNA substrates over DNA:DNA substrates, playing a crucial role in resolving 5'-overhang RNA:DNA hybrids (R-loops) and promoting transcription termination (PubMed:36864660). 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). {ECO:0000250|UniProtKB:A2AKX3, ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:19515850, ECO:0000269|PubMed:21112256, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:21700224, ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:26700805, ECO:0000269|PubMed:36864660}.
uniprot
proteins
mass_dalton
302880
uniprot
proteins
mutagenesis
MUTAGEN 65; /note="E->K: Abolishes interaction with EXOSC9 and UBE2I and decreases sumoylation."; /evidence="ECO:0000269|PubMed:24105744"; MUTAGEN 2181..2182; /note="DE->AA: Loss of ATPase and helicase activity."; /evidence="ECO:0000269|PubMed:36864660
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. {ECO:0000269|PubMed:24244371}.; PTM: Sumoylated preferentially with SUMO2 or SUMO3 (PubMed:24105744, PubMed:24244371). {ECO:0000269|PubMed:24105744, ECO:0000269|PubMed:24244371}.
uniprot
proteins
protein_family
DNA2/NAM7 helicase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14770181
uniprot
proteins
pubmed
15106121
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16644229
uniprot
proteins
pubmed
16717225
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17096168
uniprot
proteins
pubmed
17562789
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19515850
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21112256
uniprot
proteins
pubmed
21190393
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21576111
uniprot
proteins
pubmed
21700224
uniprot
proteins
pubmed
23149945
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23566282
uniprot
proteins
pubmed
23786967
uniprot
proteins
pubmed
23941260
uniprot
proteins
pubmed
24105744
uniprot
proteins
pubmed
24244371
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
26700805
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
36864660
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
2677
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:24105744}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17562789}. Nucleus, nucleolus {ECO:0000269|PubMed:17562789}. Cytoplasm {ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:21576111}. Chromosome {ECO:0000269|PubMed:23149945}. Chromosome, telomere {ECO:0000269|PubMed:21112256}. Cell projection, axon {ECO:0000269|PubMed:21576111}. Cell projection, growth cone {ECO:0000269|PubMed:21576111}. Note=May be detected in the nucleolus only in cycling cells. At pachytene stage, colocalizes predominantly to the heterochromatic XY-body of sex chromosomes with DNA damage response proteins in a BRCA1-dependent manner (By similarity). Localizes with telomeric DNA in a transcription-dependent manner (PubMed:21112256). 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 (PubMed:23149945). Localizes at limited number of nuclear foci (PubMed:24105744). Colocalizes with EXOSC9 in nuclear foci upon induction of transcription-related DNA damage at the S phase (PubMed:24105744). Most abundant in the nucleus. Detected in granules. Colocalized in cycling cells with FBL in the nucleolus. {ECO:0000250|UniProtKB:A2AKX3, ECO:0000269|PubMed:17562789, ECO:0000269|PubMed:21112256, ECO:0000269|PubMed:21576111, ECO:0000269|PubMed:23149945, ECO:0000269|PubMed:24105744}.
uniprot
proteins