TWNK
entrez
56652
canonical
uniprot
Q96RR1
canonical
ensembl
ENSG00000107815
resolver
ensp
ENSP00000309595
resolver
ensp
ENSP00000359248
resolver
ensp
ENSP00000494326
resolver
ensp
ENSP00000496012
resolver
enst
ENST00000473656
resolver
enst
ENST00000476766
resolver
genesymbol
C10orf2
resolver
genesymbol
TWNK
resolver
genesymbol_syn
C10orf2
resolver
genesymbol_syn
PEO1
resolver
hgnc
HGNC:1160
resolver
uniprot
A0A2R8Y4V4
resolver
uniprot
A0A2R8Y746
resolver
uniprot
B2CQL2
resolver
uniprot
E5KSY5
resolver
uniprot
Q6MZX2
resolver
uniprot
Q6PJP5
resolver
uniprot
Q96RR0
resolver
uniprot
Q9H6V3
resolver
uniprot_entry
A0A2R8Y4V4_HUMAN
resolver
uniprot_entry
A0A2R8Y746_HUMAN
resolver
uniprot_entry
E5KSY5_HUMAN
resolver
uniprot_entry
PEO1_HUMAN
resolver
uniprot_entry
Q9H6V3_HUMAN
resolver
uniprot_sec
B2CQL2
resolver
uniprot_sec
Q6MZX2
resolver
uniprot_sec
Q6PJP5
resolver
uniprot_sec
Q96RR0
resolver
activity_regulation
ACTIVITY REGULATION: [Isoform 1]: Strand annealing activity is inhibited by 150 mM NaCl (in vitro). {ECO:0000269|PubMed:22383523}.
uniprot
proteins
amino_acid_sequence
MWVLLRSGYPLRILLPLRGEWMGRRGLPRNLAPGPPRRRYRKETLQALDMPVLPVTATEIRQYLRGHGIPFQDGHSCLRALSPFAESSQLKGQTGVTTSFSLFIDKTTGHFLCMTSLAEGSWEDFQASVEGRGDGAREGFLLSKAPEFEDSEEVRRIWNRAIPLWELPDQEEVQLADTMFGLTKVTDDTLKRFSVRYLRPARSLVFPWFSPGGSGLRGLKLLEAKCQGDGVSYEETTIPRPSAYHNLFGLPLISRRDAEVVLTSRELDSLALNQSTGLPTLTLPRGTTCLPPALLPYLEQFRRIVFWLGDDLRSWEAAKLFARKLNPKRCFLVRPGDQQPRPLEALNGGFNLSRILRTALPAWHKSIVSFRQLREEVLGELSNVEQAAGLRWSRFPDLNRILKGHRKGELTVFTGPTGSGKTTFISEYALDLCSQGVNTLWGSFEISNVRLARVMLTQFAEGRLEDQLDKYDHWADRFEDLPLYFMTFHGQQSIRTVIDTMQHAVYVYDICHVIIDNLQFMMGHEQLSTDRIAAQDYIIGVFRKFATDNNCHVTLVIHPRKEDDDKELQTASIFGSAKASQEADNVLILQDRKLVTGPGKRYLQVSKNRFDGDVGVFPLEFNKNSLTFSIPPKNKARLKKIKDDTGPVAKKPSSGKKGATTQNSEICSGQAPTPDQPDTSKRSK
uniprot
proteins
disease_involvement
DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 3 (PEOA3) [MIM:609286]: A disorder characterized by progressive weakness of ocular muscles and levator muscle of the upper eyelid. In a minority of cases, it is associated with skeletal myopathy, which predominantly involves axial or proximal muscles and which causes abnormal fatigability and even permanent muscle weakness. Ragged-red fibers and atrophy are found on muscle biopsy. A large proportion of chronic ophthalmoplegias are associated with other symptoms, leading to a multisystemic pattern of this disease. Additional symptoms are variable, and may include cataracts, hearing loss, sensory axonal neuropathy, ataxia, depression, hypogonadism, and parkinsonism. {ECO:0000269|PubMed:11431692, ECO:0000269|PubMed:12163192, ECO:0000269|PubMed:12921794, ECO:0000269|PubMed:15668446, ECO:0000269|PubMed:16639411, ECO:0000269|PubMed:17614277, ECO:0000269|PubMed:18396044, ECO:0000269|PubMed:18575922, ECO:0000269|PubMed:19353676, ECO:0000269|PubMed:19428252, ECO:0000269|PubMed:20479361, ECO:0000269|PubMed:20880070}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mitochondrial DNA depletion syndrome 7 (MTDPS7) [MIM:271245]: A severe disease associated with mitochondrial dysfunction. Some patients are affected by progressive atrophy of the cerebellum, brain stem, the spinal cord, and sensory axonal neuropathy. Clinical features include hypotonia, athetosis, ataxia, ophthalmoplegia, sensorineural hearing deficit, sensory axonal neuropathy, epileptic encephalopathy and female hypogonadism. In some individuals liver dysfunction and multi-organ failure is present. {ECO:0000269|PubMed:16135556, ECO:0000269|PubMed:17722119, ECO:0000269|PubMed:17921179, ECO:0000269|PubMed:19853444, ECO:0000269|PubMed:22353293}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Perrault syndrome 5 (PRLTS5) [MIM:616138]: A form of Perrault syndrome, a sex-influenced disorder characterized by sensorineural deafness in both males and females, and ovarian dysgenesis in females. Affected females have primary amenorrhea, streak gonads, and infertility, whereas affected males show normal pubertal development and are fertile. PRLTS5 is an autosomal recessive form characterized by progressive ataxia, axonal neuropathy, hyporeflexia and abnormal eye movements, in addition to deafness and ovarian dysgenesis. {ECO:0000269|PubMed:25355836}. 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: [Isoform 1]: Mitochondrial helicase involved in mtDNA replication and repair (PubMed:12975372, PubMed:15167897, PubMed:17324440, PubMed:18039713, PubMed:18971204, PubMed:25824949, PubMed:26887820, PubMed:27226550). Might have a role in mtDNA repair (PubMed:27226550). Has DNA strand separation activity needed to form a processive replication fork for leading strand synthesis which is catalyzed by the formation of a replisome complex with POLG and mtSDB (PubMed:12975372, PubMed:15167897, PubMed:18039713, PubMed:22383523, PubMed:26887820, PubMed:27226550). Preferentially unwinds DNA substrates with pre-existing 5'-and 3'- single-stranded tails but is also active on a 5'- flap substrate (PubMed:12975372, PubMed:15167897, PubMed:18039713, PubMed:22383523, PubMed:26887820, PubMed:27226550). Can dissociate the invading strand of immobile or mobile D-loop DNA structures irrespective of the single strand polarity of the third strand (PubMed:27226550). In addition to its DNA strand separation activity, also has DNA strand annealing, DNA strand-exchange and DNA branch migration activities (PubMed:22383523, PubMed:26887820, PubMed:27226550). {ECO:0000269|PubMed:12975372, ECO:0000269|PubMed:15167897, ECO:0000269|PubMed:17324440, ECO:0000269|PubMed:18039713, ECO:0000269|PubMed:18971204, ECO:0000269|PubMed:22383523, ECO:0000269|PubMed:25824949, ECO:0000269|PubMed:26887820, ECO:0000269|PubMed:27226550}.; FUNCTION: [Isoform 2]: Lack DNA unwinding and ATP hydrolysis activities (PubMed:18039713). Does not bind single-stranded or double-stranded DNA (PubMed:18039713). {ECO:0000269|PubMed:18039713}.
uniprot
proteins
mass_dalton
77154
uniprot
proteins
mutagenesis
MUTAGEN 421; /note="K->A: Loss of helicase activity on 5'-tailed substrate."; /evidence="ECO:0000269|PubMed:22383523
uniprot
proteins
pubmed
11431692
uniprot
proteins
pubmed
12163192
uniprot
proteins
pubmed
12557300
uniprot
proteins
pubmed
12707443
uniprot
proteins
pubmed
12872260
uniprot
proteins
pubmed
12921794
uniprot
proteins
pubmed
12975372
uniprot
proteins
pubmed
14739292
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15167897
uniprot
proteins
pubmed
15181170
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15509589
uniprot
proteins
pubmed
15668446
uniprot
proteins
pubmed
16135556
uniprot
proteins
pubmed
16639411
uniprot
proteins
pubmed
17324440
uniprot
proteins
pubmed
17614277
uniprot
proteins
pubmed
17722119
uniprot
proteins
pubmed
17921179
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18039713
uniprot
proteins
pubmed
18396044
uniprot
proteins
pubmed
18575922
uniprot
proteins
pubmed
18971204
uniprot
proteins
pubmed
19353676
uniprot
proteins
pubmed
19428252
uniprot
proteins
pubmed
19853444
uniprot
proteins
pubmed
20479361
uniprot
proteins
pubmed
20880070
uniprot
proteins
pubmed
22353293
uniprot
proteins
pubmed
22383523
uniprot
proteins
pubmed
25355836
uniprot
proteins
pubmed
25824949
uniprot
proteins
pubmed
26887820
uniprot
proteins
pubmed
27226550
uniprot
proteins
pubmed
30496414
uniprot
proteins
pubmed
34950192
uniprot
proteins
pubmed
35914129
uniprot
proteins
sequence_length
684
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:11431692, ECO:0000269|PubMed:18971204}. Mitochondrion inner membrane {ECO:0000303|PubMed:34950192}; Peripheral membrane protein {ECO:0000269|PubMed:34950192}. Note=Colocalizes with mtDNA in mitochondrial nucleoids, a nucleoproteins complex consisting of a number of copies of proteins associated with mtDNA, probably involved in mtDNA maintenance and expression (PubMed:11431692). Associates with phospholipid membranes via electrostatic binding (By similarity). Preferentially associates with membranes enriched with cardiolipin, a lipid abundant in the mitochondrial inner membrane (PubMed:34950192). ATPase and helicase activity is enhanced by binding to lipid membranes (PubMed:34950192). {ECO:0000250|UniProtKB:Q9VL76, ECO:0000269|PubMed:11431692, ECO:0000269|PubMed:34950192}.
uniprot
proteins