HELB
entrez
92797
canonical
uniprot
Q8NG08
canonical
ensembl
ENSG00000127311
resolver
ensp
ENSP00000247815
resolver
ensp
ENSP00000439617
resolver
ensp
ENSP00000443287
resolver
enst
ENST00000542394
resolver
genesymbol
HELB
resolver
hgnc
HGNC:17196
resolver
uniprot
A8K4C9
resolver
uniprot
F5H1I4
resolver
uniprot
Q4G0T2
resolver
uniprot
Q9H7L5
resolver
uniprot_entry
F5H1I4_HUMAN
resolver
uniprot_entry
HELB_HUMAN
resolver
uniprot_sec
A8K4C9
resolver
uniprot_sec
Q4G0T2
resolver
uniprot_sec
Q9H7L5
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by salt concentration greater than 100 mM. Uses either magnesium or manganese ions to support helicase activity. Binds strongly to single-stranded DNA in the absence of ATP but dissociates readily in the presence of 1 mM ATP. {ECO:0000269|PubMed:12181327}.
uniprot
proteins
amino_acid_sequence
MARSSPYLRQLQGPLLPPRDLVEEDDDYLNDDVEEDEESVFIDAEELCSGGVKAGSLPGCLRVSICDENTQETCKVFGRFPITGAWWRVKVQVKPVVGSRSYQYQVQGFPSYFLQSDMSPPNQKHICALFLKECEVSSDDVNKFLTWVKEVSNYKNLNFENLRETLRTFHKETGRKDQKQPTQNGQEELFLDNEMSLPLENTIPFRNVMTALQFPKIMEFLPVLLPRHFKWIIGSGSKEMLKEIEEILGTHPWKLGFSKITYREWKLLRCEASWIAFCQCESLLQLMTDLEKNALIMYSRLKQICREDGHTYVEVNDLTLTLSNHMSFHAASESLKFLKDIGVVTYEKSCVFPYDLYHAERAIAFSICDLMKKPPWHLCVDVEKVLASIHTTKPENSSDDALNESKPDEVRLENPVDVVDTQDNGDHIWTNGENEINAEISEVQLDQDQVEVPLDRDQVAALEMICSNPVTVISGKGGCGKTTIVSRLFKHIEQLEEREVKKACEDFEQDQNASEEWITFTEQSQLEADKAIEVLLTAPTGKAAGLLRQKTGLHAYTLCQVNYSFYSWTQTMMTTNKPWKFSSVRVLVVDEGSLVSVGIFKSVLNLLCEHSKLSKLIILGDIRQLPSIEPGNLLKDLFETLKSRNCAIELKTNHRAESQLIVDNATRISRRQFPKFDAELNISDNPTLPISIQDKTFIFVRLPEEDASSQSSKTNHHSCLYSAVKTLLQENNLQNAKTSQFIAFRRQDCDLINDCCCKHYTGHLTKDHQSRLVFGIGDKICCTRNAYLSDLLPENISGSQQNNDLDASSEDFSGTLPDFAKNKRDFESNVRLCNGEIFFITNDVTDVTFGKRRSLTINNMAGLEVTVDFKKLMKYCRIKHAWARTIHTFQGSEEQTVVYVVGKAGRQHWQHVYTAVTRGRCRVYVIAEESQLRNAIMKNSFPRKTRLKHFLQSKLSSSGAPPADFPSPRKSSGDSGGPSTPSASPLPVVTDHAMTNDVTWSEASSPDERTLTFAERWQLSSPDGVDTDDDLPKSRASKRTCGVNDDESPSKIFMVGESPQVSSRLQNLRLNNLIPRQLFKPTDNQET
uniprot
proteins
ec_number
5.6.2.3
uniprot
proteins
function
FUNCTION: 5'-3' DNA helicase involved in DNA damage response by acting as an inhibitor of DNA end resection (PubMed:25617833, PubMed:26774285). Recruitment to single-stranded DNA (ssDNA) following DNA damage leads to inhibit the nucleases catalyzing resection, such as EXO1, BLM and DNA2, possibly via the 5'-3' ssDNA translocase activity of HELB (PubMed:26774285). As cells approach S phase, DNA end resection is promoted by the nuclear export of HELB following phosphorylation (PubMed:26774285). Acts independently of TP53BP1 (PubMed:26774285). Unwinds duplex DNA with 5'-3' polarity. Has single-strand DNA-dependent ATPase and DNA helicase activities. Prefers ATP and dATP as substrates (PubMed:12181327). During S phase, may facilitate cellular recovery from replication stress (PubMed:22194613). {ECO:0000269|PubMed:12181327, ECO:0000269|PubMed:22194613, ECO:0000269|PubMed:25617833, ECO:0000269|PubMed:26774285}.
uniprot
proteins
mass_dalton
123252
uniprot
proteins
mutagenesis
MUTAGEN 481; /note="K->A: No ATPase activity."; /evidence="ECO:0000269|PubMed:12181327, ECO:0000269|PubMed:25617833, ECO:0000269|PubMed:26774285"; MUTAGEN 499; /note="E->A: Loss of RPA1-binding, leading to impaired recruitment to sites of double-strand breaks; when associated with A-506 and A-510."; /evidence="ECO:0000269|PubMed:22194613, ECO:0000269|PubMed:26774285"; MUTAGEN 506; /note="D->A: Loss of RPA1-binding, leading to impaired recruitment to sites of double-strand breaks; when associated with A-499 and A-510."; /evidence="ECO:0000269|PubMed:22194613, ECO:0000269|PubMed:26774285"; MUTAGEN 510; /note="D->A: Loss of RPA1-binding, leading to impaired recruitment to sites of double-strand breaks; when associated with A-499 and A-506."; /evidence="ECO:0000269|PubMed:22194613, ECO:0000269|PubMed:26774285"; MUTAGEN 591; /note="E->Q: No ATPase activity."; /evidence="ECO:0000269|PubMed:12181327, ECO:0000269|PubMed:25617833, ECO:0000269|PubMed:26774285"; MUTAGEN 967; /note="S->A: Impaired phosphorylation, inducing accumulation in the nucleus."; /evidence="ECO:0000269|PubMed:15146062"; MUTAGEN 967; /note="S->D: Phosphomimetic mutant; leads to higher localization to the cytoplasm."; /evidence="ECO:0000269|PubMed:15146062"; MUTAGEN 984; /note="S->A: Does not affect subcellular location."; /evidence="ECO:0000269|PubMed:15146062"; MUTAGEN 1005; /note="S->A: Does not affect subcellular location."; /evidence="ECO:0000269|PubMed:15146062"; MUTAGEN 1021; /note="S->A: Does not affect subcellular location."; /evidence="ECO:0000269|PubMed:15146062"; MUTAGEN 1061..1065; /note="VSSRL->ASSRA: Accumulation in the nucleus due to defects in nuclear export."; /evidence="ECO:0000269|PubMed:15146062"; MUTAGEN 1068..1070; /note="LRL->ARA: Accumulation in the nucleus due to defects in nuclear export."; /evidence="ECO:0000269|PubMed:15146062
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-967 by CDK2 during the G1/S transition, resulting in its nuclear export into the cytoplasm (PubMed:15146062, PubMed:26774285). As S phase progresses, its exclusion from the nucleus promotes the activation of long-range resection (PubMed:26774285). {ECO:0000269|PubMed:15146062, ECO:0000269|PubMed:26774285}.
uniprot
proteins
protein_family
HELB subfamily
uniprot
proteins
protein_family
RecD family
uniprot
proteins
pubmed
12181327
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15146062
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22194613
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25617833
uniprot
proteins
pubmed
25933514
uniprot
proteins
pubmed
26774285
uniprot
proteins
pubmed
30304027
uniprot
proteins
sequence_length
1087
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15146062}. Cytoplasm {ECO:0000269|PubMed:15146062}. Chromosome {ECO:0000269|PubMed:26774285}. Note=Predominantly nuclear (PubMed:15146062). Phosphorylation at Ser-967 by CDK2 during the G1/S transition results in its nuclear export into the cytoplasm as cells approach and progress through S phase (PubMed:15146062). Following DNA damage, recruited to sites of double-strand breaks by the RPA complex (PubMed:26774285). Recruited to chromatin following DNA damage induced by UV irradiation, or camptothecin or hydroxyurea treatment (PubMed:22194613). {ECO:0000269|PubMed:15146062, ECO:0000269|PubMed:22194613, ECO:0000269|PubMed:26774285}.
uniprot
proteins