Helb
entrez
117599
canonical
uniprot
Q6NVF4
canonical
ensembl
ENSMUSG00000020228
resolver
ensp
ENSMUSP00000020449
resolver
enst
ENSMUST00000020449
resolver
genesymbol
Helb
resolver
uniprot
G5E835
resolver
uniprot
Q6KAT5
resolver
uniprot
Q8C930
resolver
uniprot
Q9EQT8
resolver
uniprot_entry
HELB_MOUSE
resolver
uniprot_sec
G5E835
resolver
uniprot_sec
Q6KAT5
resolver
uniprot_sec
Q8C930
resolver
uniprot_sec
Q9EQT8
resolver
amino_acid_sequence
MARQDRLRELLGPLHPYKSDDEEEDCAQEEEGEQEEEFVDAEELCSGGIKAGSLPGRARVSIPDEYTKEKCTVYGRFPLKGPWWRVKVQVLKPQRSRSYQVQGFPAYFLQVDMSPPDQKQICSLFLKECNLASERIQEFLKWVEKVSSFENLHFENLWETLRLFYRETEKKDKKLSTPREQQGEEMRVEKSFAFISAMVALQFPKVMEFLPSLFPRHFKRLISSSSDWVLGCIEDVLGTQPWKLGFRRITYREMKLVRCEASWTAFSQCPSLLQLMTPLQKNALVIYSKLRQTCREDGHTYIEVKDLTSGLSEHMSFEEACQSLAFLKDIDVVIYEKDYVFLSELYEAEQDIASSICELMSRPPWHLKVDVKNVLASIRGAKPNDPGSAEAVEGSKPEEVGSEQGDSVLDAQDGDDHVRSNGEHVANAEINDVPLDQDQVVALETICANAVTVLSGKGGCGKTTIVSRLFKHMEHLEETEVQQACEDFEQDQEASEEWLDCPKQSPAGVDKAVEVLLTAPTGKAAGLLRQRTDLPAYTLCQVNYSFYMWKTKNEVDKPWKFSTVRVLVVDEGSLVSVGIFKSVLQLLCKHSKLSKLIILGDVRQLPSIEPGNMLQDVFETLKSRQCAIELKTNHRTESQLIVDNATRISRRQFPKFDAELNICGNPTLPLSIQDKTFIFVRLPEEDSRSQSSKGEHRSNLYTAVKTLLQGKDFCSFESSKTSQFIAFRRQDCDLINDCCCKHYTGHLIKDHEKKLIFAVGDKICCTRNAYLSDLLPDKDQEAEGKGYGDAPDDDAKIKQDFESSTRLCNGEIFFITRDVTDVTFKRKRLLTINNEAGLEVTVDFSKLMANCQIKHAWARTIHTFQGSEENTVVYVVGKAGRQHWQHVYTAVTRGRSRVYIIAQESELRSATRKRGFPRQTRLKHFLQKKLSGSCAPSTGFASQPSSPRVGGRPDTQPPASHLCRTPDNKATADSARGDERWLSASVNDDVDTDEESAQLRGSKRIGDGFPFDEESPSKFRMVEAPSPQVSSVFQNMRLNTLTPRQLFKPTDNQDTGTAGVADDANDPSNQEMEM
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: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 (PubMed:2966639). Has single-strand DNA-dependent ATPase and DNA helicase activities (PubMed:3038170). Prefers ATP and dATP as substrates (PubMed:2966639, PubMed:3038170). During S phase, may facilitate cellular recovery from replication stress (PubMed:11557815, PubMed:7596831, PubMed:7794903). {ECO:0000269|PubMed:11557815, ECO:0000269|PubMed:26774285, ECO:0000269|PubMed:2966639, ECO:0000269|PubMed:3038170, ECO:0000269|PubMed:7596831, ECO:0000269|PubMed:7794903}.
uniprot
proteins
mass_dalton
121471
uniprot
proteins
mutagenesis
MUTAGEN 462; /note="K->A: No ATPase activity."; /evidence="ECO:0000269|PubMed:26774285"; MUTAGEN 1029..1038; /note="VSSVFQNMRL->ASSVAQNARA: Accumulation in the nucleus due to defects in nuclear export."; /evidence="ECO:0000269|PubMed:26774285
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-942 by CDK2 during the G1/S transition, resulting in its nuclear export into the cytoplasm. As S phase progresses, its exclusion from the nucleus promotes the activation of long-range resection. {ECO:0000250|UniProtKB:Q8NG08}.
uniprot
proteins
protein_family
HELB subfamily
uniprot
proteins
protein_family
RecD family
uniprot
proteins
pubmed
11557815
uniprot
proteins
pubmed
15449545
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26774285
uniprot
proteins
pubmed
2966639
uniprot
proteins
pubmed
3038170
uniprot
proteins
pubmed
7596831
uniprot
proteins
pubmed
7794903
uniprot
proteins
sequence_length
1074
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26774285}. Cytoplasm {ECO:0000269|PubMed:26774285}. Chromosome {ECO:0000250|UniProtKB:Q8NG08}. Note=Predominantly nuclear. Phosphorylation at Ser-942 by CDK2 during the G1/S transition results in its nuclear export into the cytoplasm as cells approach and progress through S phase. Following DNA damage, recruited to sites of double-strand breaks by the RPA complex. {ECO:0000250|UniProtKB:Q8NG08}.
uniprot
proteins