RECQL5
entrez
9400
canonical
uniprot
O94762
canonical
ensembl
ENSG00000108469
resolver
ensp
ENSP00000317636
resolver
ensp
ENSP00000341983
resolver
ensp
ENSP00000414933
resolver
ensp
ENSP00000589353
resolver
ensp
ENSP00000707023
resolver
ensp
ENSP00000707028
resolver
genesymbol
RECQL5
resolver
genesymbol_syn
RECQ5
resolver
hgnc
HGNC:9950
resolver
uniprot
B3KQK2
resolver
uniprot
Q6P4G0
resolver
uniprot
Q9H0B1
resolver
uniprot
Q9P1W7
resolver
uniprot
Q9UNC8
resolver
uniprot_entry
B3KQK2_HUMAN
resolver
uniprot_entry
RECQ5_HUMAN
resolver
uniprot_sec
Q6P4G0
resolver
uniprot_sec
Q9H0B1
resolver
uniprot_sec
Q9P1W7
resolver
uniprot_sec
Q9UNC8
resolver
amino_acid_sequence
MSSHHTTFPFDPERRVRSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCFRANLFYDVQFKELISDPYGNLKDFCLKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKASDKATIMAFDALVTFCEELGCRHAAIAKYFGDALPACAKGCDHCQNPTAVRRRLEALERSSSWSKTCIGPSQGNGFDPELYEGGRKGYGDFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMQLRKGKDPKIEEFVPPDENCPLKEASSRRIPRLTVKAREHCLRLLEEALSSNRQSTRTADEADLRAKAVELEHETFRNAKVANLYKASVLKKVADIHRASKDGQPYDMGGSAKSCSAQAEPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSIARFFCRRVESPALLASAPEAEGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPSTCPPRDQGTPEVQPTPAKDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTAQDPFQLSAPGVSLKEAANVVVKCLTPFYKEGKFASKELFKGFARHLSHLLTQKTSPGRSVKEEAQNLIRHFFHGRARCESEADWHGLCGPQR
uniprot
proteins
ec_number
5.6.2.4
uniprot
proteins
function
FUNCTION: DNA helicase that plays an important role in DNA replication, transcription and repair (PubMed:20643585, PubMed:22973052, PubMed:28100692). Probably unwinds DNA in a 3'-5' direction (Probable) (PubMed:28100692). Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability (PubMed:20231364). Also associates with POLR1A and enforces the stability of ribosomal DNA arrays (PubMed:27502483). Plays an important role in mitotic chromosome separation after cross-over events and cell cycle progress (PubMed:22013166). Mechanistically, removes RAD51 filaments protecting stalled replication forks at common fragile sites and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis (PubMed:28575661). Required for efficient DNA repair, including repair of inter-strand cross-links (PubMed:23715498). Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination. A core helicase fragment (residues 11-609) binds preferentially to splayed duplex, looped and ssDNA (PubMed:28100692). {ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20643585, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22973052, ECO:0000269|PubMed:23715498, ECO:0000269|PubMed:23748380, ECO:0000269|PubMed:27502483, ECO:0000269|PubMed:28100692, ECO:0000269|PubMed:28575661, ECO:0000305|PubMed:28100692}.
uniprot
proteins
mass_dalton
108858
uniprot
proteins
mutagenesis
MUTAGEN 157; /note="D->A: Abolishes helicase activity."; MUTAGEN 165; /note="W->A: Loss of helicase activity, reduced DNA-binding (in a residue 11-526 fragment)."; /evidence="ECO:0000269|PubMed:28100692"; MUTAGEN 167; /note="H->A: Loss of helicase activity, reduced DNA-binding (in a residue 11-526 fragment)."; /evidence="ECO:0000269|PubMed:28100692"; MUTAGEN 345; /note="Q->A: Loss of helicase activity, reduced DNA-binding (in a residue 11-526 fragment)."; /evidence="ECO:0000269|PubMed:28100692"; MUTAGEN 352; /note="R->G: Loss of helicase activity (in a residue 11-526 fragment)."; /evidence="ECO:0000269|PubMed:28100692"; MUTAGEN 504; /note="W->A: Abolishes interaction with POLR2A."; MUTAGEN 508; /note="Y->A: Abolishes interaction with POLR2A."; MUTAGEN 515; /note="R->E: Abolishes interaction with POLR2A."; MUTAGEN 516; /note="K->E: Abolishes interaction with POLR2A."; MUTAGEN 550; /note="R->A: Impairs protein folding and abolishes interaction with POLR2A."; /evidence="ECO:0000269|PubMed:20231364"; MUTAGEN 552; /note="H->A: Abolishes interaction with POLR2A."; MUTAGEN 556; /note="L->E: Abolishes interaction with POLR2A."; MUTAGEN 584; /note="E->A,D: Abolishes interaction with POLR2A."; /evidence="ECO:0000269|PubMed:20231364"; MUTAGEN 597; /note="Y->A: Reduces interaction with POLR2A."; /evidence="ECO:0000269|PubMed:20231364"; MUTAGEN 598; /note="K->E: Abolishes interaction with POLR2A."; MUTAGEN 602; /note="L->D,E: Abolishes interaction with POLR2A."; /evidence="ECO:0000269|PubMed:20231364"; MUTAGEN 603; /note="K->E: Abolishes interaction with POLR2A."; MUTAGEN 666; /note="F->A: Abolishes interaction with RAD51."; /evidence="ECO:0000269|PubMed:20348101"; MUTAGEN 727; /note="S->A: Loss of phosphorylation in early mitosis."; /evidence="ECO:0000269|PubMed:28575661
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CDK1 at Ser-727; this phosphorylation is required for RECQL5-mediated disruption of RAD51 filaments on stalled replication forks. {ECO:0000269|PubMed:28575661}.
uniprot
proteins
protein_family
Helicase family
uniprot
proteins
protein_family
RecQ subfamily
uniprot
proteins
pubmed
10471747
uniprot
proteins
pubmed
10710432
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20231364
uniprot
proteins
pubmed
20348101
uniprot
proteins
pubmed
20643585
uniprot
proteins
pubmed
22013166
uniprot
proteins
pubmed
22973052
uniprot
proteins
pubmed
23180761
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23715498
uniprot
proteins
pubmed
23748380
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27502483
uniprot
proteins
pubmed
28100692
uniprot
proteins
pubmed
28575661
uniprot
proteins
pubmed
9878247
uniprot
proteins
sequence_length
991
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform Beta]: Nucleus, nucleoplasm {ECO:0000269|PubMed:10710432, ECO:0000269|PubMed:23180761, ECO:0000269|PubMed:23715498}. Nucleus {ECO:0000269|PubMed:23180761}. Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks. Re-localizes from the nucleolus into the nucleus after replicative stress and significantly associates with WRN during S-phase (PubMed:23180761). {ECO:0000269|PubMed:20643585, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22973052, ECO:0000269|PubMed:23180761, ECO:0000269|PubMed:23715498}.; SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm {ECO:0000269|PubMed:10710432}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm {ECO:0000269|PubMed:10710432}.
uniprot
proteins