O94762 · RECQ5_HUMAN
- ProteinATP-dependent DNA helicase Q5
- GeneRECQL5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids991 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Associates also 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).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | ATP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 28 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 30 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 34 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 53 | ATP (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 55 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 56 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 57 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 58 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 59 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 411 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 427 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 431 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 434 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent DNA helicase Q5
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO94762
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform Beta
Isoform Alpha
Isoform Gamma
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 157 | Abolishes helicase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 165 | Loss of helicase activity, reduced DNA-binding (in a residue 11-526 fragment). | ||||
Sequence: W → A | ||||||
Mutagenesis | 167 | Loss of helicase activity, reduced DNA-binding (in a residue 11-526 fragment). | ||||
Sequence: H → A | ||||||
Mutagenesis | 345 | Loss of helicase activity, reduced DNA-binding (in a residue 11-526 fragment). | ||||
Sequence: Q → A | ||||||
Mutagenesis | 352 | Loss of helicase activity (in a residue 11-526 fragment). | ||||
Sequence: R → G | ||||||
Natural variant | VAR_024272 | 480 | in dbSNP:rs820196 | |||
Sequence: D → G | ||||||
Mutagenesis | 504 | Abolishes interaction with POLR2A. | ||||
Sequence: W → A | ||||||
Mutagenesis | 508 | Abolishes interaction with POLR2A. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 515 | Abolishes interaction with POLR2A. | ||||
Sequence: R → E | ||||||
Mutagenesis | 516 | Abolishes interaction with POLR2A. | ||||
Sequence: K → E | ||||||
Mutagenesis | 550 | Impairs protein folding and abolishes interaction with POLR2A. | ||||
Sequence: R → A | ||||||
Mutagenesis | 552 | Abolishes interaction with POLR2A. | ||||
Sequence: H → A | ||||||
Mutagenesis | 556 | Abolishes interaction with POLR2A. | ||||
Sequence: L → E | ||||||
Mutagenesis | 584 | Abolishes interaction with POLR2A. | ||||
Sequence: E → A or D | ||||||
Mutagenesis | 597 | Reduces interaction with POLR2A. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 598 | Abolishes interaction with POLR2A. | ||||
Sequence: K → E | ||||||
Mutagenesis | 602 | Abolishes interaction with POLR2A. | ||||
Sequence: L → D or E | ||||||
Mutagenesis | 603 | Abolishes interaction with POLR2A. | ||||
Sequence: K → E | ||||||
Natural variant | VAR_051733 | 628 | in dbSNP:rs35566780 | |||
Sequence: S → N | ||||||
Mutagenesis | 666 | Abolishes interaction with RAD51. | ||||
Sequence: F → A | ||||||
Mutagenesis | 727 | Loss of phosphorylation in early mitosis. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,219 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000205055 | 1-991 | UniProt | ATP-dependent DNA helicase Q5 | |||
Sequence: MSSHHTTFPFDPERRVRSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCFRANLFYDVQFKELISDPYGNLKDFCLKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKASDKATIMAFDALVTFCEELGCRHAAIAKYFGDALPACAKGCDHCQNPTAVRRRLEALERSSSWSKTCIGPSQGNGFDPELYEGGRKGYGDFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMQLRKGKDPKIEEFVPPDENCPLKEASSRRIPRLTVKAREHCLRLLEEALSSNRQSTRTADEADLRAKAVELEHETFRNAKVANLYKASVLKKVADIHRASKDGQPYDMGGSAKSCSAQAEPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSIARFFCRRVESPALLASAPEAEGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPSTCPPRDQGTPEVQPTPAKDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTAQDPFQLSAPGVSLKEAANVVVKCLTPFYKEGKFASKELFKGFARHLSHLLTQKTSPGRSVKEEAQNLIRHFFHGRARCESEADWHGLCGPQR | |||||||
Modified residue (large scale data) | 484 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 488 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 488 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 491 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 491 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 723 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 727 | UniProt | Phosphoserine; by CDK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 727 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 774 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 805 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 815 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 815 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 839 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 839 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 845 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 858 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 954 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Isoform beta interacts with RNA polymerase II subunit POLR2A (PubMed:20231364, PubMed:20348101, PubMed:23748380).
Identified in a complex with the RNA polymerase II core bound to DNA (PubMed:20231364, PubMed:20348101).
Interacts (via C-terminus) with POLR1A (PubMed:27502483).
Isoform beta interacts with RAD51 (PubMed:20231364, PubMed:20348101).
Interacts with WRN; this interaction stimulates WRN helicase activity on DNA fork duplexes (PubMed:23180761).
Interacts with MUS1; this interaction promotes MUS81-dependent mitotic DNA synthesis (PubMed:28575661).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O94762-1 | POLR2A P24928 | 8 | EBI-15710057, EBI-295301 | |
BINARY | O94762-1 | RECQL5 O94762-1 | 2 | EBI-15710057, EBI-15710057 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-213 | Helicase ATP-binding | ||||
Sequence: MAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPV | ||||||
Motif | 157-160 | DEAH box | ||||
Sequence: DEAH | ||||||
Domain | 241-403 | Helicase C-terminal | ||||
Sequence: NLKDFCLKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKASDKATIMAFDALV | ||||||
Region | 438-609 | Plays an important role in affinity and substrate choice in DNA binding | ||||
Sequence: TAVRRRLEALERSSSWSKTCIGPSQGNGFDPELYEGGRKGYGDFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMQLRKGKDPKIEEFVPPDENCPLKEASSRRIPRLTVKAREHCLRLLEEALSSNRQSTRTADEADLRAKAVELEHETFRNAKVANLYKASVLKKVADIH | ||||||
Region | 490-620 | Interaction with POLR2A | ||||
Sequence: GSGDEGRDEAHKREWNLFYQKQMQLRKGKDPKIEEFVPPDENCPLKEASSRRIPRLTVKAREHCLRLLEEALSSNRQSTRTADEADLRAKAVELEHETFRNAKVANLYKASVLKKVADIHRASKDGQPYDM | ||||||
Region | 613-645 | Disordered | ||||
Sequence: KDGQPYDMGGSAKSCSAQAEPPEPNEYDIPPAS | ||||||
Region | 652-725 | Interaction with RAD51 | ||||
Sequence: PKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPGGSAHYGG | ||||||
Compositional bias | 681-698 | Basic and acidic residues | ||||
Sequence: QAPQPERGGEHEPPSRPC | ||||||
Region | 681-761 | Disordered | ||||
Sequence: QAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDS | ||||||
Compositional bias | 732-746 | Polar residues | ||||
Sequence: AKSSSGGSSLAKGRA | ||||||
Region | 780-901 | Disordered | ||||
Sequence: SAPEAEGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPSTCPPRDQGTPEVQPTPAKDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTAQD | ||||||
Compositional bias | 885-901 | Polar residues | ||||
Sequence: GSVSASEQGTLNPTAQD |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O94762-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameBeta
- Length991
- Mass (Da)108,858
- Last updated2002-08-30 v2
- Checksum983668133DED865A
O94762-2
- NameAlpha
- SynonymsRecQ5b
- Differences from canonical
- 411-991: Missing
O94762-3
- NameGamma
- SynonymsRecQ5a
O94762-4
- Name4
- Differences from canonical
- 43-69: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_057431 | 43-69 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_005569 | 411-435 | in isoform Gamma | |||
Sequence: CRHAAIAKYFGDALPACAKGCDHCQ → RWGRGHGKSLRAAWCSQVVSRHAEL | ||||||
Alternative sequence | VSP_005568 | 411-991 | in isoform Alpha | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_005570 | 436-991 | in isoform Gamma | |||
Sequence: Missing | ||||||
Compositional bias | 681-698 | Basic and acidic residues | ||||
Sequence: QAPQPERGGEHEPPSRPC | ||||||
Compositional bias | 732-746 | Polar residues | ||||
Sequence: AKSSSGGSSLAKGRA | ||||||
Compositional bias | 885-901 | Polar residues | ||||
Sequence: GSVSASEQGTLNPTAQD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB006533 EMBL· GenBank· DDBJ | BAA74454.1 EMBL· GenBank· DDBJ | mRNA | ||
AF135183 EMBL· GenBank· DDBJ | AAD43061.1 EMBL· GenBank· DDBJ | mRNA | ||
AF135183 EMBL· GenBank· DDBJ | AAD43062.1 EMBL· GenBank· DDBJ | mRNA | ||
AB042823 EMBL· GenBank· DDBJ | BAA95952.1 EMBL· GenBank· DDBJ | mRNA | ||
AB042824 EMBL· GenBank· DDBJ | BAA95953.1 EMBL· GenBank· DDBJ | mRNA | ||
AB042825 EMBL· GenBank· DDBJ | BAA95954.1 EMBL· GenBank· DDBJ | mRNA | ||
AC087749 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471099 EMBL· GenBank· DDBJ | EAW89292.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC016911 EMBL· GenBank· DDBJ | AAH16911.1 EMBL· GenBank· DDBJ | mRNA | ||
BC063440 EMBL· GenBank· DDBJ | AAH63440.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136869 EMBL· GenBank· DDBJ | CAB66803.3 EMBL· GenBank· DDBJ | mRNA |