Q8NFZ0 · FBH1_HUMAN
- ProteinF-box DNA helicase 1
- GeneFBH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1043 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in genome maintenance by acting as an anti-recombinogenic helicase and preventing extensive strand exchange during homologous recombination: promotes RAD51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination (PubMed:17724085, PubMed:19736316).
Also promotes cell death and DNA double-strand breakage in response to replication stress: together with MUS81, promotes the endonucleolytic DNA cleavage following prolonged replication stress via its helicase activity, possibly to eliminate cells with excessive replication stress (PubMed:23319600, PubMed:23361013).
Plays a major role in remodeling of stalled DNA forks by catalyzing fork regression, in which the fork reverses and the two nascent DNA strands anneal (PubMed:25772361).
In addition to the helicase activity, also acts as the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex, a complex that mediates ubiquitination of RAD51, leading to regulate RAD51 subcellular location (PubMed:25585578).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Pathway
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameF-box DNA helicase 1
- EC number
- Short nameshFBH1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8NFZ0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 56 | No effect; when associated with A-583. | ||||
Sequence: S → A | ||||||
Mutagenesis | 60-64 | In PIPdeg3A; reduced ubiquitination. | ||||
Sequence: IPEFF → APAAA | ||||||
Mutagenesis | 63-64 | Impaired localization to DNA damage sites in response to UV irradiation. | ||||
Sequence: FF → AA | ||||||
Mutagenesis | 227-228 | Impairs formation of the SCF(FBH1) complex and impairs accumulation on single-stranded DNA. | ||||
Sequence: LP → AA | ||||||
Mutagenesis | 583 | No effect; when associated with A-56. | ||||
Sequence: S → A | ||||||
Mutagenesis | 647 | Abolishes helicase activity and prevents accumulation on single-stranded DNA. | ||||
Sequence: D → N | ||||||
Mutagenesis | 807-809 | Impaired localization to DNA damage sites in response to UV irradiation. | ||||
Sequence: KFI → AAA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,064 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, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000119901 | 1-1043 | UniProt | F-box DNA helicase 1 | |||
Sequence: MRRFKRKHLTAIDCQHLARSHLAVTQPFGQRWTNRDPNHGLYPKPRTKRGSRGQGSQRCIPEFFLAGKQPCTNDMAKSNSVGQDSCQDSEGDMIFPAESSCALPQEGSAGPGSPGSAPPSRKRSWSSEEESNQATGTSRWDGVSKKAPRHHLSVPCTRPREARQEAEDSTSRLSAESGETDQDAGDVGPDPIPDSYYGLLGTLPCQEALSHICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFIPWKKLYHRYLMNEEQAVSKVDGILSNCGIEKESDLCVLNLIRYTATTKCSPSVDPERVLWSLRDHPLLPEAEACVRQHLPDLYAAAGGVNIWALVAAVVLLSSSVNDIQRLLFCLRRPSSTVTMPDVTETLYCIAVLLYAMREKGINISNRIHYNIFYCLYLQENSCTQATKVKEEPSVWPGKKTIQLTHEQQLILNHKMEPLQVVKIMAFAGTGKTSTLVKYAEKWSQSRFLYVTFNKSIAKQAERVFPSNVICKTFHSMAYGHIGRKYQSKKKLNLFKLTPFMVNSVLAEGKGGFIRAKLVCKTLENFFASADEELTIDHVPIWCKNSQGQRVMVEQSEKLNGVLEASRLWDNMRKLGECTEEAHQMTHDGYLKLWQLSKPSLASFDAIFVDEAQDCTPAIMNIVLSQPCGKIFVGDPHQQIYTFRGAVNALFTVPHTHVFYLTQSFRFGVEIAYVGATILDVCKRVRKKTLVGGNHQSGIRGDAKGQVALLSRTNANVFDEAVRVTEGEFPSRIHLIGGIKSFGLDRIIDIWILLQPEEERRKQNLVIKDKFIRRWVHKEGFSGFKRYVTAAEDKELEAKIAVVEKYNIRIPELVQRIEKCHIEDLDFAEYILGTVHKAKGLEFDTVHVLDDFVKVPCARHNLPQLPHFRVESFSEDEWNLLYVAVTRAKKRLIMTKSLENILTLAGEYFLQAELTSNVLKTGVVRCCVGQCNNAIPVDTVLTMKKLPITYSNRKENKGGYLCHSCAEQRIGPLAFLTASPEQVRAMERTVENIVLPRHEALLFLVF | |||||||
Modified residue | 124 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 126 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 127 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Ubiquitination by the DCX(DTL) complex, also named CRL4(CDT2), leading to its degradation: ubiquitination takes place after its localization to DNA damage sites, possibly to facilitate the translesion synthesis (TLS) pathway (PubMed:23677613).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with RAD51 (PubMed:23393192).
Interacts with RPA2 (PubMed:23319600).
Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA (PubMed:23677613).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8NFZ0 | APBB1 O00213-2 | 3 | EBI-724767, EBI-13307975 | |
BINARY | Q8NFZ0 | GRN P28799 | 3 | EBI-724767, EBI-747754 | |
BINARY | Q8NFZ0 | HTT P42858 | 6 | EBI-724767, EBI-466029 | |
BINARY | Q8NFZ0 | SRC P12931 | 4 | EBI-724767, EBI-621482 | |
BINARY | Q8NFZ0 | WFS1 O76024 | 3 | EBI-724767, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 30-56 | Disordered | ||||
Sequence: QRWTNRDPNHGLYPKPRTKRGSRGQGS | ||||||
Motif | 57-64 | PIP-box | ||||
Sequence: QRCIPEFF | ||||||
Region | 101-191 | Disordered | ||||
Sequence: CALPQEGSAGPGSPGSAPPSRKRSWSSEEESNQATGTSRWDGVSKKAPRHHLSVPCTRPREARQEAEDSTSRLSAESGETDQDAGDVGPDP | ||||||
Domain | 138-184 | F-box | ||||
Sequence: SRWDGVSKKAPRHHLSVPCTRPREARQEAEDSTSRLSAESGETDQDA | ||||||
Compositional bias | 143-174 | Basic and acidic residues | ||||
Sequence: VSKKAPRHHLSVPCTRPREARQEAEDSTSRLS | ||||||
Domain | 442-705 | UvrD-like helicase ATP-binding | ||||
Sequence: THEQQLILNHKMEPLQVVKIMAFAGTGKTSTLVKYAEKWSQSRFLYVTFNKSIAKQAERVFPSNVICKTFHSMAYGHIGRKYQSKKKLNLFKLTPFMVNSVLAEGKGGFIRAKLVCKTLENFFASADEELTIDHVPIWCKNSQGQRVMVEQSEKLNGVLEASRLWDNMRKLGECTEEAHQMTHDGYLKLWQLSKPSLASFDAIFVDEAQDCTPAIMNIVLSQPCGKIFVGDPHQQIYTFRGAVNALFTVPHTHVFYLTQSFRFG | ||||||
Motif | 807-811 | APIM motif | ||||
Sequence: KFIRR |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8NFZ0-1
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.
- Name1
- Length1,043
- Mass (Da)117,686
- Last updated2004-03-15 v2
- ChecksumE20EB343E9D05C4D
Q8NFZ0-2
- Name2
- Differences from canonical
- 1-1: M → MSYEVTSGCHWTCQVPESCDNGLHCAGPLGHLHRRCQRTSAHLLVFTEHAEM
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6UZG9 | F6UZG9_HUMAN | FBH1 | 986 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037942 | 1 | in isoform 2 | |||
Sequence: M → MSYEVTSGCHWTCQVPESCDNGLHCAGPLGHLHRRCQRTSAHLLVFTEHAEM | ||||||
Compositional bias | 143-174 | Basic and acidic residues | ||||
Sequence: VSKKAPRHHLSVPCTRPREARQEAEDSTSRLS | ||||||
Sequence conflict | 234 | in Ref. 3; BAC04535 | ||||
Sequence: W → R | ||||||
Sequence conflict | 339 | in Ref. 2; AAP97700 and 3; BAB55154 | ||||
Sequence: Missing | ||||||
Sequence conflict | 425 | in Ref. 2; AAP97705 | ||||
Sequence: K → N | ||||||
Sequence conflict | 844 | in Ref. 3; BAC04535 | ||||
Sequence: N → S | ||||||
Sequence conflict | 984 | in Ref. 2; AAP97700 and 3; BAB55154 | ||||
Sequence: P → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF380349 EMBL· GenBank· DDBJ | AAM73631.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF454502 EMBL· GenBank· DDBJ | AAP97700.1 EMBL· GenBank· DDBJ | mRNA | ||
AF456237 EMBL· GenBank· DDBJ | AAP97705.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027381 EMBL· GenBank· DDBJ | BAB55073.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK027496 EMBL· GenBank· DDBJ | BAB55154.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK095343 EMBL· GenBank· DDBJ | BAC04535.1 EMBL· GenBank· DDBJ | mRNA | ||
AL137186 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471072 EMBL· GenBank· DDBJ | EAW86426.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC012762 EMBL· GenBank· DDBJ | AAH12762.2 EMBL· GenBank· DDBJ | mRNA | ||
BC032674 EMBL· GenBank· DDBJ | AAH32674.2 EMBL· GenBank· DDBJ | mRNA | ||
BC113377 EMBL· GenBank· DDBJ | AAI13378.1 EMBL· GenBank· DDBJ | mRNA | ||
AL133069 EMBL· GenBank· DDBJ | CAB61392.1 EMBL· GenBank· DDBJ | mRNA |