ID FBH1_HUMAN Reviewed; 1043 AA. AC Q8NFZ0; Q5JVB0; Q5JVB1; Q7Z4Q6; Q7Z4R0; Q8N1P5; Q8N586; Q96E82; Q96K67; AC Q96SW7; Q9UFB2; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2004, sequence version 2. DT 27-MAR-2024, entry version 181. DE RecName: Full=F-box DNA helicase 1 {ECO:0000303|PubMed:11956208}; DE Short=hFBH1 {ECO:0000303|PubMed:11956208, ECO:0000303|PubMed:23393192}; DE EC=5.6.2.4 {ECO:0000269|PubMed:11956208, ECO:0000269|PubMed:23393192}; DE AltName: Full=DNA 3'-5' helicase 1 {ECO:0000305}; DE AltName: Full=F-box only protein 18 {ECO:0000312|HGNC:HGNC:13620}; GN Name=FBH1 {ECO:0000312|HGNC:HGNC:13620}; Synonyms=FBX18, FBXO18; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY, RP INTERACTION WITH SKP1, AND IDENTIFICATION IN SCF COMPLEX. RX PubMed=11956208; DOI=10.1074/jbc.m201612200; RA Kim J., Kim J.-H., Lee S.-H., Kim D.-H., Kang H.-Y., Bae S.-H., Pan Z.-Q., RA Seo Y.-S.; RT "The novel human DNA helicase hFBH1 is an F-box protein."; RL J. Biol. Chem. 277:24530-24537(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Choriocarcinoma, and Testis; RA Zan Q., Guo J.H., Yu L.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Mammary gland, Testis carcinoma, and Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Pancreas, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 763-1043 (ISOFORMS 1/2). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP FUNCTION. RX PubMed=17724085; DOI=10.1128/mcb.00963-07; RA Chiolo I., Saponaro M., Baryshnikova A., Kim J.H., Seo Y.S., Liberi G.; RT "The human F-Box DNA helicase FBH1 faces Saccharomyces cerevisiae Srs2 and RT postreplication repair pathway roles."; RL Mol. Cell. Biol. 27:7439-7450(2007). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN SCF COMPLEX, AND RP MUTAGENESIS OF 227-LEU-PRO-228 AND ASP-647. RX PubMed=19736316; DOI=10.1083/jcb.200812138; RA Fugger K., Mistrik M., Danielsen J.R., Dinant C., Falck J., Bartek J., RA Lukas J., Mailand N.; RT "Human Fbh1 helicase contributes to genome maintenance via pro- and anti- RT recombinase activities."; RL J. Cell Biol. 186:655-663(2009). RN [10] RP POSSIBLE INVOLVEMENT IN MELANOMAS. RX PubMed=23466708; DOI=10.4161/cc.24165; RA Jeong Y.T., Cermak L., Guijarro M.V., Hernando E., Pagano M.; RT "FBH1 protects melanocytes from transformation and is deregulated in RT melanomas."; RL Cell Cycle 12:1128-1132(2013). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN SCF COMPLEX, INTERACTION RP WITH RPA2, AND MUTAGENESIS OF SER-56; 227-LEU-PRO-228; SER-583 AND ASP-647. RX PubMed=23319600; DOI=10.1083/jcb.201209002; RA Jeong Y.T., Rossi M., Cermak L., Saraf A., Florens L., Washburn M.P., RA Sung P., Schildkraut C.L., Schildkraut C., Pagano M.; RT "FBH1 promotes DNA double-strand breakage and apoptosis in response to DNA RT replication stress."; RL J. Cell Biol. 200:141-149(2013). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP FUNCTION. RX PubMed=23361013; DOI=10.1038/ncomms2395; RA Fugger K., Chu W.K., Haahr P., Kousholt A.N., Beck H., Payne M.J., RA Hanada K., Hickson I.D., Sorensen C.S.; RT "FBH1 co-operates with MUS81 in inducing DNA double-strand breaks and cell RT death following replication stress."; RL Nat. Commun. 4:1423-1423(2013). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RAD51, AND UBIQUITINATION. RX PubMed=23393192; DOI=10.1093/nar/gkt056; RA Masuda-Ozawa T., Hoang T., Seo Y.S., Chen L.F., Spies M.; RT "Single-molecule sorting reveals how ubiquitylation affects substrate RT recognition and activities of FBH1 helicase."; RL Nucleic Acids Res. 41:3576-3587(2013). RN [15] RP UBIQUITINATION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH PCNA, AND RP MUTAGENESIS OF 60-ILE--PHE-64; 63-PHE-PHE-64 AND 807-LYS--ILE-809. RX PubMed=23677613; DOI=10.1093/nar/gkt397; RA Bacquin A., Pouvelle C., Siaud N., Perderiset M., Salome-Desnoulez S., RA Tellier-Lebegue C., Lopez B., Charbonnier J.B., Kannouche P.L.; RT "The helicase FBH1 is tightly regulated by PCNA via CRL4(Cdt2)-mediated RT proteolysis in human cells."; RL Nucleic Acids Res. 41:6501-6513(2013). RN [16] RP FUNCTION, AND MUTAGENESIS OF ASP-647. RX PubMed=25772361; DOI=10.1016/j.celrep.2015.02.028; RA Fugger K., Mistrik M., Neelsen K.J., Yao Q., Zellweger R., Kousholt A.N., RA Haahr P., Chu W.K., Bartek J., Lopes M., Hickson I.D., Soerensen C.S.; RT "FBH1 catalyzes regression of stalled replication forks."; RL Cell Rep. 10:1749-1757(2015). RN [17] RP FUNCTION, PATHWAY, AND IDENTIFICATION IN SCF COMPLEX. RX PubMed=25585578; DOI=10.1038/ncomms6931; RA Chu W.K., Payne M.J., Beli P., Hanada K., Choudhary C., Hickson I.D.; RT "FBH1 influences DNA replication fork stability and homologous RT recombination through ubiquitylation of RAD51."; RL Nat. Commun. 6:5931-5931(2015). CC -!- FUNCTION: 3'-5' DNA helicase and substrate-recognition component of the CC SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response CC to stalled/damaged replication forks (PubMed:11956208, CC PubMed:23393192). Involved in genome maintenance by acting as an anti- CC recombinogenic helicase and preventing extensive strand exchange during CC homologous recombination: promotes RAD51 filament dissolution from CC stalled forks, thereby inhibiting homologous recombination and CC preventing excessive recombination (PubMed:17724085, PubMed:19736316). CC Also promotes cell death and DNA double-strand breakage in response to CC replication stress: together with MUS81, promotes the endonucleolytic CC DNA cleavage following prolonged replication stress via its helicase CC activity, possibly to eliminate cells with excessive replication stress CC (PubMed:23319600, PubMed:23361013). Plays a major role in remodeling of CC stalled DNA forks by catalyzing fork regression, in which the fork CC reverses and the two nascent DNA strands anneal (PubMed:25772361). In CC addition to the helicase activity, also acts as the substrate- CC recognition component of the SCF(FBH1) E3 ubiquitin ligase complex, a CC complex that mediates ubiquitination of RAD51, leading to regulate CC RAD51 subcellular location (PubMed:25585578). CC {ECO:0000269|PubMed:11956208, ECO:0000269|PubMed:17724085, CC ECO:0000269|PubMed:19736316, ECO:0000269|PubMed:23319600, CC ECO:0000269|PubMed:23361013, ECO:0000269|PubMed:25585578, CC ECO:0000269|PubMed:25772361}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by CC translocating in the 3'-5' direction.; EC=5.6.2.4; CC Evidence={ECO:0000269|PubMed:11956208, ECO:0000269|PubMed:23393192}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; CC Evidence={ECO:0000269|PubMed:11956208, ECO:0000269|PubMed:23393192}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:25585578}. CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase CC complex SCF(FBH1) composed of CUL1, SKP1, RBX1 and FBH1 CC (PubMed:11956208, PubMed:19736316, PubMed:23319600). Interacts with CC RAD51 (PubMed:23393192). Interacts with RPA2 (PubMed:23319600). CC Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA CC (PubMed:23677613). {ECO:0000269|PubMed:11956208, CC ECO:0000269|PubMed:19736316, ECO:0000269|PubMed:23319600, CC ECO:0000269|PubMed:23393192, ECO:0000269|PubMed:23677613}. CC -!- INTERACTION: CC Q8NFZ0; O00213-2: APBB1; NbExp=3; IntAct=EBI-724767, EBI-13307975; CC Q8NFZ0; P28799: GRN; NbExp=3; IntAct=EBI-724767, EBI-747754; CC Q8NFZ0; P42858: HTT; NbExp=6; IntAct=EBI-724767, EBI-466029; CC Q8NFZ0; P12931: SRC; NbExp=4; IntAct=EBI-724767, EBI-621482; CC Q8NFZ0; O76024: WFS1; NbExp=3; IntAct=EBI-724767, EBI-720609; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19736316, CC ECO:0000269|PubMed:23677613}. Chromosome {ECO:0000269|PubMed:19736316, CC ECO:0000269|PubMed:23319600, ECO:0000269|PubMed:23677613}. CC Note=Accumulates at sites of DNA damage or replication stress CC (PubMed:19736316, PubMed:23677613). PCNA is required for localization CC to DNA damage sites (PubMed:23677613). Localizes to the nucleoplasm in CC absence of DNA damage (PubMed:23677613). {ECO:0000269|PubMed:19736316, CC ECO:0000269|PubMed:23677613}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8NFZ0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NFZ0-2; Sequence=VSP_037942; CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA. CC {ECO:0000269|PubMed:23677613}. CC -!- PTM: Ubiquitinated (PubMed:23393192, PubMed:23677613). Ubiquitination CC by the DCX(DTL) complex, also named CRL4(CDT2), leading to its CC degradation: ubiquitination takes place after its localization to DNA CC damage sites, possibly to facilitate the translesion synthesis (TLS) CC pathway (PubMed:23677613). {ECO:0000269|PubMed:23393192, CC ECO:0000269|PubMed:23677613}. CC -!- DISEASE: Note=Defects in FBH1 are frequently observed in melanomas, CC resulting in increased survival in response to replicative stress. Its CC inactivation may play a role in oncogenic transformation. CC {ECO:0000269|PubMed:23466708}. CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAM73631.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB55073.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB55154.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF380349; AAM73631.1; ALT_INIT; mRNA. DR EMBL; AF454502; AAP97700.1; -; mRNA. DR EMBL; AF456237; AAP97705.1; -; mRNA. DR EMBL; AK027381; BAB55073.1; ALT_INIT; mRNA. DR EMBL; AK027496; BAB55154.1; ALT_INIT; mRNA. DR EMBL; AK095343; BAC04535.1; -; mRNA. DR EMBL; AL137186; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471072; EAW86426.1; -; Genomic_DNA. DR EMBL; BC012762; AAH12762.2; -; mRNA. DR EMBL; BC032674; AAH32674.2; -; mRNA. DR EMBL; BC113377; AAI13378.1; -; mRNA. DR EMBL; AL133069; CAB61392.1; -; mRNA. DR CCDS; CCDS7072.1; -. [Q8NFZ0-1] DR CCDS; CCDS7073.1; -. [Q8NFZ0-2] DR PIR; T42669; T42669. DR RefSeq; NP_001245381.1; NM_001258452.1. DR RefSeq; NP_001245382.1; NM_001258453.1. DR RefSeq; NP_116196.3; NM_032807.4. [Q8NFZ0-2] DR RefSeq; NP_835363.1; NM_178150.2. [Q8NFZ0-1] DR RefSeq; XP_011518050.1; XM_011519748.2. DR PDB; 8F5Q; X-ray; 1.90 A; B/D/F=56-64. DR PDBsum; 8F5Q; -. DR AlphaFoldDB; Q8NFZ0; -. DR SMR; Q8NFZ0; -. DR BioGRID; 124333; 29. DR ComplexPortal; CPX-7928; SCF E3 ubiquitin ligase complex, FBH1 variant. DR CORUM; Q8NFZ0; -. DR IntAct; Q8NFZ0; 20. DR MINT; Q8NFZ0; -. DR STRING; 9606.ENSP00000369335; -. DR GlyGen; Q8NFZ0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NFZ0; -. DR PhosphoSitePlus; Q8NFZ0; -. DR BioMuta; FBXO18; -. DR DMDM; 45476952; -. DR EPD; Q8NFZ0; -. DR jPOST; Q8NFZ0; -. DR MassIVE; Q8NFZ0; -. DR MaxQB; Q8NFZ0; -. DR PaxDb; 9606-ENSP00000369335; -. DR PeptideAtlas; Q8NFZ0; -. DR ProteomicsDB; 73393; -. [Q8NFZ0-1] DR ProteomicsDB; 73394; -. [Q8NFZ0-2] DR Pumba; Q8NFZ0; -. DR Antibodypedia; 1236; 128 antibodies from 25 providers. DR DNASU; 84893; -. DR Ensembl; ENST00000362091.9; ENSP00000355415.4; ENSG00000134452.20. [Q8NFZ0-1] DR Ensembl; ENST00000379999.6; ENSP00000369335.5; ENSG00000134452.20. [Q8NFZ0-2] DR GeneID; 84893; -. DR KEGG; hsa:84893; -. DR MANE-Select; ENST00000362091.9; ENSP00000355415.4; NM_178150.3; NP_835363.1. DR UCSC; uc001iis.5; human. [Q8NFZ0-1] DR AGR; HGNC:13620; -. DR CTD; 84893; -. DR DisGeNET; 84893; -. DR GeneCards; FBH1; -. DR HGNC; HGNC:13620; FBH1. DR HPA; ENSG00000134452; Low tissue specificity. DR MIM; 607222; gene. DR neXtProt; NX_Q8NFZ0; -. DR OpenTargets; ENSG00000134452; -. DR PharmGKB; PA134948258; -. DR VEuPathDB; HostDB:ENSG00000134452; -. DR eggNOG; KOG2108; Eukaryota. DR GeneTree; ENSGT00390000011669; -. DR InParanoid; Q8NFZ0; -. DR OrthoDB; 5490899at2759; -. DR PhylomeDB; Q8NFZ0; -. DR TreeFam; TF329020; -. DR PathwayCommons; Q8NFZ0; -. DR SignaLink; Q8NFZ0; -. DR SIGNOR; Q8NFZ0; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 84893; 9 hits in 1198 CRISPR screens. DR ChiTaRS; FBXO18; human. DR GenomeRNAi; 84893; -. DR Pharos; Q8NFZ0; Tbio. DR PRO; PR:Q8NFZ0; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q8NFZ0; Protein. DR Bgee; ENSG00000134452; Expressed in apex of heart and 177 other cell types or tissues. DR ExpressionAtlas; Q8NFZ0; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB. DR GO; GO:0015616; F:DNA translocase activity; IDA:MGI. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0006308; P:DNA catabolic process; IMP:MGI. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB. DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB. DR GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; IMP:MGI. DR CDD; cd22095; F-box_FBXO18; 1. DR CDD; cd18786; SF1_C; 1. DR Gene3D; 1.20.1280.50; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR014017; DNA_helicase_UvrD-like_C. DR InterPro; IPR000212; DNA_helicase_UvrD/REP. DR InterPro; IPR036047; F-box-like_dom_sf. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014016; UvrD-like_ATP-bd. DR PANTHER; PTHR11070:SF30; F-BOX DNA HELICASE 1; 1. DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1. DR Pfam; PF12937; F-box-like; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF81383; F-box domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50181; FBOX; 1. DR Genevisible; Q8NFZ0; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Chromosome; DNA damage; KW DNA repair; DNA-binding; Helicase; Hydrolase; Isomerase; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..1043 FT /note="F-box DNA helicase 1" FT /id="PRO_0000119901" FT DOMAIN 138..184 FT /note="F-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080" FT DOMAIN 442..705 FT /note="UvrD-like helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560" FT REGION 30..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 101..191 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 57..64 FT /note="PIP-box" FT /evidence="ECO:0000269|PubMed:23677613" FT MOTIF 807..811 FT /note="APIM motif" FT /evidence="ECO:0000269|PubMed:23677613" FT COMPBIAS 143..174 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 463..470 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560" FT MOD_RES 124 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MSYEVTSGCHWTCQVPESCDNGLHCAGPLGHLHRRCQRTSAHLLVFT FT EHAEM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11956208" FT /id="VSP_037942" FT MUTAGEN 56 FT /note="S->A: No effect; when associated with A-583." FT /evidence="ECO:0000269|PubMed:23319600" FT MUTAGEN 60..64 FT /note="IPEFF->APAAA: In PIPdeg3A; reduced ubiquitination." FT /evidence="ECO:0000269|PubMed:23677613" FT MUTAGEN 63..64 FT /note="FF->AA: Impaired localization to DNA damage sites in FT response to UV irradiation." FT /evidence="ECO:0000269|PubMed:23677613" FT MUTAGEN 227..228 FT /note="LP->AA: Impairs formation of the SCF(FBH1) complex FT and impairs accumulation on single-stranded DNA." FT /evidence="ECO:0000269|PubMed:19736316, FT ECO:0000269|PubMed:23319600" FT MUTAGEN 583 FT /note="S->A: No effect; when associated with A-56." FT /evidence="ECO:0000269|PubMed:23319600" FT MUTAGEN 647 FT /note="D->N: Abolishes helicase activity and prevents FT accumulation on single-stranded DNA." FT /evidence="ECO:0000269|PubMed:19736316, FT ECO:0000269|PubMed:23319600, ECO:0000269|PubMed:25772361" FT MUTAGEN 807..809 FT /note="KFI->AAA: Impaired localization to DNA damage sites FT in response to UV irradiation." FT /evidence="ECO:0000269|PubMed:23677613" FT CONFLICT 234 FT /note="W -> R (in Ref. 3; BAC04535)" FT /evidence="ECO:0000305" FT CONFLICT 339 FT /note="Missing (in Ref. 2; AAP97700 and 3; BAB55154)" FT /evidence="ECO:0000305" FT CONFLICT 425 FT /note="K -> N (in Ref. 2; AAP97705)" FT /evidence="ECO:0000305" FT CONFLICT 844 FT /note="N -> S (in Ref. 3; BAC04535)" FT /evidence="ECO:0000305" FT CONFLICT 984 FT /note="P -> L (in Ref. 2; AAP97700 and 3; BAB55154)" FT /evidence="ECO:0000305" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:8F5Q" SQ SEQUENCE 1043 AA; 117686 MW; E20EB343E9D05C4D CRC64; MRRFKRKHLT AIDCQHLARS HLAVTQPFGQ RWTNRDPNHG LYPKPRTKRG SRGQGSQRCI PEFFLAGKQP CTNDMAKSNS VGQDSCQDSE GDMIFPAESS CALPQEGSAG PGSPGSAPPS RKRSWSSEEE SNQATGTSRW DGVSKKAPRH HLSVPCTRPR EARQEAEDST SRLSAESGET DQDAGDVGPD PIPDSYYGLL GTLPCQEALS HICSLPSEVL RHVFAFLPVE DLYWNLSLVC HLWREIISDP LFIPWKKLYH RYLMNEEQAV SKVDGILSNC GIEKESDLCV LNLIRYTATT KCSPSVDPER VLWSLRDHPL LPEAEACVRQ HLPDLYAAAG GVNIWALVAA VVLLSSSVND IQRLLFCLRR PSSTVTMPDV TETLYCIAVL LYAMREKGIN ISNRIHYNIF YCLYLQENSC TQATKVKEEP SVWPGKKTIQ LTHEQQLILN HKMEPLQVVK IMAFAGTGKT STLVKYAEKW SQSRFLYVTF NKSIAKQAER VFPSNVICKT FHSMAYGHIG RKYQSKKKLN LFKLTPFMVN SVLAEGKGGF IRAKLVCKTL ENFFASADEE LTIDHVPIWC KNSQGQRVMV EQSEKLNGVL EASRLWDNMR KLGECTEEAH QMTHDGYLKL WQLSKPSLAS FDAIFVDEAQ DCTPAIMNIV LSQPCGKIFV GDPHQQIYTF RGAVNALFTV PHTHVFYLTQ SFRFGVEIAY VGATILDVCK RVRKKTLVGG NHQSGIRGDA KGQVALLSRT NANVFDEAVR VTEGEFPSRI HLIGGIKSFG LDRIIDIWIL LQPEEERRKQ NLVIKDKFIR RWVHKEGFSG FKRYVTAAED KELEAKIAVV EKYNIRIPEL VQRIEKCHIE DLDFAEYILG TVHKAKGLEF DTVHVLDDFV KVPCARHNLP QLPHFRVESF SEDEWNLLYV AVTRAKKRLI MTKSLENILT LAGEYFLQAE LTSNVLKTGV VRCCVGQCNN AIPVDTVLTM KKLPITYSNR KENKGGYLCH SCAEQRIGPL AFLTASPEQV RAMERTVENI VLPRHEALLF LVF //