ID FIGL1_HUMAN Reviewed; 674 AA. AC Q6PIW4; D3DVM6; Q86V18; Q8ND59; Q9H8P1; Q9H917; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 29-SEP-2021, entry version 159. DE RecName: Full=Fidgetin-like protein 1; DE EC=3.6.4.-; GN Name=FIGNL1; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ovary; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [6] 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 (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-137. RC TISSUE=Pancreas, and Skin; 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-339, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, 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 [12] RP FUNCTION, INTERACTION WITH RAD51 AND SPIDR, SUBCELLULAR LOCATION, RP MUTAGENESIS OF PHE-295; PHE-340; LYS-447 AND ASP-500, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=23754376; DOI=10.1073/pnas.1220662110; RA Yuan J., Chen J.; RT "FIGNL1-containing protein complex is required for efficient homologous RT recombination repair."; RL Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-225, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 341-674 IN COMPLEX WITH ADP. RG Structural genomics consortium (SGC); RT "Human fidgetin-like protein 1."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Involved in DNA double-strand break (DBS) repair via CC homologous recombination (HR). Recruited at DSB sites independently of CC BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May CC regulate osteoblast proliferation and differentiation CC (PubMed:23754376). May play a role in the control of male meiosis CC dynamic (By similarity). {ECO:0000250|UniProtKB:Q8BPY9, CC ECO:0000269|PubMed:23754376}. 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Hexamer (By similarity). Interacts (via N-terminal one-half CC region) with RAD51; the interaction is direct. Interacts (via N- CC terminal one-half region) with SPIDR (via the C-terminal region); the CC interaction is direct. {ECO:0000250, ECO:0000269|PubMed:23754376, CC ECO:0000269|Ref.14}. CC -!- INTERACTION: CC Q6PIW4; Q96CN9: GCC1; NbExp=3; IntAct=EBI-8468390, EBI-746252; CC Q6PIW4; O14713: ITGB1BP1; NbExp=3; IntAct=EBI-8468390, EBI-2127319; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23754376}. Cytoplasm CC {ECO:0000250|UniProtKB:Q8BPY9}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:Q8BPY9}. Note=Together with RAD51 and a subset CC of H2A histone proteins, redistributed in discrete nuclear DNA damage- CC induced foci after ionizing radiation (IR) treatment (PubMed:23754376). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6PIW4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6PIW4-2; Sequence=VSP_027937; CC -!- DOMAIN: The N-terminus is necessary for its recruitment to DNA damage CC sites. {ECO:0000269|PubMed:23754376}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB14567.1; Type=Erroneous initiation; 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; AK023142; BAB14426.1; -; mRNA. DR EMBL; AK023411; BAB14567.1; ALT_INIT; mRNA. DR EMBL; AL834387; CAD39050.1; -; mRNA. DR EMBL; AC018705; AAS01996.1; -; Genomic_DNA. DR EMBL; CH236955; EAL23899.1; -; Genomic_DNA. DR EMBL; CH471128; EAW60975.1; -; Genomic_DNA. DR EMBL; CH471128; EAW60976.1; -; Genomic_DNA. DR EMBL; BC051867; AAH51867.1; -; mRNA. DR CCDS; CCDS5510.1; -. [Q6PIW4-1] DR RefSeq; NP_001036227.1; NM_001042762.3. [Q6PIW4-1] DR RefSeq; NP_001274421.1; NM_001287492.2. [Q6PIW4-1] DR RefSeq; NP_001274422.1; NM_001287493.2. [Q6PIW4-1] DR RefSeq; NP_001274423.1; NM_001287494.2. [Q6PIW4-1] DR RefSeq; NP_001274424.1; NM_001287495.2. [Q6PIW4-1] DR RefSeq; NP_001274425.1; NM_001287496.2. [Q6PIW4-2] DR RefSeq; NP_001333487.1; NM_001346558.1. [Q6PIW4-2] DR RefSeq; NP_001333488.1; NM_001346559.1. [Q6PIW4-2] DR RefSeq; NP_001333489.1; NM_001346560.1. [Q6PIW4-1] DR RefSeq; NP_001333490.1; NM_001346561.1. [Q6PIW4-1] DR RefSeq; NP_001333491.1; NM_001346562.1. [Q6PIW4-1] DR RefSeq; NP_001333492.1; NM_001346563.1. [Q6PIW4-1] DR RefSeq; NP_001333493.1; NM_001346564.1. [Q6PIW4-1] DR RefSeq; NP_001333494.1; NM_001346565.1. [Q6PIW4-1] DR RefSeq; NP_071399.2; NM_022116.5. [Q6PIW4-1] DR RefSeq; XP_011513772.1; XM_011515470.2. [Q6PIW4-1] DR RefSeq; XP_016867990.1; XM_017012501.1. [Q6PIW4-1] DR PDB; 3D8B; X-ray; 2.00 A; A/B=341-674. DR PDBsum; 3D8B; -. DR SMR; Q6PIW4; -. DR BioGRID; 122026; 41. DR IntAct; Q6PIW4; 34. DR MINT; Q6PIW4; -. DR STRING; 9606.ENSP00000410811; -. DR GlyGen; Q6PIW4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6PIW4; -. DR MetOSite; Q6PIW4; -. DR PhosphoSitePlus; Q6PIW4; -. DR BioMuta; FIGNL1; -. DR DMDM; 158563967; -. DR CPTAC; CPTAC-1608; -. DR EPD; Q6PIW4; -. DR jPOST; Q6PIW4; -. DR MassIVE; Q6PIW4; -. DR MaxQB; Q6PIW4; -. DR PaxDb; Q6PIW4; -. DR PeptideAtlas; Q6PIW4; -. DR PRIDE; Q6PIW4; -. DR ProteomicsDB; 67182; -. [Q6PIW4-1] DR ProteomicsDB; 67183; -. [Q6PIW4-2] DR Antibodypedia; 27700; 142 antibodies. DR DNASU; 63979; -. DR Ensembl; ENST00000356889; ENSP00000349356; ENSG00000132436. [Q6PIW4-1] DR Ensembl; ENST00000395556; ENSP00000378924; ENSG00000132436. [Q6PIW4-1] DR Ensembl; ENST00000419119; ENSP00000410811; ENSG00000132436. [Q6PIW4-1] DR Ensembl; ENST00000433017; ENSP00000399997; ENSG00000132436. [Q6PIW4-1] DR Ensembl; ENST00000611938; ENSP00000484551; ENSG00000132436. [Q6PIW4-1] DR Ensembl; ENST00000613602; ENSP00000481751; ENSG00000132436. [Q6PIW4-1] DR Ensembl; ENST00000615084; ENSP00000483543; ENSG00000132436. [Q6PIW4-1] DR Ensembl; ENST00000617389; ENSP00000483126; ENSG00000132436. [Q6PIW4-1] DR GeneID; 63979; -. DR KEGG; hsa:63979; -. DR UCSC; uc003tpc.5; human. [Q6PIW4-1] DR CTD; 63979; -. DR DisGeNET; 63979; -. DR GeneCards; FIGNL1; -. DR HGNC; HGNC:13286; FIGNL1. DR HPA; ENSG00000132436; Low tissue specificity. DR MIM; 615383; gene. DR neXtProt; NX_Q6PIW4; -. DR OpenTargets; ENSG00000132436; -. DR PharmGKB; PA28148; -. DR VEuPathDB; HostDB:ENSG00000132436; -. DR eggNOG; KOG0740; Eukaryota. DR GeneTree; ENSGT00940000161552; -. DR HOGENOM; CLU_000688_21_10_1; -. DR InParanoid; Q6PIW4; -. DR OMA; YENWNRT; -. DR OrthoDB; 1176820at2759; -. DR PhylomeDB; Q6PIW4; -. DR TreeFam; TF105013; -. DR PathwayCommons; Q6PIW4; -. DR BioGRID-ORCS; 63979; 12 hits in 1021 CRISPR screens. DR EvolutionaryTrace; Q6PIW4; -. DR GenomeRNAi; 63979; -. DR Pharos; Q6PIW4; Tbio. DR PRO; PR:Q6PIW4; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q6PIW4; protein. DR Bgee; ENSG00000132436; Expressed in secondary oocyte and 203 other tissues. DR ExpressionAtlas; Q6PIW4; baseline and differential. DR Genevisible; Q6PIW4; HS. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0140603; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0016787; F:hydrolase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0008568; F:microtubule-severing ATPase activity; IBA:GO_Central. DR GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB. DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:UniProtKB. DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central. DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB. DR GO; GO:0033687; P:osteoblast proliferation; ISS:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015415; Vps4_C. DR Pfam; PF00004; AAA; 1. DR Pfam; PF09336; Vps4_C; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00674; AAA; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Hydrolase; Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..674 FT /note="Fidgetin-like protein 1" FT /id="PRO_0000302723" FT NP_BIND 444..449 FT /note="ATP" FT /evidence="ECO:0000305|Ref.14" FT REGION 157..179 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 295..344 FT /note="Necessary and sufficient for interaction with RAD51" FT /evidence="ECO:0000305|PubMed:23754376" FT COMPBIAS 164..178 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 404 FT /note="ATP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000305|Ref.14" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 339 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 225 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..111 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_027937" FT VARIANT 137 FT /note="V -> M (in dbSNP:rs10235371)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_034941" FT VARIANT 216 FT /note="H -> Y (in dbSNP:rs35929700)" FT /id="VAR_034942" FT MUTAGEN 295 FT /note="F->E: Reduces interaction with RAD51 and inhibits FT HR-mediated DNA repair. Strongly reduce, but does abolish, FT interaction with RAD51; when associated with E-340." FT /evidence="ECO:0000269|PubMed:23754376" FT MUTAGEN 340 FT /note="F->E: Reduces weakly interaction with RAD51. FT Strongly reduce, but does abolish, interaction with RAD51; FT when associated with E-295." FT /evidence="ECO:0000269|PubMed:23754376" FT MUTAGEN 447 FT /note="K->A: Inhibits HR-mediated DNA repair." FT /evidence="ECO:0000269|PubMed:23754376" FT MUTAGEN 500 FT /note="D->A: Inhibits HR-mediated DNA repair." FT /evidence="ECO:0000269|PubMed:23754376" FT CONFLICT 614 FT /note="E -> G (in Ref. 1; BAB14426)" FT /evidence="ECO:0000305" FT HELIX 381..390 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 407..416 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 418..422 FT /evidence="ECO:0007829|PDB:3D8B" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:3D8B" FT STRAND 435..442 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 447..457 FT /evidence="ECO:0007829|PDB:3D8B" FT STRAND 461..466 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 467..470 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 477..491 FT /evidence="ECO:0007829|PDB:3D8B" FT STRAND 494..500 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 502..505 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 516..529 FT /evidence="ECO:0007829|PDB:3D8B" FT STRAND 539..546 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 548..550 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 553..556 FT /evidence="ECO:0007829|PDB:3D8B" FT STRAND 561..564 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 570..582 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 590..599 FT /evidence="ECO:0007829|PDB:3D8B" FT TURN 600..602 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 605..616 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 618..622 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 633..635 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 641..651 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 652..654 FT /evidence="ECO:0007829|PDB:3D8B" FT HELIX 660..670 FT /evidence="ECO:0007829|PDB:3D8B" SQ SEQUENCE 674 AA; 74077 MW; 2EB812B407495BF2 CRC64; MQTSSSRSVH LSEWQKNYFA ITSGICTGPK ADAYRAQILR IQYAWANSEI SQVCATKLFK KYAEKYSAII DSDNVESGLN NYAENILTLA GSQQTDSDKW QSGLSINNVF KMSSVQKMMQ AGKKFKDSLL EPALASVVIH KEATVFDLPK FSVCGSSQES DSLPNSAHDR DRTQDFPESN RLKLLQNAQP PMVTNTARTC PTFSAPVGES ATAKFHVTPL FGNVKKENHS SAKENIGLNV FLSNQSCFPA ACENPQRKSF YGSGTIDALS NPILNKACSK TEDNGPKEDS SLPTFKTAKE QLWVDQQKKY HQPQRASGSS YGGVKKSLGA SRSRGILGKF VPPIPKQDGG EQNGGMQCKP YGAGPTEPAH PVDERLKNLE PKMIELIMNE IMDHGPPVNW EDIAGVEFAK ATIKEIVVWP MLRPDIFTGL RGPPKGILLF GPPGTGKTLI GKCIASQSGA TFFSISASSL TSKWVGEGEK MVRALFAVAR CQQPAVIFID EIDSLLSQRG DGEHESSRRI KTEFLVQLDG ATTSSEDRIL VVGATNRPQE IDEAARRRLV KRLYIPLPEA SARKQIVINL MSKEQCCLSE EEIEQIVQQS DAFSGADMTQ LCREASLGPI RSLQTADIAT ITPDQVRPIA YIDFENAFRT VRPSVSPKDL ELYENWNKTF GCGK //