FIGL1_HUMAN
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 03-AUG-2022, entry version 162.
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};
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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 AlphaFoldDB; Q6PIW4; -.
DR SMR; Q6PIW4; -.
DR BioGRID; 122026; 74.
DR IntAct; Q6PIW4; 36.
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; 149 antibodies from 26 providers.
DR DNASU; 63979; -.
DR Ensembl; ENST00000356889.8; ENSP00000349356.4; ENSG00000132436.12. [Q6PIW4-1]
DR Ensembl; ENST00000395556.6; ENSP00000378924.2; ENSG00000132436.12. [Q6PIW4-1]
DR Ensembl; ENST00000419119.1; ENSP00000410811.1; ENSG00000132436.12. [Q6PIW4-1]
DR Ensembl; ENST00000433017.6; ENSP00000399997.1; ENSG00000132436.12. [Q6PIW4-1]
DR Ensembl; ENST00000611938.4; ENSP00000484551.1; ENSG00000132436.12. [Q6PIW4-1]
DR Ensembl; ENST00000613602.3; ENSP00000481751.1; ENSG00000132436.12. [Q6PIW4-1]
DR Ensembl; ENST00000615084.4; ENSP00000483543.1; ENSG00000132436.12. [Q6PIW4-1]
DR Ensembl; ENST00000617389.4; ENSP00000483126.1; ENSG00000132436.12. [Q6PIW4-1]
DR GeneID; 63979; -.
DR KEGG; hsa:63979; -.
DR MANE-Select; ENST00000433017.6; ENSP00000399997.1; NM_001287492.4; NP_001274421.1.
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; YSDKWES; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q6PIW4; -.
DR TreeFam; TF105013; -.
DR PathwayCommons; Q6PIW4; -.
DR SignaLink; Q6PIW4; -.
DR BioGRID-ORCS; 63979; 15 hits in 1079 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 167 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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: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 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 /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.14"
FT BINDING 444..449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
