FIGN_HUMAN
ID FIGN_HUMAN Reviewed; 759 AA.
AC Q5HY92; B3KWM0; Q9H6M5; Q9NVZ9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Fidgetin;
GN Name=FIGN;
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].
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].
RC TISSUE=Salivary gland;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-532.
RX PubMed=22672901; DOI=10.4161/cc.20849;
RA Mukherjee S., Diaz Valencia J.D., Stewman S., Metz J., Monnier S., Rath U.,
RA Asenjo A.B., Charafeddine R.A., Sosa H.J., Ross J.L., Ma A., Sharp D.J.;
RT "Human Fidgetin is a microtubule severing the enzyme and minus-end
RT depolymerase that regulates mitosis.";
RL Cell Cycle 11:2359-2366(2012).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-400, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
CC -!- FUNCTION: ATP-dependent microtubule severing protein. Severs
CC microtubules along their length and depolymerizes their ends, primarily
CC the minus-end, that may lead to the suppression of microtubule growth
CC from and attachment to centrosomes. Microtubule severing may promote
CC rapid reorganization of cellular microtubule arrays and the release of
CC microtubules from the centrosome following nucleation. Microtubule
CC release from the mitotic spindle poles may allow depolymerization of
CC the microtubule end proximal to the spindle pole, leading to poleward
CC microtubule flux and poleward motion of chromosome.
CC {ECO:0000269|PubMed:22672901}.
CC -!- SUBUNIT: Interacts with AKAP8 (via C-terminus). {ECO:0000250}.
CC -!- INTERACTION:
CC Q5HY92; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-12297985, EBI-2555370;
CC Q5HY92; O14964: HGS; NbExp=3; IntAct=EBI-12297985, EBI-740220;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:22672901}. Note=Localizes to centrosomes throughout
CC mitosis and to the spindle midzone during telophase.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX81992.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA91590.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91590.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15231.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001267; BAA91590.1; ALT_SEQ; mRNA.
DR EMBL; AK025747; BAB15231.1; ALT_INIT; mRNA.
DR EMBL; AK125324; BAG54182.1; -; mRNA.
DR EMBL; BX649105; CAI45980.1; -; mRNA.
DR EMBL; AC093727; AAX81992.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS2221.2; -.
DR RefSeq; NP_060556.2; NM_018086.3.
DR AlphaFoldDB; Q5HY92; -.
DR SMR; Q5HY92; -.
DR BioGRID; 120441; 9.
DR IntAct; Q5HY92; 6.
DR STRING; 9606.ENSP00000333836; -.
DR iPTMnet; Q5HY92; -.
DR PhosphoSitePlus; Q5HY92; -.
DR BioMuta; FIGN; -.
DR DMDM; 115502199; -.
DR EPD; Q5HY92; -.
DR jPOST; Q5HY92; -.
DR MassIVE; Q5HY92; -.
DR PaxDb; Q5HY92; -.
DR PeptideAtlas; Q5HY92; -.
DR PRIDE; Q5HY92; -.
DR ProteomicsDB; 62925; -.
DR Antibodypedia; 47964; 137 antibodies from 18 providers.
DR DNASU; 55137; -.
DR Ensembl; ENST00000333129.4; ENSP00000333836.3; ENSG00000182263.14.
DR GeneID; 55137; -.
DR KEGG; hsa:55137; -.
DR MANE-Select; ENST00000333129.4; ENSP00000333836.3; NM_018086.4; NP_060556.2.
DR UCSC; uc002uck.2; human.
DR CTD; 55137; -.
DR DisGeNET; 55137; -.
DR GeneCards; FIGN; -.
DR HGNC; HGNC:13285; FIGN.
DR HPA; ENSG00000182263; Low tissue specificity.
DR MIM; 605295; gene.
DR neXtProt; NX_Q5HY92; -.
DR OpenTargets; ENSG00000182263; -.
DR PharmGKB; PA28147; -.
DR VEuPathDB; HostDB:ENSG00000182263; -.
DR eggNOG; KOG0740; Eukaryota.
DR GeneTree; ENSGT00940000157526; -.
DR HOGENOM; CLU_000688_21_10_1; -.
DR InParanoid; Q5HY92; -.
DR OMA; GNFSYNQ; -.
DR OrthoDB; 1176820at2759; -.
DR PhylomeDB; Q5HY92; -.
DR TreeFam; TF105015; -.
DR PathwayCommons; Q5HY92; -.
DR SignaLink; Q5HY92; -.
DR BioGRID-ORCS; 55137; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; FIGN; human.
DR GenomeRNAi; 55137; -.
DR Pharos; Q5HY92; Tbio.
DR PRO; PR:Q5HY92; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q5HY92; protein.
DR Bgee; ENSG00000182263; Expressed in buccal mucosa cell and 167 other tissues.
DR ExpressionAtlas; Q5HY92; baseline and differential.
DR Genevisible; Q5HY92; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; 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:0008568; F:microtubule severing ATPase activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..759
FT /note="Fidgetin"
FT /id="PRO_0000250748"
FT REGION 89..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT BINDING 529..534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6PIW4"
FT MOD_RES 400
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 96
FT /note="S -> L (in dbSNP:rs2231902)"
FT /id="VAR_027613"
FT VARIANT 448
FT /note="R -> C (in dbSNP:rs2231904)"
FT /id="VAR_027614"
FT VARIANT 565
FT /note="K -> R (in dbSNP:rs2231905)"
FT /id="VAR_027615"
FT MUTAGEN 532
FT /note="K->A: Inhibits the ability to sever and depolymerize
FT microtubules."
FT /evidence="ECO:0000269|PubMed:22672901"
FT CONFLICT 713
FT /note="L -> I (in Ref. 2; CAI45980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 82146 MW; 68E1C4C8CA66AE2A CRC64;
MISSTSVYGL KMQWTPEHAQ WPEQHFDITS TTRSPAHKVE AYRGHLQRTY QYAWANDDIS
ALTASNLLKK YAEKYSGILE GPVDRPVLSN YSDTPSGLVN GRKNESEPWQ PSLNSEAVYP
MNCVPDVITA SKAGVSSALP PADVSASIGS SPGVASNLTE PSYSSSTCGS HTVPSLHAGL
PSQEYAPGYN GSYLHSTYSS QPAPALPSPH PSPLHSSGLL QPPPPPPPPP ALVPGYNGTS
NLSSYSYPSA SYPPQTAVGS GYSPGGAPPP PSAYLPSGIP APTPLPPTTV PGYTYQGHGL
TPIAPSALTN SSASSLKRKA FYMAGQGDMD SSYGNYSYGQ QRSTQSPMYR MPDNSISNTN
RGNGFDRSAE TSSLAFKPTK QLMSSEQQRK FSSQSSRALT PPSYSTAKNS LGSRSSESFG
KYTSPVMSEH GDEHRQLLSH PMQGPGLRAA TSSNHSVDEQ LKNTDTHLID LVTNEIITQG
PPVDWNDIAG LDLVKAVIKE EVLWPVLRSD AFSGLTALPR SILLFGPRGT GKTLLGRCIA
SQLGATFFKI AGSGLVAKWL GEAEKIIHAS FLVARCRQPS VIFVSDIDML LSSQVNEEHS
PVSRMRTEFL MQLDTVLTSA EDQIVVICAT SKPEEIDESL RRYFMKRLLI PLPDSTARHQ
IIVQLLSQHN YCLNDKEFAL LVQRTEGFSG LDVAHLCQEA VVGPLHAMPA TDLSAIMPSQ
LRPVTYQDFE NAFCKIQPSI SQKELDMYVE WNKMFGCSQ
