FMN2_HUMAN
ID FMN2_HUMAN Reviewed; 1722 AA.
AC Q9NZ56; B0QZA7; B4DP05; Q59GF6; Q5VU37; Q9NZ55;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Formin-2;
GN Name=FMN2;
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 2).
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1722 (ISOFORM 1), AND
RP VARIANTS GLY-1148 AND HIS-1468.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 396-727 AND 1426-1722 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10781961; DOI=10.1016/s0925-4773(00)00276-8;
RA Leader B., Leder P.;
RT "Formin-2, a novel formin homology protein of the cappuccino subfamily, is
RT highly expressed in the developing and adult central nervous system.";
RL Mech. Dev. 93:221-231(2000).
RN [5]
RP INTERACTION WITH ACTIN, AND SUBCELLULAR LOCATION.
RX PubMed=20082305; DOI=10.1002/jcp.22051;
RA Shieh D.B., Li R.Y., Liao J.M., Chen G.D., Liou Y.M.;
RT "Effects of genistein on beta-catenin signaling and subcellular
RT distribution of actin-binding proteins in human umbilical CD105-positive
RT stromal cells.";
RL J. Cell. Physiol. 223:423-434(2010).
RN [6]
RP FUNCTION.
RX PubMed=22330775; DOI=10.1016/j.bbagen.2012.01.014;
RA Peng K.W., Liou Y.M.;
RT "Differential role of actin-binding proteins in controlling the adipogenic
RT differentiation of human CD105-positive Wharton's Jelly cells.";
RL Biochim. Biophys. Acta 1820:469-481(2012).
RN [7]
RP FUNCTION, INTERACTION WITH CDKN1A, SUBCELLULAR LOCATION, INDUCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23375502; DOI=10.1016/j.molcel.2012.12.023;
RA Yamada K., Ono M., Perkins N.D., Rocha S., Lamond A.I.;
RT "Identification and functional characterization of FMN2, a regulator of the
RT cyclin-dependent kinase inhibitor p21.";
RL Mol. Cell 49:922-933(2013).
RN [8]
RP INVOLVEMENT IN MRT47.
RX PubMed=25480035; DOI=10.1016/j.ajhg.2014.10.016;
RA Law R., Dixon-Salazar T., Jerber J., Cai N., Abbasi A.A., Zaki M.S.,
RA Mittal K., Gabriel S.B., Rafiq M.A., Khan V., Nguyen M., Ali G.,
RA Copeland B., Scott E., Vasli N., Mikhailov A., Khan M.N., Andrade D.M.,
RA Ayaz M., Ansar M., Ayub M., Vincent J.B., Gleeson J.G.;
RT "Biallelic truncating mutations in FMN2, encoding the actin-regulatory
RT protein Formin 2, cause nonsyndromic autosomal-recessive intellectual
RT disability.";
RL Am. J. Hum. Genet. 95:721-728(2014).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 444-LYS--ARG-446.
RX PubMed=26287480; DOI=10.7554/elife.07735;
RA Belin B.J., Lee T., Mullins R.D.;
RT "DNA damage induces nuclear actin filament assembly by Formin -2 and Spire-
RT 1/2 that promotes efficient DNA repair.";
RL Elife 4:E07735-E07735(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1694-1722 IN COMPLEX WITH SPIRE1,
RP AND INTERACTION WITH SPIRE1.
RX PubMed=21705804; DOI=10.1074/jbc.m111.257782;
RA Zeth K., Pechlivanis M., Samol A., Pleiser S., Vonrhein C., Kerkhoff E.;
RT "Molecular basis of actin nucleation factor cooperativity: crystal
RT structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2
RT formin SPIR interaction motif (FSI) complex.";
RL J. Biol. Chem. 286:30732-30739(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1701-1722 IN COMPLEX WITH SPIRE1,
RP FUNCTION, INTERACTION WITH SPIRE1, AND MUTAGENESIS OF LYS-1715; LYS-1717
RP AND LYS-1721.
RX PubMed=21730168; DOI=10.1073/pnas.1105703108;
RA Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W.,
RA Quinlan M.E., Eck M.J.;
RT "Structure and function of the interacting domains of Spire and Fmn-family
RT formins.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011).
CC -!- FUNCTION: Actin-binding protein that is involved in actin cytoskeleton
CC assembly and reorganization (PubMed:22330775, PubMed:21730168). Acts as
CC an actin nucleation factor and promotes assembly of actin filaments
CC together with SPIRE1 and SPIRE2 (PubMed:22330775, PubMed:21730168).
CC Involved in intracellular vesicle transport along actin fibers,
CC providing a novel link between actin cytoskeleton dynamics and
CC intracellular transport (By similarity). Required for asymmetric
CC spindle positioning, asymmetric oocyte division and polar body
CC extrusion during female germ cell meiosis (By similarity). Plays a role
CC in responses to DNA damage, cellular stress and hypoxia by protecting
CC CDKN1A against degradation, and thereby plays a role in stress-induced
CC cell cycle arrest (PubMed:23375502). Also acts in the nucleus: together
CC with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in
CC response to DNA damage in order to facilitate movement of chromatin and
CC repair factors after DNA damage (PubMed:26287480). Protects cells
CC against apoptosis by protecting CDKN1A against degradation
CC (PubMed:23375502). {ECO:0000250|UniProtKB:Q9JL04,
CC ECO:0000269|PubMed:21730168, ECO:0000269|PubMed:22330775,
CC ECO:0000269|PubMed:23375502, ECO:0000269|PubMed:26287480}.
CC -!- SUBUNIT: Interacts with SPIRE1 (PubMed:21705804, PubMed:21730168).
CC Binds actin (PubMed:20082305). Interacts with CDKN1A (PubMed:23375502).
CC {ECO:0000269|PubMed:20082305, ECO:0000269|PubMed:21705804,
CC ECO:0000269|PubMed:21730168, ECO:0000269|PubMed:23375502}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20082305}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:20082305}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9JL04}. Nucleus {ECO:0000269|PubMed:26287480}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:23375502}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9JL04}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9JL04}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9JL04}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9JL04}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9JL04}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9JL04}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9JL04}. Note=Colocalizes with the actin
CC cytoskeleton (PubMed:20082305). Recruited to the membranes via its
CC interaction with SPIRE1 (By similarity). Detected at the cleavage
CC furrow during asymmetric oocyte division and polar body extrusion (By
CC similarity). Accumulates in the nucleus following DNA damage
CC (PubMed:26287480). {ECO:0000250|UniProtKB:Q9JL04,
CC ECO:0000269|PubMed:20082305, ECO:0000269|PubMed:26287480}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZ56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZ56-2; Sequence=VSP_056095;
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in the developing and
CC mature central nervous system. {ECO:0000269|PubMed:10781961}.
CC -!- INDUCTION: Up-regulated in response to cellular stress, hypoxia and DNA
CC damage via NF-kappa-B. {ECO:0000269|PubMed:23375502}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 47
CC (MRT47) [MIM:616193]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT47
CC patients show delayed development, with cognition and speech more
CC affected than motor skills. {ECO:0000269|PubMed:25480035}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF72884.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AK298141; BAG60417.1; -; mRNA.
DR EMBL; AL359918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL646016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB209153; BAD92390.1; -; mRNA.
DR EMBL; AF218941; AAF72884.1; ALT_SEQ; mRNA.
DR EMBL; AF218942; AAF72885.1; -; mRNA.
DR CCDS; CCDS31069.2; -. [Q9NZ56-1]
DR RefSeq; NP_001292353.1; NM_001305424.1.
DR RefSeq; NP_064450.3; NM_020066.4. [Q9NZ56-1]
DR PDB; 2YLE; X-ray; 1.80 A; B=1694-1722.
DR PDB; 3R7G; X-ray; 2.20 A; B=1701-1722.
DR PDBsum; 2YLE; -.
DR PDBsum; 3R7G; -.
DR AlphaFoldDB; Q9NZ56; -.
DR SMR; Q9NZ56; -.
DR BioGRID; 121199; 55.
DR IntAct; Q9NZ56; 14.
DR MINT; Q9NZ56; -.
DR STRING; 9606.ENSP00000318884; -.
DR iPTMnet; Q9NZ56; -.
DR PhosphoSitePlus; Q9NZ56; -.
DR BioMuta; FMN2; -.
DR DMDM; 166215083; -.
DR jPOST; Q9NZ56; -.
DR MassIVE; Q9NZ56; -.
DR MaxQB; Q9NZ56; -.
DR PaxDb; Q9NZ56; -.
DR PeptideAtlas; Q9NZ56; -.
DR PRIDE; Q9NZ56; -.
DR ProteomicsDB; 4739; -.
DR ProteomicsDB; 83328; -. [Q9NZ56-1]
DR Antibodypedia; 20819; 136 antibodies from 28 providers.
DR DNASU; 56776; -.
DR Ensembl; ENST00000319653.14; ENSP00000318884.9; ENSG00000155816.21. [Q9NZ56-1]
DR GeneID; 56776; -.
DR KEGG; hsa:56776; -.
DR MANE-Select; ENST00000319653.14; ENSP00000318884.9; NM_020066.5; NP_064450.3.
DR UCSC; uc010pyd.3; human. [Q9NZ56-1]
DR CTD; 56776; -.
DR DisGeNET; 56776; -.
DR GeneCards; FMN2; -.
DR HGNC; HGNC:14074; FMN2.
DR HPA; ENSG00000155816; Tissue enhanced (brain, parathyroid gland, retina).
DR MalaCards; FMN2; -.
DR MIM; 606373; gene.
DR MIM; 616193; phenotype.
DR neXtProt; NX_Q9NZ56; -.
DR OpenTargets; ENSG00000155816; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA28185; -.
DR VEuPathDB; HostDB:ENSG00000155816; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000161899; -.
DR HOGENOM; CLU_002670_2_0_1; -.
DR InParanoid; Q9NZ56; -.
DR OMA; DTLQRVC; -.
DR OrthoDB; 249504at2759; -.
DR PhylomeDB; Q9NZ56; -.
DR TreeFam; TF326072; -.
DR PathwayCommons; Q9NZ56; -.
DR SignaLink; Q9NZ56; -.
DR BioGRID-ORCS; 56776; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; FMN2; human.
DR GenomeRNAi; 56776; -.
DR Pharos; Q9NZ56; Tbio.
DR PRO; PR:Q9NZ56; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NZ56; protein.
DR Bgee; ENSG00000155816; Expressed in cortical plate and 126 other tissues.
DR ExpressionAtlas; Q9NZ56; baseline and differential.
DR Genevisible; Q9NZ56; HS.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:UniProtKB.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; ISS:BHF-UCL.
DR GO; GO:0070649; P:formin-nucleated actin cable assembly; IDA:UniProtKB.
DR GO; GO:0051758; P:homologous chromosome movement towards spindle pole in meiosis I anaphase; ISS:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; ISS:BHF-UCL.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; ISS:BHF-UCL.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell membrane;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Developmental protein; DNA damage; Intellectual disability; Membrane;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Stress response; Transport.
FT CHAIN 1..1722
FT /note="Formin-2"
FT /id="PRO_0000194888"
FT DOMAIN 758..1268
FT /note="FH1"
FT DOMAIN 1283..1698
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1722
FT /note="Important for interaction with SPIRE1"
FT COILED 193..231
FT /evidence="ECO:0000255"
FT COILED 670..706
FT /evidence="ECO:0000255"
FT COILED 1567..1597
FT /evidence="ECO:0000255"
FT COILED 1677..1699
FT /evidence="ECO:0000255"
FT COMPBIAS 169..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..1243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JL04"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JL04"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JL04"
FT VAR_SEQ 2..1405
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056095"
FT VARIANT 1148
FT /note="R -> G (in dbSNP:rs12732924)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_059290"
FT VARIANT 1291
FT /note="R -> G (in dbSNP:rs12732924)"
FT /id="VAR_049094"
FT VARIANT 1468
FT /note="R -> H (in dbSNP:rs3795677)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_033932"
FT MUTAGEN 444..446
FT /note="KRR->AAA: Blocks accumulation in the nucleus in
FT response to DNA damage."
FT /evidence="ECO:0000269|PubMed:26287480"
FT MUTAGEN 1715
FT /note="K->A,E: Abolishes interaction with SPIRE1."
FT /evidence="ECO:0000269|PubMed:21730168"
FT MUTAGEN 1717
FT /note="K->A: Strongly reduces interaction with SPIRE1."
FT /evidence="ECO:0000269|PubMed:21730168"
FT MUTAGEN 1721
FT /note="K->A,E: Strongly reduces interaction with SPIRE1."
FT /evidence="ECO:0000269|PubMed:21730168"
FT CONFLICT 644
FT /note="E -> EDDGE (in Ref. 3; BAD92390)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="P -> T (in Ref. 3; BAD92390)"
FT /evidence="ECO:0000305"
FT CONFLICT 1426..1427
FT /note="EN -> TR (in Ref. 4; AAF72885)"
FT /evidence="ECO:0000305"
FT STRAND 1706..1708
FT /evidence="ECO:0007829|PDB:2YLE"
FT HELIX 1714..1719
FT /evidence="ECO:0007829|PDB:2YLE"
SQ SEQUENCE 1722 AA; 180106 MW; 26525AC7868A949C CRC64;
MGNQDGKLKR SAGDALHEGG GGAEDALGPR DVEATKKGSG GKKALGKHGK GGGGGGGGGE
SGKKKSKSDS RASVFSNLRI RKNLSKGKGA GGSREDVLDS QALQTGELDS AHSLLTKTPD
LSLSADEAGL SDTECADPFE VTGPGGPGPA EARVGGRPIA EDVETAAGAQ DGQRTSSGSD
TDIYSFHSAT EQEDLLSDIQ QAIRLQQQQQ QQLQLQLQQQ QQQQQLQGAE EPAAPPTAVS
PQPGAFLGLD RFLLGPSGGA GEAPGSPDTE QALSALSDLP ESLAAEPREP QQPPSPGGLP
VSEAPSLPAA QPAAKDSPSS TAFPFPEAGP GEEAAGAPVR GAGDTDEEGE EDAFEDAPRG
SPGEEWAPEV GEDAPQRLGE EPEEEAQGPD APAAASLPGS PAPSQRCFKP YPLITPCYIK
TTTRQLSSPN HSPSQSPNQS PRIKRRPEPS LSRGSRTALA SVAAPAKKHR ADGGLAAGLS
RSADWTEELG ARTPRVGGSA HLLERGVASD SGGGVSPALA AKASGAPAAA DGFQNVFTGR
TLLEKLFSQQ ENGPPEEAEK FCSRIIAMGL LLPFSDCFRE PCNQNAQTNA ASFDQDQLYT
WAAVSQPTHS LDYSEGQFPR RVPSMGPPSK PPDEEHRLED AETESQSAVS ETPQKRSDAV
QKEVVDMKSE GQATVIQQLE QTIEDLRTKI AELERQYPAL DTEVASGHQG LENGVTASGD
VCLEALRLEE KEVRHHRILE AKSIQTSPTE EGGVLTLPPV DGLPGRPPCP PGAESGPQTK
FCSEISLIVS PRRISVQLDS HQPTQSISQP PPPPSLLWSA GQGQPGSQPP HSISTEFQTS
HEHSVSSAFK NSCNIPSPPP LPCTESSSSM PGLGMVPPPP PPLPGMTVPT LPSTAIPQPP
PLQGTEMLPP PPPPLPGAGI PPPPPLPGAG ILPLPPLPGA GIPPPPPLPG AAIPPPPPLP
GAGIPLPPPL PGAGIPPPPP LPGAGIPPPP PLPGAGIPPP PPLPGAGIPP PPPLPGAGIP
PPPPLPGAGI PPPPPLPGAG IPPPPPLPGA GIPPPPPLPG AGIPPPPPLP GAGIPPPPPL
PGAGIPPPPP LPGAGIPPPP PLPGVGIPPP PPLPGAGIPP PPPLPGAGIP PPPPLPGAGI
PPPPPLPRVG IPPPPPLPGA GIPPPPPLPG AGIPPPPPLP GVGIPPPPPL PGVGIPPPPP
LPGAGIPPPP PLPGMGIPPA PAPPLPPPGT GIPPPPLLPV SGPPLLPQVG SSTLPTPQVC
GFLPPPLPSG LFGLGMNQDK GSRKQPIEPC RPMKPLYWTR IQLHSKRDSS TSLIWEKIEE
PSIDCHEFEE LFSKTAVKER KKPISDTISK TKAKQVVKLL SNKRSQAVGI LMSSLHLDMK
DIQHAVVNLD NSVVDLETLQ ALYENRAQSD ELEKIEKHGR SSKDKENAKS LDKPEQFLYE
LSLIPNFSER VFCILFQSTF SESICSIRRK LELLQKLCET LKNGPGVMQV LGLVLAFGNY
MNGGNKTRGQ ADGFGLDILP KLKDVKSSDN SRSLLSYIVS YYLRNFDEDA GKEQCLFPLP
EPQDLFQASQ MKFEDFQKDL RKLKKDLKAC EVEAGKVYQV SSKEHMQPFK ENMEQFIIQA
KIDQEAEENS LTETHKCFLE TTAYFFMKPK LGEKEVSPNA FFSIWHEFSS DFKDFWKKEN
KLLLQERVKE AEEVCRQKKG KSLYKIKPRH DSGIKAKISM KT
