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 27-MAR-2024, entry version 182. 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}; 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; 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; 61. DR IntAct; Q9NZ56; 19. DR MINT; Q9NZ56; -. DR STRING; 9606.ENSP00000318884; -. DR iPTMnet; Q9NZ56; -. DR PhosphoSitePlus; Q9NZ56; -. DR SwissPalm; Q9NZ56; -. DR BioMuta; FMN2; -. DR DMDM; 166215083; -. DR jPOST; Q9NZ56; -. DR MassIVE; Q9NZ56; -. DR MaxQB; Q9NZ56; -. DR PaxDb; 9606-ENSP00000318884; -. DR PeptideAtlas; Q9NZ56; -. DR ProteomicsDB; 4739; -. DR ProteomicsDB; 83328; -. [Q9NZ56-1] DR Pumba; Q9NZ56; -. DR Antibodypedia; 20819; 144 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 AGR; HGNC:14074; -. 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; CNQNAQS; -. DR OrthoDB; 53873at2759; -. DR PhylomeDB; Q9NZ56; -. DR TreeFam; TF326072; -. DR PathwayCommons; Q9NZ56; -. DR SignaLink; Q9NZ56; -. DR BioGRID-ORCS; 56776; 13 hits in 1157 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 128 other cell types or tissues. DR ExpressionAtlas; Q9NZ56; baseline and differential. 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:0030036; P:actin cytoskeleton organization; IMP:BHF-UCL. DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL. DR GO; GO:0071456; P:cellular response to hypoxia; IMP:UniProtKB. DR GO; GO:0006974; P:DNA damage response; IDA: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; Formin, FH2 domain; 1. DR InterPro; IPR000591; DEP_dom. DR InterPro; IPR015425; FH2_Formin. DR InterPro; IPR042201; FH2_Formin_sf. DR PANTHER; PTHR13037; FORMIN; 1. DR PANTHER; PTHR13037:SF16; FORMIN-2; 1. DR Pfam; PF02181; FH2; 1. DR PRINTS; PR01217; PRICHEXTENSN. DR SMART; SM00498; FH2; 1. DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1. DR PROSITE; PS51444; FH2; 1. DR Genevisible; Q9NZ56; HS. 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 //