ID FOXK1_MOUSE Reviewed; 719 AA. AC P42128; O35939; Q3UHI6; Q3UN67; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 04-NOV-2026, entry version 224. DE RecName: Full=Forkhead box protein K1 {ECO:0000303|PubMed:12446708}; DE AltName: Full=Myocyte nuclear factor {ECO:0000303|PubMed:10792059, ECO:0000303|PubMed:8007964}; DE Short=MNF {ECO:0000303|PubMed:10792059, ECO:0000303|PubMed:8007964}; GN Name=Foxk1 {ECO:0000303|PubMed:12446708, ECO:0000312|MGI:MGI:1347488}; GN Synonyms=Mnf {ECO:0000303|PubMed:10792059}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND RP PHOSPHORYLATION. RC TISSUE=Pancreatic acinar cell; RX PubMed=8007964; DOI=10.1128/mcb.14.7.4596-4605.1994; RA Bassel-Duby R., Hernandez M.D., Yang Q., Rochelle J.M., Seldin M.F., RA Williams R.S.; RT "Myocyte nuclear factor, a novel winged-helix transcription factor under RT both developmental and neural regulation in striated myocytes."; RL Mol. Cell. Biol. 14:4596-4605(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Diencephalon; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-411, FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Skeletal muscle; RX PubMed=9271401; DOI=10.1128/mcb.17.9.5236; RA Yang Q., Bassel-Duby R., Williams R.S.; RT "Transient expression of a winged-helix protein, MNF-beta, during RT myogenesis."; RL Mol. Cell. Biol. 17:5236-5243(1997). RN [4] RP INTERACTION WITH SIN3B. RC TISSUE=Heart; RX PubMed=10620510; DOI=10.1042/bj3450335; RA Yang Q., Kong Y., Rothermel B., Garry D.J., Bassel-Duby R., Williams R.S.; RT "The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta) RT forms a co-repressor complex with mammalian Sin3B."; RL Biochem. J. 345:335-343(2000). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=10792059; DOI=10.1073/pnas.100501197; RA Garry D.J., Meeson A., Elterman J., Zhao Y., Yang P., Bassel-Duby R., RA Williams R.S.; RT "Myogenic stem cell function is impaired in mice lacking the RT forkhead/winged helix protein MNF."; RL Proc. Natl. Acad. Sci. U.S.A. 97:5416-5421(2000). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12446708; DOI=10.1074/jbc.m209200200; RA Hawke T.J., Jiang N., Garry D.J.; RT "Absence of p21CIP rescues myogenic progenitor cell proliferative and RT regenerative capacity in Foxk1 null mice."; RL J. Biol. Chem. 278:4015-4020(2003). RN [7] RP TISSUE SPECIFICITY. RX PubMed=16376864; DOI=10.1016/j.brainres.2005.11.022; RA Wijchers P.J.E.C., Hoekman M.F.M., Burbach J.P.H., Smidt M.P.; RT "Identification of forkhead transcription factors in cortical and RT dopaminergic areas of the adult murine brain."; RL Brain Res. 1068:23-33(2006). RN [8] RP DEVELOPMENTAL STAGE. RX PubMed=17363903; DOI=10.1038/sj.emboj.7601635; RA Meeson A.P., Shi X., Alexander M.S., Williams R.S., Allen R.E., Jiang N., RA Adham I.M., Goetsch S.C., Hammer R.E., Garry D.J.; RT "Sox15 and Fhl3 transcriptionally coactivate Foxk1 and regulate myogenic RT progenitor cells."; RL EMBO J. 26:1902-1912(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-422, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-209; SER-225; RP SER-229; THR-231; THR-233; SER-239; SER-243; SER-281; SER-285; THR-422; RP SER-427 AND SER-431, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH FHL2. RX PubMed=20013826; DOI=10.1002/stem.274; RA Shi X., Bowlin K.M., Garry D.J.; RT "Fhl2 interacts with Foxk1 and corepresses Foxo4 activity in myogenic RT progenitors."; RL Stem Cells 28:462-469(2010). RN [12] RP FUNCTION, INTERACTION WITH FOXO4 AND MEF2C, MUTAGENESIS OF LYS-333 AND RP ARG-340, AND DNA-BINDING. RX PubMed=22956541; DOI=10.1242/jcs.105239; RA Shi X., Wallis A.M., Gerard R.D., Voelker K.A., Grange R.W., DePinho R.A., RA Garry M.G., Garry D.J.; RT "Foxk1 promotes cell proliferation and represses myogenic differentiation RT by regulating Foxo4 and Mef2."; RL J. Cell Sci. 125:5329-5337(2012). RN [13] RP INTERACTION WITH SIN3A AND SIN3B. RX PubMed=22476904; DOI=10.1007/s11010-012-1302-2; RA Shi X., Garry D.J.; RT "Sin3 interacts with Foxk1 and regulates myogenic progenitors."; RL Mol. Cell. Biochem. 366:251-258(2012). RN [14] RP TISSUE SPECIFICITY. RX PubMed=23714736; DOI=10.1016/j.gep.2013.05.003; RA Sel S., Muenzenberg C., Nass N., Kalinski T., Datan M., Auffarth G.U., RA Toeteberg-Harms M., Zenkel M., Kruse F.E., Paulsen F., Schicht M.; RT "The transcription factor Foxk1 is expressed in developing and adult mouse RT neuroretina."; RL Gene Expr. Patterns 13:280-286(2013). RN [15] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-147, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SIN3A. RX PubMed=25402684; DOI=10.1038/ncb3062; RA Bowman C.J., Ayer D.E., Dynlacht B.D.; RT "Foxk proteins repress the initiation of starvation-induced atrophy and RT autophagy programs."; RL Nat. Cell Biol. 16:1202-1214(2014). RN [17] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAE, PHOSPHORYLATION AT RP SER-402; SER-406; SER-427 AND SER-431, AND MUTAGENESIS OF 402-SER--SER-406 RP AND 417-SER--SER-431. RX PubMed=29861159; DOI=10.1016/j.molcel.2018.04.024; RA He L., Gomes A.P., Wang X., Yoon S.O., Lee G., Nagiec M.J., Cho S., RA Chavez A., Islam T., Yu Y., Asara J.M., Kim B.Y., Blenis J.; RT "mTORC1 promotes metabolic reprogramming by the suppression of GSK3- RT dependent foxk1 phosphorylation."; RL Mol. Cell 70:949-960(2018). RN [18] RP FUNCTION. RX PubMed=30700909; DOI=10.1038/s41586-019-0900-5; RA Sukonina V., Ma H., Zhang W., Bartesaghi S., Subhash S., Heglind M., RA Foyn H., Betz M.J., Nilsson D., Lidell M.E., Naumann J., Haufs-Brusberg S., RA Palmgren H., Mondal T., Beg M., Jedrychowski M.P., Tasken K., Pfeifer A., RA Peng X.R., Kanduri C., Enerbaeck S.; RT "FOXK1 and FOXK2 regulate aerobic glycolysis."; RL Nature 566:279-283(2019). RN [19] RP FUNCTION. RX PubMed=32747411; DOI=10.1101/gr.261016.120; RA Kolovos P., Nishimura K., Sankar A., Sidoli S., Cloos P.A., Helin K., RA Christensen J.; RT "PR-DUB maintains the expression of critical genes through FOXK1/2- and RT ASXL1/2/3-dependent recruitment to chromatin and H2AK119ub1 RT deubiquitination."; RL Genome Res. 30:1119-1130(2020). RN [20] RP STRUCTURE BY NMR OF 289-389. RX PubMed=12449423; DOI=10.1023/a:1020616926152; RA Chuang W.J., Yeh I.J., Hsieh Y.H., Liu P.P., Chen S.W., Jeng W.Y.; RT "1H, 15N and 13C resonance assignments for the DNA-binding domain of RT myocyte nuclear factor (Foxk1)."; RL J. Biomol. NMR 24:75-76(2002). CC -!- FUNCTION: Transcriptional regulator involved in different processes CC such as glucose metabolism, aerobic glycolysis, muscle cell CC differentiation and autophagy (PubMed:25402684, PubMed:29861159, CC PubMed:30700909). Recognizes and binds the forkhead DNA sequence motif CC (5'-GTAAACA-3') and can both act as a transcription activator or CC repressor, depending on the context (PubMed:25402684, PubMed:29861159, CC PubMed:30700909). Together with FOXK2, acts as a key regulator of CC metabolic reprogramming towards aerobic glycolysis, a process in which CC glucose is converted to lactate in the presence of oxygen CC (PubMed:30700909). Acts by promoting expression of enzymes for CC glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate CC kinase (PKLR) and lactate dehydrogenase), while suppressing further CC oxidation of pyruvate in the mitochondria by up-regulating pyruvate CC dehydrogenase kinases PDK1 and PDK4 (PubMed:30700909). Probably plays a CC role in gluconeogenesis during overnight fasting, when lactate from CC white adipose tissue and muscle is the main substrate CC (PubMed:30700909). Involved in mTORC1-mediated metabolic reprogramming: CC in response to mTORC1 signaling, translocates into the nucleus and CC regulates the expression of genes associated with glycolysis and CC downstream anabolic pathways, such as HIF1A, thereby regulating glucose CC metabolism (PubMed:29861159). Together with FOXK2, acts as a negative CC regulator of autophagy in skeletal muscle: in response to starvation, CC enters the nucleus, binds the promoters of autophagy genes and CC represses their expression, preventing proteolysis of skeletal muscle CC proteins (PubMed:25402684). Acts as a transcriptional regulator of the CC myogenic progenitor cell population in skeletal muscle CC (PubMed:12446708, PubMed:22956541, PubMed:8007964, PubMed:9271401). CC Binds to the upstream enhancer region (CCAC box) of myoglobin (MB) CC gene, regulating the myogenic progenitor cell population CC (PubMed:8007964, PubMed:9271401). Promotes muscle progenitor cell CC proliferation by repressing the transcriptional activity of FOXO4, CC thereby inhibiting myogenic differentiation (PubMed:12446708, CC PubMed:22956541). Involved in remodeling processes of adult muscles CC that occur in response to physiological stimuli (PubMed:22956541, CC PubMed:9271401). Required to correct temporal orchestration of CC molecular and cellular events necessary for muscle repair CC (PubMed:10792059). Represses myogenic differentiation by inhibiting CC MEFC activity (PubMed:22956541). Positively regulates Wnt/beta-catenin CC signaling by translocating DVL into the nucleus (By similarity). CC Reduces virus replication, probably by binding the interferon CC stimulated response element (ISRE) to promote antiviral gene expression CC (By similarity). Accessory component of the polycomb repressive CC deubiquitinase (PR-DUB) complex; recruits the PR-DUB complex to CC specific FOXK1-bound genes (PubMed:32747411). CC {ECO:0000250|UniProtKB:P85037, ECO:0000269|PubMed:10792059, CC ECO:0000269|PubMed:12446708, ECO:0000269|PubMed:22956541, CC ECO:0000269|PubMed:25402684, ECO:0000269|PubMed:29861159, CC ECO:0000269|PubMed:30700909, ECO:0000269|PubMed:32747411, CC ECO:0000269|PubMed:8007964, ECO:0000269|PubMed:9271401}. CC -!- SUBUNIT: Interacts with SIN3A and SIN3B (via PAH2) to form a complex CC which represses transcription (PubMed:10620510). Component of SIN3A-, CC but not SIN3B-, containing multiprotein complexes (PubMed:25402684). CC Interacts with FOXO4 and MEF2C; both interactions inhibit FOXO4 and CC MEF2C transactivation activity (PubMed:22956541). Interacts (when CC phosphorylated) with YWHAE/14-3-3-epsilon; promotes sequestration in CC the cytoplasm and leads to impaired ability to bind DNA CC (PubMed:29861159). Interacts with FHL2 (PubMed:20013826). Interacts CC with SRF (By similarity). Interacts with DVL2 and DVL3; the interaction CC induces DVL2 nuclear translocation (By similarity). Interacts with BAP1 CC (when phosphorylated) (By similarity). Accessory component of the CC polycomb repressive deubiquitinase (PR-DUB) complex, at least composed CC of BAP1, one of ASXL1, ASXL2 or (probably) ASXL3 and one of MBD5 or CC MBD6 (PubMed:32747411). The PR-DUB core associates with a number of CC accessory proteins, including FOXK1, FOXK2, KDM1B, HCFC1 and OGT (By CC similarity). {ECO:0000250|UniProtKB:P85037, CC ECO:0000269|PubMed:10620510, ECO:0000269|PubMed:20013826, CC ECO:0000269|PubMed:22956541, ECO:0000269|PubMed:25402684, CC ECO:0000269|PubMed:29861159, ECO:0000269|PubMed:32747411}. CC -!- INTERACTION: CC P42128; Q62141-2: Sin3b; NbExp=11; IntAct=EBI-878270, EBI-591466; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20013826, CC ECO:0000269|PubMed:25402684, ECO:0000269|PubMed:29861159}. Cytoplasm CC {ECO:0000269|PubMed:25402684, ECO:0000269|PubMed:29861159}. CC Note=Translocation to the nucleus is regulated by phosphorylation: CC phosphorylation by GSK3 (GSK3A or GSK3B) promotes interaction with 14- CC 3-3 proteins and sequestration in the cytoplasm (PubMed:29861159). CC Dephosphorylation promotes translocation to the nucleus CC (PubMed:29861159). {ECO:0000269|PubMed:29861159}. CC -!- TISSUE SPECIFICITY: Expressed in tissues and cells in which the CC myoglobin gene is transcriptionally active including cardiac and CC skeletal myocytes, brain and kidney (PubMed:8007964, PubMed:9271401). CC In the adult brain, expressed in the piriform cortex and the indusium CC griseum. In the hippocampus, expression is localized to the dentate CC gyrus and CA3 area (PubMed:16376864). In the cerebellum, expression is CC confined to the Purkinje cell layer (PubMed:16376864). Present in CC neuroretinal cells: expressed in rod bipolar cells, amacrine cells and CC ganglion cells (at protein level) (PubMed:23714736). CC {ECO:0000269|PubMed:16376864, ECO:0000269|PubMed:23714736, CC ECO:0000269|PubMed:8007964, ECO:0000269|PubMed:9271401}. CC -!- DEVELOPMENTAL STAGE: Expressed at 13.5 dpc in developing muscle, limbs, CC trunk, and heart. {ECO:0000269|PubMed:17363903}. CC -!- PTM: Phosphorylation by GSK3 (GSK3A or GSK3B) promotes interaction with CC YWHAE/14-3-3-epsilon and retention in the cytoplasm (PubMed:29861159). CC In response to mTORC1 signaling, phosphorylation by GSK3 is prevented, CC leading to translocation to the nucleus (PubMed:29861159). CC {ECO:0000269|PubMed:29861159}. CC -!- DISRUPTION PHENOTYPE: Mutants exhibit a growth deficiency and a severe CC impairment in skeletal muscle regeneration following injury CC (PubMed:10792059, PubMed:12446708). They show atrophic skeletal muscles CC and their satellite cell function is impaired (PubMed:10792059). Double CC knockouts of CDKN1A and FOXK1 don't show significant differences CC compared to wild-type (PubMed:12446708). {ECO:0000269|PubMed:10792059, CC ECO:0000269|PubMed:12446708}. CC -!- CAUTION: The mode of regulation of FOXK1 by mTORC1 is controversial. CC According to a first report, mTORC1 signaling promotes phosphorylation CC of FOXK1 and nuclear exclusion (PubMed:25402684). According to a second CC report, mTORC1 signaling prevents phosphorylation by GSK3 (GSK3A or CC GSK3B), thereby promoting translocation to the nucleus CC (PubMed:29861159). {ECO:0000269|PubMed:25402684, CC ECO:0000269|PubMed:29861159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA37529.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAB69641.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAE25880.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; L26507; AAA37529.1; ALT_FRAME; mRNA. DR EMBL; AK144418; BAE25880.1; ALT_INIT; mRNA. DR EMBL; AK147375; BAE27871.1; -; mRNA. DR EMBL; U95016; AAB69641.1; ALT_FRAME; mRNA. DR CCDS; CCDS19826.1; -. DR PIR; A56051; A56051. DR RefSeq; NP_951031.2; NM_199068.2. DR PDB; 2A3S; NMR; -; A=289-389. DR PDB; 2D2W; NMR; -; A=289-389. DR BMRB; P42128; -. DR SMR; P42128; -. DR BioGRID; 201459; 7. DR IntAct; P42128; 2. DR STRING; 10090.ENSMUSP00000072616; -. DR GlyCosmos; P42128; 8 sites, 1 glycan. DR GlyGen; P42128; 11 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (9 sites). DR iPTMnet; P42128; -. DR PhosphoSitePlus; P42128; -. DR SwissPalm; P42128; -. DR PaxDb; 10090-ENSMUSP00000072616; -. DR PeptideAtlas; P42128; -. DR ProteomicsDB; 271796; -. DR Pumba; P42128; -. DR jPOST; P42128; -. DR DNASU; 17425; -. DR Ensembl; ENSMPUT00000016798; ENSMPUP00000016552; ENSMPUG00000016655. DR Ensembl; ENSMUST00000072837.7; ENSMUSP00000072616.6; ENSMUSG00000056493.10. DR GeneID; 17425; -. DR KEGG; mmu:17425; -. DR UCSC; uc009aio.1; mouse. DR CTD; 221937; -. DR VEuPathDB; HostDB:ENSMUSG00000056493; -. DR AGR; MGI:1347488; -. DR MGI; MGI:1347488; Foxk1. DR eggNOG; KOG2294; Eukaryota. DR GeneTree; ENSGT00940000159507; -. DR HOGENOM; CLU_022344_0_0_1; -. DR InParanoid; P42128; -. DR OMA; AAAAFPX; -. DR OrthoDB; 691130at2759; -. DR PhylomeDB; P42128; -. DR Reactome; R-MMU-5689603; UCH proteinases. DR EvolutionaryTrace; P42128; -. DR PRO; PR:P42128; -. DR Bgee; ENSMUSG00000056493; Expressed in ascending aorta and 233 other cell types or tissues. DR ExpressionAtlas; P42128; baseline and differential. DR CDD; cd20054; FH_FOXK1; 1. DR FunFam; 2.60.200.20:FF:000049; Forkhead box protein K1; 1. DR FunFam; 1.10.10.10:FF:000030; Forkhead box protein K2; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR047394; FH_FOXK1. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR001766; Fork_head_dom. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR InterPro; IPR018122; TF_fork_head_CS_1. DR InterPro; IPR030456; TF_fork_head_CS_2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR45881; CHECKPOINT SUPPRESSOR 1-LIKE, ISOFORM A-RELATED; 1. DR PANTHER; PTHR45881:SF4; FORKHEAD BOX PROTEIN K1; 1. DR Pfam; PF00498; FHA; 1. DR Pfam; PF00250; Forkhead; 1. DR PRINTS; PR00053; FORKHEAD. DR SMART; SM00339; FH; 1. DR SMART; SM00240; FHA; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0071889; F:14-3-3 protein binding; ISO:GO_Central. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:GO_Central. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:GO_Central. DR GO; GO:0061621; P:canonical glycolysis; ISO:GO_Central. DR GO; GO:0001678; P:intracellular glucose homeostasis; ISO:GO_Central. DR GO; GO:0010507; P:negative regulation of autophagy; ISO:GO_Central. DR GO; GO:0045786; P:negative regulation of cell cycle; TAS:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010906; P:regulation of glucose metabolic process; ISO:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0042594; P:response to starvation; ISO:GO_Central. DR Proteomes; UP000000589; Chromosome 5. DR Antibodypedia; 11250; 283 antibodies from 34 providers. DR RNAct; P42128; protein. DR BioGRID-ORCS; 17425; 2 hits in 79 CRISPR screens. DR AlphaFoldDB; P42128; -. DR FunCoup; P42128; 3078. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Cytoplasm; Developmental protein; KW Differentiation; DNA-binding; Methylation; Myogenesis; Nucleus; KW Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P85037" FT CHAIN 2..719 FT /note="Forkhead box protein K1" FT /id="PRO_0000091857" FT DOMAIN 109..161 FT /note="FHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086" FT DNA_BIND 291..386 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 2..40 FT /note="Interaction with SIN3A and SIN3B" FT /evidence="ECO:0000269|PubMed:10620510, FT ECO:0000269|PubMed:22476904" FT REGION 35..67 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 81..406 FT /note="Required for interaction with FOXO4 and MEF2C" FT /evidence="ECO:0000269|PubMed:22956541" FT REGION 399..443 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 665..719 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..62 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 665..685 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 686..695 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 696..712 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P85037" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P85037" FT MOD_RES 147 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 177 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P85037" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 225 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 231 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 233 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 239 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 243 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 281 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 402 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:29861159" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:29861159" FT MOD_RES 408 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P85037" FT MOD_RES 414 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P85037" FT MOD_RES 422 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:29861159, FT ECO:0007744|PubMed:21183079" FT MOD_RES 431 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:29861159, FT ECO:0007744|PubMed:21183079" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P85037" FT MUTAGEN 333 FT /note="K->A: Decreases DNA-binding. No effect on FT transcriptional repression." FT /evidence="ECO:0000269|PubMed:22956541" FT MUTAGEN 340 FT /note="R->A: Abolishes DNA-binding. No effect on FT transcriptional repression." FT /evidence="ECO:0000269|PubMed:22956541" FT MUTAGEN 402..406 FT /note="SAPAS->AAPAA: Decreased phosphorylation by GSK3A and FT interaction with 14-3-3 proteins." FT /evidence="ECO:0000269|PubMed:29861159" FT MUTAGEN 427..431 FT /note="SREGS->AREGA: Decreased phosphorylation by GSK3A and FT interaction with 14-3-3 proteins." FT /evidence="ECO:0000269|PubMed:29861159" FT CONFLICT 43 FT /note="Missing (in Ref. 1; AAA37529 and 3; AAB69641)" FT /evidence="ECO:0000305" FT CONFLICT 402..403 FT /note="SA -> RS (in Ref. 1; AAA37529)" FT /evidence="ECO:0000305" FT CONFLICT 407..411 FT /note="PTHPG -> HTSHA (in Ref. 3; AAB69641)" FT /evidence="ECO:0000305" FT CONFLICT 551 FT /note="R -> A (in Ref. 1; AAA37529)" FT /evidence="ECO:0000305" FT STRAND 292..294 FT /evidence="ECO:0007829|PDB:2A3S" FT HELIX 298..304 FT /evidence="ECO:0007829|PDB:2A3S" FT STRAND 307..312 FT /evidence="ECO:0007829|PDB:2A3S" FT HELIX 314..324 FT /evidence="ECO:0007829|PDB:2A3S" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:2D2W" FT HELIX 335..345 FT /evidence="ECO:0007829|PDB:2A3S" FT STRAND 347..356 FT /evidence="ECO:0007829|PDB:2A3S" FT STRAND 360..362 FT /evidence="ECO:0007829|PDB:2A3S" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:2A3S" FT HELIX 372..380 FT /evidence="ECO:0007829|PDB:2A3S" SQ SEQUENCE 719 AA; 74920 MW; 0A0D3049B7846328 CRC64; MAEVGEDSGA RALLALRSAP CSPVLCAAAA AAAFPATTSP PPPAQPPPGP PALPAEPGPG PVPSTVATAT TTAPALVAAA AASVRQSPGP ALARLEGREF EFLMRQPSVT IGRNSSQGSV DLSMGLSSFI SRRHLQLSFQ EPHFYLRCLG KNGVFVDGAF QRRGAPALQL PQQCTFRFPS TAIKIQFTSL YHKEEAPASP LRPLYPQISP LKIHIPEPDL RSLVSPIPSP TGTISVPNSC PASPRGAGSS SYRFVQNVTS DLQLAAEFAA KAASEQQADA SGGDSPKDES KPPYSYAQLI VQAISSAQDR QLTLSGIYAH ITKHYPYYRT ADKGWQNSIR HNLSLNRYFI KVPRSQEEPG KGSFWRIDPA SEAKLVEQAF RKRRQRGVSC FRTPFGPLSS RSAPASPTHP GLMSPRSSGL QTPECLSREG SPIPHDPDLG SKLASVPEYR YSQSAPGSPV SAQPVIMAVP PRPSNLVAKP VAYMPASIVT SQQPSGHAIH VVQQAPTVTM VRVVTTSANS ANGYILASQG STGTSHDTAG TAVLDLGNEA RGLEEKPTIA FATIPAASRV IQTVASQMAP GVPGHTVTIL QPATPVTIGQ HHLPVRAVTQ NGKHAVPTNS LTGNAYALSS PLQLLAAQAS SSTPVVITRV CEVGPEEPAA AVSVAANAAP TPAASTTTSA SSSGEPEVKR SRVEEPGGTA TTQPTAMAAT GPQGPGTGE //