ID FOXK1_HUMAN Reviewed; 733 AA. AC P85037; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Forkhead box protein K1 {ECO:0000303|PubMed:15202027, ECO:0000303|PubMed:15289879}; DE AltName: Full=Myocyte nuclear factor {ECO:0000303|PubMed:15289879}; DE Short=MNF {ECO:0000303|PubMed:15289879}; GN Name=FOXK1 {ECO:0000303|PubMed:15202027, ECO:0000303|PubMed:15289879, GN ECO:0000312|HGNC:HGNC:23480}; GN Synonyms=MNF {ECO:0000303|PubMed:15289879}; 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=Testis; 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=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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-169 (ISOFORM 1). RC TISSUE=Brain, and Placenta; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-238 (ISOFORM 1). RC TISSUE=Lung; RG The Cancer Genome Anatomy Project (CGAP) at the National Cancer Institute; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP IDENTIFICATION (ISOFORM 1). RX PubMed=15202027; RA Katoh M., Katoh M.; RT "Identification and characterization of human FOXK1 gene in silico."; RL Int. J. Mol. Med. 14:127-132(2004). RN [6] RP IDENTIFICATION (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. RX PubMed=15289879; RA Huang J.T., Lee V.; RT "Identification and characterization of a novel human FOXK1 gene in RT silico."; RL Int. J. Oncol. 25:751-757(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-223; SER-416; RP THR-436 AND SER-441, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF HIS-355. RX PubMed=17670796; DOI=10.1093/nar/gkm528; RA Freddie C.T., Ji Z., Marais A., Sharrocks A.D.; RT "Functional interactions between the Forkhead transcription factor FOXK1 RT and the MADS-box protein SRF."; RL Nucleic Acids Res. 35:5203-5212(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-223; SER-239; RP SER-243; SER-253; SER-257; SER-416; SER-428; SER-441 AND SER-445, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-299; SER-416; RP SER-428 AND SER-445, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-223, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-213; SER-223; RP SER-416; SER-420; SER-428; THR-436; SER-441; SER-445 AND SER-459, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-213; SER-257; RP SER-299; SER-416; SER-420; THR-422; THR-436 AND SER-445, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-161 AND ARG-191, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; 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 [20] RP INTERACTION WITH BAP1, AND MUTAGENESIS OF ARG-127. RX PubMed=25451922; DOI=10.1074/jbc.m114.609834; RA Okino Y., Machida Y., Frankland-Searby S., Machida Y.J.; RT "BRCA1-associated protein 1 (BAP1) deubiquitinase antagonizes the RT ubiquitin-mediated activation of FoxK2 target genes."; RL J. Biol. Chem. 290:1580-1591(2015). RN [21] RP FUNCTION, MUTAGENESIS OF HIS-355, INTERACTION WITH DVL2 AND DVL3, AND RP SUBCELLULAR LOCATION. RX PubMed=25805136; DOI=10.1016/j.devcel.2015.01.031; RA Wang W., Li X., Lee M., Jun S., Aziz K.E., Feng L., Tran M.K., Li N., RA McCrea P.D., Park J.I., Chen J.; RT "FOXKs promote Wnt/beta-catenin signaling by translocating DVL into the RT nucleus."; RL Dev. Cell 32:707-718(2015). RN [22] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25852164; DOI=10.1128/mbio.02509-14; RA Panda D., Gold B., Tartell M.A., Rausch K., Casas-Tinto S., Cherry S.; RT "The transcription factor FoxK participates with Nup98 to regulate RT antiviral gene expression."; RL MBio 6:E02509-E02514(2015). CC -!- FUNCTION: Transcriptional regulator involved in different processes CC such as glucose metabolism, aerobic glycolysis, muscle cell CC differentiation and autophagy (By similarity). Recognizes and binds the CC forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a CC transcription activator or repressor, depending on the context CC (PubMed:17670796). 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 (By CC similarity). Acts by promoting expression of enzymes for glycolysis CC (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase CC (PKLR) and lactate dehydrogenase), while suppressing further oxidation CC of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase CC kinases PDK1 and PDK4 (By similarity). Probably plays a role in CC gluconeogenesis during overnight fasting, when lactate from white CC adipose tissue and muscle is the main substrate (By similarity). CC Involved in mTORC1-mediated metabolic reprogramming: in response to CC mTORC1 signaling, translocates into the nucleus and regulates the CC expression of genes associated with glycolysis and downstream anabolic CC pathways, such as HIF1A, thereby regulating glucose metabolism (By CC similarity). Together with FOXK2, acts as a negative regulator of CC autophagy in skeletal muscle: in response to starvation, enters the CC nucleus, binds the promoters of autophagy genes and represses their CC expression, preventing proteolysis of skeletal muscle proteins (By CC similarity). Acts as a transcriptional regulator of the myogenic CC progenitor cell population in skeletal muscle (By similarity). Binds to CC the upstream enhancer region (CCAC box) of myoglobin (MB) gene, CC regulating the myogenic progenitor cell population (By similarity). CC Promotes muscle progenitor cell proliferation by repressing the CC transcriptional activity of FOXO4, thereby inhibiting myogenic CC differentiation (By similarity). Involved in remodeling processes of CC adult muscles that occur in response to physiological stimuli (By CC similarity). Required to correct temporal orchestration of molecular CC and cellular events necessary for muscle repair (By similarity). CC Represses myogenic differentiation by inhibiting MEFC activity (By CC similarity). Positively regulates Wnt/beta-catenin signaling by CC translocating DVL into the nucleus (PubMed:25805136). Reduces virus CC replication, probably by binding the interferon stimulated response CC element (ISRE) to promote antiviral gene expression (PubMed:25852164). CC {ECO:0000250|UniProtKB:P42128, ECO:0000269|PubMed:17670796, CC ECO:0000269|PubMed:25805136, ECO:0000269|PubMed:25852164}. CC -!- SUBUNIT: Interacts with SIN3A and SIN3B (via PAH2) to form a complex CC which represses transcription (By similarity). Component of SIN3A-, but CC not SIN3B-, containing multiprotein complexes (By similarity). CC Interacts with FOXO4 and MEF2C; both interactions inhibit FOXO4 and CC MEF2C transactivation activity (By similarity). Interacts (when CC phosphorylated) with YWHAE/14-3-3-epsilon; promotes sequestration in CC the cytoplasm and leads to impaired ability to bind DNA (By CC similarity). Interacts with FHL2 (By similarity). Interacts with SRF CC (PubMed:17670796). Interacts with DVL2 and DVL3; the interaction CC induces DVL2 nuclear translocation (PubMed:25805136). Interacts with CC BAP1 (when phosphorylated) (PubMed:25451922). CC {ECO:0000250|UniProtKB:P42128, ECO:0000269|PubMed:17670796, CC ECO:0000269|PubMed:25451922, ECO:0000269|PubMed:25805136}. CC -!- INTERACTION: CC P85037; O43524: FOXO3; NbExp=2; IntAct=EBI-2509974, EBI-1644164; CC P85037; P14316: IRF2; NbExp=3; IntAct=EBI-2509974, EBI-2866589; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25805136, CC ECO:0000269|PubMed:25852164}. Cytoplasm {ECO:0000269|PubMed:25805136, CC ECO:0000269|PubMed:25852164}. Note=Translocation to the nucleus is CC regulated by phosphorylation: phosphorylation by GSK3 (GSK3A or GSK3B) CC promotes interaction with 14-3-3 proteins and sequestration in the CC cytoplasm. Dephosphorylation promotes translocation to the nucleus (By CC similarity). Accumulates in the nucleus upon viral infection CC (PubMed:25852164). {ECO:0000250|UniProtKB:P42128, CC ECO:0000269|PubMed:25852164}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000303|PubMed:15202027, ECO:0000303|PubMed:15289879}; CC Synonyms=a {ECO:0000303|PubMed:15289879}; CC IsoId=P85037-1; Sequence=Displayed; CC Name=2 {ECO:0000303|PubMed:15289879}; Synonyms=b CC {ECO:0000303|PubMed:15289879}; CC IsoId=P85037-2; Sequence=VSP_052239, VSP_052240; CC -!- TISSUE SPECIFICITY: Expressed both developing and adult tissues CC (PubMed:15289879). In adults, significant expression is seen in tumors CC of the brain, colon and lymph node (PubMed:15289879). CC {ECO:0000269|PubMed:15289879}. CC -!- PTM: Phosphorylation by GSK3 (GSK3A or GSK3B) promotes interaction with CC YWHAE/14-3-3-epsilon and retention in the cytoplasm. In response to CC mTORC1 signaling, phosphorylation by GSK3 is prevented, leading to CC translocation to the nucleus. {ECO:0000250|UniProtKB:P42128}. 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; AK122663; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC072054; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092428; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092610; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC038434; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CB959941; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AW206906; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS34591.1; -. [P85037-1] DR RefSeq; NP_001032242.1; NM_001037165.1. [P85037-1] DR RefSeq; XP_011513493.1; XM_011515191.2. DR AlphaFoldDB; P85037; -. DR BMRB; P85037; -. DR SMR; P85037; -. DR BioGRID; 128769; 248. DR IntAct; P85037; 117. DR MINT; P85037; -. DR STRING; 9606.ENSP00000328720; -. DR GlyCosmos; P85037; 28 sites, 2 glycans. DR GlyGen; P85037; 34 sites, 3 O-linked glycans (34 sites). DR iPTMnet; P85037; -. DR PhosphoSitePlus; P85037; -. DR SwissPalm; P85037; -. DR BioMuta; FOXK1; -. DR DMDM; 118572324; -. DR EPD; P85037; -. DR jPOST; P85037; -. DR MassIVE; P85037; -. DR MaxQB; P85037; -. DR PaxDb; 9606-ENSP00000328720; -. DR PeptideAtlas; P85037; -. DR ProteomicsDB; 57762; -. [P85037-1] DR ProteomicsDB; 57763; -. [P85037-2] DR Pumba; P85037; -. DR Antibodypedia; 11250; 268 antibodies from 30 providers. DR DNASU; 221937; -. DR Ensembl; ENST00000328914.5; ENSP00000328720.4; ENSG00000164916.11. [P85037-1] DR GeneID; 221937; -. DR KEGG; hsa:221937; -. DR MANE-Select; ENST00000328914.5; ENSP00000328720.4; NM_001037165.2; NP_001032242.1. DR UCSC; uc003snc.2; human. [P85037-1] DR AGR; HGNC:23480; -. DR CTD; 221937; -. DR DisGeNET; 221937; -. DR GeneCards; FOXK1; -. DR HGNC; HGNC:23480; FOXK1. DR HPA; ENSG00000164916; Low tissue specificity. DR MIM; 616302; gene. DR neXtProt; NX_P85037; -. DR OpenTargets; ENSG00000164916; -. DR PharmGKB; PA134978307; -. DR VEuPathDB; HostDB:ENSG00000164916; -. DR eggNOG; KOG2294; Eukaryota. DR GeneTree; ENSGT00940000159507; -. DR HOGENOM; CLU_022344_0_0_1; -. DR InParanoid; P85037; -. DR OMA; QTHDPRK; -. DR OrthoDB; 5385885at2759; -. DR PhylomeDB; P85037; -. DR TreeFam; TF325718; -. DR PathwayCommons; P85037; -. DR Reactome; R-HSA-5689603; UCH proteinases. DR SignaLink; P85037; -. DR BioGRID-ORCS; 221937; 103 hits in 1195 CRISPR screens. DR ChiTaRS; FOXK1; human. DR GeneWiki; FOXK1; -. DR GenomeRNAi; 221937; -. DR Pharos; P85037; Tbio. DR PRO; PR:P85037; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P85037; Protein. DR Bgee; ENSG00000164916; Expressed in upper arm skin and 193 other cell types or tissues. DR ExpressionAtlas; P85037; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0071889; F:14-3-3 protein binding; IPI:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0061621; P:canonical glycolysis; IDA:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0001678; P:intracellular glucose homeostasis; IDA:UniProtKB. DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW. DR GO; GO:0010507; P:negative regulation of autophagy; 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; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0042594; P:response to starvation; IDA:UniProtKB. DR CDD; cd20054; FH_FOXK1; 1. DR CDD; cd22722; FHA_FOXK1; 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 Genevisible; P85037; HS. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Cytoplasm; KW Developmental protein; Differentiation; DNA-binding; KW Host-virus interaction; Methylation; Myogenesis; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; Transcription; Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..733 FT /note="Forkhead box protein K1" FT /id="PRO_0000261667" FT DOMAIN 123..175 FT /note="FHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086" FT DNA_BIND 305..400 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:0000250|UniProtKB:P42128" FT REGION 36..79 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 95..420 FT /note="Required for interaction with FOXO4 and MEF2C" FT /evidence="ECO:0000250|UniProtKB:P42128" FT REGION 287..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 413..436 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 676..733 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..64 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 679..700 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 101 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 161 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 191 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 223 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 239 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 243 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 245 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P42128" FT MOD_RES 247 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P42128" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 257 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P42128" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 416 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 420 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 422 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 428 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 436 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 441 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 459 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..163 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15289879, FT ECO:0000303|PubMed:15489334" FT /id="VSP_052239" FT VAR_SEQ 164..187 FT /note="GKNGVFVDGAFQRRGAPALQLPKQ -> MAYCLGVNFVPSRFCYQLHRLLLR FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15289879, FT ECO:0000303|PubMed:15489334" FT /id="VSP_052240" FT MUTAGEN 127 FT /note="R->A: Reduced interaction with BAP1." FT /evidence="ECO:0000269|PubMed:25451922" FT MUTAGEN 355 FT /note="H->A: Reduced DNA-binding and ability to repress FT transcription without affecting interaction with SRF. No FT effect on interaction with DVL2." FT /evidence="ECO:0000269|PubMed:17670796, FT ECO:0000269|PubMed:25805136" FT CONFLICT 144 FT /note="I -> V (in Ref. 3; CB959941)" FT /evidence="ECO:0000305" FT CONFLICT 154..155 FT /note="QE -> KS (in Ref. 3; CB959941)" FT /evidence="ECO:0000305" FT CONFLICT 159 FT /note="Y -> S (in Ref. 3; CB959941)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="P -> A (in Ref. 4; AW206906)" FT /evidence="ECO:0000305" FT CONFLICT 232 FT /note="P -> T (in Ref. 4; AW206906)" FT /evidence="ECO:0000305" FT CONFLICT 437..445 FT /note="Missing (in Ref. 1; AK122663)" FT /evidence="ECO:0000305" SQ SEQUENCE 733 AA; 75457 MW; C9EF4AC3C959A1C3 CRC64; MAEVGEDSGA RALLALRSAP CSPVLCAAAA AAAFPAAAPP PAPAQPQPPP GPPPPPPPPL PPGAIAGAGS SGGSSGVSGD SAVAGAAPAL VAAAAASVRQ SPGPALARLE GREFEFLMRQ PSVTIGRNSS QGSVDLSMGL SSFISRRHLQ LSFQEPHFYL RCLGKNGVFV DGAFQRRGAP ALQLPKQCTF RFPSTAIKIQ FTSLYHKEEA PASPLRPLYP QISPLKIHIP EPDLRSMVSP VPSPTGTISV PNSCPASPRG AGSSSYRFVQ NVTSDLQLAA EFAAKAASEQ QADTSGGDSP KDESKPPFSY AQLIVQAISS AQDRQLTLSG IYAHITKHYP YYRTADKGWQ NSIRHNLSLN RYFIKVPRSQ EEPGKGSFWR IDPASEAKLV EQAFRKRRQR GVSCFRTPFG PLSSRSAPAS PTHPGLMSPR SGGLQTPECL SREGSPIPHD PEFGSKLASV PEYRYSQSAP GSPVSAQPVI MAVPPRPSSL VAKPVAYMPA SIVTSQQPAG HAIHVVQQAP TVTMVRVVTT SANSANGYIL TSQGAAGGSH DAAGAAVLDL GSEARGLEEK PTIAFATIPA AGGVIQTVAS QMAPGVPGHT VTILQPATPV TLGQHHLPVR AVTQNGKHAV PTNSLAGNAY ALTSPLQLLA TQASSSAPVV VTRVCEVGPK EPAAAVAATA TTTPATATTA SASASSTGEP EVKRSRVEEP SGAVTTPAGV IAAAGPQGPG TGE //