FOXK1_HUMAN
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 03-AUG-2022, entry version 153.
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}; 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}.
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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; 208.
DR IntAct; P85037; 111.
DR MINT; P85037; -.
DR STRING; 9606.ENSP00000328720; -.
DR GlyGen; P85037; 28 sites, 2 O-linked glycans (28 sites).
DR iPTMnet; P85037; -.
DR PhosphoSitePlus; P85037; -.
DR BioMuta; FOXK1; -.
DR DMDM; 118572324; -.
DR EPD; P85037; -.
DR jPOST; P85037; -.
DR MassIVE; P85037; -.
DR MaxQB; P85037; -.
DR PaxDb; P85037; -.
DR PeptideAtlas; P85037; -.
DR PRIDE; P85037; -.
DR ProteomicsDB; 57762; -. [P85037-1]
DR ProteomicsDB; 57763; -. [P85037-2]
DR Antibodypedia; 11250; 230 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 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; VTIGQHH; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; P85037; -.
DR TreeFam; TF325718; -.
DR PathwayCommons; P85037; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR SignaLink; P85037; -.
DR BioGRID-ORCS; 221937; 98 hits in 1117 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 191 other tissues.
DR ExpressionAtlas; P85037; baseline and differential.
DR Genevisible; P85037; HS.
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:cellular 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 transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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; cd00059; FH; 1.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 1.10.10.10; -; 1.
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 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF49879; SSF49879; 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.
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
