ID FOXK2_MOUSE Reviewed; 651 AA.
AC Q3UCQ1; A2AN27; B5AZX0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 01-MAY-2013, entry version 75.
DE RecName: Full=Forkhead box protein K2;
DE AltName: Full=Cellular transcription factor ILF-1;
DE AltName: Full=Interleukin enhancer-binding factor 1;
GN Name=Foxk2; Synonyms=Ilf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6; TISSUE=Midbrain;
RA Wijchers P.J.E.C., van der Heidee L.P., van den Akker W.M.R.,
RA Adolfs Y., Durston A.J., Hoekman M.F.M., Burbach J.P.H., Smidt M.P.;
RT "Foxk2 is the mammalian homolog of yeast Fkh2, but is functionally
RT distinct.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-651 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
CC -!- FUNCTION: Recognizes the core sequence 5'-TAAACA-3'. Binds to
CC NFAT-like motifs (purine-rich) in the IL2 promoter (By
CC similarity).
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UCQ1-1; Sequence=Displayed;
CC Note=No experimental confirmation available;
CC Name=2;
CC IsoId=Q3UCQ1-2; Sequence=VSP_052236;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of adult brain
CC regions, namely the piriform cortex, the major islands of Calleja
CC and cells lining the lateral ventricles, the bed nucleus of stria
CC terminalis, the paraventricular thalamic nucleus, habenula and all
CC structures of the hippocampus. Also present in the hypothalamus,
CC cerebral cortex and in the Purkinje cell layer in the cerebellum.
CC Additionally expressed in dopamine neurons of the substantia and
CC more sparsely in the ventral tegmental area.
CC -!- DEVELOPMENTAL STAGE: At E12.5, expressed ubiquitously in the
CC developing central nervous system. This pattern persists at E14.5
CC and E16.5, with expression levels varying.
CC -!- DOMAIN: The C-terminal part of the DNA-binding domain may
CC contribute to DNA recognition specificity (By similarity).
CC -!- SIMILARITY: Contains 1 FHA domain.
CC -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
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DR EMBL; EU882160; ACG63496.1; -; mRNA.
DR EMBL; AL808021; CAM21743.1; -; Genomic_DNA.
DR EMBL; AK150439; BAE29561.1; -; mRNA.
DR IPI; IPI00808277; -.
DR IPI; IPI00854998; -.
DR RefSeq; NP_001074401.2; NM_001080932.2.
DR UniGene; Mm.209750; -.
DR HSSP; Q01167; 2C6Y.
DR ProteinModelPortal; Q3UCQ1; -.
DR SMR; Q3UCQ1; 247-344.
DR PhosphoSite; Q3UCQ1; -.
DR PaxDb; Q3UCQ1; -.
DR PRIDE; Q3UCQ1; -.
DR DNASU; 68837; -.
DR Ensembl; ENSMUST00000106113; ENSMUSP00000101719; ENSMUSG00000039275.
DR GeneID; 68837; -.
DR KEGG; mmu:68837; -.
DR UCSC; uc007mvs.1; mouse.
DR CTD; 3607; -.
DR MGI; MGI:1916087; Foxk2.
DR eggNOG; COG5025; -.
DR GeneTree; ENSGT00700000104094; -.
DR HOGENOM; HOG000072588; -.
DR HOVERGEN; HBG051649; -.
DR InParanoid; B5AZX0; -.
DR KO; K09404; -.
DR OMA; HGQVNNA; -.
DR OrthoDB; EOG4XD3QX; -.
DR NextBio; 328023; -.
DR ArrayExpress; Q3UCQ1; -.
DR Bgee; Q3UCQ1; -.
DR CleanEx; MM_FOXK2; -.
DR Genevestigator; Q3UCQ1; -.
DR GermOnline; ENSMUSG00000039275; Mus musculus.
DR GO; GO:0005667; C:transcription factor complex; IBA:RefGenome.
DR GO; GO:0008301; F:DNA binding, bending; IBA:RefGenome.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:RefGenome.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0003705; F:RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity; IBA:RefGenome.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IBA:RefGenome.
DR GO; GO:0009790; P:embryo development; IBA:RefGenome.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:RefGenome.
DR GO; GO:0007389; P:pattern specification process; IBA:RefGenome.
DR GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IBA:RefGenome.
DR GO; GO:0009888; P:tissue development; IBA:RefGenome.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_domain.
DR InterPro; IPR001766; TF_fork_head.
DR InterPro; IPR018122; TF_fork_head_CS.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00250; Fork_head; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SMAD_FHA; 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 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; DNA-binding; Magnesium;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription.
FT CHAIN 1 651 Forkhead box protein K2.
FT /FTId=PRO_0000261668.
FT DOMAIN 48 119 FHA.
FT DNA_BIND 249 344 Fork-head.
FT REGION 291 309 DNA-binding; major groove (By
FT similarity).
FT REGION 319 323 DNA-binding; minor groove (By
FT similarity).
FT REGION 339 344 DNA-binding; minor groove (By
FT similarity).
FT METAL 301 301 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 302 302 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 304 304 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 307 307 Magnesium; via carbonyl oxygen (By
FT similarity).
FT MOD_RES 24 24 Phosphoserine (By similarity).
FT MOD_RES 230 230 Phosphoserine (By similarity).
FT MOD_RES 389 389 Phosphoserine (By similarity).
FT MOD_RES 415 415 Phosphoserine (By similarity).
FT MOD_RES 419 419 Phosphoserine (By similarity).
FT VAR_SEQ 517 586 Missing (in isoform 2).
FT /FTId=VSP_052236.
FT CONFLICT 104 104 L -> M (in Ref. 3; BAE29561).
SQ SEQUENCE 651 AA; 68446 MW; DFD83C2A8EF52EF0 CRC64;
MAAAAALSGA GAPPAGGGAG GGGSPPGGWA VARLEGREFE YLMKKRSVTI GRNSSQGSVD
VSMGHSSFIS RRHLEIFTPP GGGHSAAAPE PAQPRPDAGG DFYLRCLGKN GVFVDGVFQR
RGAPPLQLPR VCTFRFPSTN IKITFTALSS EKREKQEAPE SPVKPVQPHI SPLTINIPDT
MAHLISPLPS PTGTISAANS CPSSPRGAGS SGYKVGRVMP SDLSLMADNS QPENEKEASG
GDSPKDDSKP PYSYAQLIVQ AITMAPDKQL TLNGIYTHIT KNYPYYRTAD KGWQNSIRHN
LSLNRYFIKV PRSQEEPGKG SFWRIDPASE SKLVEQAFRK RRPRGVPCFR TPLGPLSSRS
APASPNHAGV LSAHSSGAQT PESLSREGSP APLEPEPGAS QPKLAVIQEA RFAQSAPGSP
LSSQPVLITV QRQLPPAIKP VTYTVATPVT TPTSQPPVVQ TVHVVHQIPA VSVTSVAGLA
PANTYTVAGQ AVVTQAAVLA PPNPEPQENG DHREVRVKVE PVPAISPATL GAASRIIQTS
QGTPVQTVTI VQQAPLGQHQ LPIKTVTQNG AHVVPMPTAV HSQVNNAAAS PLHMLATHAS
ASASLPTKRQ NGDQAEQPEL KRVKAEDGES IVIALSVDAP PAAVREKAIQ N
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