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Database: UniProt
Entry: Q3UCQ1
LinkDB: Q3UCQ1
Original site: Q3UCQ1 
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   16-APR-2014, entry version 84.
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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION
RP   BY 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).
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   RefSeq; NP_001074401.2; NM_001080932.2.
DR   RefSeq; XP_006534145.1; XM_006534082.1.
DR   UniGene; Mm.209750; -.
DR   ProteinModelPortal; Q3UCQ1; -.
DR   SMR; Q3UCQ1; 35-141, 247-344.
DR   STRING; 10090.ENSMUSP00000101720; -.
DR   PhosphoSite; Q3UCQ1; -.
DR   PaxDb; Q3UCQ1; -.
DR   PRIDE; Q3UCQ1; -.
DR   DNASU; 68837; -.
DR   Ensembl; ENSMUST00000106113; ENSMUSP00000101719; ENSMUSG00000039275. [Q3UCQ1-1]
DR   GeneID; 68837; -.
DR   KEGG; mmu:68837; -.
DR   UCSC; uc007mvs.1; mouse. [Q3UCQ1-2]
DR   UCSC; uc011yjl.1; mouse. [Q3UCQ1-1]
DR   CTD; 3607; -.
DR   MGI; MGI:1916087; Foxk2.
DR   eggNOG; COG5025; -.
DR   GeneTree; ENSGT00750000117242; -.
DR   HOGENOM; HOG000072588; -.
DR   HOVERGEN; HBG051649; -.
DR   InParanoid; B5AZX0; -.
DR   KO; K09404; -.
DR   OMA; HGQVNNA; -.
DR   OrthoDB; EOG7CRTS2; -.
DR   TreeFam; TF325718; -.
DR   NextBio; 328023; -.
DR   PRO; PR:Q3UCQ1; -.
DR   Bgee; Q3UCQ1; -.
DR   CleanEx; MM_FOXK2; -.
DR   Genevestigator; Q3UCQ1; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008301; F:DNA binding, bending; IBA:RefGenome.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0009790; P:embryo development; IBA:RefGenome.
DR   GO; GO:0007389; P:pattern specification process; IBA:RefGenome.
DR   GO; GO:0009888; P:tissue development; IBA:RefGenome.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; 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   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.
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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