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Q01167

- FOXK2_HUMAN

UniProt

Q01167 - FOXK2_HUMAN

Protein

Forkhead box protein K2

Gene

FOXK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    Recognizes the core sequence 5'-TAAACA-3'. Binds to NFAT-like motifs (purine-rich) in the IL2 promoter. Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements.2 Publications

    Cofactori

    Binds 1 magnesium ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi310 – 3101Magnesium; via carbonyl oxygen
    Metal bindingi311 – 3111Magnesium; via carbonyl oxygen
    Metal bindingi313 – 3131Magnesium; via carbonyl oxygen
    Metal bindingi316 – 3161Magnesium; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi258 – 35396Fork-headPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    5. sequence-specific DNA binding Source: UniProtKB
    6. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    2. regulation of transcription, DNA-templated Source: UniProtKB
    3. regulation of transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Forkhead box protein K2
    Alternative name(s):
    Cellular transcription factor ILF-1
    FOXK1
    Interleukin enhancer-binding factor 1
    Gene namesi
    Name:FOXK2
    Synonyms:ILF, ILF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6036. FOXK2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi258 – 2581K → A: Decreases DNA-binding to 40%. 1 Publication
    Mutagenesisi300 – 3001K → A: Decreases DNA-binding to 20%. 1 Publication
    Mutagenesisi305 – 3051S → A: Decreases DNA-binding to 70%. 1 Publication
    Mutagenesisi307 – 3071R → A: Abolishes DNA-binding. 1 Publication
    Mutagenesisi328 – 3281K → A: Decreases DNA-binding to 25%. 1 Publication

    Organism-specific databases

    PharmGKBiPA29851.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 660659Forkhead box protein K2PRO_0000091858Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei30 – 301Phosphoserine1 Publication
    Modified residuei239 – 2391Phosphoserine1 Publication
    Modified residuei398 – 3981Phosphoserine3 Publications
    Modified residuei424 – 4241Phosphoserine1 Publication
    Modified residuei428 – 4281Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ01167.
    PaxDbiQ01167.
    PRIDEiQ01167.

    PTM databases

    PhosphoSiteiQ01167.

    Expressioni

    Tissue specificityi

    Expressed in both lymphoid and non-lymphoid cells.1 Publication

    Gene expression databases

    ArrayExpressiQ01167.
    BgeeiQ01167.
    CleanExiHS_FOXK2.
    GenevestigatoriQ01167.

    Organism-specific databases

    HPAiHPA027523.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IRF2P143162EBI-2509991,EBI-2866589

    Protein-protein interaction databases

    BioGridi109820. 7 interactions.
    IntActiQ01167. 9 interactions.
    MINTiMINT-1522265.
    STRINGi9606.ENSP00000335677.

    Structurei

    Secondary structure

    1
    660
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi263 – 27210
    Beta strandi277 – 2793
    Helixi281 – 29111
    Beta strandi295 – 2984
    Helixi300 – 31213
    Beta strandi316 – 3194
    Beta strandi324 – 3296
    Beta strandi331 – 3344
    Helixi336 – 34611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JXSNMR-A256-353[»]
    2C6YX-ray2.40A/B256-353[»]
    ProteinModelPortaliQ01167.
    SMRiQ01167. Positions 256-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01167.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 12875FHAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni300 – 31819DNA-binding; major grooveAdd
    BLAST
    Regioni328 – 3325DNA-binding; minor groove
    Regioni348 – 3536DNA-binding; minor groove

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 9384Gly-richAdd
    BLAST

    Domaini

    The C-terminal part of the DNA-binding domain may contribute to DNA recognition specificity.1 Publication

    Sequence similaritiesi

    Contains 1 FHA domain.PROSITE-ProRule annotation
    Contains 1 fork-head DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5025.
    HOGENOMiHOG000072588.
    HOVERGENiHBG051649.
    InParanoidiQ01167.
    KOiK09404.
    OMAiHGQVNNA.
    OrthoDBiEOG7CRTS2.
    PhylomeDBiQ01167.
    TreeFamiTF325718.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    2.60.200.20. 1 hit.
    InterProiIPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    IPR001766. TF_fork_head.
    IPR018122. TF_fork_head_CS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00498. FHA. 1 hit.
    PF00250. Fork_head. 1 hit.
    [Graphical view]
    PRINTSiPR00053. FORKHEAD.
    SMARTiSM00339. FH. 1 hit.
    SM00240. FHA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    PROSITEiPS50006. FHA_DOMAIN. 1 hit.
    PS00657. FORK_HEAD_1. 1 hit.
    PS00658. FORK_HEAD_2. 1 hit.
    PS50039. FORK_HEAD_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q01167-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAAAAALSG AGTPPAGGGA GGGGAGGGGS PPGGWAVARL EGREFEYLMK    50
    KRSVTIGRNS SQGSVDVSMG HSSFISRRHL EIFTPPGGGG HGGAAPELPP 100
    AQPRPDAGGD FYLRCLGKNG VFVDGVFQRR GAPPLQLPRV CTFRFPSTNI 150
    KITFTALSSE KREKQEASES PVKAVQPHIS PLTINIPDTM AHLISPLPSP 200
    TGTISAANSC PSSPRGAGSS GYKVGRVMPS DLNLMADNSQ PENEKEASGG 250
    DSPKDDSKPP YSYAQLIVQA ITMAPDKQLT LNGIYTHITK NYPYYRTADK 300
    GWQNSIRHNL SLNRYFIKVP RSQEEPGKGS FWRIDPASES KLIEQAFRKR 350
    RPRGVPCFRT PLGPLSSRSA PASPNHAGVL SAHSSGAQTP ESLSREGSPA 400
    PLEPEPGAAQ PKLAVIQEAR FAQSAPGSPL SSQPVLITVQ RQLPQAIKPV 450
    TYTVATPVTT STSQPPVVQT VHVVHQIPAV SVTSVAGLAP ANTYTVSGQA 500
    VVTPAAVLAP PKAEAQENGD HREVKVKVEP IPAIGHATLG TASRIIQTAQ 550
    TTPVQTVTIV QQAPLGQHQL PIKTVTQNGT HVASVPTAVH GQVNNAAASP 600
    LHMLATHASA SASLPTKRHN GDQPEQPELK RIKTEDGEGI VIALSVDTPP 650
    AAVREKGVQN 660
    Length:660
    Mass (Da):69,062
    Last modified:November 28, 2006 - v3
    Checksum:iE11C0B24370F1260
    GO
    Isoform 2 (identifier: Q01167-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         596-660: AAASPLHMLA...AAVREKGVQN → GPLGLRRPPCASSDWSCLS

    Show »
    Length:614
    Mass (Da):64,256
    Checksum:iF5BE52BA84587655
    GO
    Isoform 3 (identifier: Q01167-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         304-328: NSIRHNLSLNRYFIKVPRSQEEPGK → RGESFAHVGNTRIRIGLPAHKAPQR
         329-660: Missing.

    Show »
    Length:328
    Mass (Da):34,325
    Checksum:i4FCFB7F9FA67C9CA
    GO

    Sequence cautioni

    The sequence AAB02820.1 differs from that shown. Reason: The N-terminal sequence differs due to frameshifts and sequencing errors.
    The sequence AAB02821.1 differs from that shown. Reason: The N-terminal sequence differs due to frameshifts and sequencing errors.
    The sequence AAB02822.1 differs from that shown. Reason: The N-terminal sequence differs due to frameshifts and sequencing errors.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 120118AAAAA…LGKNG → Q in CAA43200. (PubMed:1909027)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei304 – 32825NSIRH…EEPGK → RGESFAHVGNTRIRIGLPAH KAPQR in isoform 3. CuratedVSP_001560Add
    BLAST
    Alternative sequencei329 – 660332Missing in isoform 3. CuratedVSP_001561Add
    BLAST
    Alternative sequencei596 – 66065AAASP…KGVQN → GPLGLRRPPCASSDWSCLS in isoform 2. 1 PublicationVSP_001559Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60787 mRNA. Translation: CAA43200.1.
    U58196 mRNA. Translation: AAB02820.1. Sequence problems.
    U58197 mRNA. Translation: AAB02821.1. Sequence problems.
    U58198 mRNA. Translation: AAB02822.1. Sequence problems.
    AC124287 Genomic DNA. No translation available.
    CCDSiCCDS11813.1. [Q01167-1]
    PIRiA41285.
    RefSeqiNP_004505.2. NM_004514.3. [Q01167-1]
    UniGeneiHs.591140.

    Genome annotation databases

    EnsembliENST00000335255; ENSP00000335677; ENSG00000141568. [Q01167-1]
    ENST00000473637; ENSP00000436108; ENSG00000141568. [Q01167-2]
    GeneIDi3607.
    KEGGihsa:3607.
    UCSCiuc002kfm.1. human. [Q01167-2]
    uc002kfn.3. human. [Q01167-1]
    uc010diu.3. human. [Q01167-3]

    Polymorphism databases

    DMDMi118572648.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60787 mRNA. Translation: CAA43200.1 .
    U58196 mRNA. Translation: AAB02820.1 . Sequence problems.
    U58197 mRNA. Translation: AAB02821.1 . Sequence problems.
    U58198 mRNA. Translation: AAB02822.1 . Sequence problems.
    AC124287 Genomic DNA. No translation available.
    CCDSi CCDS11813.1. [Q01167-1 ]
    PIRi A41285.
    RefSeqi NP_004505.2. NM_004514.3. [Q01167-1 ]
    UniGenei Hs.591140.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JXS NMR - A 256-353 [» ]
    2C6Y X-ray 2.40 A/B 256-353 [» ]
    ProteinModelPortali Q01167.
    SMRi Q01167. Positions 256-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109820. 7 interactions.
    IntActi Q01167. 9 interactions.
    MINTi MINT-1522265.
    STRINGi 9606.ENSP00000335677.

    PTM databases

    PhosphoSitei Q01167.

    Polymorphism databases

    DMDMi 118572648.

    Proteomic databases

    MaxQBi Q01167.
    PaxDbi Q01167.
    PRIDEi Q01167.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335255 ; ENSP00000335677 ; ENSG00000141568 . [Q01167-1 ]
    ENST00000473637 ; ENSP00000436108 ; ENSG00000141568 . [Q01167-2 ]
    GeneIDi 3607.
    KEGGi hsa:3607.
    UCSCi uc002kfm.1. human. [Q01167-2 ]
    uc002kfn.3. human. [Q01167-1 ]
    uc010diu.3. human. [Q01167-3 ]

    Organism-specific databases

    CTDi 3607.
    GeneCardsi GC17P080477.
    H-InvDB HIX0014279.
    HGNCi HGNC:6036. FOXK2.
    HPAi HPA027523.
    MIMi 147685. gene.
    neXtProti NX_Q01167.
    PharmGKBi PA29851.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5025.
    HOGENOMi HOG000072588.
    HOVERGENi HBG051649.
    InParanoidi Q01167.
    KOi K09404.
    OMAi HGQVNNA.
    OrthoDBi EOG7CRTS2.
    PhylomeDBi Q01167.
    TreeFami TF325718.

    Miscellaneous databases

    ChiTaRSi FOXK2. human.
    EvolutionaryTracei Q01167.
    GeneWikii FOXK2.
    GenomeRNAii 3607.
    NextBioi 14097.
    PROi Q01167.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01167.
    Bgeei Q01167.
    CleanExi HS_FOXK2.
    Genevestigatori Q01167.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    2.60.200.20. 1 hit.
    InterProi IPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    IPR001766. TF_fork_head.
    IPR018122. TF_fork_head_CS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00498. FHA. 1 hit.
    PF00250. Fork_head. 1 hit.
    [Graphical view ]
    PRINTSi PR00053. FORKHEAD.
    SMARTi SM00339. FH. 1 hit.
    SM00240. FHA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    PROSITEi PS50006. FHA_DOMAIN. 1 hit.
    PS00657. FORK_HEAD_1. 1 hit.
    PS00658. FORK_HEAD_2. 1 hit.
    PS50039. FORK_HEAD_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a cellular factor, interleukin binding factor, that binds to NFAT-like motifs in the human immunodeficiency virus long terminal repeat."
      Li C., Lai C., Sigman D.S., Gaynor R.B.
      Proc. Natl. Acad. Sci. U.S.A. 88:7739-7743(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Tissue: Cervix carcinoma.
    2. "Characterization and chromosomal mapping of the gene encoding the cellular DNA binding protein ILF."
      Li C., Lusis A.J., Sparkes R., Nirula A., Gaynor R.B.
      Genomics 13:665-671(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma and Lymphoid tissue.
    3. Nirula A., Moore D.J., Li C., Gaynor R.B.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION (ISOFORMS 1; 2 AND 3).
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-398; SER-424 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a)."
      Liu P.-P., Chen Y.-C., Li C., Hsieh Y.-H., Chen S.-W., Chen S.-H., Jeng W.-Y., Chuang W.-J.
      Proteins 49:543-553(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 256-353 (ISOFORM 1), DNA-BINDING.
    13. "Crystal structure of the human FOXK1a-DNA complex and its implications on the diverse binding specificity of winged helix/forkhead proteins."
      Tsai K.-L., Huang C.-Y., Chang C.-H., Sun Y.-J., Chuang W.-J., Hsiao C.-D.
      J. Biol. Chem. 281:17400-17409(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 256-353 (ISOFORM 1) IN COMPLEX WITH MAGNESIUM AND DUPLEX DNA, DNA-BINDING, COFACTOR, DOMAIN, MUTAGENESIS OF LYS-258; LYS-300; SER-305; ARG-307 AND LYS-328.

    Entry informationi

    Entry nameiFOXK2_HUMAN
    AccessioniPrimary (citable) accession number: Q01167
    Secondary accession number(s): A6NEP5
    , Q13622, Q13623, Q13624
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3