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Q60793

- KLF4_MOUSE

UniProt

Q60793 - KLF4_MOUSE

Protein

Krueppel-like factor 4

Gene

Klf4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri400 – 42425C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri430 – 45425C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri460 – 48223C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. core promoter proximal region sequence-specific DNA binding Source: Ensembl
    2. DNA binding Source: MGI
    3. double-stranded DNA binding Source: Ensembl
    4. metal ion binding Source: UniProtKB-KW
    5. phosphatidylinositol 3-kinase regulator activity Source: Ensembl
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    7. RNA polymerase II transcription factor binding Source: BHF-UCL
    8. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    9. sequence-specific DNA binding Source: MGI
    10. sequence-specific DNA binding transcription factor activity Source: MGI
    11. sequence-specific DNA binding transcription factor recruiting transcription factor activity Source: BHF-UCL
    12. transcription factor binding Source: UniProtKB
    13. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: MGI
    2. cellular response to cycloheximide Source: Ensembl
    3. cellular response to growth factor stimulus Source: Ensembl
    4. cellular response to hydrogen peroxide Source: Ensembl
    5. cellular response to peptide Source: Ensembl
    6. epidermal cell differentiation Source: MGI
    7. epidermis morphogenesis Source: MGI
    8. fat cell differentiation Source: BHF-UCL
    9. negative regulation of cell migration involved in sprouting angiogenesis Source: Ensembl
    10. negative regulation of cell proliferation Source: MGI
    11. negative regulation of chemokine (C-X-C motif) ligand 2 production Source: Ensembl
    12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    13. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
    14. negative regulation of heterotypic cell-cell adhesion Source: Ensembl
    15. negative regulation of interleukin-8 biosynthetic process Source: Ensembl
    16. negative regulation of muscle hyperplasia Source: Ensembl
    17. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    18. negative regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    19. negative regulation of protein kinase B signaling Source: Ensembl
    20. negative regulation of response to cytokine stimulus Source: Ensembl
    21. negative regulation of smooth muscle cell proliferation Source: Ensembl
    22. negative regulation of transcription, DNA-templated Source: UniProtKB
    23. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    24. positive regulation of hemoglobin biosynthetic process Source: Ensembl
    25. positive regulation of transcription, DNA-templated Source: UniProtKB
    26. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    27. post-embryonic camera-type eye development Source: MGI
    28. post-embryonic hemopoiesis Source: Ensembl
    29. regulation of cell differentiation Source: UniProtKB
    30. regulation of cell proliferation Source: MGI
    31. regulation of transcription from RNA polymerase II promoter Source: MGI
    32. response to organic substance Source: MGI
    33. response to retinoic acid Source: MGI
    34. stem cell maintenance Source: UniProtKB
    35. transcription from RNA polymerase II promoter Source: BHF-UCL

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_216222. Transcriptional regulation of pluripotent stem cells.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Krueppel-like factor 4
    Alternative name(s):
    Epithelial zinc finger protein EZF
    Gut-enriched krueppel-like factor
    Gene namesi
    Name:Klf4
    Synonyms:Ezf, Gklf, Zie
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1342287. Klf4.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nuclear chromatin Source: Ensembl
    2. nucleus Source: UniProtKB
    3. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Biotechnological usei

    POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes.2 Publications

    Disruption phenotypei

    Death shortly after birth due to loss of epidermal barrier function resulting from perturbation of late-stage epidermal differentiation structures including the cornified envelope. When selectively deleted in the surface ectoderm-derived structures of the eye, embryos develop normally and adults are viable and fertile but mutants display down-regulation of Krt12 and Aqp5 and multiple ocular defects including corneal epithelial fragility, stromal edema, defective lens and loss of conjunctival goblet cells.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 483483Krueppel-like factor 4PRO_0000047168Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki32 – 32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei251 – 2511PhosphoserineBy similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ60793.

    PTM databases

    PhosphoSiteiQ60793.

    Expressioni

    Tissue specificityi

    Highest expression in the colon. Lower levels in testis, lung and small intestine.

    Inductioni

    By interferon-gamma in Stat1-dependent manner.1 Publication

    Gene expression databases

    ArrayExpressiQ60793.
    BgeeiQ60793.
    CleanExiMM_KLF4.
    GenevestigatoriQ60793.

    Interactioni

    Subunit structurei

    Interacts with MUC1 (via the C-terminal domain) By similarity. Interacts with POU5F1/OCT4 and SOX2. Interacts with MEIS2 isoform MeisD and PBX1 isoform PBX1a.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi200966. 5 interactions.
    DIPiDIP-59920N.
    IntActiQ60793. 1 interaction.

    Structurei

    Secondary structure

    1
    483
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni405 – 4073
    Beta strandi410 – 4134
    Helixi414 – 4218
    Turni435 – 4373
    Beta strandi440 – 4434
    Helixi444 – 45512
    Beta strandi463 – 4664
    Beta strandi468 – 4714
    Helixi472 – 4787
    Helixi479 – 4824

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WBSX-ray1.70A395-483[»]
    2WBUX-ray2.50A396-483[»]
    4M9EX-ray1.85A396-483[»]
    ProteinModelPortaliQ60793.
    SMRiQ60793. Positions 397-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60793.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni443 – 47432Interaction with target DNAAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi176 – 385210Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 3 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri400 – 42425C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri430 – 45425C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri460 – 48223C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    GeneTreeiENSGT00750000117252.
    HOGENOMiHOG000060173.
    HOVERGENiHBG006220.
    InParanoidiQ78K30.
    KOiK17846.
    OMAiCTVGRPL.
    OrthoDBiEOG747PJ4.
    PhylomeDBiQ60793.
    TreeFamiTF350556.

    Family and domain databases

    Gene3Di3.30.160.60. 3 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 3 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60793-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRQPPGESDM AVSDALLPSF STFASGPAGR EKTLRPAGAP TNRWREELSH    50
    MKRLPPLPGR PYDLAATVAT DLESGGAGAA CSSNNPALLA RRETEEFNDL 100
    LDLDFILSNS LTHQESVAAT VTTSASASSS SSPASSGPAS APSTCSFSYP 150
    IRAGGDPGVA ASNTGGGLLY SRESAPPPTA PFNLADINDV SPSGGFVAEL 200
    LRPELDPVYI PPQQPQPPGG GLMGKFVLKA SLTTPGSEYS SPSVISVSKG 250
    SPDGSHPVVV APYSGGPPRM CPKIKQEAVP SCTVSRSLEA HLSAGPQLSN 300
    GHRPNTHDFP LGRQLPTRTT PTLSPEELLN SRDCHPGLPL PPGFHPHPGP 350
    NYPPFLPDQM QSQVPSLHYQ ELMPPGSCLP EEPKPKRGRR SWPRKRTATH 400
    TCDYAGCGKT YTKSSHLKAH LRTHTGEKPY HCDWDGCGWK FARSDELTRH 450
    YRKHTGHRPF QCQKCDRAFS RSDHLALHMK RHF 483
    Length:483
    Mass (Da):51,880
    Last modified:February 10, 2009 - v3
    Checksum:i5D1B0BF7948C49B3
    GO

    Sequence cautioni

    The sequence AAC52939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH10301.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621S → R in AAC52939. (PubMed:8940147)Curated
    Sequence conflicti185 – 1851A → G in AAC52939. (PubMed:8940147)Curated
    Sequence conflicti302 – 3021H → Q in BAE33205. (PubMed:16141072)Curated
    Sequence conflicti350 – 3501P → A in AAC52939. (PubMed:8940147)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20344 mRNA. Translation: AAC04892.1.
    U70662 mRNA. Translation: AAC52939.1. Different initiation.
    AF117109 Genomic DNA. Translation: AAD17223.1.
    AY071827 Genomic DNA. Translation: AAL60058.1.
    AK141244 mRNA. Translation: BAE24612.1.
    AK144942 mRNA. Translation: BAE26147.1.
    AK155343 mRNA. Translation: BAE33205.1.
    AL732494 Genomic DNA. Translation: CAM20848.1.
    CH466565 Genomic DNA. Translation: EDL02262.1.
    BC010301 mRNA. Translation: AAH10301.2. Different initiation.
    CCDSiCCDS18195.2.
    RefSeqiNP_034767.2. NM_010637.3.
    UniGeneiMm.4325.

    Genome annotation databases

    EnsembliENSMUST00000107619; ENSMUSP00000103245; ENSMUSG00000003032.
    GeneIDi16600.
    KEGGimmu:16600.
    UCSCiuc008sxk.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20344 mRNA. Translation: AAC04892.1 .
    U70662 mRNA. Translation: AAC52939.1 . Different initiation.
    AF117109 Genomic DNA. Translation: AAD17223.1 .
    AY071827 Genomic DNA. Translation: AAL60058.1 .
    AK141244 mRNA. Translation: BAE24612.1 .
    AK144942 mRNA. Translation: BAE26147.1 .
    AK155343 mRNA. Translation: BAE33205.1 .
    AL732494 Genomic DNA. Translation: CAM20848.1 .
    CH466565 Genomic DNA. Translation: EDL02262.1 .
    BC010301 mRNA. Translation: AAH10301.2 . Different initiation.
    CCDSi CCDS18195.2.
    RefSeqi NP_034767.2. NM_010637.3.
    UniGenei Mm.4325.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WBS X-ray 1.70 A 395-483 [» ]
    2WBU X-ray 2.50 A 396-483 [» ]
    4M9E X-ray 1.85 A 396-483 [» ]
    ProteinModelPortali Q60793.
    SMRi Q60793. Positions 397-483.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200966. 5 interactions.
    DIPi DIP-59920N.
    IntActi Q60793. 1 interaction.

    PTM databases

    PhosphoSitei Q60793.

    Proteomic databases

    PRIDEi Q60793.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000107619 ; ENSMUSP00000103245 ; ENSMUSG00000003032 .
    GeneIDi 16600.
    KEGGi mmu:16600.
    UCSCi uc008sxk.2. mouse.

    Organism-specific databases

    CTDi 9314.
    MGIi MGI:1342287. Klf4.

    Phylogenomic databases

    eggNOGi COG5048.
    GeneTreei ENSGT00750000117252.
    HOGENOMi HOG000060173.
    HOVERGENi HBG006220.
    InParanoidi Q78K30.
    KOi K17846.
    OMAi CTVGRPL.
    OrthoDBi EOG747PJ4.
    PhylomeDBi Q60793.
    TreeFami TF350556.

    Enzyme and pathway databases

    Reactomei REACT_216222. Transcriptional regulation of pluripotent stem cells.
    REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    EvolutionaryTracei Q60793.
    NextBioi 290177.
    PROi Q60793.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60793.
    Bgeei Q60793.
    CleanExi MM_KLF4.
    Genevestigatori Q60793.

    Family and domain databases

    Gene3Di 3.30.160.60. 3 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 3 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
    PS50157. ZINC_FINGER_C2H2_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a gene encoding a gut-enriched Kruppel-like factor expressed during growth arrest."
      Shields J.M., Christy R.J., Yang V.W.
      J. Biol. Chem. 271:20009-20017(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A gene for a novel zinc-finger protein expressed in differentiated epithelial cells and transiently in certain mesenchymal cells."
      Garrett-Sinha L.A., Eberspaecher H., Seldin M.F., de Crombrugghe B.
      J. Biol. Chem. 271:31384-31390(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X DBA/2.
      Tissue: Embryonic fibroblast.
    3. "Characterization of the structure and regulation of the murine gene encoding gut-enriched Kruppel-like factor (Kruppel-like factor 4)."
      Mahatan C.S., Kaestner K.H., Geiman D.E., Yang V.W.
      Nucleic Acids Res. 27:4562-4569(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: 129/SvJ.
    4. "STAT1 is required for IFN-gamma-mediated gut-enriched Kruppel-like factor expression."
      Chen Z.-Y., Shie J.-L., Tseng C.-C.
      Exp. Cell Res. 281:19-27(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: C57BL/6.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Dendritic cell, Embryonic stem cell and Mammary gland.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    9. "Klf4 is a transcription factor required for establishing the barrier function of the skin."
      Segre J.A., Bauer C., Fuchs E.
      Nat. Genet. 22:356-360(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    10. "Murine embryonic stem cell differentiation is promoted by SOCS-3 and inhibited by the zinc finger transcription factor Klf4."
      Li Y., McClintick J., Zhong L., Edenberg H.J., Yoder M.C., Chan R.J.
      Blood 105:635-637(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors."
      Takahashi K., Yamanaka S.
      Cell 126:663-676(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOTECHNOLOGY.
    12. "Klf4 cooperates with Oct3/4 and Sox2 to activate the Lefty1 core promoter in embryonic stem cells."
      Nakatake Y., Fukui N., Iwamatsu Y., Masui S., Takahashi K., Yagi R., Yagi K., Miyazaki J., Matoba R., Ko M.S., Niwa H.
      Mol. Cell. Biol. 26:7772-7782(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Conditional deletion of the mouse Klf4 gene results in corneal epithelial fragility, stromal edema, and loss of conjunctival goblet cells."
      Swamynathan S.K., Katz J.P., Kaestner K.H., Ashery-Padan R., Crawford M.A., Piatigorsky J.
      Mol. Cell. Biol. 27:182-194(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    14. "Klf4 interacts directly with Oct4 and Sox2 to promote reprogramming."
      Wei Z., Yang Y., Zhang P., Andrianakos R., Hasegawa K., Lyu J., Chen X., Bai G., Liu C., Pera M., Lu W.
      Stem Cells 27:2969-2978(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH POU5F1/OCT4 AND SOX2, BIOTECHNOLOGY.
    15. "Kruppel-like factor 4 (Klf4) prevents embryonic stem (ES) cell differentiation by regulating Nanog gene expression."
      Zhang P., Andrianakos R., Yang Y., Liu C., Lu W.
      J. Biol. Chem. 285:9180-9189(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Crystal structure in complex with DNA."
      Schuetz A., Zocher G., Carstanjen D., Heinemann U.
      Submitted (APR-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 395-483 IN COMPLEX WITH ZINC IONS AND DNA.

    Entry informationi

    Entry nameiKLF4_MOUSE
    AccessioniPrimary (citable) accession number: Q60793
    Secondary accession number(s): P70421
    , Q3U2D6, Q3URS6, Q78K30, Q9R255
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3