Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O35284

- BATF_MOUSE

UniProt

O35284 - BATF_MOUSE

Protein

Basic leucine zipper transcriptional factor ATF-like

Gene

Batf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8+ dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8+ dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8+ T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs.11 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. sequence-specific DNA binding Source: UniProtKB
    3. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. cytokine production Source: UniProtKB
    3. defense response to protozoan Source: UniProtKB
    4. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    5. hematopoietic stem cell differentiation Source: UniProtKB
    6. isotype switching Source: UniProtKB
    7. lymphoid progenitor cell differentiation Source: UniProtKB
    8. myeloid dendritic cell differentiation Source: UniProtKB
    9. T-helper 17 cell differentiation Source: UniProtKB
    10. T-helper 17 cell lineage commitment Source: UniProtKB
    11. T-helper 2 cell differentiation Source: UniProtKB
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Basic leucine zipper transcriptional factor ATF-like
    Alternative name(s):
    B-cell-activating transcription factor
    Short name:
    B-ATF
    Gene namesi
    Name:Batf
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1859147. Batf.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice are fertile and healthy. They display a normal thymus, spleen and lymph node development, and normal CD4+ and CD8+ T-cell development. They also show normal development of natural killer T-cells, B-cells, and conventional and plasmacytoid dendritic cells. They however show defects in T-helper 17 cells (Th17) differentiation and are resistant to experimental autoimmune encephalomyelitis. Loss of follicular T-helper cells (TfH), as well as less production of antibodies with switched isotypes in B-cells is also observed.4 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431S → A: Decreased phosphorylation; when associated with A-48. 1 Publication
    Mutagenesisi43 – 431S → D: Retains the ability to dimerize with JUNB and localization in the nucleus but abolishes DNA-binding. 1 Publication
    Mutagenesisi48 – 481T → A: Decreased phosphorylation; when associated with A-43. 1 Publication
    Mutagenesisi55 – 551H → Q: Impairs interaction with IRF4 and the recruitment of IRF4 to AICE motifs, leading to defects in mediate differentiation of Th17 cells. Loss of function; when associated with A-56; D-63 and K-77. 2 Publications
    Mutagenesisi56 – 561L → A: Loss of function; when associated with Q-55; D-63 and K-77. 1 Publication
    Mutagenesisi63 – 631K → D: Retains 50% of activity; when associated with 69-Q-T-70 and K-77. Loss of function; when associated with Q-55; A-56 and K-77. 1 Publication
    Mutagenesisi69 – 702RK → QT: Retains 50% of activity; when associated with D-63 and K-77.
    Mutagenesisi77 – 771E → K: Does not affect interaction with IRF4 and ability to mediate differentiation of Th17 cells. Retains 50% of activity; when associated with D63 and 69-Q-T-70. Loss of function; when associated with Q-55; A-56 and D-63. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 125125Basic leucine zipper transcriptional factor ATF-likePRO_0000076596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431Phosphoserine1 Publication
    Modified residuei48 – 481Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiO35284.

    PTM databases

    PhosphoSiteiO35284.

    Expressioni

    Tissue specificityi

    Detected in postnatal and adult lymphoid tissues such as thymus, spleen and lymph nodes. In thymus most concentrated expression is found in the immediate cortical layer. Differentially expressed during T-cell development in thymus. Highly expressed in Th17, Th1 and Th2 cells and in activated B-cells.3 Publications

    Inductioni

    Up-regulated by STAT3 in response to DNA damage. Induces by IL12 at late effector stage. Down-regulated by STAT5 in follicular T-helper cells (TfH).4 Publications

    Gene expression databases

    BgeeiO35284.
    GenevestigatoriO35284.

    Interactioni

    Subunit structurei

    Heterodimer; mainly heterodimerizes with JUNB. The BATF-JUNB heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP domain) with IRF4 and IRF8; the interaction is direct. Also forms heterodimers with JUN and JUND. Also Interacts with IFI35.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Irf4Q642877EBI-6398523,EBI-6398485

    Protein-protein interaction databases

    BioGridi207278. 1 interaction.
    IntActiO35284. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliO35284.
    SMRiO35284. Positions 31-77.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 8964bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni28 – 5023Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni54 – 7522Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the bZIP family.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG257556.
    GeneTreeiENSGT00390000016869.
    HOGENOMiHOG000236325.
    HOVERGENiHBG039173.
    InParanoidiA2RT86.
    KOiK09034.
    OMAiEEMKHFT.
    OrthoDBiEOG7H794S.
    PhylomeDBiO35284.
    TreeFamiTF332340.

    Family and domain databases

    InterProiIPR004827. bZIP.
    IPR000837. Leuzip_Fos.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    [Graphical view]
    PRINTSiPR00042. LEUZIPPRFOS.
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O35284-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPHSSDSSDS SFSRSPPPGK QDSSDDVRKV QRREKNRIAA QKSRQRQTQK    50
    ADTLHLESED LEKQNAALRK EIKQLTEELK YFTSVLSSHE PLCSVLASGT 100
    PSPPEVVYSA HAFHQPHISS PRFQP 125
    Length:125
    Mass (Da):14,065
    Last modified:January 1, 1998 - v1
    Checksum:iA23B00D6E0827938
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017021 mRNA. Translation: AAB70251.1.
    AK018587 mRNA. Translation: BAB31294.1.
    BC132410 mRNA. Translation: AAI32411.1.
    BC132412 mRNA. Translation: AAI32413.1.
    CCDSiCCDS26061.1.
    RefSeqiNP_058047.1. NM_016767.2.
    UniGeneiMm.6672.

    Genome annotation databases

    EnsembliENSMUST00000040536; ENSMUSP00000040706; ENSMUSG00000034266.
    GeneIDi53314.
    KEGGimmu:53314.
    UCSCiuc007ohd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017021 mRNA. Translation: AAB70251.1 .
    AK018587 mRNA. Translation: BAB31294.1 .
    BC132410 mRNA. Translation: AAI32411.1 .
    BC132412 mRNA. Translation: AAI32413.1 .
    CCDSi CCDS26061.1.
    RefSeqi NP_058047.1. NM_016767.2.
    UniGenei Mm.6672.

    3D structure databases

    ProteinModelPortali O35284.
    SMRi O35284. Positions 31-77.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207278. 1 interaction.
    IntActi O35284. 1 interaction.

    PTM databases

    PhosphoSitei O35284.

    Proteomic databases

    PRIDEi O35284.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040536 ; ENSMUSP00000040706 ; ENSMUSG00000034266 .
    GeneIDi 53314.
    KEGGi mmu:53314.
    UCSCi uc007ohd.1. mouse.

    Organism-specific databases

    CTDi 10538.
    MGIi MGI:1859147. Batf.

    Phylogenomic databases

    eggNOGi NOG257556.
    GeneTreei ENSGT00390000016869.
    HOGENOMi HOG000236325.
    HOVERGENi HBG039173.
    InParanoidi A2RT86.
    KOi K09034.
    OMAi EEMKHFT.
    OrthoDBi EOG7H794S.
    PhylomeDBi O35284.
    TreeFami TF332340.

    Miscellaneous databases

    NextBioi 310101.
    PROi O35284.
    SOURCEi Search...

    Gene expression databases

    Bgeei O35284.
    Genevestigatori O35284.

    Family and domain databases

    InterProi IPR004827. bZIP.
    IPR000837. Leuzip_Fos.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00042. LEUZIPPRFOS.
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of murine BATF: a negative regulator of activator protein-1 activity in the thymus."
      Williams K.L., Nanda I., Lyons G.E., Kuo C.T., Schmid M., Leiden J.M., Kaplan M.H., Taparowsky E.J.
      Eur. J. Immunol. 31:1620-1627(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    2. "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.
      Tissue: Cecum.
    3. "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].
      Tissue: Lung.
    4. "Stat3-dependent induction of BATF in M1 mouse myeloid leukemia cells."
      Senga T., Iwamoto T., Humphrey S.E., Yokota T., Taparowsky E.J., Hamaguchi M.
      Oncogene 21:8186-8191(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY STAT3.
    5. "Phosphorylation of BATF regulates DNA binding: a novel mechanism for AP-1 (activator protein-1) regulation."
      Deppmann C.D., Thornton T.M., Utama F.E., Taparowsky E.J.
      Biochem. J. 374:423-431(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH JUNB, PHOSPHORYLATION AT SER-43 AND THR-48, MUTAGENESIS OF SER-43 AND THR-48.
    6. "BATF transgenic mice reveal a role for activator protein-1 in NKT cell development."
      Williams K.L., Zullo A.J., Kaplan M.H., Brutkiewicz R.R., Deppmann C.D., Vinson C., Taparowsky E.J.
      J. Immunol. 170:2417-2426(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION WITH JUNB.
    8. "Batf coordinates multiple aspects of B and T cell function required for normal antibody responses."
      Betz B.C., Jordan-Williams K.L., Wang C., Kang S.G., Liao J., Logan M.R., Kim C.H., Taparowsky E.J.
      J. Exp. Med. 207:933-942(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    9. "The transcription factor BATF controls the global regulators of class-switch recombination in both B cells and T cells."
      Ise W., Kohyama M., Schraml B.U., Zhang T., Schwer B., Basu U., Alt F.W., Tang J., Oltz E.M., Murphy T.L., Murphy K.M.
      Nat. Immunol. 12:536-543(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE.
    10. "Transcription factor c-Maf mediates the TGF-beta-dependent suppression of IL-22 production in T(H)17 cells."
      Rutz S., Noubade R., Eidenschenk C., Ota N., Zeng W., Zheng Y., Hackney J., Ding J., Singh H., Ouyang W.
      Nat. Immunol. 12:1238-1245(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Basic leucine zipper transcription factor, ATF-like (BATF) regulates epigenetically and energetically effector CD8 T-cell differentiation via Sirt1 expression."
      Kuroda S., Yamazaki M., Abe M., Sakimura K., Takayanagi H., Iwai Y.
      Proc. Natl. Acad. Sci. U.S.A. 108:14885-14889(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, INDUCTION.
    12. Cited for: FUNCTION, INDUCTION BY STAT3.
    13. Cited for: FUNCTION.
    14. "STAT5 protein negatively regulates T follicular helper (Tfh) cell generation and function."
      Nurieva R.I., Podd A., Chen Y., Alekseev A.M., Yu M., Qi X., Huang H., Wen R., Wang J., Li H.S., Watowich S.S., Qi H., Dong C., Wang D.
      J. Biol. Chem. 287:11234-11239(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY STAT5.
    15. Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH IRF4; IRF8 AND JUNB, MUTAGENESIS OF HIS-55; LEU-56; LYS-63; 69-ARG-LYS-70 AND GLU-77.
    16. "BATF-JUN is critical for IRF4-mediated transcription in T cells."
      Li P., Spolski R., Liao W., Wang L., Murphy T.L., Murphy K.M., Leonard W.J.
      Nature 490:543-546(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH IRF4 AND JUNB.
    17. Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH IRF4 AND JUNB, MUTAGENESIS OF HIS-55 AND GLU-77.

    Entry informationi

    Entry nameiBATF_MOUSE
    AccessioniPrimary (citable) accession number: O35284
    Secondary accession number(s): A2RT86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3