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Q16520

- BATF_HUMAN

UniProt

Q16520 - BATF_HUMAN

Protein

Basic leucine zipper transcriptional factor ATF-like

Gene

BATF

Organism
Homo sapiens (Human)
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 By similarity.By similarity

    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
    SF-HT-activated gene 2 protein
    Short name:
    SFA-2
    Gene namesi
    Name:BATF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:958. BATF.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25268.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 125125Basic leucine zipper transcriptional factor ATF-likePRO_0000076595Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431PhosphoserineBy similarity
    Modified residuei48 – 481PhosphothreonineBy similarity

    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 By similarity.By similarity
    Phosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ16520.
    PaxDbiQ16520.
    PRIDEiQ16520.

    PTM databases

    PhosphoSiteiQ16520.

    Expressioni

    Tissue specificityi

    Expressed at highest levels in lung, and at lower levels in placenta, liver, kidney, spleen, and peripheral blood. Detected in SW480 colorectal cancer cell line and several hematopoietic tumor cell lines, including Raji Burkitt's lymphoma. Strongly expressed in mature B- and T-lymphocytes. Also expressed in moderate levels in lymph node and appendix and at low levels in thymus and bone marrow (PubMed:10777209).3 Publications

    Inductioni

    Up-regulated by PDCD1 following infection by HIV-1 virus, leading to inhibit T-cell functions and exhaust T-cells. Up-regulated by Epstein-Barr virus (EBV) protein EBNA2 following infection by EBV.2 Publications

    Gene expression databases

    ArrayExpressiQ16520.
    BgeeiQ16520.
    CleanExiHS_BATF.
    GenevestigatoriQ16520.

    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 By similarity. Also forms heterodimers with JUN and JUND. Also interacts with IFI35.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi115792. 18 interactions.
    IntActiQ16520. 4 interactions.
    MINTiMINT-1440747.
    STRINGi9606.ENSP00000286639.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16520.
    SMRiQ16520. Positions 32-77.
    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.
    HOGENOMiHOG000236325.
    HOVERGENiHBG039173.
    InParanoidiQ16520.
    KOiK09034.
    OMAiEEMKHFT.
    OrthoDBiEOG7H794S.
    PhylomeDBiQ16520.
    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.

    Q16520-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK    50
    ADTLHLESED LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST 100
    PSPPEVVYSA HAFHQPHVSS PRFQP 125
    Length:125
    Mass (Da):14,120
    Last modified:November 1, 1996 - v1
    Checksum:i7FD633C6F1963DF4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15460 mRNA. Translation: AAC50314.1.
    D42106 mRNA. Translation: BAA07686.1.
    AF016898 Genomic DNA. Translation: AAC78243.1.
    AC007182 Genomic DNA. Translation: AAD51372.1.
    BC032294 mRNA. Translation: AAH32294.1.
    CCDSiCCDS9843.1.
    PIRiJC4799.
    RefSeqiNP_006390.1. NM_006399.3.
    UniGeneiHs.509964.

    Genome annotation databases

    EnsembliENST00000286639; ENSP00000286639; ENSG00000156127.
    GeneIDi10538.
    KEGGihsa:10538.
    UCSCiuc001xrr.3. human.

    Polymorphism databases

    DMDMi32171340.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15460 mRNA. Translation: AAC50314.1 .
    D42106 mRNA. Translation: BAA07686.1 .
    AF016898 Genomic DNA. Translation: AAC78243.1 .
    AC007182 Genomic DNA. Translation: AAD51372.1 .
    BC032294 mRNA. Translation: AAH32294.1 .
    CCDSi CCDS9843.1.
    PIRi JC4799.
    RefSeqi NP_006390.1. NM_006399.3.
    UniGenei Hs.509964.

    3D structure databases

    ProteinModelPortali Q16520.
    SMRi Q16520. Positions 32-77.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115792. 18 interactions.
    IntActi Q16520. 4 interactions.
    MINTi MINT-1440747.
    STRINGi 9606.ENSP00000286639.

    PTM databases

    PhosphoSitei Q16520.

    Polymorphism databases

    DMDMi 32171340.

    Proteomic databases

    MaxQBi Q16520.
    PaxDbi Q16520.
    PRIDEi Q16520.

    Protocols and materials databases

    DNASUi 10538.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286639 ; ENSP00000286639 ; ENSG00000156127 .
    GeneIDi 10538.
    KEGGi hsa:10538.
    UCSCi uc001xrr.3. human.

    Organism-specific databases

    CTDi 10538.
    GeneCardsi GC14P075988.
    HGNCi HGNC:958. BATF.
    MIMi 612476. gene.
    neXtProti NX_Q16520.
    PharmGKBi PA25268.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG257556.
    HOGENOMi HOG000236325.
    HOVERGENi HBG039173.
    InParanoidi Q16520.
    KOi K09034.
    OMAi EEMKHFT.
    OrthoDBi EOG7H794S.
    PhylomeDBi Q16520.
    TreeFami TF332340.

    Miscellaneous databases

    GeneWikii BATF_(gene).
    GenomeRNAii 10538.
    NextBioi 39981.
    PROi Q16520.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16520.
    Bgeei Q16520.
    CleanExi HS_BATF.
    Genevestigatori Q16520.

    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. "B-ATF: a novel human bZIP protein that associates with members of the AP-1 transcription factor family."
      Dorsey M.J., Tae H.-J., Sollenberger K.G., Mascarenhas N.T., Johansen L.M., Taparowsky E.J.
      Oncogene 11:2255-2265(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH JUN PROTEINS, TISSUE SPECIFICITY.
    2. "SFA-2, a novel bZIP transcription factor induced by human T-cell leukemia virus type I, is highly expressed in mature lymphocytes."
      Hasegawa H., Utsunomiya Y., Kishimoto K., Tange Y., Yasukawa M., Fujita S.
      Biochem. Biophys. Res. Commun. 222:164-170(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    3. "Genomic organization of human B-ATF, a target for regulation by EBV and HTLV-1."
      Meyer N.P., Johansen L.M., Tae H.-J., Budde P.P., Williams K.L., Taparowsky E.J.
      Mamm. Genome 9:849-852(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Melanoma.
    6. "IFP 35 forms complexes with B-ATF, a member of the AP1 family of transcription factors."
      Wang X., Johansen L.M., Tae H.-J., Taparowsky E.J.
      Biochem. Biophys. Res. Commun. 229:316-322(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFI35.
    7. "B-ATF functions as a negative regulator of AP-1 mediated transcription and blocks cellular transformation by Ras and Fos."
      Echlin D.R., Tae H.-J., Mitin N., Taparowsky E.J.
      Oncogene 19:1752-1763(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. Cited for: INDUCTION.
    9. Cited for: INDUCTION.

    Entry informationi

    Entry nameiBATF_HUMAN
    AccessioniPrimary (citable) accession number: Q16520
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3