BATF_HUMAN
ID BATF_HUMAN Reviewed; 125 AA.
AC Q16520;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Basic leucine zipper transcriptional factor ATF-like;
DE AltName: Full=B-cell-activating transcription factor;
DE Short=B-ATF;
DE AltName: Full=SF-HT-activated gene 2 protein;
DE Short=SFA-2;
GN Name=BATF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH JUN PROTEINS, AND TISSUE
RP SPECIFICITY.
RX PubMed=8570175;
RA Dorsey M.J., Tae H.-J., Sollenberger K.G., Mascarenhas N.T., Johansen L.M.,
RA Taparowsky E.J.;
RT "B-ATF: a novel human bZIP protein that associates with members of the AP-1
RT transcription factor family.";
RL Oncogene 11:2255-2265(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8630063; DOI=10.1006/bbrc.1996.0700;
RA Hasegawa H., Utsunomiya Y., Kishimoto K., Tange Y., Yasukawa M., Fujita S.;
RT "SFA-2, a novel bZIP transcription factor induced by human T-cell leukemia
RT virus type I, is highly expressed in mature lymphocytes.";
RL Biochem. Biophys. Res. Commun. 222:164-170(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9745044; DOI=10.1007/s003359900881;
RA Meyer N.P., Johansen L.M., Tae H.-J., Budde P.P., Williams K.L.,
RA Taparowsky E.J.;
RT "Genomic organization of human B-ATF, a target for regulation by EBV and
RT HTLV-1.";
RL Mamm. Genome 9:849-852(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH IFI35.
RX PubMed=8954125; DOI=10.1006/bbrc.1996.1799;
RA Wang X., Johansen L.M., Tae H.-J., Taparowsky E.J.;
RT "IFP 35 forms complexes with B-ATF, a member of the AP1 family of
RT transcription factors.";
RL Biochem. Biophys. Res. Commun. 229:316-322(1996).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=10777209; DOI=10.1038/sj.onc.1203491;
RA Echlin D.R., Tae H.-J., Mitin N., Taparowsky E.J.;
RT "B-ATF functions as a negative regulator of AP-1 mediated transcription and
RT blocks cellular transformation by Ras and Fos.";
RL Oncogene 19:1752-1763(2000).
RN [8]
RP INDUCTION.
RX PubMed=12719594; DOI=10.1128/jvi.77.10.6029-6040.2003;
RA Johansen L.M., Deppmann C.D., Erickson K.D., Coffin W.F. III,
RA Thornton T.M., Humphrey S.E., Martin J.M., Taparowsky E.J.;
RT "EBNA2 and activated Notch induce expression of BATF.";
RL J. Virol. 77:6029-6040(2003).
RN [9]
RP INDUCTION.
RX PubMed=20890291; DOI=10.1038/nm.2232;
RA Quigley M., Pereyra F., Nilsson B., Porichis F., Fonseca C., Eichbaum Q.,
RA Julg B., Jesneck J.L., Brosnahan K., Imam S., Russell K., Toth I.,
RA Piechocka-Trocha A., Dolfi D., Angelosanto J., Crawford A., Shin H.,
RA Kwon D.S., Zupkosky J., Francisco L., Freeman G.J., Wherry E.J.,
RA Kaufmann D.E., Walker B.D., Ebert B., Haining W.N.;
RT "Transcriptional analysis of HIV-specific CD8+ T cells shows that PD-1
RT inhibits T cell function by upregulating BATF.";
RL Nat. Med. 16:1147-1151(2010).
CC -!- FUNCTION: AP-1 family transcription factor that controls the
CC differentiation of lineage-specific cells in the immune system:
CC specifically mediates the differentiation of T-helper 17 cells (Th17),
CC follicular T-helper cells (TfH), CD8(+) dendritic cells and class-
CC switch recombination (CSR) in B-cells. Acts via the formation of a
CC heterodimer with JUNB that recognizes and binds DNA sequence 5'-
CC TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4
CC (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-
CC TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by
CC cooperative binding of BATF and IRF4 (or IRF8) and activation of genes.
CC Controls differentiation of T-helper cells producing interleukin-17
CC (Th17 cells) by binding to Th17-associated gene promoters: regulates
CC expression of the transcription factor RORC itself and RORC target
CC genes such as IL17 (IL17A or IL17B). Also involved in differentiation
CC of follicular T-helper cells (TfH) by directing expression of BCL6 and
CC MAF. In B-cells, involved in class-switch recombination (CSR) by
CC controlling the expression of both AICDA and of germline transcripts of
CC the intervening heavy-chain region and constant heavy-chain region
CC (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic
CC cell differentiation via interaction with IRF4 and IRF8 to mediate
CC cooperative gene activation. Regulates effector CD8(+) T-cell
CC differentiation by regulating expression of SIRT1. Following DNA
CC damage, part of a differentiation checkpoint that limits self-renewal
CC of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to
CC differentiation of HSCs, thereby restricting self-renewal of HSCs (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; mainly heterodimerizes with JUNB. The BATF-JUNB
CC heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP domain)
CC with IRF4 and IRF8; the interaction is direct (By similarity). Also
CC forms heterodimers with JUN and JUND. Also interacts with IFI35.
CC {ECO:0000250, ECO:0000269|PubMed:8570175, ECO:0000269|PubMed:8954125}.
CC -!- INTERACTION:
CC Q16520; P15336: ATF2; NbExp=2; IntAct=EBI-749503, EBI-1170906;
CC Q16520; P18847: ATF3; NbExp=2; IntAct=EBI-749503, EBI-712767;
CC Q16520; P18848: ATF4; NbExp=3; IntAct=EBI-749503, EBI-492498;
CC Q16520; P49715: CEBPA; NbExp=3; IntAct=EBI-749503, EBI-1172054;
CC Q16520; P17676: CEBPB; NbExp=2; IntAct=EBI-749503, EBI-969696;
CC Q16520; Q15744: CEBPE; NbExp=2; IntAct=EBI-749503, EBI-3907048;
CC Q16520; P53567: CEBPG; NbExp=4; IntAct=EBI-749503, EBI-740209;
CC Q16520; P10176: COX8A; NbExp=3; IntAct=EBI-749503, EBI-3904738;
CC Q16520; Q10586: DBP; NbExp=2; IntAct=EBI-749503, EBI-3908088;
CC Q16520; P35638: DDIT3; NbExp=8; IntAct=EBI-749503, EBI-742651;
CC Q16520; G5E9A7: DMWD; NbExp=3; IntAct=EBI-749503, EBI-10976677;
CC Q16520; P22607: FGFR3; NbExp=3; IntAct=EBI-749503, EBI-348399;
CC Q16520; P41250: GARS1; NbExp=3; IntAct=EBI-749503, EBI-724143;
CC Q16520; Q53GS7: GLE1; NbExp=3; IntAct=EBI-749503, EBI-1955541;
CC Q16520; Q9HD26: GOPC; NbExp=3; IntAct=EBI-749503, EBI-349832;
CC Q16520; P06396: GSN; NbExp=3; IntAct=EBI-749503, EBI-351506;
CC Q16520; Q16534: HLF; NbExp=2; IntAct=EBI-749503, EBI-2798854;
CC Q16520; P42858: HTT; NbExp=12; IntAct=EBI-749503, EBI-466029;
CC Q16520; P05412: JUN; NbExp=4; IntAct=EBI-749503, EBI-852823;
CC Q16520; P17275: JUNB; NbExp=32; IntAct=EBI-749503, EBI-748062;
CC Q16520; P17535: JUND; NbExp=2; IntAct=EBI-749503, EBI-2682803;
CC Q16520; O60333-2: KIF1B; NbExp=3; IntAct=EBI-749503, EBI-10975473;
CC Q16520; O43933: PEX1; NbExp=3; IntAct=EBI-749503, EBI-988601;
CC Q16520; P60891: PRPS1; NbExp=3; IntAct=EBI-749503, EBI-749195;
CC Q16520; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-749503, EBI-5235340;
CC Q16520; O76024: WFS1; NbExp=3; IntAct=EBI-749503, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC Cytoplasm {ECO:0000250}. Note=Present in the nucleus and cytoplasm, but
CC shows increased nuclear translocation after activation of T-cells.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in lung, and at lower
CC levels in placenta, liver, kidney, spleen, and peripheral blood.
CC Detected in SW480 colorectal cancer cell line and several hematopoietic
CC tumor cell lines, including Raji Burkitt's lymphoma. Strongly expressed
CC in mature B- and T-lymphocytes. Also expressed in moderate levels in
CC lymph node and appendix and at low levels in thymus and bone marrow
CC (PubMed:10777209). {ECO:0000269|PubMed:10777209,
CC ECO:0000269|PubMed:8570175, ECO:0000269|PubMed:8630063}.
CC -!- INDUCTION: Up-regulated by PDCD1 following infection by HIV-1 virus,
CC leading to inhibit T-cell functions and exhaust T-cells. Up-regulated
CC by Epstein-Barr virus (EBV) protein EBNA2 following infection by EBV.
CC {ECO:0000269|PubMed:12719594, ECO:0000269|PubMed:20890291}.
CC -!- PTM: Phosphorylated on serine and threonine residues and at least one
CC tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding
CC activity and transforms it as a negative regulator of AP-1 mediated
CC transcription (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; U15460; AAC50314.1; -; mRNA.
DR EMBL; D42106; BAA07686.1; -; mRNA.
DR EMBL; AF016898; AAC78243.1; -; Genomic_DNA.
DR EMBL; AC007182; AAD51372.1; -; Genomic_DNA.
DR EMBL; BC032294; AAH32294.1; -; mRNA.
DR CCDS; CCDS9843.1; -.
DR PIR; JC4799; JC4799.
DR RefSeq; NP_006390.1; NM_006399.3.
DR AlphaFoldDB; Q16520; -.
DR SMR; Q16520; -.
DR BioGRID; 115792; 21.
DR ComplexPortal; CPX-6413; bZIP transcription factor complex, ATF2-BATF.
DR ComplexPortal; CPX-6467; bZIP transcription factor complex, ATF3-BATF.
DR ComplexPortal; CPX-6522; bZIP transcription factor complex, ATF4-BATF.
DR ComplexPortal; CPX-6585; bZIP transcription factor complex, ATF5-BATF.
DR ComplexPortal; CPX-7002; bZIP transcription factor complex, BATF-BATF.
DR ComplexPortal; CPX-7003; bZIP transcription factor complex, BATF-JUNB.
DR ComplexPortal; CPX-7004; bZIP transcription factor complex, BATF-DDIT3.
DR ComplexPortal; CPX-7005; bZIP transcription factor complex, BATF-JUN.
DR ComplexPortal; CPX-7006; bZIP transcription factor complex, BATF-CEBPA.
DR ComplexPortal; CPX-7007; bZIP transcription factor complex, BATF-CEBPB.
DR ComplexPortal; CPX-7008; bZIP transcription factor complex, BATF-CEBPG.
DR ComplexPortal; CPX-7009; bZIP transcription factor complex, BATF-CEBPD.
DR ComplexPortal; CPX-7010; bZIP transcription factor complex, BATF-CEBPE.
DR ComplexPortal; CPX-7011; bZIP transcription factor complex, BATF-HLF.
DR ComplexPortal; CPX-7012; bZIP transcription factor complex, BACH1-BATF.
DR ComplexPortal; CPX-7013; bZIP transcription factor complex, BATF-JUND.
DR ComplexPortal; CPX-7014; bZIP transcription factor complex, BATF-DBP.
DR ComplexPortal; CPX-7015; bZIP transcription factor complex, BATF-NFE2L1.
DR ComplexPortal; CPX-7017; bZIP transcription factor complex, BATF-NFIL3.
DR ComplexPortal; CPX-7018; bZIP transcription factor complex, BATF-BATF3.
DR DIP; DIP-52482N; -.
DR IntAct; Q16520; 35.
DR MINT; Q16520; -.
DR STRING; 9606.ENSP00000286639; -.
DR GlyGen; Q16520; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16520; -.
DR PhosphoSitePlus; Q16520; -.
DR BioMuta; BATF; -.
DR DMDM; 32171340; -.
DR EPD; Q16520; -.
DR MassIVE; Q16520; -.
DR MaxQB; Q16520; -.
DR PaxDb; Q16520; -.
DR PeptideAtlas; Q16520; -.
DR PRIDE; Q16520; -.
DR ProteomicsDB; 60892; -.
DR Antibodypedia; 25838; 410 antibodies from 35 providers.
DR DNASU; 10538; -.
DR Ensembl; ENST00000286639.8; ENSP00000286639.6; ENSG00000156127.8.
DR GeneID; 10538; -.
DR KEGG; hsa:10538; -.
DR MANE-Select; ENST00000286639.8; ENSP00000286639.6; NM_006399.5; NP_006390.1.
DR UCSC; uc001xrr.4; human.
DR CTD; 10538; -.
DR DisGeNET; 10538; -.
DR GeneCards; BATF; -.
DR HGNC; HGNC:958; BATF.
DR HPA; ENSG00000156127; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 612476; gene.
DR neXtProt; NX_Q16520; -.
DR OpenTargets; ENSG00000156127; -.
DR PharmGKB; PA25268; -.
DR VEuPathDB; HostDB:ENSG00000156127; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000159745; -.
DR HOGENOM; CLU_088612_4_0_1; -.
DR InParanoid; Q16520; -.
DR OMA; CTGLTPQ; -.
DR OrthoDB; 1544557at2759; -.
DR PhylomeDB; Q16520; -.
DR TreeFam; TF332340; -.
DR PathwayCommons; Q16520; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; Q16520; -.
DR BioGRID-ORCS; 10538; 13 hits in 1088 CRISPR screens.
DR ChiTaRS; BATF; human.
DR GeneWiki; BATF_(gene); -.
DR GenomeRNAi; 10538; -.
DR Pharos; Q16520; Tbio.
DR PRO; PR:Q16520; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q16520; protein.
DR Bgee; ENSG00000156127; Expressed in granulocyte and 130 other tissues.
DR ExpressionAtlas; Q16520; baseline and differential.
DR Genevisible; Q16520; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0042832; P:defense response to protozoan; ISS:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:2000319; P:regulation of T-helper 17 cell differentiation; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072539; P:T-helper 17 cell differentiation; ISS:UniProtKB.
DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; ISS:UniProtKB.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR029820; BATF.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF14; PTHR23351:SF14; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Differentiation; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..125
FT /note="Basic leucine zipper transcriptional factor ATF-
FT like"
FT /id="PRO_0000076595"
FT DOMAIN 26..89
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..50
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 54..75
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35284"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35284"
SQ SEQUENCE 125 AA; 14120 MW; 7FD633C6F1963DF4 CRC64;
MPHSSDSSDS SFSRSPPPGK QDSSDDVRRV QRREKNRIAA QKSRQRQTQK ADTLHLESED
LEKQNAALRK EIKQLTEELK YFTSVLNSHE PLCSVLAAST PSPPEVVYSA HAFHQPHVSS
PRFQP
