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Basic leucine zipper transcriptional factor ATF-like (B-cell-activating transcription factor) (B-ATF)

 BATF_MOUSE              Reviewed;         125 AA.
O35284; A2RT86;
20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=Basic leucine zipper transcriptional factor ATF-like;
AltName: Full=B-cell-activating transcription factor;
Short=B-ATF;
Name=Batf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11466704;
DOI=10.1002/1521-4141(200105)31:5<1620::AID-IMMU1620>3.0.CO;2-3;
Williams K.L., Nanda I., Lyons G.E., Kuo C.T., Schmid M., Leiden J.M.,
Kaplan M.H., Taparowsky E.J.;
"Characterization of murine BATF: a negative regulator of activator
protein-1 activity in the thymus.";
Eur. J. Immunol. 31:1620-1627(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cecum;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INDUCTION BY STAT3.
PubMed=12444555; DOI=10.1038/sj.onc.1205918;
Senga T., Iwamoto T., Humphrey S.E., Yokota T., Taparowsky E.J.,
Hamaguchi M.;
"Stat3-dependent induction of BATF in M1 mouse myeloid leukemia
cells.";
Oncogene 21:8186-8191(2002).
[5]
SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH JUNB,
PHOSPHORYLATION AT SER-43 AND THR-48, AND MUTAGENESIS OF SER-43 AND
THR-48.
PubMed=12809553; DOI=10.1042/BJ20030455;
Deppmann C.D., Thornton T.M., Utama F.E., Taparowsky E.J.;
"Phosphorylation of BATF regulates DNA binding: a novel mechanism for
AP-1 (activator protein-1) regulation.";
Biochem. J. 374:423-431(2003).
[6]
FUNCTION.
PubMed=12594265; DOI=10.4049/jimmunol.170.5.2417;
Williams K.L., Zullo A.J., Kaplan M.H., Brutkiewicz R.R.,
Deppmann C.D., Vinson C., Taparowsky E.J.;
"BATF transgenic mice reveal a role for activator protein-1 in NKT
cell development.";
J. Immunol. 170:2417-2426(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, TISSUE SPECIFICITY,
DISRUPTION PHENOTYPE, AND INTERACTION WITH JUNB.
PubMed=19578362; DOI=10.1038/nature08114;
Schraml B.U., Hildner K., Ise W., Lee W.L., Smith W.A., Solomon B.,
Sahota G., Sim J., Mukasa R., Cemerski S., Hatton R.D., Stormo G.D.,
Weaver C.T., Russell J.H., Murphy T.L., Murphy K.M.;
"The AP-1 transcription factor Batf controls T(H)17 differentiation.";
Nature 460:405-409(2009).
[8]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=20421391; DOI=10.1084/jem.20091548;
Betz B.C., Jordan-Williams K.L., Wang C., Kang S.G., Liao J.,
Logan M.R., Kim C.H., Taparowsky E.J.;
"Batf coordinates multiple aspects of B and T cell function required
for normal antibody responses.";
J. Exp. Med. 207:933-942(2010).
[9]
FUNCTION, DNA-BINDING, AND DISRUPTION PHENOTYPE.
PubMed=21572431; DOI=10.1038/ni.2037;
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.;
"The transcription factor BATF controls the global regulators of
class-switch recombination in both B cells and T cells.";
Nat. Immunol. 12:536-543(2011).
[10]
FUNCTION.
PubMed=22001828; DOI=10.1038/ni.2134;
Rutz S., Noubade R., Eidenschenk C., Ota N., Zeng W., Zheng Y.,
Hackney J., Ding J., Singh H., Ouyang W.;
"Transcription factor c-Maf mediates the TGF-beta-dependent
suppression of IL-22 production in T(H)17 cells.";
Nat. Immunol. 12:1238-1245(2011).
[11]
DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=21873234; DOI=10.1073/pnas.1105133108;
Kuroda S., Yamazaki M., Abe M., Sakimura K., Takayanagi H., Iwai Y.;
"Basic leucine zipper transcription factor, ATF-like (BATF) regulates
epigenetically and energetically effector CD8 T-cell differentiation
via Sirt1 expression.";
Proc. Natl. Acad. Sci. U.S.A. 108:14885-14889(2011).
[12]
FUNCTION, AND INDUCTION BY STAT3.
PubMed=22385964; DOI=10.1016/j.cell.2012.01.040;
Wang J., Sun Q., Morita Y., Jiang H., Gross A., Lechel A., Hildner K.,
Guachalla L.M., Gompf A., Hartmann D., Schambach A., Wuestefeld T.,
Dauch D., Schrezenmeier H., Hofmann W.K., Nakauchi H., Ju Z.,
Kestler H.A., Zender L., Rudolph K.L.;
"A differentiation checkpoint limits hematopoietic stem cell self-
renewal in response to DNA damage.";
Cell 148:1001-1014(2012).
[13]
FUNCTION.
PubMed=23021777; DOI=10.1016/j.cell.2012.09.016;
Ciofani M., Madar A., Galan C., Sellars M., Mace K., Pauli F.,
Agarwal A., Huang W., Parkurst C.N., Muratet M., Newberry K.M.,
Meadows S., Greenfield A., Yang Y., Jain P., Kirigin F.K.,
Birchmeier C., Wagner E.F., Murphy K.M., Myers R.M., Bonneau R.,
Littman D.R.;
"A validated regulatory network for Th17 cell specification.";
Cell 151:289-303(2012).
[14]
INDUCTION BY STAT5.
PubMed=22318729; DOI=10.1074/jbc.M111.324046;
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.;
"STAT5 protein negatively regulates T follicular helper (Tfh) cell
generation and function.";
J. Biol. Chem. 287:11234-11239(2012).
[15]
FUNCTION, DNA-BINDING, INTERACTION WITH IRF4; IRF8 AND JUNB, AND
MUTAGENESIS OF HIS-55; LEU-56; LYS-63; 69-ARG-LYS-70 AND GLU-77.
PubMed=22992524; DOI=10.1038/nature11531;
Tussiwand R., Lee W.L., Murphy T.L., Mashayekhi M., Kc W.,
Albring J.C., Satpathy A.T., Rotondo J.A., Edelson B.T., Kretzer N.M.,
Wu X., Weiss L.A., Glasmacher E., Li P., Liao W., Behnke M., Lam S.S.,
Aurthur C.T., Leonard W.J., Singh H., Stallings C.L., Sibley L.D.,
Schreiber R.D., Murphy K.M.;
"Compensatory dendritic cell development mediated by BATF-IRF
interactions.";
Nature 490:502-507(2012).
[16]
FUNCTION, DNA-BINDING, AND INTERACTION WITH IRF4 AND JUNB.
PubMed=22992523; DOI=10.1038/nature11530;
Li P., Spolski R., Liao W., Wang L., Murphy T.L., Murphy K.M.,
Leonard W.J.;
"BATF-JUN is critical for IRF4-mediated transcription in T cells.";
Nature 490:543-546(2012).
[17]
FUNCTION, DNA-BINDING, INTERACTION WITH IRF4 AND JUNB, AND MUTAGENESIS
OF HIS-55 AND GLU-77.
PubMed=22983707; DOI=10.1126/science.1228309;
Glasmacher E., Agrawal S., Chang A.B., Murphy T.L., Zeng W.,
Vander Lugt B., Khan A.A., Ciofani M., Spooner C., Rutz S.,
Hackney J., Nurieva R., Escalante C.R., Ouyang W., Littman D.R.,
Murphy K.M., Singh H.;
"A genomic regulatory element that directs assembly and function of
immune-specific AP-1-IRF complexes.";
Science 338:975-980(2012).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:12594265,
ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391,
ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:22001828,
ECO:0000269|PubMed:22385964, ECO:0000269|PubMed:22983707,
ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524,
ECO:0000269|PubMed:23021777}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:12809553, ECO:0000269|PubMed:19578362,
ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523,
ECO:0000269|PubMed:22992524}.
-!- INTERACTION:
Q64287:Irf4; NbExp=7; IntAct=EBI-6398523, EBI-6398485;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Present in the
nucleus and cytoplasm, but shows increased nuclear translocation
after activation of T-cells.
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:19578362,
ECO:0000269|PubMed:20421391}.
-!- INDUCTION: 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). {ECO:0000269|PubMed:12444555,
ECO:0000269|PubMed:21873234, ECO:0000269|PubMed:22318729,
ECO:0000269|PubMed:22385964}.
-!- PTM: 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. {ECO:0000269|PubMed:12809553}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391,
ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:21873234}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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EMBL; AF017021; AAB70251.1; -; mRNA.
EMBL; AK018587; BAB31294.1; -; mRNA.
EMBL; BC132410; AAI32411.1; -; mRNA.
EMBL; BC132412; AAI32413.1; -; mRNA.
CCDS; CCDS26061.1; -.
RefSeq; NP_058047.1; NM_016767.2.
UniGene; Mm.6672; -.
ProteinModelPortal; O35284; -.
SMR; O35284; -.
BioGrid; 207278; 1.
IntAct; O35284; 1.
STRING; 10090.ENSMUSP00000040706; -.
iPTMnet; O35284; -.
PhosphoSitePlus; O35284; -.
EPD; O35284; -.
PaxDb; O35284; -.
PRIDE; O35284; -.
Ensembl; ENSMUST00000040536; ENSMUSP00000040706; ENSMUSG00000034266.
GeneID; 53314; -.
KEGG; mmu:53314; -.
UCSC; uc007ohd.1; mouse.
CTD; 10538; -.
MGI; MGI:1859147; Batf.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00390000016869; -.
HOGENOM; HOG000236325; -.
HOVERGEN; HBG039173; -.
InParanoid; O35284; -.
KO; K09034; -.
OMA; QKSRMRQ; -.
OrthoDB; EOG091G0YSM; -.
PhylomeDB; O35284; -.
TreeFam; TF332340; -.
PRO; PR:O35284; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000034266; -.
Genevisible; O35284; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0001816; P:cytokine production; IMP:UniProtKB.
GO; GO:0042832; P:defense response to protozoan; IMP:UniProtKB.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:UniProtKB.
GO; GO:0045190; P:isotype switching; IMP:UniProtKB.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IMP:UniProtKB.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:NTNU_SB.
GO; GO:0072539; P:T-helper 17 cell differentiation; IMP:UniProtKB.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; IMP:UniProtKB.
GO; GO:0045064; P:T-helper 2 cell differentiation; IMP:UniProtKB.
InterPro; IPR000837; AP-1.
InterPro; IPR029820; BATF.
InterPro; IPR004827; bZIP.
PANTHER; PTHR23351; PTHR23351; 1.
PANTHER; PTHR23351:SF14; PTHR23351:SF14; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00042; LEUZIPPRFOS.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; Differentiation; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 125 Basic leucine zipper transcriptional
factor ATF-like.
/FTId=PRO_0000076596.
DOMAIN 26 89 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 28 50 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 54 75 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000269|PubMed:12809553}.
MOD_RES 48 48 Phosphothreonine.
{ECO:0000269|PubMed:12809553}.
MUTAGEN 43 43 S->A: Decreased phosphorylation; when
associated with A-48.
{ECO:0000269|PubMed:12809553}.
MUTAGEN 43 43 S->D: Retains the ability to dimerize
with JUNB and localization in the nucleus
but abolishes DNA-binding.
{ECO:0000269|PubMed:12809553}.
MUTAGEN 48 48 T->A: Decreased phosphorylation; when
associated with A-43.
{ECO:0000269|PubMed:12809553}.
MUTAGEN 55 55 H->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. {ECO:0000269|PubMed:22983707,
ECO:0000269|PubMed:22992524}.
MUTAGEN 56 56 L->A: Loss of function; when associated
with Q-55; D-63 and K-77.
{ECO:0000269|PubMed:22992524}.
MUTAGEN 63 63 K->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.
{ECO:0000269|PubMed:22992524}.
MUTAGEN 69 70 RK->QT: Retains 50% of activity; when
associated with D-63 and K-77.
{ECO:0000269|PubMed:22992524}.
MUTAGEN 77 77 E->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.
{ECO:0000269|PubMed:22983707,
ECO:0000269|PubMed:22992524}.
SEQUENCE 125 AA; 14065 MW; A23B00D6E0827938 CRC64;
MPHSSDSSDS SFSRSPPPGK QDSSDDVRKV QRREKNRIAA QKSRQRQTQK ADTLHLESED
LEKQNAALRK EIKQLTEELK YFTSVLSSHE PLCSVLASGT PSPPEVVYSA HAFHQPHISS
PRFQP


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BAD BACH1 Gene BTB and CNC homology 1, basic leucine zipper transcription factor 1


 

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