AC T04793
XX
ID T04793
XX
DT 19.09.2001 (created); mas.
DT 09.06.2015 (updated); mkl.
CO Copyright (C), QIAGEN.
XX
FA Bach1
XX
SY BTB and CNC homolog 1; transcription regulator protein BACH1.
XX
OS mouse, Mus musculus
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae; murinae
XX
GE G002725 Bach1.
XX
CL C0008; bZIP; 1.1.1.2.5.
XX
SF 38% amino acid identity to Bach2 T04792 [1];
SF contains a BTB (Broad complex-Tramtrack-Bric-a-brac) domain and a CNC (Cap'n'collar) domain [1];
SF bZIP (basic leucine zipper) is of CNC-type which is characterized by an additional conserved region preceding bZIP domain [1];
SF BTB domain is important for (homo-)oligomer formation [1] [3];
SF BTB domain also seems to allow Bach1/MafK heterodimers to interact with each other [3];
SF obviously expressed from the earliest phase of hematopoietic cell development onwards [3];
SF binds porphyrin hemin (Kd of 140 nM) and also heme [4];
SF binding to hemin (heme) abolished if CP motifs (dipeptide of C and P) no. 3-6 act deleted (act together in a cooperative manner) [4];
SF hemin (heme) binding abolishes DNA-binding (e.g. heterodimer to site R01946) independent of presence of BTB-domain [4];
SF heme does not interfere with heterodimer formation with MafK T01435 [4];
SF hemin (heme) abolishes transcriptional repressor activity obviously via binding to the CP motifs [4];
XX
CP (embryo:) expressed at embryonic day 13 and probably day 10 and 17 [1]; expressed in fetal liver at embryonic day 13.5 [3]; (adult:) high levels in intestine [1]; expressed in liver [1], bone marrow, thymus [3]; lower levels in brain, spleen [1]; (adult cell types:) expressed in fractions of Ter-119, Mac-1 (mono-macrophage), Gr-1 (granulocyte), B220 (B cells), CD4/8-double positive cells (T cells) [3]; (cell lines:) expressed in C1300 (neuroblastoma), NIH 3T3, P815 (mastocytoma), FDCP-1 (bipotential myeloid progenitor) M1 (myelomonocytic leukemic) MEL (murine erythroleukemia), BW5147 cell lines [1] [1] [3].
EX bone marrow,,,adult; high; Northern blot; total RNA; [3].
EX brain,,,Theiler Stage 27; detectable; Northern blot; mRNA (poly-A); [1].
EX brain,,,adult; detectable; Northern blot; mRNA (poly-A); [1].
EX brain,,,adult; low; Northern blot; total RNA; [3].
EX heart,,,adult; detectable; Northern blot; mRNA (poly-A); [1].
EX kidney (right and left),,,adult; detectable; Northern blot; mRNA (poly-A); [1].
EX liver,,,Theiler Stage 21; very high; Northern blot; total RNA; [3].
EX liver,,,Theiler Stage 25; very low; Northern blot; mRNA (poly-A); [1].
EX liver,,,adult; detectable; Northern blot; mRNA (poly-A); [1].
EX mouse, Mus musculus,,,Theiler Stage 16; detectable; Northern blot; mRNA (poly-A); [1].
EX mouse, Mus musculus,,,Theiler Stage 21; detectable; Northern blot; mRNA (poly-A); [1].
EX mouse, Mus musculus,,,Theiler Stage 25; detectable; Northern blot; mRNA (poly-A); [1].
EX muscles,,,adult; detectable; Northern blot; mRNA (poly-A); [1].
EX small intestine,,,adult; very high; Northern blot; mRNA (poly-A); [1].
EX spleen,,,adult; medium; Northern blot; mRNA (poly-A); [1].
EX spleen,,,adult; medium; Northern blot; total RNA; [3].
EX thymus,,,adult; very high; Northern blot; total RNA; [3].
XX
FF may act as transcriptional repressor [1];
FF lacks functional transcriptional activation activity under certain conditions [3];
FF transactivates transcription of its own gene via MARE-like sequences probably not through direct binding to its promoter but through inactivating another repressing factor [2];
FF heterodimerization with MafK T01435 [1];
FF binds to DNA (beta-globin promotor R01946) with MafK T01435 in a cooperative manner [1];
FF binds also to DNA as homodimer [1];
FF competes with NF-E2 p45 (compare to ) for binding to heterodimeric partner MafK (compare to ) and to DNA (MARE sequence) [3];
XX
IN T01435 MafK; mouse, Mus musculus.
XX
MX M00495 V$BACH1_01.
MX M07374 V$BACH1_Q3.
MX M07296 V$MAF_Q4.
MX M00983 V$MAF_Q6_01.
XX
BS R65703.
BS R65701.
BS R32838.
BS R21670.
BS R11224.
BS R65711.
BS R34734.
XX
DR TRANSPATH: MO000028603.
DR UniProtKB: P97302;
XX
RN [1]; RE0016914.
RX PUBMED: 8887638.
RA Oyake T., Itoh K., Motohashi H., Hayashi N., Hoshino H., Nishizawa M., Yamamoto M., Igarashi K.
RT Bach proteins belong to a novel family of BTB-basic leucine zipper transcription factors that interact with MafK and regulate transcription through the NF-E2 site
RL Mol. Cell. Biol. 16:6083-6095 (1996).
RN [2]; RE0016916.
RX PUBMED: 11530014.
RA Sun J., Muto A., Hoshino H., Kobayashi A., Nishimura S., Yamamoto M., Hayashi N., Ito E., Igarashi K.
RT The Promoter of Mouse Transcription Repressor bach1 Is Regulated by Sp1 and Trans-Activated by Bach1
RL J. Biochem. 130:385-392 (2001).
RN [3]; RE0016917.
RX PUBMED: 9565602.
RA Igarashi K., Hoshino H., Muto A., Suwabe N., Nishikawa S., Nakauchi H., Yamamoto M.
RT Multivalent DNA binding complex generated by small Maf and Bach1 as a possible biochemical basis for beta-globin locus control region complex
RL J. Biol. Chem. 273:11783-11790 (1998).
RN [4]; RE0016931.
RX PUBMED: 11387216.
RA Ogawa K., Sun J., Taketani S., Nakajima O., Nishitani C., Sassa S., Hayashi N., Yamamoto M., Shibahara S., Fujita H., Igarashi K.
RT Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1
RL EMBO J. 20:2835-2843 (2001).
RN [5]; RE0022882.
RX PUBMED: 12356737.
RA Sun J., Hoshino H., Takaku K., Nakajima O., Muto A., Suzuki H., Tashiro S., Takahashi S., Shibahara S., Alam J., Taketo M. M., Yamamoto M., Igarashi K.
RT Hemoprotein Bach1 regulates enhancer availability of heme oxygenase-1 gene.
RL EMBO J. 21:5216-5224 (2002).
XX
//