ID   BACH1_HUMAN             Reviewed;         736 AA.
AC   O14867; O43285; Q6ICU0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   05-FEB-2025, entry version 217.
DE   RecName: Full=Transcription regulator protein BACH1 {ECO:0000305};
DE   AltName: Full=BTB and CNC homolog 1 {ECO:0000303|PubMed:9544839};
DE   AltName: Full=HA2303;
GN   Name=BACH1 {ECO:0000303|PubMed:9544839, ECO:0000312|HGNC:HGNC:935};
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].
RX   PubMed=9544839; DOI=10.1007/s004390050692;
RA   Blouin J.-L., Duriaux Sail G., Guipponi M., Rossier C., Pappasavas M.-P.,
RA   Antonarakis S.E.;
RT   "Isolation of the human BACH1 transcription regulator gene, which maps to
RT   chromosome 21q22.1.";
RL   Hum. Genet. 102:282-288(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9479503; DOI=10.1006/geno.1997.5080;
RA   Ohira M., Seki N., Nagase T., Ishikawa K., Nomura N., Ohara O.;
RT   "Characterization of a human homolog (BACH1) of the mouse Bach1 gene
RT   encoding a BTB-basic leucine zipper transcription factor and its mapping to
RT   chromosome 21q22.1.";
RL   Genomics 47:300-306(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J.,
RA   Schattevoy R., Yaspo M.-L., Rosenthal A.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Trachea {ECO:0000312|EMBL:BAG36528.1};
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-364 AND SER-445, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX   PubMed=24035498; DOI=10.1016/j.molcel.2013.08.018;
RA   Tan M.K., Lim H.J., Bennett E.J., Shi Y., Harper J.W.;
RT   "Parallel SCF adaptor capture proteomics reveals a role for SCFFBXL17 in
RT   NRF2 activation via BACH1 repressor turnover.";
RL   Mol. Cell 52:9-24(2013).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH FBXO22 AND FBXL17.
RX   PubMed=39504958; DOI=10.1016/j.cell.2024.10.012;
RA   Cao S., Garcia S.F., Shi H., James E.I., Kito Y., Shi H., Mao H.,
RA   Kaisari S., Rona G., Deng S., Goldberg H.V., Ponce J., Ueberheide B.,
RA   Lignitto L., Guttman M., Pagano M., Zheng N.;
RT   "Recognition of BACH1 quaternary structure degrons by two F-box proteins
RT   under oxidative stress.";
RL   Cell 0:0-0(2024).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 7-128.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of the bric-a-brac (BTB) domain of human BACH1.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Transcriptional regulator that acts as a repressor or
CC       activator, depending on the context. Binds to NF-E2 DNA binding sites.
CC       Plays important roles in coordinating transcription activation and
CC       repression by MAFK (By similarity). Together with MAF, represses the
CC       transcription of genes under the control of the NFE2L2 oxidative stress
CC       pathway (PubMed:24035498). {ECO:0000250|UniProtKB:P97302,
CC       ECO:0000269|PubMed:24035498, ECO:0000269|PubMed:39504958}.
CC   -!- SUBUNIT: Heterodimer of BACH1 and MAFK. {ECO:0000250|UniProtKB:P97302}.
CC   -!- INTERACTION:
CC       O14867; P15336: ATF2; NbExp=3; IntAct=EBI-1263541, EBI-1170906;
CC       O14867; P17544: ATF7; NbExp=3; IntAct=EBI-1263541, EBI-765623;
CC       O14867; P35638: DDIT3; NbExp=2; IntAct=EBI-1263541, EBI-742651;
CC       O14867; P63167: DYNLL1; NbExp=3; IntAct=EBI-1263541, EBI-349105;
CC       O14867; O75444: MAF; NbExp=2; IntAct=EBI-1263541, EBI-2805091;
CC       O14867; Q9Y5Q3: MAFB; NbExp=5; IntAct=EBI-1263541, EBI-3649340;
CC       O14867; Q9ULX9: MAFF; NbExp=6; IntAct=EBI-1263541, EBI-721128;
CC       O14867; O15525: MAFG; NbExp=8; IntAct=EBI-1263541, EBI-713514;
CC       O14867; O60260-5: PRKN; NbExp=3; IntAct=EBI-1263541, EBI-21251460;
CC       O14867; P40337-2: VHL; NbExp=3; IntAct=EBI-1263541, EBI-12157263;
CC       O14867; Q9DGW5: MDV005; Xeno; NbExp=2; IntAct=EBI-1263541, EBI-10889526;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC       ECO:0000269|PubMed:24035498}.
CC   -!- PTM: Ubiquitinated by the SCF(FBXL17) complex or by the by the
CC       SCF(FBXO22) complex, leading to its degradation by the proteasome.
CC       Under oxidative stress, reactive oxygen species covalently modify
CC       cysteine residues on the bZIP domain of BACH1 and release it from
CC       chromatin. If the BTB domain of BACH1 remains intact, its beta1-alpha6
CC       degron is recognized by FBXO22, promoting its ubiquitination and
CC       degradation. If the structural integrity of the beta1-alpha6 degron is
CC       compromised, FBXL17 will transiently associate with the BACH1 BTB dimer
CC       and remodel it into stably bound monomer for ubiquitination and
CC       degradation (PubMed:39504958). {ECO:0000269|PubMed:24035498,
CC       ECO:0000269|PubMed:39504958}.
CC   -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily. {ECO:0000305}.
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DR   EMBL; AF026199; AAB84100.1; -; mRNA.
DR   EMBL; AF026200; AAB84101.1; -; mRNA.
DR   EMBL; AB002803; BAA24932.1; -; mRNA.
DR   EMBL; AF124731; AAD14689.1; -; Genomic_DNA.
DR   EMBL; AK313791; BAG36528.1; -; mRNA.
DR   EMBL; CR450303; CAG29299.1; -; mRNA.
DR   EMBL; AL163249; CAB90435.1; -; Genomic_DNA.
DR   EMBL; AP001705; BAA95505.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09913.1; -; Genomic_DNA.
DR   EMBL; BC063307; AAH63307.1; -; mRNA.
DR   CCDS; CCDS13585.1; -.
DR   PIR; T00023; T00023.
DR   RefSeq; NP_001177.1; NM_001186.3.
DR   RefSeq; NP_996749.1; NM_206866.2.
DR   PDB; 2IHC; X-ray; 2.44 A; A/B/C/D=7-128.
DR   PDBsum; 2IHC; -.
DR   AlphaFoldDB; O14867; -.
DR   SMR; O14867; -.
DR   BioGRID; 107047; 108.
DR   ComplexPortal; CPX-2491; bZIP transcription factor complex, BACH1-FOS.
DR   ComplexPortal; CPX-2493; bZIP transcription factor complex, BACH1-MAFK.
DR   ComplexPortal; CPX-2494; bZIP transcription factor complex, BACH1-CREB1.
DR   ComplexPortal; CPX-2496; bZIP transcription factor complex, BACH1-DDIT3.
DR   ComplexPortal; CPX-2497; bZIP transcription factor complex, BACH1-MAFB.
DR   ComplexPortal; CPX-2500; bZIP transcription factor complex, BACH1-MAF.
DR   ComplexPortal; CPX-2720; bZIP transcription factor complex, BACH1-BACH1.
DR   ComplexPortal; CPX-2872; bZIP transcription factor complex, BACH1-MAFG.
DR   ComplexPortal; CPX-6402; bZIP transcription factor complex, ATF1-BACH1.
DR   ComplexPortal; CPX-6412; bZIP transcription factor complex, ATF2-BACH1.
DR   ComplexPortal; CPX-6781; bZIP transcription factor complex, ATF7-BACH1.
DR   ComplexPortal; CPX-7012; bZIP transcription factor complex, BACH1-BATF.
DR   ComplexPortal; CPX-7165; bZIP transcription factor complex, BACH1-MAFF.
DR   CORUM; O14867; -.
DR   DIP; DIP-24223N; -.
DR   IntAct; O14867; 74.
DR   MINT; O14867; -.
DR   STRING; 9606.ENSP00000382805; -.
DR   ChEMBL; CHEMBL4295651; -.
DR   iPTMnet; O14867; -.
DR   PhosphoSitePlus; O14867; -.
DR   BioMuta; BACH1; -.
DR   jPOST; O14867; -.
DR   MassIVE; O14867; -.
DR   PaxDb; 9606-ENSP00000382805; -.
DR   PeptideAtlas; O14867; -.
DR   ProteomicsDB; 48277; -.
DR   Pumba; O14867; -.
DR   Antibodypedia; 920; 466 antibodies from 39 providers.
DR   DNASU; 571; -.
DR   Ensembl; ENST00000286800.8; ENSP00000286800.3; ENSG00000156273.16.
DR   Ensembl; ENST00000399921.5; ENSP00000382805.1; ENSG00000156273.16.
DR   GeneID; 571; -.
DR   KEGG; hsa:571; -.
DR   MANE-Select; ENST00000286800.8; ENSP00000286800.3; NM_001186.4; NP_001177.1.
DR   UCSC; uc002ynj.4; human.
DR   AGR; HGNC:935; -.
DR   CTD; 571; -.
DR   DisGeNET; 571; -.
DR   GeneCards; BACH1; -.
DR   HGNC; HGNC:935; BACH1.
DR   HPA; ENSG00000156273; Tissue enhanced (bone).
DR   MIM; 602751; gene.
DR   neXtProt; NX_O14867; -.
DR   OpenTargets; ENSG00000156273; -.
DR   PharmGKB; PA25234; -.
DR   VEuPathDB; HostDB:ENSG00000156273; -.
DR   eggNOG; KOG3863; Eukaryota.
DR   GeneTree; ENSGT00940000158923; -.
DR   HOGENOM; CLU_015243_2_0_1; -.
DR   InParanoid; O14867; -.
DR   OMA; RRSECPW; -.
DR   OrthoDB; 6365358at2759; -.
DR   PhylomeDB; O14867; -.
DR   TreeFam; TF326681; -.
DR   BRENDA; 3.6.4.12; 2681.
DR   PathwayCommons; O14867; -.
DR   Reactome; R-HSA-9707587; Regulation of HMOX1 expression and activity.
DR   Reactome; R-HSA-9707616; Heme signaling.
DR   Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR   Reactome; R-HSA-9818027; NFE2L2 regulating anti-oxidant/detoxification enzymes.
DR   SignaLink; O14867; -.
DR   SIGNOR; O14867; -.
DR   BioGRID-ORCS; 571; 16 hits in 1215 CRISPR screens.
DR   ChiTaRS; BACH1; human.
DR   EvolutionaryTrace; O14867; -.
DR   GeneWiki; BACH1; -.
DR   GenomeRNAi; 571; -.
DR   Pharos; O14867; Tbio.
DR   PRO; PR:O14867; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; O14867; protein.
DR   Bgee; ENSG00000156273; Expressed in secondary oocyte and 180 other cell types or tissues.
DR   ExpressionAtlas; O14867; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA: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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; NAS:UniProtKB.
DR   GO; GO:0098531; F:ligand-activated transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IMP:CACAO.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0019222; P:regulation of metabolic process; NAS:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd18277; BTB_POZ_BACH1; 1.
DR   CDD; cd14719; bZIP_BACH; 1.
DR   FunFam; 1.10.880.10:FF:000002; transcription regulator protein BACH2 isoform X1; 1.
DR   FunFam; 3.30.710.10:FF:000033; transcription regulator protein BACH2 isoform X1; 1.
DR   Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1.
DR   Gene3D; 1.10.880.10; Transcription factor, Skn-1-like, DNA-binding domain; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR043321; bZIP_BACH.
DR   InterPro; IPR004826; bZIP_Maf.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   InterPro; IPR050457; ZnFinger_BTB_dom_contain.
DR   PANTHER; PTHR46105; AGAP004733-PA; 1.
DR   PANTHER; PTHR46105:SF1; TRANSCRIPTION REGULATOR PROTEIN BACH1; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF03131; bZIP_Maf; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..736
FT                   /note="Transcription regulator protein BACH1"
FT                   /id="PRO_0000076454"
FT   DOMAIN          34..100
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          557..620
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          286..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..578
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          582..589
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          680..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT   VARIANT         314
FT                   /note="S -> P (in dbSNP:rs35474725)"
FT                   /id="VAR_048441"
FT   CONFLICT        158
FT                   /note="S -> T (in Ref. 1; AAB84100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="E -> G (in Ref. 1; AAB84100)"
FT                   /evidence="ECO:0000305"
FT   STRAND          8..12
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   HELIX           16..30
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   HELIX           49..55
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   HELIX           57..63
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   HELIX           81..93
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   TURN            100..102
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   HELIX           103..113
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:2IHC"
FT   HELIX           120..124
FT                   /evidence="ECO:0007829|PDB:2IHC"
SQ   SEQUENCE   736 AA;  81958 MW;  CAAEECC63D46571B CRC64;
     MSLSENSVFA YESSVHSTNV LLSLNDQRKK DVLCDVTIFV EGQRFRAHRS VLAACSSYFH
     SRIVGQADGE LNITLPEEVT VKGFEPLIQF AYTAKLILSK ENVDEVCKCV EFLSVHNIEE
     SCFQFLKFKF LDSTADQQEC PRKKCFSSHC QKTDLKLSLL DQRDLETDEV EEFLENKNVQ
     TPQCKLRRYQ GNAKASPPLQ DSASQTYESM CLEKDAALAL PSLCPKYRKF QKAFGTDRVR
     TGESSVKDIH ASVQPNERSE NECLGGVPEC RDLQVMLKCD ESKLAMEPEE TKKDPASQCP
     TEKSEVTPFP HNSSIDPHGL YSLSLLHTYD QYGDLNFAGM QNTTVLTEKP LSGTDVQEKT
     FGESQDLPLK SDLGTREDSS VASSDRSSVE REVAEHLAKG FWSDICSTDT PCQMQLSPAV
     AKDGSEQISQ KRSECPWLGI RISESPEPGQ RTFTTLSSVN CPFISTLSTE GCSSNLEIGN
     DDYVSEPQQE PCPYACVISL GDDSETDTEG DSESCSAREQ ECEVKLPFNA QRIISLSRND
     FQSLLKMHKL TPEQLDCIHD IRRRSKNRIA AQRCRKRKLD CIQNLESEIE KLQSEKESLL
     KERDHILSTL GETKQNLTGL CQKVCKEAAL SQEQIQILAK YSAADCPLSF LISEKDKSTP
     DGELALPSIF SLSDRPPAVL PPCARGNSEP GYARGQESQQ MSTATSEQAG PAEQCRQSGG
     ISDFCQQMTD KCTTDE
//