BACH2_HUMAN
ID BACH2_HUMAN Reviewed; 841 AA.
AC Q9BYV9; E1P518; Q59H70; Q5T793; Q9NTS5;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Transcription regulator protein BACH2;
DE AltName: Full=BTB and CNC homolog 2;
GN Name=BACH2;
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=10949928; DOI=10.1038/sj.onc.1203716;
RA Sasaki S., Ito E., Toki T., Maekawa T., Kanezaki R., Umenai T., Muto A.,
RA Nagai H., Kinoshita T., Yamamoto M., Inazawa J., Taketo M.M., Nakahata T.,
RA Igarashi K., Yokoyama M.;
RT "Cloning and expression of human B cell-specific transcription factor BACH2
RT mapped to chromosome 6q15.";
RL Oncogene 19:3739-3749(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11746976; DOI=10.1002/gcc.1200;
RA Vieira S.A.D., Deininger M.W.N., Sorour A., Sinclair P., Foroni L.,
RA Goldman J.M., Melo J.V.;
RT "Transcription factor BACH2 is transcriptionally regulated by the BCR/ABL
RT oncogene.";
RL Genes Chromosomes Cancer 32:353-363(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-521, AND MUTAGENESIS
RP OF SER-521.
RX PubMed=17018862; DOI=10.1182/blood-2005-12-040972;
RA Yoshida C., Yoshida F., Sears D.E., Hart S.M., Ikebe D., Muto A., Basu S.,
RA Igarashi K., Melo J.V.;
RT "Bcr-Abl signaling through the PI-3/S6 kinase pathway inhibits nuclear
RT translocation of the transcription factor Bach2, which represses the
RT antiapoptotic factor heme oxygenase-1.";
RL Blood 109:1211-1219(2007).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-382 AND LYS-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN IMD60, VARIANTS IMD60 PRO-24
RP AND LYS-788, AND CHARACTERIZATION OF VARIANTS IMD60 PRO-24 AND LYS-788.
RX PubMed=28530713; DOI=10.1038/ni.3753;
RA Afzali B., Groenholm J., Vandrovcova J., O'Brien C., Sun H.W.,
RA Vanderleyden I., Davis F.P., Khoder A., Zhang Y., Hegazy A.N.,
RA Villarino A.V., Palmer I.W., Kaufman J., Watts N.R., Kazemian M.,
RA Kamenyeva O., Keith J., Sayed A., Kasperaviciute D., Mueller M.,
RA Hughes J.D., Fuss I.J., Sadiyah M.F., Montgomery-Recht K., McElwee J.,
RA Restifo N.P., Strober W., Linterman M.A., Wingfield P.T., Uhlig H.H.,
RA Roychoudhuri R., Aitman T.J., Kelleher P., Lenardo M.J., O'Shea J.J.,
RA Cooper N., Laurence A.D.J.;
RT "BACH2 immunodeficiency illustrates an association between super-enhancers
RT and haploinsufficiency.";
RL Nat. Immunol. 18:813-823(2017).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 9-129, SUBUNIT, AND INTERCHAIN
RP DISULFIDE BOND.
RX PubMed=22194330; DOI=10.1107/s0907444911048335;
RA Rosbrook G.O., Stead M.A., Carr S.B., Wright S.C.;
RT "The structure of the Bach2 POZ-domain dimer reveals an intersubunit
RT disulfide bond.";
RL Acta Crystallogr. D 68:26-34(2012).
CC -!- FUNCTION: Transcriptional regulator that acts as repressor or activator
CC (By similarity). Binds to Maf recognition elements (MARE) (By
CC similarity). Plays an important role in coordinating transcription
CC activation and repression by MAFK (By similarity). Induces apoptosis in
CC response to oxidative stress through repression of the antiapoptotic
CC factor HMOX1 (PubMed:17018862). Positively regulates the nuclear import
CC of actin (By similarity). Is a key regulator of adaptive immunity,
CC crucial for the maintenance of regulatory T-cell function and B-cell
CC maturation (PubMed:28530713). {ECO:0000250|UniProtKB:P97303,
CC ECO:0000269|PubMed:17018862, ECO:0000269|PubMed:28530713}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:22194330). Heterodimer of
CC BACH2 and Maf-related transcription factors (By similarity).
CC {ECO:0000250|UniProtKB:P97303, ECO:0000269|PubMed:22194330}.
CC -!- INTERACTION:
CC Q9BYV9; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-1642333, EBI-14493093;
CC Q9BYV9; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-1642333, EBI-541426;
CC Q9BYV9; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-1642333, EBI-742750;
CC Q9BYV9; Q9NR55: BATF3; NbExp=5; IntAct=EBI-1642333, EBI-10312707;
CC Q9BYV9; Q9HC52: CBX8; NbExp=3; IntAct=EBI-1642333, EBI-712912;
CC Q9BYV9; Q8N715: CCDC185; NbExp=3; IntAct=EBI-1642333, EBI-740814;
CC Q9BYV9; Q6IPU0: CENPP; NbExp=3; IntAct=EBI-1642333, EBI-10250303;
CC Q9BYV9; Q5T655: CFAP58; NbExp=3; IntAct=EBI-1642333, EBI-10245749;
CC Q9BYV9; Q9UBR2: CTSZ; NbExp=3; IntAct=EBI-1642333, EBI-8636823;
CC Q9BYV9; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-1642333, EBI-5453285;
CC Q9BYV9; Q14241: ELOA; NbExp=3; IntAct=EBI-1642333, EBI-742350;
CC Q9BYV9; Q6UWV6: ENPP7; NbExp=3; IntAct=EBI-1642333, EBI-12047821;
CC Q9BYV9; Q3B820: FAM161A; NbExp=3; IntAct=EBI-1642333, EBI-719941;
CC Q9BYV9; O95363: FARS2; NbExp=3; IntAct=EBI-1642333, EBI-2513774;
CC Q9BYV9; P15408: FOSL2; NbExp=4; IntAct=EBI-1642333, EBI-3893419;
CC Q9BYV9; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-1642333, EBI-740641;
CC Q9BYV9; Q6ZSG2: INSYN2A; NbExp=3; IntAct=EBI-1642333, EBI-12146621;
CC Q9BYV9; Q92993: KAT5; NbExp=3; IntAct=EBI-1642333, EBI-399080;
CC Q9BYV9; Q9P127: LUZP4; NbExp=3; IntAct=EBI-1642333, EBI-10198848;
CC Q9BYV9; Q9ULX9: MAFF; NbExp=3; IntAct=EBI-1642333, EBI-721128;
CC Q9BYV9; O15525: MAFG; NbExp=5; IntAct=EBI-1642333, EBI-713514;
CC Q9BYV9; O60675: MAFK; NbExp=3; IntAct=EBI-1642333, EBI-2559512;
CC Q9BYV9; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-1642333, EBI-348259;
CC Q9BYV9; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-1642333, EBI-8852072;
CC Q9BYV9; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-1642333, EBI-398874;
CC Q9BYV9; P62195: PSMC5; NbExp=3; IntAct=EBI-1642333, EBI-357745;
CC Q9BYV9; P32969: RPL9P9; NbExp=3; IntAct=EBI-1642333, EBI-358122;
CC Q9BYV9; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-1642333, EBI-366570;
CC Q9BYV9; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-1642333, EBI-748391;
CC Q9BYV9; O75387: SLC43A1; NbExp=3; IntAct=EBI-1642333, EBI-9661945;
CC Q9BYV9; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-1642333, EBI-8463848;
CC Q9BYV9; Q15560: TCEA2; NbExp=3; IntAct=EBI-1642333, EBI-710310;
CC Q9BYV9; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-1642333, EBI-3650647;
CC Q9BYV9; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-1642333, EBI-5235829;
CC Q9BYV9; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-1642333, EBI-10687282;
CC Q9BYV9; O75386: TULP3; NbExp=4; IntAct=EBI-1642333, EBI-5357290;
CC Q9BYV9; O43167: ZBTB24; NbExp=3; IntAct=EBI-1642333, EBI-744471;
CC Q9BYV9; Q8NCN2: ZBTB34; NbExp=3; IntAct=EBI-1642333, EBI-11317716;
CC Q9BYV9; Q15973: ZNF124; NbExp=3; IntAct=EBI-1642333, EBI-2555767;
CC Q9BYV9; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-1642333, EBI-11962468;
CC Q9BYV9; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-1642333, EBI-10251462;
CC Q9BYV9; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-1642333, EBI-10240849;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17018862,
CC ECO:0000269|PubMed:28530713}. Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00978, ECO:0000269|PubMed:17018862,
CC ECO:0000269|PubMed:28530713}. Note=Nucleocytoplasmic shuttling is
CC controlled by phosphorylation. {ECO:0000269|PubMed:17018862}.
CC -!- TISSUE SPECIFICITY: B-cell specific.
CC -!- PTM: Phosphorylation at Ser-521 downstream of the PI-3K pathway
CC promotes nuclear export. {ECO:0000269|PubMed:17018862}.
CC -!- PTM: The reversible disulfide bond may provide a mechanism to regulate
CC the activity in oxidative stress responses.
CC {ECO:0000269|PubMed:22194330}.
CC -!- DISEASE: Immunodeficiency 60 and autoimmunity (IMD60) [MIM:618394]: An
CC autosomal dominant primary immunologic disorder characterized by
CC intestinal inflammation, recurrent sino-pulmonary infections, impaired
CC lymphocyte maturation, and variably decreased immunoglobulin
CC production. {ECO:0000269|PubMed:28530713}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the bZIP family. CNC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92126.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BACH2ID741ch6q15.html";
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DR EMBL; AF357835; AAK48898.1; -; mRNA.
DR EMBL; AJ271878; CAC28130.1; -; mRNA.
DR EMBL; AB208889; BAD92126.1; ALT_INIT; mRNA.
DR EMBL; AL353692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48530.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48531.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48532.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48533.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48534.1; -; Genomic_DNA.
DR CCDS; CCDS5026.1; -.
DR RefSeq; NP_001164265.1; NM_001170794.1.
DR RefSeq; NP_068585.1; NM_021813.3.
DR RefSeq; XP_005248816.1; XM_005248759.4.
DR RefSeq; XP_011534341.1; XM_011536039.2.
DR RefSeq; XP_011534342.1; XM_011536040.2.
DR RefSeq; XP_016866654.1; XM_017011165.1.
DR RefSeq; XP_016866655.1; XM_017011166.1.
DR PDB; 3OHU; X-ray; 2.10 A; A/B/C/D/E/F=9-129.
DR PDB; 3OHV; X-ray; 2.20 A; A/B/C/D/E/F=9-129.
DR PDBsum; 3OHU; -.
DR PDBsum; 3OHV; -.
DR AlphaFoldDB; Q9BYV9; -.
DR SMR; Q9BYV9; -.
DR BioGRID; 121913; 82.
DR ComplexPortal; CPX-2471; bZIP transcription factor complex, BACH2-NFE2L3.
DR ComplexPortal; CPX-2473; bZIP transcription factor complex, BACH2-NFE2L1.
DR ComplexPortal; CPX-2479; bZIP transcription factor complex, BACH2-MAFB.
DR ComplexPortal; CPX-2482; bZIP transcription factor complex, BACH2-MAFK.
DR ComplexPortal; CPX-2483; bZIP transcription factor complex, BACH2-MAF.
DR ComplexPortal; CPX-2484; bZIP transcription factor complex, BACH2-MAFF.
DR ComplexPortal; CPX-2485; bZIP transcription factor complex, BACH2-MAFG.
DR ComplexPortal; CPX-2487; bZIP transcription factor complex, BACH2-BACH2.
DR ComplexPortal; CPX-7093; bZIP transcription factor complex, BACH2-BATF3.
DR IntAct; Q9BYV9; 49.
DR STRING; 9606.ENSP00000257749; -.
DR GlyGen; Q9BYV9; 9 sites, 2 O-linked glycans (9 sites).
DR iPTMnet; Q9BYV9; -.
DR PhosphoSitePlus; Q9BYV9; -.
DR BioMuta; BACH2; -.
DR DMDM; 17433037; -.
DR jPOST; Q9BYV9; -.
DR MassIVE; Q9BYV9; -.
DR MaxQB; Q9BYV9; -.
DR PaxDb; Q9BYV9; -.
DR PeptideAtlas; Q9BYV9; -.
DR PRIDE; Q9BYV9; -.
DR ProteomicsDB; 79726; -.
DR Antibodypedia; 31919; 243 antibodies from 30 providers.
DR DNASU; 60468; -.
DR Ensembl; ENST00000257749.9; ENSP00000257749.4; ENSG00000112182.15.
DR Ensembl; ENST00000343122.7; ENSP00000345642.3; ENSG00000112182.15.
DR Ensembl; ENST00000537989.5; ENSP00000437473.1; ENSG00000112182.15.
DR GeneID; 60468; -.
DR KEGG; hsa:60468; -.
DR MANE-Select; ENST00000257749.9; ENSP00000257749.4; NM_021813.4; NP_068585.1.
DR UCSC; uc003pnw.4; human.
DR CTD; 60468; -.
DR DisGeNET; 60468; -.
DR GeneCards; BACH2; -.
DR HGNC; HGNC:14078; BACH2.
DR HPA; ENSG00000112182; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; BACH2; -.
DR MIM; 605394; gene.
DR MIM; 618394; phenotype.
DR neXtProt; NX_Q9BYV9; -.
DR OpenTargets; ENSG00000112182; -.
DR PharmGKB; PA25235; -.
DR VEuPathDB; HostDB:ENSG00000112182; -.
DR eggNOG; KOG3863; Eukaryota.
DR GeneTree; ENSGT00940000158228; -.
DR HOGENOM; CLU_015243_0_0_1; -.
DR InParanoid; Q9BYV9; -.
DR OMA; ESMQCCS; -.
DR OrthoDB; 521871at2759; -.
DR PhylomeDB; Q9BYV9; -.
DR TreeFam; TF326681; -.
DR PathwayCommons; Q9BYV9; -.
DR SignaLink; Q9BYV9; -.
DR SIGNOR; Q9BYV9; -.
DR BioGRID-ORCS; 60468; 12 hits in 1130 CRISPR screens.
DR ChiTaRS; BACH2; human.
DR EvolutionaryTrace; Q9BYV9; -.
DR GeneWiki; BACH2; -.
DR GenomeRNAi; 60468; -.
DR Pharos; Q9BYV9; Tbio.
DR PRO; PR:Q9BYV9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BYV9; protein.
DR Bgee; ENSG00000112182; Expressed in cortical plate and 172 other tissues.
DR ExpressionAtlas; Q9BYV9; baseline and differential.
DR Genevisible; Q9BYV9; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
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; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0051170; P:import into nucleus; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0090721; P:primary adaptive immune response involving T cells and B cells; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd14719; bZIP_BACH; 1.
DR Gene3D; 3.30.710.10; -; 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 Pfam; PF00651; BTB; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57959; SSF57959; 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; Cytoplasm; Disease variant; Disulfide bond;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..841
FT /note="Transcription regulator protein BACH2"
FT /id="PRO_0000076456"
FT DOMAIN 37..103
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 646..709
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 153..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..667
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 671..678
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 777..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 821..841
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 246..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97303"
FT MOD_RES 521
FT /note="Phosphoserine; by RPS6KB1"
FT /evidence="ECO:0000269|PubMed:17018862"
FT DISULFID 20
FT /note="Interchain; redox-active"
FT /evidence="ECO:0000269|PubMed:22194330"
FT CROSSLNK 382
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 24
FT /note="L -> P (in IMD60; impairs protein stability; the
FT mutant is unsoluble and forms multiple aggregates)"
FT /evidence="ECO:0000269|PubMed:28530713"
FT /id="VAR_082216"
FT VARIANT 418
FT /note="A -> T (in dbSNP:rs34335140)"
FT /id="VAR_033535"
FT VARIANT 788
FT /note="E -> K (in IMD60; unknown pathological significance;
FT severely decreased localization in the nucleus; the mutant
FT aggregates in the cytoplasm; dbSNP:rs757652995)"
FT /evidence="ECO:0000269|PubMed:28530713"
FT /id="VAR_082217"
FT MUTAGEN 521
FT /note="S->A: Leads to nuclear accumulation."
FT /evidence="ECO:0000269|PubMed:17018862"
FT CONFLICT 75
FT /note="V -> A (in Ref. 3; BAD92126)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="L -> F (in Ref. 1; AAK48898)"
FT /evidence="ECO:0000305"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3OHU"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:3OHU"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:3OHU"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3OHU"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:3OHU"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:3OHU"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3OHU"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:3OHU"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3OHU"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3OHU"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:3OHU"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3OHU"
SQ SEQUENCE 841 AA; 92537 MW; 4E926AC325952A93 CRC64;
MSVDEKPDSP MYVYESTVHC TNILLGLNDQ RKKDILCDVT LIVERKEFRA HRAVLAACSE
YFWQALVGQT KNDLVVSLPE EVTARGFGPL LQFAYTAKLL LSRENIREVI RCAEFLRMHN
LEDSCFSFLQ TQLLNSEDGL FVCRKDAACQ RPHEDCENSA GEEEDEEEET MDSETAKMAC
PRDQMLPEPI SFEAAAIPVA EKEEALLPEP DVPTDTKESS EKDALTQYPR YKKYQLACTK
NVYNASSHST SGFASTFRED NSSNSLKPGL ARGQIKSEPP SEENEEESIT LCLSGDEPDA
KDRAGDVEMD RKQPSPAPTP TAPAGAACLE RSRSVASPSC LRSLFSITKS VELSGLPSTS
QQHFARSPAC PFDKGITQGD LKTDYTPFTG NYGQPHVGQK EVSNFTMGSP LRGPGLEALC
KQEGELDRRS VIFSSSACDQ VSTSVHSYSG VSSLDKDLSE PVPKGLWVGA GQSLPSSQAY
SHGGLMADHL PGRMRPNTSC PVPIKVCPRS PPLETRTRTS SSCSSYSYAE DGSGGSPCSL
PLCEFSSSPC SQGARFLATE HQEPGLMGDG MYNQVRPQIK CEQSYGTNSS DESGSFSEAD
SESCPVQDRG QEVKLPFPVD QITDLPRNDF QMMIKMHKLT SEQLEFIHDV RRRSKNRIAA
QRCRKRKLDC IQNLECEIRK LVCEKEKLLS ERNQLKACMG ELLDNFSCLS QEVCRDIQSP
EQIQALHRYC PVLRPMDLPT ASSINPAPLG AEQNIAASQC AVGENVPCCL EPGAAPPGPP
WAPSNTSENC TSGRRLEGTD PGTFSERGPP LEPRSQTVTV DFCQEMTDKC TTDEQPRKDY
T
