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Q9BYV9

- BACH2_HUMAN

UniProt

Q9BYV9 - BACH2_HUMAN

Protein

Transcription regulator protein BACH2

Gene

BACH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Transcriptional regulator that acts as repressor or activator. Binds to Maf recognition elements (MARE). Play important roles in coordinating transcription activation and repression by MAFK By similarity. Induces apoptosis in response to oxidative stress through repression of the antiapoptotic factor HMOX1.By similarity1 Publication

    GO - Molecular functioni

    1. sequence-specific DNA binding Source: InterPro
    2. sequence-specific DNA binding transcription factor activity Source: Ensembl

    GO - Biological processi

    1. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiQ9BYV9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription regulator protein BACH2
    Alternative name(s):
    BTB and CNC homolog 2
    Gene namesi
    Name:BACH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:14078. BACH2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 PublicationPROSITE-ProRule annotation
    Note: Nucleocytoplasmic shuttling is controlled by phosphorylation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi521 – 5211S → A: Leads to nuclear accumulation. 1 Publication

    Organism-specific databases

    PharmGKBiPA25235.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 841841Transcription regulator protein BACH2PRO_0000076456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi20 – 20Interchain; redox-active
    Modified residuei521 – 5211Phosphoserine; by RPS6KB11 Publication

    Post-translational modificationi

    Phosphorylation at Ser-521 downstream of the PI-3K pathway promotes nuclear export.1 Publication
    The reversible disulfide bond may provide mechanism to regulate the activity in oxidative stress responses.

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BYV9.
    PaxDbiQ9BYV9.
    PRIDEiQ9BYV9.

    PTM databases

    PhosphoSiteiQ9BYV9.

    Expressioni

    Tissue specificityi

    B-cell specific.

    Gene expression databases

    ArrayExpressiQ9BYV9.
    BgeeiQ9BYV9.
    CleanExiHS_BACH2.
    GenevestigatoriQ9BYV9.

    Organism-specific databases

    HPAiHPA051384.

    Interactioni

    Subunit structurei

    Heterodimer of BACH2 and Maf-related transcription factors By similarity. Homodimer; disulfide-linked.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi121913. 14 interactions.
    IntActiQ9BYV9. 2 interactions.
    STRINGi9606.ENSP00000257749.

    Structurei

    Secondary structure

    1
    841
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 154
    Helixi19 – 3315
    Beta strandi39 – 435
    Beta strandi46 – 505
    Helixi52 – 587
    Helixi60 – 667
    Beta strandi75 – 773
    Helixi84 – 9411
    Beta strandi97 – 1015
    Turni103 – 1053
    Helixi106 – 11611
    Beta strandi118 – 1203

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OHUX-ray2.10A/B/C/D/E/F9-129[»]
    3OHVX-ray2.20A/B/C/D/E/F9-129[»]
    ProteinModelPortaliQ9BYV9.
    SMRiQ9BYV9. Positions 10-129, 609-706.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYV9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 10367BTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini646 – 70964bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni651 – 66717Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni671 – 6788Leucine-zipperPROSITE-ProRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi821 – 84121Nuclear export signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi162 – 1698Poly-Glu

    Sequence similaritiesi

    Belongs to the bZIP family. CNC subfamily.Curated
    Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG276808.
    HOGENOMiHOG000231712.
    HOVERGENiHBG050655.
    InParanoidiQ9BYV9.
    KOiK09042.
    OMAiLHRYCPV.
    OrthoDBiEOG7WMCHX.
    PhylomeDBiQ9BYV9.
    TreeFamiTF326681.

    Family and domain databases

    Gene3Di1.10.880.10. 1 hit.
    3.30.710.10. 1 hit.
    InterProiIPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR004827. bZIP.
    IPR004826. bZIP_Maf.
    IPR008917. TF_DNA-bd.
    [Graphical view]
    PfamiPF00651. BTB. 1 hit.
    PF03131. bZIP_Maf. 1 hit.
    [Graphical view]
    SMARTiSM00338. BRLZ. 1 hit.
    SM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF47454. SSF47454. 1 hit.
    SSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9BYV9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVDEKPDSP MYVYESTVHC TNILLGLNDQ RKKDILCDVT LIVERKEFRA    50
    HRAVLAACSE YFWQALVGQT KNDLVVSLPE EVTARGFGPL LQFAYTAKLL 100
    LSRENIREVI RCAEFLRMHN LEDSCFSFLQ TQLLNSEDGL FVCRKDAACQ 150
    RPHEDCENSA GEEEDEEEET MDSETAKMAC PRDQMLPEPI SFEAAAIPVA 200
    EKEEALLPEP DVPTDTKESS EKDALTQYPR YKKYQLACTK NVYNASSHST 250
    SGFASTFRED NSSNSLKPGL ARGQIKSEPP SEENEEESIT LCLSGDEPDA 300
    KDRAGDVEMD RKQPSPAPTP TAPAGAACLE RSRSVASPSC LRSLFSITKS 350
    VELSGLPSTS QQHFARSPAC PFDKGITQGD LKTDYTPFTG NYGQPHVGQK 400
    EVSNFTMGSP LRGPGLEALC KQEGELDRRS VIFSSSACDQ VSTSVHSYSG 450
    VSSLDKDLSE PVPKGLWVGA GQSLPSSQAY SHGGLMADHL PGRMRPNTSC 500
    PVPIKVCPRS PPLETRTRTS SSCSSYSYAE DGSGGSPCSL PLCEFSSSPC 550
    SQGARFLATE HQEPGLMGDG MYNQVRPQIK CEQSYGTNSS DESGSFSEAD 600
    SESCPVQDRG QEVKLPFPVD QITDLPRNDF QMMIKMHKLT SEQLEFIHDV 650
    RRRSKNRIAA QRCRKRKLDC IQNLECEIRK LVCEKEKLLS ERNQLKACMG 700
    ELLDNFSCLS QEVCRDIQSP EQIQALHRYC PVLRPMDLPT ASSINPAPLG 750
    AEQNIAASQC AVGENVPCCL EPGAAPPGPP WAPSNTSENC TSGRRLEGTD 800
    PGTFSERGPP LEPRSQTVTV DFCQEMTDKC TTDEQPRKDY T 841
    Length:841
    Mass (Da):92,537
    Last modified:June 1, 2001 - v1
    Checksum:i4E926AC325952A93
    GO

    Sequence cautioni

    The sequence BAD92126.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751V → A in BAD92126. 1 PublicationCurated
    Sequence conflicti291 – 2911L → F in AAK48898. (PubMed:10949928)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti418 – 4181A → T.
    Corresponds to variant rs34335140 [ dbSNP | Ensembl ].
    VAR_033535

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF357835 mRNA. Translation: AAK48898.1.
    AJ271878 mRNA. Translation: CAC28130.1.
    AB208889 mRNA. Translation: BAD92126.1. Different initiation.
    AL353692, AL121787 Genomic DNA. Translation: CAI16237.1.
    AL121787, AL353692 Genomic DNA. Translation: CAI21648.1.
    CH471051 Genomic DNA. Translation: EAW48530.1.
    CH471051 Genomic DNA. Translation: EAW48531.1.
    CH471051 Genomic DNA. Translation: EAW48532.1.
    CH471051 Genomic DNA. Translation: EAW48533.1.
    CH471051 Genomic DNA. Translation: EAW48534.1.
    CCDSiCCDS5026.1.
    RefSeqiNP_001164265.1. NM_001170794.1.
    NP_068585.1. NM_021813.3.
    XP_005248816.1. XM_005248759.2.
    UniGeneiHs.269764.

    Genome annotation databases

    EnsembliENST00000257749; ENSP00000257749; ENSG00000112182.
    ENST00000343122; ENSP00000345642; ENSG00000112182.
    ENST00000537989; ENSP00000437473; ENSG00000112182.
    GeneIDi60468.
    KEGGihsa:60468.
    UCSCiuc003pnw.3. human.

    Polymorphism databases

    DMDMi17433037.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF357835 mRNA. Translation: AAK48898.1 .
    AJ271878 mRNA. Translation: CAC28130.1 .
    AB208889 mRNA. Translation: BAD92126.1 . Different initiation.
    AL353692 , AL121787 Genomic DNA. Translation: CAI16237.1 .
    AL121787 , AL353692 Genomic DNA. Translation: CAI21648.1 .
    CH471051 Genomic DNA. Translation: EAW48530.1 .
    CH471051 Genomic DNA. Translation: EAW48531.1 .
    CH471051 Genomic DNA. Translation: EAW48532.1 .
    CH471051 Genomic DNA. Translation: EAW48533.1 .
    CH471051 Genomic DNA. Translation: EAW48534.1 .
    CCDSi CCDS5026.1.
    RefSeqi NP_001164265.1. NM_001170794.1.
    NP_068585.1. NM_021813.3.
    XP_005248816.1. XM_005248759.2.
    UniGenei Hs.269764.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OHU X-ray 2.10 A/B/C/D/E/F 9-129 [» ]
    3OHV X-ray 2.20 A/B/C/D/E/F 9-129 [» ]
    ProteinModelPortali Q9BYV9.
    SMRi Q9BYV9. Positions 10-129, 609-706.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121913. 14 interactions.
    IntActi Q9BYV9. 2 interactions.
    STRINGi 9606.ENSP00000257749.

    PTM databases

    PhosphoSitei Q9BYV9.

    Polymorphism databases

    DMDMi 17433037.

    Proteomic databases

    MaxQBi Q9BYV9.
    PaxDbi Q9BYV9.
    PRIDEi Q9BYV9.

    Protocols and materials databases

    DNASUi 60468.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257749 ; ENSP00000257749 ; ENSG00000112182 .
    ENST00000343122 ; ENSP00000345642 ; ENSG00000112182 .
    ENST00000537989 ; ENSP00000437473 ; ENSG00000112182 .
    GeneIDi 60468.
    KEGGi hsa:60468.
    UCSCi uc003pnw.3. human.

    Organism-specific databases

    CTDi 60468.
    GeneCardsi GC06M090636.
    HGNCi HGNC:14078. BACH2.
    HPAi HPA051384.
    MIMi 605394. gene.
    neXtProti NX_Q9BYV9.
    PharmGKBi PA25235.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276808.
    HOGENOMi HOG000231712.
    HOVERGENi HBG050655.
    InParanoidi Q9BYV9.
    KOi K09042.
    OMAi LHRYCPV.
    OrthoDBi EOG7WMCHX.
    PhylomeDBi Q9BYV9.
    TreeFami TF326681.

    Enzyme and pathway databases

    SignaLinki Q9BYV9.

    Miscellaneous databases

    EvolutionaryTracei Q9BYV9.
    GeneWikii BACH2.
    GenomeRNAii 60468.
    NextBioi 65347.
    PROi Q9BYV9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BYV9.
    Bgeei Q9BYV9.
    CleanExi HS_BACH2.
    Genevestigatori Q9BYV9.

    Family and domain databases

    Gene3Di 1.10.880.10. 1 hit.
    3.30.710.10. 1 hit.
    InterProi IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR004827. bZIP.
    IPR004826. bZIP_Maf.
    IPR008917. TF_DNA-bd.
    [Graphical view ]
    Pfami PF00651. BTB. 1 hit.
    PF03131. bZIP_Maf. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    SM00225. BTB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47454. SSF47454. 1 hit.
    SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of human B cell-specific transcription factor BACH2 mapped to chromosome 6q15."
      Sasaki S., Ito E., Toki T., Maekawa T., Kanezaki R., Umenai T., Muto A., Nagai H., Kinoshita T., Yamamoto M., Inazawa J., Taketo M.M., Nakahata T., Igarashi K., Yokoyama M.
      Oncogene 19:3739-3749(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Transcription factor BACH2 is transcriptionally regulated by the BCR/ABL oncogene."
      Vieira S.A.D., Deininger M.W.N., Sorour A., Sinclair P., Foroni L., Goldman J.M., Melo J.V.
      Genes Chromosomes Cancer 32:353-363(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Bcr-Abl signaling through the PI-3/S6 kinase pathway inhibits nuclear translocation of the transcription factor Bach2, which represses the antiapoptotic factor heme oxygenase-1."
      Yoshida C., Yoshida F., Sears D.E., Hart S.M., Ikebe D., Muto A., Basu S., Igarashi K., Melo J.V.
      Blood 109:1211-1219(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-521, MUTAGENESIS OF SER-521.
    7. "The structure of the Bach2 POZ-domain dimer reveals an intersubunit disulfide bond."
      Rosbrook G.O., Stead M.A., Carr S.B., Wright S.C.
      Acta Crystallogr. D 68:26-34(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 9-129, SUBUNIT, INTERCHAIN DISULFIDE BOND.

    Entry informationi

    Entry nameiBACH2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYV9
    Secondary accession number(s): E1P518
    , Q59H70, Q5T793, Q9NTS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3