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Protein

Transcription regulator protein BACH2

Gene

BACH2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  2. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
Complete GO annotation...

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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:14078. BACH2.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus PROSITE-ProRule annotation1 Publication

  3. Note: Nucleocytoplasmic shuttling is controlled by phosphorylation.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiBACH2.
DMDMi17433037.

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

BgeeiQ9BYV9.
CleanExiHS_BACH2.
ExpressionAtlasiQ9BYV9. baseline and differential.
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 – 154Combined sources
Helixi19 – 3315Combined sources
Beta strandi39 – 435Combined sources
Beta strandi46 – 505Combined sources
Helixi52 – 587Combined sources
Helixi60 – 667Combined sources
Beta strandi75 – 773Combined sources
Helixi84 – 9411Combined sources
Beta strandi97 – 1015Combined sources
Turni103 – 1053Combined sources
Helixi106 – 11611Combined sources
Beta strandi118 – 1203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 609-703.
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.
GeneTreeiENSGT00550000074399.
HOGENOMiHOG000231712.
HOVERGENiHBG050655.
InParanoidiQ9BYV9.
KOiK09042.
OMAiLHRYCPV.
OrthoDBiEOG7WMCHX.
PhylomeDBiQ9BYV9.
TreeFamiTF326681.

Family and domain databases

Gene3Di1.10.880.10. 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

        10         20         30         40         50
MSVDEKPDSP MYVYESTVHC TNILLGLNDQ RKKDILCDVT LIVERKEFRA
60 70 80 90 100
HRAVLAACSE YFWQALVGQT KNDLVVSLPE EVTARGFGPL LQFAYTAKLL
110 120 130 140 150
LSRENIREVI RCAEFLRMHN LEDSCFSFLQ TQLLNSEDGL FVCRKDAACQ
160 170 180 190 200
RPHEDCENSA GEEEDEEEET MDSETAKMAC PRDQMLPEPI SFEAAAIPVA
210 220 230 240 250
EKEEALLPEP DVPTDTKESS EKDALTQYPR YKKYQLACTK NVYNASSHST
260 270 280 290 300
SGFASTFRED NSSNSLKPGL ARGQIKSEPP SEENEEESIT LCLSGDEPDA
310 320 330 340 350
KDRAGDVEMD RKQPSPAPTP TAPAGAACLE RSRSVASPSC LRSLFSITKS
360 370 380 390 400
VELSGLPSTS QQHFARSPAC PFDKGITQGD LKTDYTPFTG NYGQPHVGQK
410 420 430 440 450
EVSNFTMGSP LRGPGLEALC KQEGELDRRS VIFSSSACDQ VSTSVHSYSG
460 470 480 490 500
VSSLDKDLSE PVPKGLWVGA GQSLPSSQAY SHGGLMADHL PGRMRPNTSC
510 520 530 540 550
PVPIKVCPRS PPLETRTRTS SSCSSYSYAE DGSGGSPCSL PLCEFSSSPC
560 570 580 590 600
SQGARFLATE HQEPGLMGDG MYNQVRPQIK CEQSYGTNSS DESGSFSEAD
610 620 630 640 650
SESCPVQDRG QEVKLPFPVD QITDLPRNDF QMMIKMHKLT SEQLEFIHDV
660 670 680 690 700
RRRSKNRIAA QRCRKRKLDC IQNLECEIRK LVCEKEKLLS ERNQLKACMG
710 720 730 740 750
ELLDNFSCLS QEVCRDIQSP EQIQALHRYC PVLRPMDLPT ASSINPAPLG
760 770 780 790 800
AEQNIAASQC AVGENVPCCL EPGAAPPGPP WAPSNTSENC TSGRRLEGTD
810 820 830 840
PGTFSERGPP LEPRSQTVTV DFCQEMTDKC TTDEQPRKDY T
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751V → A in BAD92126 (Ref. 3) Curated
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:
EMBLi
GenBanki
DDBJi
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_005248759.3.
UniGeneiHs.269764.

Genome annotation databases

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

Polymorphism and mutation databases

BioMutaiBACH2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005248759.3.
UniGeneiHs.269764.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 609-703.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9BYV9.

Polymorphism and mutation databases

BioMutaiBACH2.
DMDMi17433037.

Proteomic databases

MaxQBiQ9BYV9.
PaxDbiQ9BYV9.
PRIDEiQ9BYV9.

Protocols and materials databases

DNASUi60468.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi60468.
GeneCardsiGC06M090636.
HGNCiHGNC:14078. BACH2.
HPAiHPA051384.
MIMi605394. gene.
neXtProtiNX_Q9BYV9.
PharmGKBiPA25235.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG276808.
GeneTreeiENSGT00550000074399.
HOGENOMiHOG000231712.
HOVERGENiHBG050655.
InParanoidiQ9BYV9.
KOiK09042.
OMAiLHRYCPV.
OrthoDBiEOG7WMCHX.
PhylomeDBiQ9BYV9.
TreeFamiTF326681.

Enzyme and pathway databases

SignaLinkiQ9BYV9.

Miscellaneous databases

ChiTaRSiBACH2. human.
EvolutionaryTraceiQ9BYV9.
GeneWikiiBACH2.
GenomeRNAii60468.
NextBioi65347.
PROiQ9BYV9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BYV9.
CleanExiHS_BACH2.
ExpressionAtlasiQ9BYV9. baseline and differential.
GenevestigatoriQ9BYV9.

Family and domain databases

Gene3Di1.10.880.10. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.