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Q9BYV9

- BACH2_HUMAN

UniProt

Q9BYV9 - BACH2_HUMAN

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Protein

Transcription regulator protein BACH2

Gene
BACH2
Organism
Homo sapiens (Human)
Status
Reviewed - 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 HMOX1.1 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
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: Chromosome 6

Organism-specific databases

HGNCiHGNC:14078. BACH2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Nucleocytoplasmic shuttling is controlled by phosphorylation.1 Publication

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.

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-active1 Publication
Modified residuei521 – 5211Phosphoserine; by RPS6KB11 Publication

Post-translational modificationi

Phosphorylation at Ser-521 downstream of the PI-3K pathway promotes nuclear export.
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.1 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.

Miscellaneous databases

EvolutionaryTraceiQ9BYV9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 10367BTBAdd
BLAST
Domaini646 – 70964bZIPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni651 – 66717Basic motif By similarityAdd
BLAST
Regioni671 – 6788Leucine-zipper By similarity

Motif

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

Compositional bias

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

Sequence similaritiesi

Belongs to the bZIP family. CNC subfamily.
Contains 1 BTB (POZ) domain.

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.

Natural variant

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

Sequence conflict

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

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

« 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: July 9, 2014
This is version 117 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

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