O14867 (BACH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription regulator protein BACH1

Alternative name(s):
BTB and CNC homolog 1
HA2303

Gene names

Name:

BACH1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	736 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional regulator that acts as repressor or activator. Binds, in-vitro, to NF-E2 binding sites. Play important roles in coordinating transcription activation and repression by MAFK.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the bZIP family. CNC subfamily. Contains 1 BTB (POZ) domain. Contains 1 bZIP domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription from RNA polymerase II promoter in response to stress Inferred from direct assay. Source: UniProtKB regulation of transcription involved in G1/S phase of mitotic cell cycle Inferred from mutant phenotype. Source: UniProtKB regulation of transcription involved in G2/M-phase of mitotic cell cycle Inferred from mutant phenotype. Source: UniProtKB
Cellular component	nucleus Inferred from direct assay. Source: UniProtKB
Molecular function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Inferred from direct assay. Source: UniProtKB heme binding Non-traceable author statement. Source: UniProtKB protein dimerization activity Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 736

736

Transcription regulator protein BACH1

PRO_0000076454

Regions

Domain

34 – 100

67

BTB

Domain

585 – 607

23

Leucine-zipper

DNA binding

562 – 577

16

Basic motif

Amino acid modifications

Modified residue

196

1

Phosphoserine Ref.6

Modified residue

321

1

Phosphotyrosine Ref.9

Modified residue

322

1

Phosphoserine Ref.9

Modified residue

328

1

Phosphothreonine Ref.9

Modified residue

445

1

Phosphoserine Ref.6 Ref.7 Ref.8

Natural variations

Natural variant

314

1

S → P.
Corresponds to variant rs35474725 [ dbSNP | Ensembl ].

VAR_048441

Experimental info

Sequence conflict

158

1

S → T in AAB84100. Ref.1

Sequence conflict

171

1

E → G in AAB84100. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

736

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Helix

16 – 30

15

Beta strand

36 – 40

5

Beta strand

43 – 47

5

Helix

49 – 55

7

Helix

57 – 63

7

Beta strand

71 – 74

4

Helix

81 – 93

13

Beta strand

94 – 99

6

Turn

100 – 102

3

Helix

103 – 113

11

Beta strand

115 – 117

3

Helix

120 – 124

5

Sequences

	Sequence		Length	Mass (Da)
	O14867 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: CAAEECC63D46571B	FASTA	736	81,958
	10 20 30 40 50 60 MSLSENSVFA YESSVHSTNV LLSLNDQRKK DVLCDVTIFV EGQRFRAHRS VLAACSSYFH 70 80 90 100 110 120 SRIVGQADGE LNITLPEEVT VKGFEPLIQF AYTAKLILSK ENVDEVCKCV EFLSVHNIEE 130 140 150 160 170 180 SCFQFLKFKF LDSTADQQEC PRKKCFSSHC QKTDLKLSLL DQRDLETDEV EEFLENKNVQ 190 200 210 220 230 240 TPQCKLRRYQ GNAKASPPLQ DSASQTYESM CLEKDAALAL PSLCPKYRKF QKAFGTDRVR 250 260 270 280 290 300 TGESSVKDIH ASVQPNERSE NECLGGVPEC RDLQVMLKCD ESKLAMEPEE TKKDPASQCP 310 320 330 340 350 360 TEKSEVTPFP HNSSIDPHGL YSLSLLHTYD QYGDLNFAGM QNTTVLTEKP LSGTDVQEKT 370 380 390 400 410 420 FGESQDLPLK SDLGTREDSS VASSDRSSVE REVAEHLAKG FWSDICSTDT PCQMQLSPAV 430 440 450 460 470 480 AKDGSEQISQ KRSECPWLGI RISESPEPGQ RTFTTLSSVN CPFISTLSTE GCSSNLEIGN 490 500 510 520 530 540 DDYVSEPQQE PCPYACVISL GDDSETDTEG DSESCSAREQ ECEVKLPFNA QRIISLSRND 550 560 570 580 590 600 FQSLLKMHKL TPEQLDCIHD IRRRSKNRIA AQRCRKRKLD CIQNLESEIE KLQSEKESLL 610 620 630 640 650 660 KERDHILSTL GETKQNLTGL CQKVCKEAAL SQEQIQILAK YSAADCPLSF LISEKDKSTP 670 680 690 700 710 720 DGELALPSIF SLSDRPPAVL PPCARGNSEP GYARGQESQQ MSTATSEQAG PAEQCRQSGG 730 ISDFCQQMTD KCTTDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of the human BACH1 transcription regulator gene, which maps to chromosome 21q22.1." Blouin J.-L., Duriaux Sail G., Guipponi M., Rossier C., Pappasavas M.-P., Antonarakis S.E. Hum. Genet. 102:282-288(1998) [PubMed: 9544839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of a human homolog (BACH1) of the mouse Bach1 gene encoding a BTB-basic leucine zipper transcription factor and its mapping to chromosome 21q22.1." Ohira M., Seki N., Nagase T., Ishikawa K., Nomura N., Ohara O. Genomics 47:300-306(1998) [PubMed: 9479503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J., Schattevoy R., Yaspo M.-L., Rosenthal A. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed: 10830953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 AND SER-445, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321; SER-322 AND THR-328, MASS SPECTROMETRY.
[10]	"Crystal structure of the bric-a-brac (BTB) domain of human BACH1." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 7-128.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF026199 mRNA. Translation: AAB84100.1.
AF026200 mRNA. Translation: AAB84101.1.
AB002803 mRNA. Translation: BAA24932.1.
AF124731 Genomic DNA. Translation: AAD14689.1.
AL163249 Genomic DNA. Translation: CAB90435.1.
AP001705 Genomic DNA. Translation: BAA95505.1.
BC063307 mRNA. Translation: AAH63307.1.

IPI

IPI00024235.

PIR

T00023.

RefSeq

NP_001177.1. NM_001186.2.
NP_996749.1. NM_206866.1.

UniGene

Hs.154276.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IHC	X-ray	2.44	A/B/C/D	7-128	[»]

ProteinModelPortal

O14867.

SMR

O14867. Positions 7-126, 515-621.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24223N.

IntAct

O14867. 2 interactions.

STRING

O14867.

PTM databases

PhosphoSite

O14867.

Proteomic databases

PRIDE

O14867.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000286800; ENSP00000286800; ENSG00000156273.
ENST00000399921; ENSP00000382805; ENSG00000156273.

GeneID

571.

KEGG

hsa:571.

UCSC

uc002ynj.1. human.

Organism-specific databases

CTD

571.

GeneCards

GC21P030567.

H-InvDB

HIX0040836.

HGNC

HGNC:935. BACH1.

HPA

HPA003175.

MIM

602751. gene.

neXtProt

NX_O14867.

PharmGKB

PA25234.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14589.

HOGENOM

HBG715857.

HOVERGEN

HBG099852.

InParanoid

O14867.

OMA

VQPNETS.

OrthoDB

EOG4CJVH8.

PhylomeDB

O14867.

Gene expression databases

ArrayExpress

O14867.

Bgee

O14867.

CleanEx

HS_BACH1.

Genevestigator

O14867.

GermOnline

ENSG00000156273. Homo sapiens.

Family and domain databases

InterPro

IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR004827. bZIP.
IPR011616. bZIP_1.
IPR008917. Euk_TF_DNA-bd.
[Graphical view]

Gene3D

G3DSA:3.30.710.10. BTB/POZ_fold. 1 hit.
G3DSA:1.10.880.10. G3DSA:1.10.880.10. 1 hit.

KO

K09042.

Pfam

PF00651. BTB. 1 hit.
PF00170. bZIP_1. 1 hit.
[Graphical view]

SMART

SM00338. BRLZ. 1 hit.
SM00225. BTB. 1 hit.
[Graphical view]

SUPFAM

SSF54695. BTB/POZ_fold. 1 hit.
SSF47454. Euk_transcr_DNA. 1 hit.

PROSITE

PS50097. BTB. 1 hit.
PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

2323.

SOURCE

Search...

Entry information

Entry name

BACH1_HUMAN

Accession

Primary (citable) accession number: O14867
Secondary accession number(s): O43285

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.