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Protein

Bromo adjacent homology domain-containing 1 protein

Gene

BAHD1

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

Functioni

Heterochromatin protein that acts as a transcription repressor and has the ability to promote the formation of large heterochromatic domains. May act by recruiting heterochromatin proteins such as CBX5 (HP1 alpha), HDAC5 and MBD1. Represses IGF2 expression by binding to its CpG-rich P3 promoter and recruiting heterochromatin proteins. At specific stages of Listeria infection, in complex with TRIM28, corepresses interferon-stimulated genes, including IFNL1, IFNL2 and IFNL3.2 Publications

GO - Molecular functioni

GO - Biological processi

  • chromatin silencing Source: GO_Central
  • heterochromatin assembly Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Bromo adjacent homology domain-containing 1 protein
Short name:
BAH domain-containing protein 1
Gene namesi
Name:BAHD1
Synonyms:KIAA0945
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:29153. BAHD1.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: GO_Central
  • chromatin silencing complex Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394592.

Polymorphism and mutation databases

BioMutaiBAHD1.
DMDMi152040006.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 780780Bromo adjacent homology domain-containing 1 proteinPRO_0000287918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineCombined sources
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei184 – 1841PhosphoserineCombined sources
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei588 – 5881PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8TBE0.
MaxQBiQ8TBE0.
PaxDbiQ8TBE0.
PeptideAtlasiQ8TBE0.
PRIDEiQ8TBE0.
TopDownProteomicsiQ8TBE0-3. [Q8TBE0-3]

PTM databases

iPTMnetiQ8TBE0.
PhosphoSiteiQ8TBE0.

Expressioni

Gene expression databases

BgeeiQ8TBE0.
CleanExiHS_BAHD1.
ExpressionAtlasiQ8TBE0. baseline and differential.
GenevisibleiQ8TBE0. HS.

Organism-specific databases

HPAiHPA040461.
HPA041196.

Interactioni

Subunit structurei

Interacts with CBX5 (HP1 alpha), HDAC5, MBD1 and SP1. Forms a transcription silencing complex with at least CBX3 (HP1 gamma), HDAC1, HDAC2 and TRIM28. Interacts with L.monocytogenes LntA; this interaction, occurring at a late Listeria infection stage, relieves transcription repression, mostly that of interferon-stimulated genes.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-742750,EBI-717810
CALCOCO2Q131373EBI-742750,EBI-739580
GOLGA2Q083793EBI-742750,EBI-618309
KHDRBS3O755254EBI-742750,EBI-722504
KRT40Q6A1623EBI-742750,EBI-10171697
KRTAP10-7P604093EBI-742750,EBI-10172290
LZTS2Q9BRK44EBI-742750,EBI-741037
MDFIQ997504EBI-742750,EBI-724076
TRAF4Q9BUZ43EBI-742750,EBI-3650647

Protein-protein interaction databases

BioGridi116558. 24 interactions.
IntActiQ8TBE0. 18 interactions.
MINTiMINT-1463761.
STRINGi9606.ENSP00000396976.

Structurei

3D structure databases

ProteinModelPortaliQ8TBE0.
SMRiQ8TBE0. Positions 618-720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini624 – 779156BAHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi239 – 361123Pro-richAdd
BLAST
Compositional biasi556 – 58732Arg-richAdd
BLAST

Domaini

The BAH domain is required for localization at H3K27me3.1 Publication

Sequence similaritiesi

Contains 1 BAH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1886. Eukaryota.
ENOG410XQP1. LUCA.
GeneTreeiENSGT00390000003967.
HOGENOMiHOG000095173.
HOVERGENiHBG106654.
InParanoidiQ8TBE0.
OMAiRACPQSA.
OrthoDBiEOG7G4QDF.
PhylomeDBiQ8TBE0.
TreeFamiTF350135.

Family and domain databases

InterProiIPR001025. BAH_dom.
[Graphical view]
PfamiPF01426. BAH. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
[Graphical view]
PROSITEiPS51038. BAH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TBE0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTHTRRKSLP MLSSGLTGRR EPLQMEDSNM EQGVEGVEPG MPESPGHLTG
60 70 80 90 100
RRKNYPLRKR PLVPEKPKAC KVLLTRLENV AGPRSADEAD ELPPDLPKPP
110 120 130 140 150
SPAPSSEDPG LAQPRKRRLA SLNAEALNNL LLEREDTSSL AGTRRSRAGD
160 170 180 190 200
PHRSRDRDRA TGGWSSSKKR PRLGDLGGGS RDLSPEPAPD EGPRRDGDPA
210 220 230 240 250
PKRLASLNAA AFLKLSQERE LPLRLPRAHA EVDGRSTEPP APKAPRPKWP
260 270 280 290 300
KVNGKNYPKA WQGASSGEAA GPPGWQGCPD EPWPSATPCG PSVQPSHQPL
310 320 330 340 350
SKALESPLGL RPHLPLLMGG QAALKPEPGR PGEESPAPKQ ELHQPSFPTP
360 370 380 390 400
QLSPLPMPGN PADYNGLCVG PELTALGSFY LYCGQEGLQC GGYSPCPMLP
410 420 430 440 450
EGKLSPVAAP HEEGLLLAPS SVPSGTPFQH PPWGSSRYCS SEDTGVNGYS
460 470 480 490 500
ICGVLPLSVT HAGTTCGGCP YKMPFAAEGC RSLGQLEFPL PEAGHPASPA
510 520 530 540 550
HPLLGCPVPS VPPAAEPVPH LQTPTSEPQT VARACPQSAK PPSGSKSGLR
560 570 580 590 600
TGSSCRHTAR SKAARRPSHP KQPRVQRPRP RRRRRRRTNG WVPVGAACEK
610 620 630 640 650
AVYVLDEPEP AIRKSYQAVE RHGETIRVRD TVLLKSGPRK TSTPYVAKIS
660 670 680 690 700
ALWENPESGE LMMSLLWYYR PEHLQGGRSP SMHEPLQNEV FASRHQDQNS
710 720 730 740 750
VACIEEKCYV LTFAEYCRFC AMAKRRGEGL PSRKTALVPP SADYSTPPHR
760 770 780
TVPEDTDPEL VFLCRHVYDF RHGRILKNPQ
Length:780
Mass (Da):84,652
Last modified:May 29, 2007 - v2
Checksum:iDDCAA05DFAA6D982
GO
Isoform 2 (identifier: Q8TBE0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     478-478: Missing.

Show »
Length:779
Mass (Da):84,523
Checksum:i025D321FEB463C3B
GO
Isoform 3 (identifier: Q8TBE0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     685-687: Missing.

Show »
Length:777
Mass (Da):84,314
Checksum:iBFBD1A288566FFA1
GO

Sequence cautioni

The sequence BAA76789.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261E → G.
Corresponds to variant rs3743143 [ dbSNP | Ensembl ].
VAR_032359
Natural varianti182 – 1821D → H.1 Publication
Corresponds to variant rs17856679 [ dbSNP | Ensembl ].
VAR_032360
Natural varianti298 – 2981Q → K.3 Publications
Corresponds to variant rs3803357 [ dbSNP | Ensembl ].
VAR_032361

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei478 – 4781Missing in isoform 2. 1 PublicationVSP_025623
Alternative sequencei685 – 6873Missing in isoform 3. 1 PublicationVSP_025624

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023162 mRNA. Translation: BAA76789.2. Different initiation.
BC022782 mRNA. Translation: AAH22782.1.
AC013356 Genomic DNA. No translation available.
AL833923 mRNA. Translation: CAD38779.1.
CCDSiCCDS10058.1. [Q8TBE0-1]
CCDS73705.1. [Q8TBE0-2]
RefSeqiNP_001288061.1. NM_001301132.1. [Q8TBE0-2]
NP_055767.3. NM_014952.4. [Q8TBE0-1]
XP_011519668.1. XM_011521366.1. [Q8TBE0-1]
XP_011519669.1. XM_011521367.1. [Q8TBE0-2]
XP_011519670.1. XM_011521368.1. [Q8TBE0-3]
XP_011519671.1. XM_011521369.1. [Q8TBE0-1]
UniGeneiHs.22109.

Genome annotation databases

EnsembliENST00000416165; ENSP00000396976; ENSG00000140320. [Q8TBE0-1]
ENST00000560846; ENSP00000454101; ENSG00000140320. [Q8TBE0-3]
ENST00000561234; ENSP00000454150; ENSG00000140320. [Q8TBE0-2]
GeneIDi22893.
KEGGihsa:22893.
UCSCiuc001zlt.3. human. [Q8TBE0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023162 mRNA. Translation: BAA76789.2. Different initiation.
BC022782 mRNA. Translation: AAH22782.1.
AC013356 Genomic DNA. No translation available.
AL833923 mRNA. Translation: CAD38779.1.
CCDSiCCDS10058.1. [Q8TBE0-1]
CCDS73705.1. [Q8TBE0-2]
RefSeqiNP_001288061.1. NM_001301132.1. [Q8TBE0-2]
NP_055767.3. NM_014952.4. [Q8TBE0-1]
XP_011519668.1. XM_011521366.1. [Q8TBE0-1]
XP_011519669.1. XM_011521367.1. [Q8TBE0-2]
XP_011519670.1. XM_011521368.1. [Q8TBE0-3]
XP_011519671.1. XM_011521369.1. [Q8TBE0-1]
UniGeneiHs.22109.

3D structure databases

ProteinModelPortaliQ8TBE0.
SMRiQ8TBE0. Positions 618-720.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116558. 24 interactions.
IntActiQ8TBE0. 18 interactions.
MINTiMINT-1463761.
STRINGi9606.ENSP00000396976.

PTM databases

iPTMnetiQ8TBE0.
PhosphoSiteiQ8TBE0.

Polymorphism and mutation databases

BioMutaiBAHD1.
DMDMi152040006.

Proteomic databases

EPDiQ8TBE0.
MaxQBiQ8TBE0.
PaxDbiQ8TBE0.
PeptideAtlasiQ8TBE0.
PRIDEiQ8TBE0.
TopDownProteomicsiQ8TBE0-3. [Q8TBE0-3]

Protocols and materials databases

DNASUi22893.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000416165; ENSP00000396976; ENSG00000140320. [Q8TBE0-1]
ENST00000560846; ENSP00000454101; ENSG00000140320. [Q8TBE0-3]
ENST00000561234; ENSP00000454150; ENSG00000140320. [Q8TBE0-2]
GeneIDi22893.
KEGGihsa:22893.
UCSCiuc001zlt.3. human. [Q8TBE0-1]

Organism-specific databases

CTDi22893.
GeneCardsiBAHD1.
H-InvDBHIX0012131.
HGNCiHGNC:29153. BAHD1.
HPAiHPA040461.
HPA041196.
MIMi613880. gene.
neXtProtiNX_Q8TBE0.
PharmGKBiPA128394592.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1886. Eukaryota.
ENOG410XQP1. LUCA.
GeneTreeiENSGT00390000003967.
HOGENOMiHOG000095173.
HOVERGENiHBG106654.
InParanoidiQ8TBE0.
OMAiRACPQSA.
OrthoDBiEOG7G4QDF.
PhylomeDBiQ8TBE0.
TreeFamiTF350135.

Miscellaneous databases

ChiTaRSiBAHD1. human.
GenomeRNAii22893.
PROiQ8TBE0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TBE0.
CleanExiHS_BAHD1.
ExpressionAtlasiQ8TBE0. baseline and differential.
GenevisibleiQ8TBE0. HS.

Family and domain databases

InterProiIPR001025. BAH_dom.
[Graphical view]
PfamiPF01426. BAH. 1 hit.
[Graphical view]
SMARTiSM00439. BAH. 1 hit.
[Graphical view]
PROSITEiPS51038. BAH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LYS-298.
    Tissue: Brain.
  2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS HIS-182 AND LYS-298.
    Tissue: Pancreas.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 260-780 (ISOFORM 3), VARIANT LYS-298.
    Tissue: Testis.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAH, INTERACTION WITH CBX5; HDAC5; MBD1 AND SP1.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-121 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A bacterial protein targets the BAHD1 chromatin complex to stimulate type III interferon response."
    Lebreton A., Lakisic G., Job V., Fritsch L., Tham T.N., Camejo A., Mattei P.J., Regnault B., Nahori M.A., Cabanes D., Gautreau A., Ait-Si-Ali S., Dessen A., Cossart P., Bierne H.
    Science 331:1319-1321(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LISTERIA INFECTION, INTERACTION WITH LNTA, IDENTIFICATION IN A COMPLEX WITH CBX3; HDAC1; HDAC2 AND TRIM28.
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-121; SER-184; SER-206 AND THR-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiBAHD1_HUMAN
AccessioniPrimary (citable) accession number: Q8TBE0
Secondary accession number(s): Q8NDF7, Q9Y2F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 6, 2016
This is version 108 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.