Q9UIF8 · BAZ2B_HUMAN

  • Protein
    Bromodomain adjacent to zinc finger domain protein 2B
  • Gene
    BAZ2B
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Regulatory subunit of the ATP-dependent BRF-1 and BRF-5 ISWI chromatin remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:28801535).
Both complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535).
The BRF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the BRF-5 ISWI chromatin remodeling complex (PubMed:28801535).
Chromatin reader protein, which may play a role in transcriptional regulation via interaction with ISWI (By similarity) (PubMed:10662543).
Involved in positively modulating the rate of age-related behavioral deterioration (By similarity).
Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with histone methyltransferase EHMT1 (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular Functionmetal ion binding
Biological Processchromatin remodeling
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Community curation (1)

The subsequence CRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPDGDWFCPACIAKASGQTLKIKKLHVKGKKTNESKKGKKVTLTGDTED shows transcriptional repressor activity in a high-throughput recruitment assay.

Names & Taxonomy

Protein names

  • Recommended name
    Bromodomain adjacent to zinc finger domain protein 2B
  • Alternative names
    • hWALp4

Gene names

    • Name
      BAZ2B
    • Synonyms
      KIAA1476
Community curation (1)

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9UIF8
  • Secondary accessions
    • D3DPA8
    • Q96EA1
    • Q96SQ8
    • Q9P252
    • Q9Y4N8

Proteomes

Organism-specific databases

Subcellular Location

Nucleus

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_05554971in dbSNP:rs10202670
Natural variantVAR_055550422in dbSNP:rs3213790
Natural variantVAR_055551530in dbSNP:rs3732287
Natural variantVAR_055552702in dbSNP:rs2302924
Natural variantVAR_0555532024in dbSNP:rs415793

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2,234 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), cross-link, modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00002111741-2168UniProtBromodomain adjacent to zinc finger domain protein 2B
Modified residue (large scale data)335PRIDEPhosphoserine
Modified residue (large scale data)405PRIDEPhosphoserine
Modified residue (large scale data)533PRIDEPhosphoserine
Modified residue (large scale data)544PRIDEPhosphothreonine
Modified residue (large scale data)549PRIDEPhosphothreonine
Modified residue (large scale data)554PRIDEPhosphoserine
Modified residue (large scale data)556PRIDEPhosphoserine
Modified residue (large scale data)681PRIDEPhosphoserine
Modified residue (large scale data)683PRIDEPhosphoserine
Modified residue (large scale data)728PRIDEPhosphoserine
Modified residue (large scale data)1269PRIDEPhosphoserine
Modified residue (large scale data)1283PRIDEPhosphothreonine
Modified residue (large scale data)1285PRIDEPhosphothreonine
Cross-link1425UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1462UniProtN6-acetyllysine
Modified residue1465UniProtPhosphoserine
Modified residue (large scale data)1465PRIDEPhosphoserine
Modified residue1467UniProtPhosphoserine
Modified residue (large scale data)1467PRIDEPhosphoserine
Modified residue (large scale data)1507PRIDEPhosphoserine
Modified residue (large scale data)1541PRIDEPhosphoserine
Modified residue1680UniProtPhosphoserine
Modified residue (large scale data)1680PRIDEPhosphoserine
Modified residue (large scale data)2011PRIDEPhosphothreonine
Modified residue2014UniProtPhosphothreonine
Modified residue (large scale data)2014PRIDEPhosphothreonine
Modified residue2019UniProtPhosphoserine
Modified residue (large scale data)2019PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed at varying levels in several tissues, whereas a smaller transcript was expressed specifically in testis.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the BRF-1 ISWI chromatin remodeling complex, at least composed of SMARCA1 and BAZ2B, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (PubMed:28801535).
Within the BRF-1 ISWI chromatin remodeling complex interacts with SMARCA1; the interaction is direct (PubMed:28801535).
Component of the BRF-5 ISWI chromatin remodeling complex, at least composed of SMARCA5/SNF2H and BAZ2B, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (PubMed:28801535).
Within the BRF-5 ISWI chromatin remodeling complex interacts with SMARCA5/SNF2H; the interaction is direct (PubMed:28801535).
Interacts with acetylated lysine residues on histone H1.4, H2A, H2B, H3 and H4 (in vitro). Interacts with EHMT1 (By similarity).

Binary interactions

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain, coiled coil, zinc finger.

TypeIDPosition(s)Description
Region1-29Disordered
Region140-348Disordered
Compositional bias144-220Polar residues
Compositional bias221-242Basic and acidic residues
Compositional bias243-262Polar residues
Compositional bias263-288Acidic residues
Compositional bias311-325Basic and acidic residues
Compositional bias330-348Polar residues
Region409-428Disordered
Region459-479Disordered
Compositional bias528-556Polar residues
Region528-698Disordered
Compositional bias563-580Polar residues
Compositional bias604-660Acidic residues
Compositional bias670-692Polar residues
Compositional bias719-733Polar residues
Region719-740Disordered
Domain739-810MBD
Compositional bias841-870Basic and acidic residues
Region841-872Disordered
Coiled coil883-1061
Region1021-1043Disordered
Domain1087-1152DDT
Region1265-1341Disordered
Compositional bias1299-1320Acidic residues
Coiled coil1334-1375
Region1503-1542Disordered
Region1582-1607Disordered
Compositional bias1670-1691Polar residues
Region1670-1694Disordered
Zinc finger1931-1981PHD-type
Region1998-2040Disordered
Domain2077-2147Bromo

Sequence similarities

Belongs to the WAL family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

This entry describes 5 isoforms produced by Alternative splicing. Experimental confirmation may be lacking for some isoforms.

Q9UIF8-1

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.

  • Length
    2,168
  • Mass (Da)
    240,459
  • Last updated
    2009-05-05 v3
  • Checksum
    C64EEEE6243CF779
MESGERLPSSAASSTTPTSSSTPSVASVVSKGGLSTGVASLSSTINPCGHLFRTAGDQPFNLSTVSSAFPMVSHPVFGLHSASSGHSEFGGLGTLGTPTALAAHPQLASFPGAEWWRTTDAHTRTGATFFPPLLGIPPLFAPPAQNHDSSSFHSRTSGKSNRNGPEKGVNGSINGSNTSSVIGINTSVLSTTASSSMGQTKSTSSGGGNRKCNQEQSKNQPLDARVDKIKDKKPRKKAMESSSNSDSDSGTSSDTSSEGISSSDSDDLEEDEEEEDQSIEESEDDDSDSESEAQHKSNNQVLLHGISDPKADGQKATEKAQEKRIHQPLPLASESQTHSFQSQQKQPQVLSQQLPFIFQSSQAKEESVNKHTSVIQSTGLVSNVKPLSLVNQAKKETYMKLIVPSPDVLKAGNKNTSEESSLLTSELRSKREQYKQAFPSQLKKQESSKSLKKVIAALSNPKATSSSPAHPKQTLENNHPNPFLTNALLGNHQPNGVIQSVIQEAPLALTTKTKMQSKINENIAAASSTPFSSPVNLSTSGRRTPGNQTPVMPSASPILHSQGKEKAVSNNVNPVKTQHHSHPAKSLVEQFRGTDSDIPSSKDSEDSNEDEEEDDEEEDEEDDEDDESDDSQSESDSNSESDTEGSEEEDDDDKDQDESDSDTEGEKTSMKLNKTTSSVKSPSMSLTGHSTPRNLHIAKAPGSAPAALCSESQSPAFLGTSSSTLTSSPHSGTSKRRRVTDERELRIPLEYGWQRETRIRNFGGRLQGEVAYYAPCGKKLRQYPEVIKYLSRNGIMDISRDNFSFSAKIRVGDFYEARDGPQGMQWCLLKEEDVIPRIRAMEGRRGRPPNPDRQRAREESRMRRRKGRPPNVGNAEFLDNADAKLLRKLQAQEIARQAAQIKLLRKLQKQEQARVAKEAKKQQAIMAAEEKRKQKEQIKIMKQQEKIKRIQQIRMEKELRAQQILEAKKKKKEEAANAKLLEAEKRIKEKEMRRQQAVLLKHQERERRRQHMMLMKAMEARKKAEEKERLKQEKRDEKRLNKERKLEQRRLELEMAKELKKPNEDMCLADQKPLPELPRIPGLVLSGSTFSDCLMVVQFLRNFGKVLGFDVNIDVPNLSVLQEGLLNIGDSMGEVQDLLVRLLSAAVCDPGLITGYKAKTALGEHLLNVGVNRDNVSEILQIFMEAHCGQTELTESLKTKAFQAHTPAQKASVLAFLINELACSKSVVSEIDKNIDYMSNLRRDKWVVEGKLRKLRIIHAKKTGKRDTSGGIDLGEEQHPLGTPTPGRKRRRKGGDSDYDDDDDDDSDDQGDEDDEDEEDKEDKKGKKTDICEDEDEGDQAASVEELEKQIEKLSKQQSQYRRKLFDASHSLRSVMFGQDRYRRRYWILPQCGGIFVEGMESGEGLEEIAKEREKLKKAESVQIKEEMFETSGDSLNCSNTDHCEQKEDLKEKDNTNLFLQKPGSFSKLSKLLEVAKMPPESEVMTPKPNAGANGCTLSYQNSGKHSLGSVQSTATQSNVEKADSNNLFNTGSSGPGKFYSPLPNDQLLKTLTEKNRQWFSLLPRTPCDDTSLTHADMSTASLVTPQSQPPSKSPSPTPAPLGSSAQNPVGLNPFALSPLQVKGGVSMMGLQFCGWPTGVVTSNIPFTSSVPSLGSGLGLSEGNGNSFLTSNVASSKSESPVPQNEKATSAQPAAVEVAKPVDFPSPKPIPEEMQFGWWRIIDPEDLKALLKVLHLRGIREKALQKQIQKHLDYITQACLKNKDVAIIELNENEENQVTRDIVENWSVEEQAMEMDLSVLQQVEDLERRVASASLQVKGWMCPEPASEREDLVYFEHKSFTKLCKEHDGEFTGEDESSAHALERKSDNPLDIAVTRLADLERNIERRIEEDIAPGLRVWRRALSEARSAAQVALCIQQLQKSIAWEKSIMKVYCQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPDGDWFCPACIAKASGQTLKIKKLHVKGKKTNESKKGKKVTLTGDTEDEDSASTSSSLKRGNKDLKKRKMEENTSINLSKQESFTSVKKPKRDDSKDLALCSMILTEMETHEDAWPFLLPVNLKLVPGYKKVIKKPMDFSTIREKLSSGQYPNLETFALDVRLVFDNCETFNEDDSDIGRAGHNMRKYFEKKWTDTFKVS

Q9UIF8-2

Q9UIF8-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9UIF8-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9UIF8-5

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F6VJC3F6VJC3_HUMANBAZ2B95
C9JCA6C9JCA6_HUMANBAZ2B142
H7BXK5H7BXK5_HUMANBAZ2B211
H7C1I6H7C1I6_HUMANBAZ2B179
H7C092H7C092_HUMANBAZ2B194

Sequence caution

The sequence AAH12576.1 differs from that shown. Reason: Frameshift
The sequence AAH12576.1 differs from that shown. Reason: Miscellaneous discrepancy contaminating sequence. Potential poly-A sequence.
The sequence BAA96000.2 differs from that shown. Reason: Erroneous initiation
The sequence BAB55231.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0371141-196in isoform 4
Sequence conflict95in Ref. 6; AAH12576
Alternative sequenceVSP_037115112-113in isoform 2 and isoform 5
Compositional bias144-220Polar residues
Compositional bias221-242Basic and acidic residues
Compositional bias243-262Polar residues
Compositional bias263-288Acidic residues
Compositional bias311-325Basic and acidic residues
Compositional bias330-348Polar residues
Sequence conflict333in Ref. 1; BAA89212
Compositional bias528-556Polar residues
Compositional bias563-580Polar residues
Compositional bias604-660Acidic residues
Alternative sequenceVSP_000553633-730in isoform 2
Compositional bias670-692Polar residues
Compositional bias719-733Polar residues
Alternative sequenceVSP_000554789-822in isoform 3 and isoform 5
Sequence conflict823in Ref. 1; BAA89212
Compositional bias841-870Basic and acidic residues
Sequence conflict918in Ref. 6; AAH12576
Sequence conflict986in Ref. 6; AAH12576
Compositional bias1299-1320Acidic residues
Sequence conflict1324in Ref. 1; BAA89212
Sequence conflict1379in Ref. 1; BAA89212
Sequence conflict1391in Ref. 1; BAA89212
Sequence conflict1649in Ref. 1; BAA89212
Compositional bias1670-1691Polar residues
Sequence conflict2034in Ref. 1; BAA89212

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB032255
EMBL· GenBank· DDBJ
BAA89212.1
EMBL· GenBank· DDBJ
mRNA
AB040909
EMBL· GenBank· DDBJ
BAA96000.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AL080173
EMBL· GenBank· DDBJ
CAB45759.1
EMBL· GenBank· DDBJ
mRNA
AL834381
EMBL· GenBank· DDBJ
CAD39044.2
EMBL· GenBank· DDBJ
mRNA
CH471058
EMBL· GenBank· DDBJ
EAX11404.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471058
EMBL· GenBank· DDBJ
EAX11405.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471058
EMBL· GenBank· DDBJ
EAX11407.1
EMBL· GenBank· DDBJ
Genomic DNA
BC012576
EMBL· GenBank· DDBJ
AAH12576.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AK027612
EMBL· GenBank· DDBJ
BAB55231.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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