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Q86TJ2 · TAD2B_HUMAN

  • Protein
    Transcriptional adapter 2-beta
  • Gene
    TADA2B
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Coactivates PAX5-dependent transcription together with either SMARCA4 or GCN5L2.

Features

Showing features for binding site.

142050100150200250300350400
TypeIDPosition(s)Description
Binding site9Zn2+ 1 (UniProtKB | ChEBI)
Binding site12Zn2+ 1 (UniProtKB | ChEBI)
Binding site23Zn2+ 2 (UniProtKB | ChEBI)
Binding site26Zn2+ 2 (UniProtKB | ChEBI)
Binding site32Zn2+ 1 (UniProtKB | ChEBI)
Binding site35Zn2+ 1 (UniProtKB | ChEBI)
Binding site45Zn2+ 2 (UniProtKB | ChEBI)
Binding site49Zn2+ 2 (UniProtKB | ChEBI)

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 Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentSAGA complex
Cellular ComponentSAGA-type complex
Molecular Functionchromatin binding
Molecular Functiontranscription coactivator activity
Molecular Functionzinc ion binding
Biological Processchromatin remodeling
Biological Processpositive regulation of DNA-templated transcription
Biological Processregulation of DNA repair
Biological Processregulation of RNA splicing
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Transcriptional adapter 2-beta
  • Alternative names
    • ADA2-like protein beta (ADA2-beta)

Gene names

    • Name
      TADA2B
    • Synonyms
      ADA2B

Organism names

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

Accessions

  • Primary accession
    Q86TJ2
  • Secondary accessions
    • A0AUJ8
    • A4QMR7
    • B3KSN0
    • B3KU86
    • Q6MZG9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Variants

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

The viewer provides 379 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

Type
IDPosition(s)Source
Description
ChainPRO_00003137111-420UniProtTranscriptional adapter 2-beta
Modified residue (large scale data)144PRIDEPhosphoserine
Modified residue (large scale data)365PRIDEPhosphoserine

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with GCN5L2, SMARCA4, SMARCE1 and PAX5. Component of the TFTC-HAT complex.

Binary interactions

TypeEntry 1
Entry 2Number of experimentsIntAct
BINARY Q86TJ2AATF Q9NY614EBI-2512219, EBI-372428
BINARY Q86TJ2-3ANKRD11 X5D7783EBI-18173581, EBI-17183751
BINARY Q86TJ2-3CFAP206 Q8IYR03EBI-18173581, EBI-749051
BINARY Q86TJ2-3HTT P428583EBI-18173581, EBI-466029
BINARY Q86TJ2-3KIF1B O60333-23EBI-18173581, EBI-10975473
BINARY Q86TJ2-3MCRS1 Q96EZ83EBI-18173581, EBI-348259
BINARY Q86TJ2-3NEFL P071963EBI-18173581, EBI-475646
BINARY Q86TJ2-3WFS1 O760243EBI-18173581, EBI-720609
BINARY Q86TJ2-3ZGPAT Q8N5A5-23EBI-18173581, EBI-10183064

Complex viewer

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, domain, region.

Type
IDPosition(s)Description
Zinc finger4-59ZZ-type
Domain65-118SANT
Region305-335Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q86TJ2-1

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
    420
  • Mass (Da)
    48,470
  • Last updated
    2008-01-15 v2
  • MD5 Checksum
    4627AAAB49A9C1A2D676CEA904DA1771
MAELGKKYCVYCLAEVSPLRFRCTECQDIELCPECFSAGAEIGHHRRYHGYQLVDGGRFTLWGPEAEGGWTSREEQLLLDAIEQFGFGNWEDMAAHVGASRTPQEVMEHYVSMYIHGNLGKACIPDTIPNRVTDHTCPSGGPLSPSLTTPLPPLDISVAEQQQLGYMPLRDDYEIEYDQDAETLISGLSVNYDDDDVEIELKRAHVDMYVRKLKERQRRKNIARDYNLVPAFLGKDKKEKEKALKRKITKEEKELRLKLRPLYQFMSCKEFDDLFENMHKEKMLRAKIRELQRYRRNGITKMEESAEYEAARHKREKRKENKNLAGSKRGKEDGKDSEFAAIENLPGFELLSDREKVLCSSLNLSPARYVTVKTIIIKDHLQKRQGIPSKSRLPSYLDKVLKKRILNFLTESGWISRDAS

Q86TJ2-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86TJ2-3

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

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D6RJ05D6RJ05_HUMANTADA2B129
D6RC20D6RC20_HUMANTADA2B121

Sequence caution

The sequence AAH47794.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.
The sequence AAI01338.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for alternative sequence, sequence conflict.

Type
IDPosition(s)Description
Alternative sequenceVSP_0301091-92in isoform 3
Alternative sequenceVSP_03011016-90in isoform 2
Sequence conflict251in Ref. 5; CAE46064

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK093974
EMBL· GenBank· DDBJ
BAG52792.1
EMBL· GenBank· DDBJ
mRNA
AK096655
EMBL· GenBank· DDBJ
BAG53348.1
EMBL· GenBank· DDBJ
mRNA
AC097382
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471131
EMBL· GenBank· DDBJ
EAW82372.1
EMBL· GenBank· DDBJ
Genomic DNA
BC047794
EMBL· GenBank· DDBJ
AAH47794.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC101334
EMBL· GenBank· DDBJ
AAI01335.1
EMBL· GenBank· DDBJ
mRNA
BC101335
EMBL· GenBank· DDBJ
AAI01336.1
EMBL· GenBank· DDBJ
mRNA
BC101336
EMBL· GenBank· DDBJ
AAI01337.1
EMBL· GenBank· DDBJ
mRNA
BC101337
EMBL· GenBank· DDBJ
AAI01338.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BX641147
EMBL· GenBank· DDBJ
CAE46064.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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