Q6UXN9 · WDR82_HUMAN

  • Protein
    WD repeat-containing protein 82
  • Gene
    WDR82
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Regulatory component of the SET1/COMPASS complex implicated in the tethering of this complex to transcriptional start sites of active genes (PubMed:17998332, PubMed:18838538, PubMed:20516061).
Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (PubMed:17998332, PubMed:18838538).
Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061).
Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) (PubMed:33767452, PubMed:33913806).
The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452).

Caution

The gene encoding this protein shares one overlapping exon with TMEM113.

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 Componenthistone methyltransferase complex
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular ComponentPTW/PP1 phosphatase complex
Cellular ComponentSet1C/COMPASS complex
Molecular Functionchromatin binding
Biological ProcessDNA-templated transcription termination
Biological ProcesslncRNA catabolic process
Biological Processnegative regulation of DNA-templated transcription, elongation
Biological Processnegative regulation of lncRNA transcription
Biological Processnuclear RNA surveillance

Keywords

Enzyme and pathway databases

Community curation (1)

A complex of WDR82 with ZC3H4 suppresses extragenic transcription in mammalian cells.

Names & Taxonomy

Protein names

  • Recommended name
    WD repeat-containing protein 82

Gene names

    • Name
      WDR82
    • Synonyms
      SWD2, TMEM113, WDR82A
    • ORF names
      UNQ9342/PRO34047

Organism names

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

Accessions

  • Primary accession
    Q6UXN9
  • Secondary accessions
    • A8K5R5
    • Q8TEB2

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Chromosome
Note: Associates with chromatin (PubMed:20516061).
Recruited at sites of high RNA polymerase II occupancy (By similarity).

Keywords

Disease & Variants

Variants

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

The viewer provides 183 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).

TypeIDPosition(s)SourceDescription
ChainPRO_00002796851-313UniProtWD repeat-containing protein 82
Modified residue (large scale data)6PRIDEPhosphoserine
Modified residue (large scale data)10PRIDEPhosphoserine

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the SET1/COMPASS complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 (PubMed:16253997, PubMed:17355966, PubMed:17998332, PubMed:18838538).
Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC (PubMed:20516061).
Associated with multiple protein complexes including an RNA polymerase II complex, MLL3/MLL4 complex and a chaperonin-containing TCP1 complex (PubMed:20516061).
Interacts with SETD1B (via N-terminal region); the interaction is direct (PubMed:17998332, PubMed:37030068).
Interacts with SETD1A (via N-terminal region); the interaction is direct (PubMed:17998332, PubMed:37030068).
Interacts with CUL4B (PubMed:17041588).
Interacts with RBBP5 (PubMed:18838538).
Interacts with POLR2B (PubMed:17998332).
Interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (PubMed:17998332).
Binds specifically to CTD heptad repeats phosphorylated on 'Ser-5' of each heptad (PubMed:17998332).
SETD1A enhances its interaction with POLR2A (PubMed:17998332).
Interacts with PPP1R10/PNUTS (PubMed:20516061).
Interacts with PPP1CA in the presence of PPP1R10/PNUTS (PubMed:20516061).
Interacts with ZC3H4; interaction is independent of the SET1 complex and promotes transcription termination of long non-coding RNAs (lncRNAs) (PubMed:33913806).
View interactors in UniProtKB
View CPX-7110 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat19-58WD 1
Repeat105-144WD 2
Repeat146-184WD 3
Repeat192-231WD 4
Repeat236-276WD 5
Repeat280-313WD 6

Sequence similarities

Belongs to the WD repeat SWD2 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    313
  • Mass (Da)
    35,079
  • Last updated
    2004-07-05 v1
  • Checksum
    FD3505A9B89863A0
MKLTDSVLRSFRVAKVFRENSDKINCFDFSPNGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVALSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTGLKFSNDGKLILISTNGSFIRLIDAFKGVVMHTFGGYANSKAVTLEASFTPDSQFIMIGSEDGKIHVWNGESGIKVAVLDGKHTGPITCLQFNPKFMTFASACSNMAFWLPTIDD

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
C9JBU3C9JBU3_HUMANWDR82199

Sequence caution

The sequence BAB85039.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY358264
EMBL· GenBank· DDBJ
AAQ88631.1
EMBL· GenBank· DDBJ
mRNA
AK074290
EMBL· GenBank· DDBJ
BAB85039.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK291380
EMBL· GenBank· DDBJ
BAF84069.1
EMBL· GenBank· DDBJ
mRNA
CH471055
EMBL· GenBank· DDBJ
EAW65202.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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