Q924H7 · WAC_MOUSE

  • Protein
    WW domain-containing adapter protein with coiled-coil
  • Gene
    Wac
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. Also acts as a negative regulator of basal autophagy. Positively regulates MTOR activity by promoting, in an energy-dependent manner, the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex. This leads to the dimerization of the mTORC1 complex and its subsequent activation. May negatively regulate the ubiquitin proteasome pathway.

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 Componentnuclear speck
Cellular Componentnucleus
Cellular Componentspliceosomal complex
Molecular Functionchromatin binding
Molecular FunctionRNA polymerase II complex binding
Biological Processchromatin remodeling
Biological ProcessDNA damage response
Biological Processmitotic G1 DNA damage checkpoint signaling
Biological Processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of macroautophagy
Biological Processpositive regulation of TORC1 signaling
Biological Processregulation of autophagy

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    WW domain-containing adapter protein with coiled-coil

Gene names

    • Name
      Wac
    • Synonyms
      Kiaa1844

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • NOD
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q924H7
  • Secondary accessions
    • Q3U0K1
    • Q66JM9
    • Q69Z92
    • Q8C2W2
    • Q8C8Q8

Proteomes

Organism-specific databases

Subcellular Location

Nucleus speckle
Nucleus
Note: In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002545591-646WW domain-containing adapter protein with coiled-coil
Modified residue53Phosphoserine
Modified residue131Phosphoserine
Modified residue142Phosphoserine
Modified residue225Phosphoserine
Modified residue293Phosphothreonine
Modified residue302N6-acetyllysine
Modified residue446Phosphoserine
Modified residue471Phosphothreonine
Modified residue511Phosphoserine
Modified residue523Phosphoserine
Modified residue525Phosphoserine

Post-translational modification

Phosphorylated on tyrosine residues.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts (via coiled coil domain) with RNF20, RNF40 and UBE2A. Interacts (via WW domain) with RNA polymerase II. Interacts with MTOR and other components of the MTOR pathway including RPTOR, RUVBL1, RUVBL2, TTI1 and TTI2.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Region1-138Disordered
Compositional bias35-51Basic and acidic residues
Compositional bias57-79Polar residues
Compositional bias90-129Polar residues
Domain129-162WW
Compositional bias158-191Basic and acidic residues
Region158-352Disordered
Compositional bias194-225Polar residues
Compositional bias258-302Polar residues
Compositional bias313-347Polar residues
Region428-541Disordered
Coiled coil617-643

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q924H7-1

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
    646
  • Mass (Da)
    70,680
  • Last updated
    2006-10-31 v2
  • Checksum
    62914680DB435756
MVMYARKQQRLSDGCHDRRGDSQPFQALKYSSKSHPSSGDHRHEKMRDAADPSPPNKMLRRSNSPENKYSDSTGHNKAKNVHTQRVRERDGGTSYSPQENSHNHSALHSSNSHSSNPSNNPSKTSDAPYDSADDWSEHISSSGKKYYYNCRTEVSQWEKPKEWLEREQRQKEANKLAVNSFPKDRDYRREVMQATATSGFTSGMEDKHSSDASSLLPQNILSQTSRHNDKDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQKTERKESAPGDKSISHSCTTPSTSSASGLNPTSAPPTSASAVPVSPVPQSTIPPLLQDPNLFRQLLPALQATLQLNNSNVDISKINEVLTAAVTQASLQSIIHKFLTAGPSAFNITSLISQAAQLSTQAQPSNQSPMSLTSDASSPRSYVSPRISTPQTNTVPMKPLISTPPVSSQPKVSTPVVKQGPVSHSATQQPVTADKQQSHDPVSPRSLQRLSSQRSPSPGPNHTCSSNASTATVVPQNASARPACSLTPTLAAHFNDNLIKHVQGWPADHAEKQASRLREEAHNMGSVHMSEICTELKNLRSLVRVCEIQATLREQRILFLRQQIKELEKLKNQNSFMV

Q924H7-2

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

Q924H7-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 204-307: MEDKHSSDASSLLPQNILSQTSRHNDKDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQKTERKE → K

Computationally mapped potential isoform sequences

There are 10 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9PXS5E9PXS5_MOUSEWac222
E9PZH6E9PZH6_MOUSEWac339
E9PVK9E9PVK9_MOUSEWac113
E9Q5D5E9Q5D5_MOUSEWac597
E9Q6U6E9Q6U6_MOUSEWac27
E9Q4Y9E9Q4Y9_MOUSEWac494
E9Q020E9Q020_MOUSEWac495
F7CLA8F7CLA8_MOUSEWac212
F6Z247F6Z247_MOUSEWac295
F7A7S5F7A7S5_MOUSEWac241

Sequence caution

The sequence BAD32552.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0212371-45in isoform 2
Compositional bias35-51Basic and acidic residues
Compositional bias57-79Polar residues
Compositional bias90-129Polar residues
Compositional bias158-191Basic and acidic residues
Compositional bias194-225Polar residues
Alternative sequenceVSP_021238204-307in isoform 3
Compositional bias258-302Polar residues
Sequence conflict265in Ref. 3; BAC40017
Compositional bias313-347Polar residues
Sequence conflict334in Ref. 1; AAK73808
Sequence conflict509in Ref. 4; AAH80851

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF320996
EMBL· GenBank· DDBJ
AAK73808.1
EMBL· GenBank· DDBJ
mRNA
AK173274
EMBL· GenBank· DDBJ
BAD32552.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK044675
EMBL· GenBank· DDBJ
BAC32029.1
EMBL· GenBank· DDBJ
mRNA
AK087826
EMBL· GenBank· DDBJ
BAC40017.1
EMBL· GenBank· DDBJ
mRNA
AK156780
EMBL· GenBank· DDBJ
BAE33852.1
EMBL· GenBank· DDBJ
mRNA
BC080851
EMBL· GenBank· DDBJ
AAH80851.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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