Q924H7 · WAC_MOUSE
- ProteinWW domain-containing adapter protein with coiled-coil
- GeneWac
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids646 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nuclear speck | |
Cellular Component | nucleus | |
Cellular Component | spliceosomal complex | |
Molecular Function | chromatin binding | |
Molecular Function | RNA polymerase II complex binding | |
Biological Process | chromatin remodeling | |
Biological Process | DNA damage response | |
Biological Process | mitotic G1 DNA damage checkpoint signaling | |
Biological Process | negative regulation of proteasomal ubiquitin-dependent protein catabolic process | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | positive regulation of macroautophagy | |
Biological Process | positive regulation of TORC1 signaling | |
Biological Process | regulation of autophagy |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameWW domain-containing adapter protein with coiled-coil
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ924H7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000254559 | 1-646 | WW domain-containing adapter protein with coiled-coil | |||
Sequence: MVMYARKQQRLSDGCHDRRGDSQPFQALKYSSKSHPSSGDHRHEKMRDAADPSPPNKMLRRSNSPENKYSDSTGHNKAKNVHTQRVRERDGGTSYSPQENSHNHSALHSSNSHSSNPSNNPSKTSDAPYDSADDWSEHISSSGKKYYYNCRTEVSQWEKPKEWLEREQRQKEANKLAVNSFPKDRDYRREVMQATATSGFTSGMEDKHSSDASSLLPQNILSQTSRHNDKDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQKTERKESAPGDKSISHSCTTPSTSSASGLNPTSAPPTSASAVPVSPVPQSTIPPLLQDPNLFRQLLPALQATLQLNNSNVDISKINEVLTAAVTQASLQSIIHKFLTAGPSAFNITSLISQAAQLSTQAQPSNQSPMSLTSDASSPRSYVSPRISTPQTNTVPMKPLISTPPVSSQPKVSTPVVKQGPVSHSATQQPVTADKQQSHDPVSPRSLQRLSSQRSPSPGPNHTCSSNASTATVVPQNASARPACSLTPTLAAHFNDNLIKHVQGWPADHAEKQASRLREEAHNMGSVHMSEICTELKNLRSLVRVCEIQATLREQRILFLRQQIKELEKLKNQNSFMV | ||||||
Modified residue | 53 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 131 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 142 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 225 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 293 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 302 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 446 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 471 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 511 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 523 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 525 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on tyrosine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-138 | Disordered | ||||
Sequence: MVMYARKQQRLSDGCHDRRGDSQPFQALKYSSKSHPSSGDHRHEKMRDAADPSPPNKMLRRSNSPENKYSDSTGHNKAKNVHTQRVRERDGGTSYSPQENSHNHSALHSSNSHSSNPSNNPSKTSDAPYDSADDWSEH | ||||||
Compositional bias | 35-51 | Basic and acidic residues | ||||
Sequence: HPSSGDHRHEKMRDAAD | ||||||
Compositional bias | 57-79 | Polar residues | ||||
Sequence: KMLRRSNSPENKYSDSTGHNKAK | ||||||
Compositional bias | 90-129 | Polar residues | ||||
Sequence: DGGTSYSPQENSHNHSALHSSNSHSSNPSNNPSKTSDAPY | ||||||
Domain | 129-162 | WW | ||||
Sequence: YDSADDWSEHISSSGKKYYYNCRTEVSQWEKPKE | ||||||
Compositional bias | 158-191 | Basic and acidic residues | ||||
Sequence: EKPKEWLEREQRQKEANKLAVNSFPKDRDYRREV | ||||||
Region | 158-352 | Disordered | ||||
Sequence: EKPKEWLEREQRQKEANKLAVNSFPKDRDYRREVMQATATSGFTSGMEDKHSSDASSLLPQNILSQTSRHNDKDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQKTERKESAPGDKSISHSCTTPSTSSASGLNPTSAPPTSASAVPVSPVPQST | ||||||
Compositional bias | 194-225 | Polar residues | ||||
Sequence: ATATSGFTSGMEDKHSSDASSLLPQNILSQTS | ||||||
Compositional bias | 258-302 | Polar residues | ||||
Sequence: ATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQK | ||||||
Compositional bias | 313-347 | Polar residues | ||||
Sequence: KSISHSCTTPSTSSASGLNPTSAPPTSASAVPVSP | ||||||
Region | 428-541 | Disordered | ||||
Sequence: TQAQPSNQSPMSLTSDASSPRSYVSPRISTPQTNTVPMKPLISTPPVSSQPKVSTPVVKQGPVSHSATQQPVTADKQQSHDPVSPRSLQRLSSQRSPSPGPNHTCSSNASTATV | ||||||
Coiled coil | 617-643 | |||||
Sequence: QATLREQRILFLRQQIKELEKLKNQNS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length646
- Mass (Da)70,680
- Last updated2006-10-31 v2
- Checksum62914680DB435756
Q924H7-2
- Name2
- Differences from canonical
- 1-45: Missing
Q924H7-3
- Name3
- Differences from canonical
- 204-307: MEDKHSSDASSLLPQNILSQTSRHNDKDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQKTERKE → K
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_021237 | 1-45 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 35-51 | Basic and acidic residues | ||||
Sequence: HPSSGDHRHEKMRDAAD | ||||||
Compositional bias | 57-79 | Polar residues | ||||
Sequence: KMLRRSNSPENKYSDSTGHNKAK | ||||||
Compositional bias | 90-129 | Polar residues | ||||
Sequence: DGGTSYSPQENSHNHSALHSSNSHSSNPSNNPSKTSDAPY | ||||||
Compositional bias | 158-191 | Basic and acidic residues | ||||
Sequence: EKPKEWLEREQRQKEANKLAVNSFPKDRDYRREV | ||||||
Compositional bias | 194-225 | Polar residues | ||||
Sequence: ATATSGFTSGMEDKHSSDASSLLPQNILSQTS | ||||||
Alternative sequence | VSP_021238 | 204-307 | in isoform 3 | |||
Sequence: MEDKHSSDASSLLPQNILSQTSRHNDKDYRLPRAETHSSSTPVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQKTERKE → K | ||||||
Compositional bias | 258-302 | Polar residues | ||||
Sequence: ATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQK | ||||||
Sequence conflict | 265 | in Ref. 3; BAC40017 | ||||
Sequence: S → F | ||||||
Compositional bias | 313-347 | Polar residues | ||||
Sequence: KSISHSCTTPSTSSASGLNPTSAPPTSASAVPVSP | ||||||
Sequence conflict | 334 | in Ref. 1; AAK73808 | ||||
Sequence: S → P | ||||||
Sequence conflict | 509 | in Ref. 4; AAH80851 | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |