Q498T3 · ING3_RAT
- ProteinInhibitor of growth protein 3
- GeneIng3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids421 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (By similarity).
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 365 | Histone H3K4me3 binding | ||||
Sequence: Y | ||||||
Binding site | 366 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 368 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 376 | Histone H3K4me3 binding | ||||
Sequence: M | ||||||
Binding site | 379 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 380 | Histone H3K4me3 binding | ||||
Sequence: D | ||||||
Binding site | 384 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 388 | Histone H3K4me3 binding | ||||
Sequence: W | ||||||
Binding site | 390 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 393 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 406 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 409 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | NuA4 histone acetyltransferase complex | |
Cellular Component | nucleosome | |
Cellular Component | piccolo histone acetyltransferase complex | |
Cellular Component | Swr1 complex | |
Molecular Function | histone H2A acetyltransferase activity | |
Molecular Function | histone H4K12 acetyltransferase activity | |
Molecular Function | histone H4K16 acetyltransferase activity | |
Molecular Function | histone H4K5 acetyltransferase activity | |
Molecular Function | histone H4K8 acetyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | methylated histone binding | |
Biological Process | positive regulation of double-strand break repair via homologous recombination | |
Biological Process | regulation of cell cycle | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameInhibitor of growth protein 3
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ498T3
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000354692 | 1-421 | Inhibitor of growth protein 3 | |||
Sequence: MLYLEDYLEMIEQLPMDLRDRFTEMREMDLQVQNAMDQLEQRVSEFFMNAKKNKPEWREEQMASIKKDYYKALEDADEKVQLANQIYDLVDRHLRKLDQELAKFKMELEADNAGITEILERRSLELDAPSQPVNNHHAHSHTPVEKRKYNPTSHHTATDHIPEKKFKSEALLSTLTSDASKENTLGCRNNNSTASCNNAYNVNSSQPLASYNIGSLSSGAGAGAITMAAAQAVQATAQMKEGRRTSSLKASYEAFKNNDFQLGKEFSMPRETAGYSSSSALMTTLTQNASSSAADSRSGRKSKNNTKSSSQQSSSSSSSSSSSSLSLCSSSSTVVQEVSQQTTVVPESDSNSQVDWTYDPNEPRYCICNQVSYGEMVGCDNQDCPIEWFHYGCVGLTEAPKGKWFCPQCTAAMKRRGSRHK | ||||||
Cross-link | 148 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 165 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 167 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 181 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 256 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 264 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with H3K4me3 and to a lesser extent with H3K4me2 (By similarity).
Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. Component of a SWR1-like complex (By similarity).
Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. Component of a SWR1-like complex (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 129-164 | Disordered | ||||
Sequence: PSQPVNNHHAHSHTPVEKRKYNPTSHHTATDHIPEK | ||||||
Compositional bias | 144-164 | Basic and acidic residues | ||||
Sequence: VEKRKYNPTSHHTATDHIPEK | ||||||
Region | 286-324 | Disordered | ||||
Sequence: TQNASSSAADSRSGRKSKNNTKSSSQQSSSSSSSSSSSS | ||||||
Zinc finger | 363-412 | PHD-type | ||||
Sequence: PRYCICNQVSYGEMVGCDNQDCPIEWFHYGCVGLTEAPKGKWFCPQCTAA |
Domain
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence similarities
Belongs to the ING family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length421
- Mass (Da)46,925
- Last updated2005-09-13 v1
- Checksum9002A15417B0CF3C
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6A977 | A0A8I6A977_RAT | Ing3 | 395 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 144-164 | Basic and acidic residues | ||||
Sequence: VEKRKYNPTSHHTATDHIPEK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH473959 EMBL· GenBank· DDBJ | EDM15142.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC100082 EMBL· GenBank· DDBJ | AAI00083.1 EMBL· GenBank· DDBJ | mRNA |