Q498T3
Gene name |
Ing3 |
Protein name |
Inhibitor of growth protein 3 |
Names |
|
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:312154 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for Q498T3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 8COK | X-ray | 291 A | A/B | 1-102 | PDB |
| AF-Q498T3-F1 | Predicted | AlphaFoldDB |
No variants for Q498T3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q498T3 | |||||
No associated diseases with Q498T3
5 regional properties for Q498T3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, PHD-type | 365 - 410 | IPR001965 |
| conserved_site | Zinc finger, PHD-type, conserved site | 366 - 409 | IPR019786 |
| domain | Zinc finger, PHD-finger | 363 - 412 | IPR019787 |
| domain | Inhibitor of growth protein, N-terminal histone-binding | 3 - 104 | IPR024610 |
| domain | ING3, PHD domain | 365 - 409 | IPR042020 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| NuA4 histone acetyltransferase complex | A complex having histone acetylase activity on chromatin, as well as ATPase, DNA helicase and structural DNA binding activities. The complex is thought to be involved in double-strand DNA break repair. Subunits of the human complex include HTATIP/TIP60, TRRAP, RUVBL1, BUVBL2, beta-actin and BAF53/ACTL6A. In yeast, the complex has 13 subunits, including the catalytic subunit Esa1 (homologous to human Tip60). |
| nucleosome | A complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures. |
| Piccolo NuA4 histone acetyltransferase complex | A heterotrimeric H4/H2A histone acetyltransferase complex with a substrate preference of chromatin over free histones. It contains a subset of the proteins found in the larger NuA4 histone acetyltransferase complex; for example, the S. cerevisiae complex contains Esa1p, Yng2p, and Epl1p. |
| Swr1 complex | A multisubunit protein complex that is involved in chromatin remodeling. It is required for the incorporation of the histone variant H2AZ into chromatin. In S. cerevisiae, the complex contains Swr1p, a Swi2/Snf2-related ATPase, and 12 additional subunits. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| methylated histone binding | Binding to a histone in which a residue has been modified by methylation. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| chromatin organization | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. |
| histone acetylation | The modification of a histone by the addition of an acetyl group. |
| histone H2A acetylation | The modification of histone H2A by the addition of an acetyl group. |
| histone H4 acetylation | The modification of histone H4 by the addition of an acetyl group. |
| positive regulation of apoptotic process | Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process. |
| positive regulation of double-strand break repair via homologous recombination | Any process that activates or increases the frequency, rate or extent of double-strand break repair via homologous recombination. |
| regulation of cell cycle | Any process that modulates the rate or extent of progression through the cell cycle. |
| regulation of DNA-templated transcription | Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLYLEDYLEM | IEQLPMDLRD | RFTEMREMDL | QVQNAMDQLE | QRVSEFFMNA | KKNKPEWREE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QMASIKKDYY | KALEDADEKV | QLANQIYDLV | DRHLRKLDQE | LAKFKMELEA | DNAGITEILE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RRSLELDAPS | QPVNNHHAHS | HTPVEKRKYN | PTSHHTATDH | IPEKKFKSEA | LLSTLTSDAS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KENTLGCRNN | NSTASCNNAY | NVNSSQPLAS | YNIGSLSSGA | GAGAITMAAA | QAVQATAQMK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EGRRTSSLKA | SYEAFKNNDF | QLGKEFSMPR | ETAGYSSSSA | LMTTLTQNAS | SSAADSRSGR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KSKNNTKSSS | QQSSSSSSSS | SSSSLSLCSS | SSTVVQEVSQ | QTTVVPESDS | NSQVDWTYDP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NEPRYCICNQ | VSYGEMVGCD | NQDCPIEWFH | YGCVGLTEAP | KGKWFCPQCT | AAMKRRGSRH |
| K |