Q0VBY8
PR
Gene name |
DDB2 |
Protein name |
DNA damage-binding protein 2 |
Names |
Damage-specific DNA-binding protein 2 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:519357 |
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
1 structures for Q0VBY8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0VBY8-F1 | Predicted | AlphaFoldDB |
111 variants for Q0VBY8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs448454618 | 2 | A>G | No | EVA | |
| rs434626387 | 6 | R>L | No | EVA | |
| rs453217511 | 8 | E>* | No | EVA | |
| rs432132269 | 13 | P>H | No | EVA | |
| rs471620960 | 13 | P>S | No | EVA | |
| rs457011015 | 15 | V>E | No | EVA | |
| rs475509298 | 17 | V>G | No | EVA | |
| rs719563393 | 21 | S>N | No | EVA | |
| rs442397621 | 27 | P>A | No | EVA | |
| rs442397621 | 27 | P>T | No | EVA | |
| rs460732548 | 34 | A>T | No | EVA | |
| rs459225373 | 41 | G>C | No | EVA | |
| rs450813081 | 44 | S>P | No | EVA | |
| rs462671528 | 45 | S>R | No | EVA | |
| rs481039783 | 47 | R>S | No | EVA | |
| rs448165406 | 48 | F>I | No | EVA | |
| rs433629372 | 49 | D>A | No | EVA | |
| rs445682997 | 49 | D>E | No | EVA | |
| rs466509161 | 49 | D>N | No | EVA | |
| rs456861659 | 51 | G>A | No | EVA | |
| rs437563760 | 51 | G>R | No | EVA | |
| rs475264942 | 52 | L>F | No | EVA | |
| rs475264942 | 52 | L>I | No | EVA | |
| rs454273282 | 53 | W>G | No | EVA | |
| rs472694474 | 54 | A>G | No | EVA | |
| rs439721781 | 55 | G>V | No | EVA | |
| rs462708394 | 56 | L>F | No | EVA | |
| rs443565981 | 56 | L>S | No | EVA | |
| rs476667662 | 56 | L>V | No | EVA | |
| rs443565981 | 56 | L>W | No | EVA | |
| rs481075235 | 57 | A>P | No | EVA | |
| rs448202407 | 58 | S>G | No | EVA | |
| rs478847024 | 58 | S>R | No | EVA | |
| rs460218275 | 58 | S>T | No | EVA | |
| rs445751010 | 59 | L>R | No | EVA | |
| rs464207352 | 60 | R>G | No | EVA | |
| rs450298430 | 60 | R>L | No | EVA | |
| rs450298430 | 60 | R>P | No | EVA | |
| rs450298430 | 60 | R>Q | No | EVA | |
| rs468871072 | 61 | V>A | No | EVA | |
| rs468871072 | 61 | V>D | No | EVA | |
| rs468871072 | 61 | V>G | No | EVA | |
| rs449675180 | 61 | V>L | No | EVA | |
| rs435833839 | 63 | P>A | No | EVA | |
| rs472880501 | 69 | V>G | No | EVA | |
| rs454410265 | 69 | V>I | No | EVA | |
| rs433347514 | 71 | A>G | No | EVA | |
| rs443592972 | 73 | H>Q | No | EVA | |
| rs476704658 | 73 | H>R | No | EVA | |
| rs451797565 | 73 | H>Y | No | EVA | |
| rs473995801 | 75 | H>D | No | EVA | |
| rs473995801 | 75 | H>Y | No | EVA | |
| rs441916620 | 76 | K>Q | No | EVA | |
| rs460254991 | 76 | K>R | No | EVA | |
| rs460254991 | 76 | K>T | No | EVA | |
| rs478889647 | 77 | L>P | No | EVA | |
| rs457864082 | 78 | G>S | No | EVA | |
| rs468208271 | 82 | W>R | No | EVA | |
| rs480207381 | 86 | Q>L | No | EVA | |
| rs474023217 | 93 | F>L | No | EVA | |
| rs452946597 | 94 | L>P | No | EVA | |
| rs438386453 | 106 | A>S | No | EVA | |
| rs456732207 | 118 | W>G | No | EVA | |
| rs475198107 | 119 | H>P | No | EVA | |
| rs443129329 | 122 | H>P | No | EVA | |
| rs461456718 | 130 | S>P | No | EVA | |
| rs480102881 | 138 | W>R | No | EVA | |
| rs440550045 | 138 | W>S | No | EVA | |
| rs459001988 | 139 | N>I | No | EVA | |
| rs469422627 | 147 | T>A | No | EVA | |
| rs481392267 | 149 | I>L | No | EVA | |
| rs480243176 | 168 | T>P | No | EVA | |
| rs447912904 | 171 | F>Y | No | EVA | |
| rs460018025 | 178 | G>V | No | EVA | |
| rs475863249 | 260 | A>D | No | EVA | |
| rs443006374 | 270 | D>A | No | EVA | |
| rs461596496 | 272 | R>P | No | EVA | |
| rs473589192 | 276 | G>W | No | EVA | |
| rs459015525 | 278 | S>T | No | EVA | |
| rs477413843 | 279 | S>T | No | EVA | |
| rs463662220 | 282 | H>P | No | EVA | |
| rs449085220 | 284 | L>R | No | EVA | |
| rs434566376 | 288 | H>P | No | EVA | |
| rs431955555 | 290 | V>A | No | EVA | |
| rs431955555 | 290 | V>D | No | EVA | |
| rs464867643 | 290 | V>L | No | EVA | |
| rs456730201 | 291 | N>S | No | EVA | |
| rs456730201 | 291 | N>T | No | EVA | |
| rs475194333 | 292 | A>P | No | EVA | |
| rs468776377 | 311 | I>T | No | EVA | |
| rs435766083 | 314 | Y>C | No | EVA | |
| rs447703966 | 317 | C>G | No | EVA | |
| rs466074637 | 320 | D>A | No | EVA | |
| rs433147763 | 330 | H>P | No | EVA | |
| rs451555121 | 336 | L>M | No | EVA | |
| rs476412239 | 337 | T>P | No | EVA | |
| rs437917478 | 338 | P>H | No | EVA | |
| rs441781115 | 340 | K>N | No | EVA | |
| rs474825233 | 340 | K>R | No | EVA | |
| rs452492938 | 352 | V>L | No | EVA | |
| rs41780096 | 358 | P>R | No | EVA | |
| rs470992823 | 392 | G>V | No | EVA | |
| rs469957720 | 400 | N>H | No | EVA | |
| rs444345920 | 411 | G>V | No | EVA | |
| rs463678085 | 417 | W>R | No | EVA | |
| rs482220187 | 418 | S>C | No | EVA | |
| rs442710489 | 421 | D>Y | No | EVA | |
| rs461011480 | 422 | A>D | No | EVA | |
| rs446513678 | 424 | T>S | No | EVA | |
| rs464865829 | 425 | Q>K | No | EVA | |
| rs477040007 | 427 | K>G | No | EVA |
No associated diseases with Q0VBY8
5 regional properties for Q0VBY8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | WD40 repeat | 99 - 139 | IPR001680-1 |
| repeat | WD40 repeat | 143 - 184 | IPR001680-2 |
| repeat | WD40 repeat | 230 - 279 | IPR001680-3 |
| repeat | WD40 repeat | 277 - 315 | IPR001680-4 |
| conserved_site | WD40 repeat, conserved site | 257 - 271 | IPR019775 |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell junction | A cellular component that forms a specialized region of connection between two or more cells, or between a cell and the extracellular matrix, or between two membrane-bound components of a cell, such as flagella. |
| Cul4B-RING E3 ubiquitin ligase complex | A ubiquitin ligase complex in which a cullin from the Cul4B subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by unknown subunits. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| site of DNA damage | A region of a chromosome at which DNA damage has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| damaged DNA binding | Binding to damaged DNA. |
| protein-containing complex binding | Binding to a macromolecular complex. |
| ubiquitin-protein transferase activity | Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| histone H2A monoubiquitination | The modification of histone H2A by addition of a single ubiquitin group. |
| nucleotide-excision repair | A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). |
| protein autoubiquitination | The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink. |
| protein polyubiquitination | Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. |
| pyrimidine dimer repair | The repair of UV-induced T-T, C-T and C-C dimers. |
| response to UV | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers. |
| UV-damage excision repair | A DNA repair process that is initiated by an endonuclease that introduces a single-strand incision immediately 5' of a UV-induced damage site. UV-damage excision repair acts on both cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone 6-4 photoproducts (6-4PPs). |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q92466 | DDB2 | DNA damage-binding protein 2 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAPRKRPENQ | KTPEVVVRPK | SKRNRSPREL | EPEAKKLCVK | GPGSSRRFDS | GLWAGLASLR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VPPLCSSIVR | ALHQHKLGTA | AWPSLQQGLQ | QSFLNSLASY | RIFQKAAPFD | RRATSLAWHP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| THPSTLAVGS | KGGDILLWNF | GIKDKPTFIK | GIGAGGSITG | MKFNPLNTNQ | FFTSSMEGTT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLQDFKGNTL | RVFASSDTCN | VWFCSLDVSV | KSRVVVTGDN | VGHVILLNMD | GRELWNLRMH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KKKVTHVALN | PCCDWLLATA | SVDQTVKIWD | LRQVRGKSSF | LHSLPHRHPV | NAAHFSPDGA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QLLTTDQKSE | IRVYSACQWD | CPPSLIPHPH | RHFQHLTPIK | ASWHPRYNLI | VVGRYPDPNF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KSCSPHELRT | IDVFDGSSGK | IMYQLYDPES | SGIMSLNEFN | PMGDTLASVM | GYHILVWSPE |
| DAGTQK |