P14736
PR
Gene name |
RAD4 (YER162C) |
Protein name |
DNA repair protein RAD4 |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YER162C |
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
12 structures for P14736
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2M14 | NMR | - | B | 76-115 | PDB |
| 2QSF | X-ray | 235 A | A | 101-632 | PDB |
| 2QSG | X-ray | 310 A | A | 101-632 | PDB |
| 2QSH | X-ray | 281 A | A | 101-632 | PDB |
| 4YIR | X-ray | 305 A | A | 101-632 | PDB |
| 6CFI | X-ray | 336 A | A | 101-632 | PDB |
| 6UBF | X-ray | 460 A | A | 101-632 | PDB |
| 6UG1 | X-ray | 283 A | A | 129-632 | PDB |
| 6UIN | X-ray | 335 A | A | 101-632 | PDB |
| 7K04 | EM | 925 A | A | 1-754 | PDB |
| 7M2U | EM | 820 A | A | 1-754 | PDB |
| AF-P14736-F1 | Predicted | AlphaFoldDB |
25 variants for P14736
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s05-502667 | 75 | P>S | No | SGRP | |
| s05-502528 | 121 | N>S | No | SGRP | |
| s05-502363 | 176 | P>L | No | SGRP | |
| s05-502240 | 217 | T>I | No | SGRP | |
| s05-502226 | 222 | N>H | No | SGRP | |
| s05-502205 | 229 | T>S | No | SGRP | |
| s05-502199 | 231 | K>E | No | SGRP | |
| s05-502189 | 234 | E>V | No | SGRP | |
| s05-502182 | 236 | S>R | No | SGRP | |
| s05-502180 | 237 | A>V | No | SGRP | |
| s05-502166 | 242 | K>E | No | SGRP | |
| s05-502164 | 242 | K>N | No | SGRP | |
| s05-502159 | 244 | K>M | No | SGRP | |
| s05-502062 | 276 | C>* | No | SGRP | |
| s05-501702 | 396 | D>E | No | SGRP | |
| s05-501529 | 454 | K>R | No | SGRP | |
| s05-501306 | 528 | D>E | No | SGRP | |
| s05-501065 | 609 | L>V | No | SGRP | |
| s05-500980 | 637 | N>S | No | SGRP | |
| s05-500845 | 682 | I>T | No | SGRP | |
| s05-500792 | 700 | G>S | No | SGRP | |
| s05-500778 | 704 | H>Q | No | SGRP | |
| s05-500733 | 719 | L>F | No | SGRP | |
| s05-500707 | 728 | E>V | No | SGRP | |
| s05-500675 | 739 | D>N | No | SGRP |
No associated diseases with P14736
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| nucleotide-excision repair factor 2 complex | One of several protein complexes involved in nucleotide-excision repair; possesses damaged DNA binding activity. In S. cerevisiae, it is composed of Rad4p and Rad23p. |
| 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. |
| XPC complex | A nucleotide-excision repair complex that is involved in damage sensing during global genome nucleotide excision repair (GG-NER). It is part of the pre-incision (or initial recognition) complex bound to sites of DNA damage. In human, it is composed of XPC, RAD23B and CETN2. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| damaged DNA binding | Binding to damaged DNA. |
| single-strand break-containing DNA binding | Binding to damaged DNA containing single-strand breaks (SSBs). |
| single-stranded DNA binding | Binding to single-stranded DNA. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA topological change | The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number. |
| mismatch repair | A system for the correction of errors in which an incorrect base, which cannot form hydrogen bonds with the corresponding base in the parent strand, is incorporated into the daughter strand. The mismatch repair system promotes genomic fidelity by repairing base-base mismatches, insertion-deletion loops and heterologies generated during DNA replication and recombination. |
| negative regulation of transcription by RNA polymerase II | Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. |
| 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). |
| nucleotide-excision repair, DNA damage recognition | The identification of lesions in DNA, such as pyrimidine-dimers, intrastrand cross-links, and bulky adducts. The wide range of substrate specificity suggests the repair complex recognizes distortions in the DNA helix. |
| proteasome-mediated ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNEDLPKEYF | ELIRKALNEK | EAEKAPLSRR | RRVRRKNQPL | PDAKKKFKTG | LNELPRESVV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TVNLDSSDDG | VVTVPTDDSV | EEIQSSEEDY | DSEEFEDVTD | GNEVAGVEDI | SVEIKPSSKR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NSDARRTSRN | VCSNEERKRR | KYFHMLYLVC | LMVHGFIRNE | WINSKRLSRK | LSNLVPEKVF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELLHPQKDEE | LPLRSTRKLL | DGLKKCMELW | QKHWKITKKY | DNVGLYMRTW | KEIEMSANNK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RKFKTLKRSD | FLRAVSKGHG | DPDISVQGFV | AMLRACNVNA | RLIMSCQPPD | FTNMKIDTSL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NGNNAYKDMV | KYPIFWCEVW | DKFSKKWITV | DPVNLKTIEQ | VRLHSKLAPK | GVACCERNML |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RYVIAYDRKY | GCRDVTRRYA | QWMNSKVRKR | RITKDDFGEK | WFRKVITALH | HRKRTKIDDY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EDQYFFQRDE | SEGIPDSVQD | LKNHPYYVLE | QDIKQTQIVK | PGCKECGYLK | VHGKVGKVLK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VYAKRDIADL | KSARQWYMNG | RILKTGSRCK | KVIKRTVGRP | KGEAEEEDER | LYSFEDTELY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IPPLASASGE | ITKNTFGNIE | VFAPTMIPGN | CCLVENPVAI | KAARFLGVEF | APAVTSFKFE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RGSTVKPVLS | GIVVAKWLRE | AIETAIDGIE | FIQEDDNRKE | HLLGALESWN | TLLLKLRIRS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KLNSTYGKIA | EEEPNVTKEQ | NIADNHDNTE | TFMGGGFLPG | IANHEARPYS | EPSEPEDSLD |
| 730 | 740 | 750 | |||
| YVSVDKAEES | ATDDDVGEDY | SDFMKELEMS | EESD |