Q60452
PR
Gene name |
ERCC2 (XPD) |
Protein name |
General transcription and DNA repair factor IIH helicase subunit XPD |
Names |
TFIIH subunit XPD, CXPD, DNA excision repair protein ERCC-2, DNA repair protein complementing XP-D cells, Xeroderma pigmentosum group D-complementing protein |
Species |
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
KEGG Pathway |
|
EC number |
3.6.4.12: Acting on ATP; involved in cellular and subcellular movement |
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 Q60452
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q60452-F1 | Predicted | AlphaFoldDB |
1 variants for Q60452
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 286 | R>Q | No |
No associated diseases with Q60452
6 regional properties for Q60452
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site | 229 - 238 | IPR002464 |
| domain | Helicase-like, DEXD box c2 type | 8 - 280 | IPR006554 |
| domain | ATP-dependent helicase, C-terminal | 524 - 699 | IPR006555 |
| domain | RAD3-like helicase, DEAD | 72 - 256 | IPR010614 |
| domain | Helical and beta-bridge domain | 272 - 413 | IPR010643 |
| domain | Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type | 7 - 283 | IPR014013 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.4.12 | Acting on ATP; involved in cellular and subcellular movement |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| CAK-ERCC2 complex | A protein complex formed by the association of the cyclin-dependent protein kinase activating kinase (CAK) holoenzyme complex with ERCC2. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| MMXD complex | A protein complex that contains the proteins MMS19, MIP18 and XPD, localizes to mitotic spindle during mitosis, and is required for proper chromosome segregation. |
| 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. |
| spindle | The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart. |
| transcription factor TFIIH holo complex | A complex that is capable of kinase activity directed towards the C-terminal Domain (CTD) of the largest subunit of RNA polymerase II and is essential for initiation at RNA polymerase II promoters in vitro. It is composed of the core TFIIH complex and the TFIIK complex. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| 5'-3' DNA helicase activity | Unwinding a DNA helix in the 5' to 3' direction, driven by ATP hydrolysis. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| metal ion binding | Binding to a metal ion. |
| protein C-terminus binding | Binding to a protein C-terminus, the end of a peptide chain at which the 1-carboxyl function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. |
| protein N-terminus binding | Binding to a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
| chromosome segregation | The process in which genetic material, in the form of chromosomes, is organized into specific structures and then physically separated and apportioned to two or more sets. In eukaryotes, chromosome segregation begins with the condensation of chromosomes, includes chromosome separation, and ends when chromosomes have completed movement to the spindle poles. |
| hair cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of a hair cell. |
| 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). |
| regulation of mitotic cell cycle phase transition | Any process that modulates the frequency, rate or extent of mitotic cell cycle phase transition. |
| response to oxidative stress | 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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. |
| transcription by RNA polymerase II | The synthesis of RNA from a DNA template by RNA polymerase II (RNAP II), originating at an RNA polymerase II promoter. Includes transcription of messenger RNA (mRNA) and certain small nuclear RNAs (snRNAs). |
| transcription-coupled nucleotide-excision repair | The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKLNVDGLLV | YFPYDYIYPE | QFSYMLELKR | TLDAKGHGVL | EMPSGTGKTV | SLLALIVAYQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RAFPLEVTKL | IYCSRTVPEI | EKVIEELRKL | LSFYEQQEGE | KLPFLGLALS | SRKNLCIHPE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VTPLRFGKDV | DGKCHSLTAS | YVRAQYQQDA | SLPHCRFYEE | FDAHGRQVPL | PAGIYNLDDL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KALGQRQGWC | PYFLARYSIL | HANVVVYSYH | YLLDPKIADL | VSKELARKAV | VVFDEAHNID |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NVCIDSMSVN | LTRRTLDRCQ | SNLDTLQKTV | LRIKETDEQR | LRDEYRRLVE | GLREASAARE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TDAHLANPVL | PDEVLQEAVP | GSIRTAEHFL | GFLRRLLEYV | KWRLRVQHVV | QESPPAFLSG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LAQRVCIQRK | PLRFCAERLR | SLLHTLEIAD | LADFSPLTLL | ANFATLVSTY | AKGFTIIIEP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FDDRTPTIAN | PILHFSCMDA | SLAIKPVFER | FQSVIITSGT | LSPLDIYPKI | LDFHPVTMAT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FTMTLARVCL | CPMIIGRGND | QVAISSKFET | REDIAVIRNY | GNLLLEMSAV | VPDGIVAFFT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SYQYMESTVA | SWYEQGILEN | IQRNKLLFIE | TQDGAETSVA | LEKYQEACEN | GRGAILLSVA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RGKVSEGIDF | VHHYGRAVIM | FGVPYVYTQS | RILKARLEYL | RDQFQIREND | FLTFDAMRHA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| AQCVGRAIRG | KTDYGLMVFA | DKRFARADKR | GKLPRWIQEH | LTDSNLNLTV | DEGVQVAKYF |
| 730 | 740 | 750 | |||
| LRQMAQPFHR | EDQLGLSLLS | LEQLQSEETL | RRVEQIAQQL |