Q9Z1X9
PR
Gene name |
Cdc45 (Cdc45l, Cdc45l2) |
Protein name |
Cell division control protein 45 homolog |
Names |
PORC-PI-1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:12544 |
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 Q9Z1X9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9Z1X9-F1 | Predicted | AlphaFoldDB |
19 variants for Q9Z1X9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389407981 | 44 | H>R | No | EVA | |
| rs3389397178 | 52 | V>F | No | EVA | |
| rs3389422062 | 94 | I>L | No | EVA | |
| rs3389397156 | 95 | F>Y | No | EVA | |
| rs3389397111 | 96 | F>L | No | EVA | |
| rs3389397125 | 121 | Q>* | No | EVA | |
| rs3389321600 | 122 | E>D | No | EVA | |
| rs3389398775 | 147 | D>E | No | EVA | |
| rs3389402681 | 162 | E>* | No | EVA | |
| rs3389414581 | 176 | E>K | No | EVA | |
| rs3413052092 | 177 | W>R | No | EVA | |
| rs3389354580 | 191 | Y>C | No | EVA | |
| rs3389402302 | 237 | K>Q | No | EVA | |
| rs3389385821 | 238 | Y>F | No | EVA | |
| rs3389398755 | 242 | V>I | No | EVA | |
| rs3389397120 | 246 | Q>* | No | EVA | |
| rs3389402313 | 248 | H>L | No | EVA | |
| rs3389405136 | 512 | E>K | No | EVA | |
| rs3389405067 | 517 | D>Y | No | EVA |
No associated diseases with Q9Z1X9
No regional properties for Q9Z1X9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9Z1X9 | |||
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| centrosome | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. |
| ciliary basal body | A membrane-tethered, short cylindrical array of microtubules and associated proteins found at the base of a eukaryotic cilium (also called flagellum) that is similar in structure to a centriole and derives from it. The cilium basal body is the site of assembly and remodelling of the cilium and serves as a nucleation site for axoneme growth. As well as anchoring the cilium, it is thought to provide a selective gateway regulating the entry of ciliary proteins and vesicles by intraflagellar transport. |
| CMG complex | A protein complex that contains the GINS complex, Cdc45p, and the heterohexameric MCM complex, and that is involved in unwinding DNA during replication. |
| DNA replication preinitiation complex | A protein-DNA complex assembled at eukaryotic DNA replication origins immediately prior to the initiation of DNA replication. The preinitiation complex is formed by the assembly of additional proteins onto an existing prereplicative complex. In budding yeast, the additional proteins might include Cdc45p, Sld2p, Sld3p, Dpb11p, DNA polymerases, and others; in fission yeast the GINS complex is present. |
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| chromatin binding | Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. |
| DNA replication origin binding | Binding to a DNA replication origin, a unique DNA sequence of a replicon at which DNA replication is initiated and proceeds bidirectionally or unidirectionally. |
| single-stranded DNA binding | Binding to single-stranded DNA. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA replication initiation | The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate. |
| DNA unwinding involved in DNA replication | The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication. |
| double-strand break repair via break-induced replication | The error-free repair of a double-strand break in DNA in which the centromere-proximal end of a broken chromosome searches for a homologous region in an intact chromosome. DNA synthesis initiates from the 3' end of the invading DNA strand, using the intact chromosome as the template, and progresses to the end of the chromosome. |
| mitotic DNA replication preinitiation complex assembly | Any DNA replication preinitiation complex assembly that is involved in mitotic cell cycle. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O75419 | CDC45 | Cell division control protein 45 homolog | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFVTDFRKEF | YETVHNQRVL | LFVASDVDAL | CACKILQALF | QCDHVQYTLV | PVSGWQELET |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AYLEHKEQFS | YFILINCGAN | VDLLDILQPD | EDSIFFVCDT | HRPVNVVNVY | NDTQIKLLIK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QEDDLEVPAY | DDIFRDEAED | EDLSDSDGDG | SEPSEKRTRL | EEEIVERNRK | RRQRREWEAR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RKDILFDYEQ | YEYYGTSSAM | VMFDLAWMMS | KDLNDMLWWA | IVGLTDQWVH | DKITQMKYVT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DVGILQRHVS | RHNHRNEAEE | NMLSVDCTRI | SFEYDLCLVL | YQHWSLHESL | YNTSYTAARF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KLWSVHGQKR | LQEFLADMGL | PLKQVKQKFQ | SMDVSLKGNL | REMIEESANK | FGMKDMRVQT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FSIQFGFKHK | FLASDVVFAT | MSLMESPEKD | GSGTDHFIQA | LDSLSRSNLD | KLYLGLELAK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KHLQATQQTI | ASCLCTNLVT | SQGPFLYCSL | MEGTPDVTLF | SKPASLSLLS | RHLLKSFVYS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TKNRRCKLLP | LVMAAPLSVE | QGTVTVVGIP | PETDSSDRKN | FFGRAFEKAA | ESTSSRTLHN |
| 550 | 560 | ||||
| YFDLSVIELK | AEDRSKFLDA | LVSLLS |