P35601
PR
Gene name |
Rfc1 (Ibf-1, Recc1) |
Protein name |
Replication factor C subunit 1 |
Names |
A1-P145, Activator 1 140 kDa subunit, A1 140 kDa subunit, Activator 1 large subunit, Activator 1 subunit 1, Differentiation-specific element-binding protein, ISRE-binding protein, Replication factor C 140 kDa subunit, RF-C 140 kDa subunit, RFC140, Replication factor C large subunit |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:19687 |
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 P35601
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P35601-F1 | Predicted | AlphaFoldDB |
No variants for P35601
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P35601 | |||||
No associated diseases with P35601
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| DNA replication factor C complex | A complex that loads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) onto DNA, thereby permitting processive DNA synthesis catalyzed by DNA polymerase. In eukaryotes the complex consists of five polypeptides. |
| Elg1 RFC-like complex | A pentameric replication factor C (RLC) complex, which unloads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) from chromatin and has roles in telomere length regulation and other aspects of genome stability. In Saccharomyces the subunits are known as Elg1p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p. |
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| 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. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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). |
| DNA clamp loader activity | Facilitating the opening of the ring structure of the PCNA complex, or any of the related sliding clamp complexes, and their closing around the DNA duplex, driven by ATP hydrolysis. |
| DNA clamp unloader activity | Facilitating the opening of the ring structure of the PCNA complex, or any of the related sliding clamp complexes, and their removal from the DNA duplex, driven by ATP hydrolysis. |
| double-stranded DNA binding | Binding to double-stranded DNA. |
| protein domain specific binding | Binding to a specific domain of a protein. |
| sequence-specific DNA binding | Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA clamp unloading | The process of removing the PCNA complex from DNA when Okazaki fragments are completed or the replication fork terminates. |
| 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. |
| DNA replication | The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. |
| negative regulation of DNA-templated transcription | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. |
| 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. |
| positive regulation of DNA-templated transcription | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDIRKFFGVI | SSGKKPVNET | VKNEKTKASE | GTVKGKKGVK | EAKVNNSGKE | DASKPKQHSK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKRIIYDSDS | ESEETVQVKN | AKKKSEKLSL | SYKPGKVSQK | DPVTYVSETD | EDDDFVCKKA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ASKSKENGVS | TNSYLGTSNV | KKNEENVKTK | NKPLSPIKLT | PTSVLDYFGT | ESVQRSGKKM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VTSKRKESSQ | NTEDSRLNDE | AIAKQLQLDE | DAELERQLHE | DEEFARTLAL | LDEEPKIKKA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RKDSEEGEES | FSSVQDDLSK | AEKQKSPNKA | ELFSTARKTY | SPAKHGKGRA | SEDAKQPCKS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AHRKEACSSP | KASAKLALMK | AKEESSYNET | ELLAARRKES | ATEPKGEKTT | PKKTKVSPTK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RESVSPEDSE | KKRTNYQAYR | SYLNREGPKA | LGSKEIPKGA | ENCLEGLTFV | ITGVLESIER |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DEAKSLIERY | GGKVTGNVSK | KTNYLVMGRD | SGQSKSDKAA | ALGTKILDED | GLLDLIRTMP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GKRSKYEMAA | EAEMKKEKSK | LERTPQKNDQ | GKRKISPAKK | ESESKKCKLT | LLKNSPMKAV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KKEASTCPRG | LDVKETHGNR | SSNKEECLLW | VDKYKPASLK | NIIGQQGDQS | CANKLLRWLR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NWHKSSPEEK | KHAAKFGKLA | SKDDGSSFKA | ALLSGPPGVG | KTTTASLVCQ | ELGYSYVELN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ASDTRSKNSL | KAVVAESLNN | TSIKGFYTSG | AAPSVSARHA | LIMDEVDGMA | GNEDRGGIQE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LIGLIKHTKI | PIICMCNDRN | HPKIRSLVHY | CFDLRFQRPR | VEQIKSAMLS | IAFKEGLKIP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PPAMNEIILG | ANQDVRQVLH | NLSMWCAQSK | ALTYDQAKAD | SQRAKKDIRL | GPFDVTRKVF |
| 850 | 860 | 870 | 880 | 890 | 900 |
| AAGEETAHMS | LMDKSDLFFH | DYSIAPLFVQ | ENYLHVKPVA | AGGDMKKHLM | LLSRAADSIC |
| 910 | 920 | 930 | 940 | 950 | 960 |
| DGDLVDNQIR | SKQNWSLLPT | QAIYASVLPG | ELMRGYMTQF | PSFPSWLGKH | SSTGKHDRIV |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| QDLSLHMSLR | TYSSKRTVNM | DYLSHIRDAL | VRPLTSQGVE | GAQHVIKLMD | TYYLMKEDFE |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| NIMEVSSWGG | KPSAFSKLDP | KVKAAFTRAY | NKEAHLTPYS | LQVVKTSRLS | TGPALDSEYS |
| 1090 | 1100 | 1110 | 1120 | 1130 | |
| EEFQEDDTQS | EKEQDAVETD | AMIKKKTRSS | KPSKSEREKE | SKKGKGKNWK | K |