P35601 · RFC1_MOUSE
- ProteinReplication factor C subunit 1
- GeneRfc1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1131 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | DNA replication factor C complex | |
Cellular Component | Elg1 RFC-like complex | |
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA clamp loader activity | |
Molecular Function | DNA clamp unloader activity | |
Molecular Function | DNA-binding transcription factor binding | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | protein domain specific binding | |
Molecular Function | sequence-specific DNA binding | |
Biological Process | DNA repair | |
Biological Process | DNA-templated DNA replication | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReplication factor C subunit 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP35601
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000121773 | 1-1131 | Replication factor C subunit 1 | |||
Sequence: MDIRKFFGVISSGKKPVNETVKNEKTKASEGTVKGKKGVKEAKVNNSGKEDASKPKQHSKKKRIIYDSDSESEETVQVKNAKKKSEKLSLSYKPGKVSQKDPVTYVSETDEDDDFVCKKAASKSKENGVSTNSYLGTSNVKKNEENVKTKNKPLSPIKLTPTSVLDYFGTESVQRSGKKMVTSKRKESSQNTEDSRLNDEAIAKQLQLDEDAELERQLHEDEEFARTLALLDEEPKIKKARKDSEEGEESFSSVQDDLSKAEKQKSPNKAELFSTARKTYSPAKHGKGRASEDAKQPCKSAHRKEACSSPKASAKLALMKAKEESSYNETELLAARRKESATEPKGEKTTPKKTKVSPTKRESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAENCLEGLTFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKILDEDGLLDLIRTMPGKRSKYEMAAEAEMKKEKSKLERTPQKNDQGKRKISPAKKESESKKCKLTLLKNSPMKAVKKEASTCPRGLDVKETHGNRSSNKEECLLWVDKYKPASLKNIIGQQGDQSCANKLLRWLRNWHKSSPEEKKHAAKFGKLASKDDGSSFKAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKNSLKAVVAESLNNTSIKGFYTSGAAPSVSARHALIMDEVDGMAGNEDRGGIQELIGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKSAMLSIAFKEGLKIPPPAMNEIILGANQDVRQVLHNLSMWCAQSKALTYDQAKADSQRAKKDIRLGPFDVTRKVFAAGEETAHMSLMDKSDLFFHDYSIAPLFVQENYLHVKPVAAGGDMKKHLMLLSRAADSICDGDLVDNQIRSKQNWSLLPTQAIYASVLPGELMRGYMTQFPSFPSWLGKHSSTGKHDRIVQDLSLHMSLRTYSSKRTVNMDYLSHIRDALVRPLTSQGVEGAQHVIKLMDTYYLMKEDFENIMEVSSWGGKPSAFSKLDPKVKAAFTRAYNKEAHLTPYSLQVVKTSRLSTGPALDSEYSEEFQEDDTQSEKEQDAVETDAMIKKKTRSSKPSKSEREKESKKGKGKNWKK | ||||||
Cross-link | 49 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 66 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 68 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 70 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 72 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 107 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 109 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 155 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 160 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 162 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 163 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 172 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 189 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 244 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 250 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 253 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 281 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 309 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 365 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 535 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1090 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can form a complex either with RFC1 or with RAD17. The former interacts with PCNA in the presence of ATP, while the latter has ATPase activity but is not stimulated by PCNA (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 14-87 | Disordered | ||||
Sequence: KKPVNETVKNEKTKASEGTVKGKKGVKEAKVNNSGKEDASKPKQHSKKKRIIYDSDSESEETVQVKNAKKKSEK | ||||||
Compositional bias | 18-87 | Basic and acidic residues | ||||
Sequence: NETVKNEKTKASEGTVKGKKGVKEAKVNNSGKEDASKPKQHSKKKRIIYDSDSESEETVQVKNAKKKSEK | ||||||
Region | 92-111 | Disordered | ||||
Sequence: YKPGKVSQKDPVTYVSETDE | ||||||
Region | 120-201 | Disordered | ||||
Sequence: AASKSKENGVSTNSYLGTSNVKKNEENVKTKNKPLSPIKLTPTSVLDYFGTESVQRSGKKMVTSKRKESSQNTEDSRLNDEA | ||||||
Compositional bias | 124-142 | Polar residues | ||||
Sequence: SKENGVSTNSYLGTSNVKK | ||||||
Compositional bias | 178-201 | Basic and acidic residues | ||||
Sequence: KKMVTSKRKESSQNTEDSRLNDEA | ||||||
Compositional bias | 225-267 | Basic and acidic residues | ||||
Sequence: ARTLALLDEEPKIKKARKDSEEGEESFSSVQDDLSKAEKQKSP | ||||||
Region | 225-378 | Disordered | ||||
Sequence: ARTLALLDEEPKIKKARKDSEEGEESFSSVQDDLSKAEKQKSPNKAELFSTARKTYSPAKHGKGRASEDAKQPCKSAHRKEACSSPKASAKLALMKAKEESSYNETELLAARRKESATEPKGEKTTPKKTKVSPTKRESVSPEDSEKKRTNYQA | ||||||
Compositional bias | 285-309 | Basic and acidic residues | ||||
Sequence: HGKGRASEDAKQPCKSAHRKEACSS | ||||||
Compositional bias | 322-375 | Basic and acidic residues | ||||
Sequence: KEESSYNETELLAARRKESATEPKGEKTTPKKTKVSPTKRESVSPEDSEKKRTN | ||||||
Region | 354-528 | Interferon-stimulated-response-element binding region | ||||
Sequence: TKVSPTKRESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAENCLEGLTFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKILDEDGLLDLIRTMPGKRSKYEMAAEAEMKKEKSKLERTPQKNDQGKRKISPAKKESESKKCK | ||||||
Domain | 399-489 | BRCT | ||||
Sequence: GAENCLEGLTFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKILDEDGLLDLIRTMPGKRSKYEMA | ||||||
Region | 491-525 | Disordered | ||||
Sequence: EAEMKKEKSKLERTPQKNDQGKRKISPAKKESESK | ||||||
Region | 1073-1131 | Disordered | ||||
Sequence: PALDSEYSEEFQEDDTQSEKEQDAVETDAMIKKKTRSSKPSKSEREKESKKGKGKNWKK | ||||||
Compositional bias | 1079-1093 | Acidic residues | ||||
Sequence: YSEEFQEDDTQSEKE | ||||||
Compositional bias | 1094-1123 | Basic and acidic residues | ||||
Sequence: QDAVETDAMIKKKTRSSKPSKSEREKESKK | ||||||
Motif | 1104-1108 | Nuclear localization signal | ||||
Sequence: KKKTR |
Sequence similarities
Belongs to the activator 1 large subunit family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P35601-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,131
- Mass (Da)125,985
- Last updated1996-10-01 v2
- ChecksumA6F4F970A7F9EE94
P35601-2
- Name2
- NoteAlternative use of an acceptor site.
- Differences from canonical
- 614-614: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5U4B1 | Q5U4B1_MOUSE | Rfc1 | 1132 | ||
A0A0N4SVN6 | A0A0N4SVN6_MOUSE | Rfc1 | 212 | ||
A0A0N5E9G7 | A0A0N5E9G7_MOUSE | Rfc1 | 1130 | ||
G3UWX1 | G3UWX1_MOUSE | Rfc1 | 1145 | ||
G3X8Z6 | G3X8Z6_MOUSE | Rfc1 | 1131 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 18-87 | Basic and acidic residues | ||||
Sequence: NETVKNEKTKASEGTVKGKKGVKEAKVNNSGKEDASKPKQHSKKKRIIYDSDSESEETVQVKNAKKKSEK | ||||||
Sequence conflict | 66 | in Ref. 3; AAA79698 | ||||
Sequence: Y → N | ||||||
Compositional bias | 124-142 | Polar residues | ||||
Sequence: SKENGVSTNSYLGTSNVKK | ||||||
Compositional bias | 178-201 | Basic and acidic residues | ||||
Sequence: KKMVTSKRKESSQNTEDSRLNDEA | ||||||
Sequence conflict | 187 | in Ref. 4; AAC52140 | ||||
Sequence: E → EPDFCLSCLIFFGIQ | ||||||
Compositional bias | 225-267 | Basic and acidic residues | ||||
Sequence: ARTLALLDEEPKIKKARKDSEEGEESFSSVQDDLSKAEKQKSP | ||||||
Sequence conflict | 254 | in Ref. 5; AAB60452 | ||||
Sequence: V → A | ||||||
Compositional bias | 285-309 | Basic and acidic residues | ||||
Sequence: HGKGRASEDAKQPCKSAHRKEACSS | ||||||
Compositional bias | 322-375 | Basic and acidic residues | ||||
Sequence: KEESSYNETELLAARRKESATEPKGEKTTPKKTKVSPTKRESVSPEDSEKKRTN | ||||||
Sequence conflict | 559 | in Ref. 4; AAC52140 | ||||
Sequence: N → S | ||||||
Alternative sequence | VSP_008444 | 614 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 945 | in Ref. 1; AAA21643 | ||||
Sequence: S → N | ||||||
Sequence conflict | 1071 | in Ref. 3; AAA79698 | ||||
Sequence: T → A | ||||||
Compositional bias | 1079-1093 | Acidic residues | ||||
Sequence: YSEEFQEDDTQSEKE | ||||||
Compositional bias | 1094-1123 | Basic and acidic residues | ||||
Sequence: QDAVETDAMIKKKTRSSKPSKSEREKESKK | ||||||
Sequence conflict | 1104 | in Ref. 4; AAC52140 | ||||
Sequence: K → KQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U01222 EMBL· GenBank· DDBJ | AAA21643.1 EMBL· GenBank· DDBJ | mRNA | ||
X72711 EMBL· GenBank· DDBJ | CAA51260.1 EMBL· GenBank· DDBJ | mRNA | ||
U36441 EMBL· GenBank· DDBJ | AAA79698.1 EMBL· GenBank· DDBJ | mRNA | ||
U07157 EMBL· GenBank· DDBJ | AAC52140.1 EMBL· GenBank· DDBJ | mRNA | ||
U15037 EMBL· GenBank· DDBJ | AAB60452.1 EMBL· GenBank· DDBJ | mRNA |