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Protein

Replication factor C subunit 3

Gene

Rfc3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-110312. Translesion synthesis by REV1.
R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-110320. Translesion Synthesis by POLH.
R-MMU-174411. Polymerase switching on the C-strand of the telomere.
R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69091. Polymerase switching.
R-MMU-69473. G2/M DNA damage checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C subunit 3
Alternative name(s):
Activator 1 38 kDa subunit
Short name:
A1 38 kDa subunit
Activator 1 subunit 3
Replication factor C 38 kDa subunit
Short name:
RF-C 38 kDa subunit
Short name:
RFC38
Gene namesi
Name:Rfc3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1916513. Rfc3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Replication factor C subunit 3PRO_0000121762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N6-acetyllysineBy similarity
Modified residuei125 – 1251PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8R323.
MaxQBiQ8R323.
PaxDbiQ8R323.
PRIDEiQ8R323.

PTM databases

iPTMnetiQ8R323.
PhosphoSiteiQ8R323.

Expressioni

Gene expression databases

BgeeiQ8R323.
CleanExiMM_RFC3.
ExpressionAtlasiQ8R323. baseline and differential.
GenevisibleiQ8R323. MM.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi213324. 2 interactions.
IntActiQ8R323. 3 interactions.
STRINGi10090.ENSMUSP00000039621.

Structurei

3D structure databases

ProteinModelPortaliQ8R323.
SMRiQ8R323. Positions 4-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

eggNOGiKOG2035. Eukaryota.
COG0470. LUCA.
GeneTreeiENSGT00550000075006.
HOGENOMiHOG000224153.
HOVERGENiHBG040509.
InParanoidiQ8R323.
KOiK10756.
OMAiQREFKVV.
OrthoDBiEOG7FXZZD.
PhylomeDBiQ8R323.
TreeFamiTF105724.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8R323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLWVDKYRP SSLARLDYHK EQAAQLRNLV QCGDFPHLLV YGPSGAGKKT
60 70 80 90 100
RIMCILRELY GIGVEKLRIE HQTITTPSKK KIEISTIASN YHLEVNPSDA
110 120 130 140 150
GNSDRVVIQE MLKTVAQSQQ LETSSQRDFK VVLLTEVDKL TKDAQHALRR
160 170 180 190 200
TMEKYMSTCR LILCCNSTSK VIPPIRSRCL AVRVPAPSIE DICSVLSTVC
210 220 230 240 250
RKEGLALPST LARRLAEKSC RNLRKALLMC EACRVQQYPF TEDQEIPETD
260 270 280 290 300
WEVYLRETAN AIVSQQTPQR LLEVRGRLYE LLTHCIPPEI IMKGLLSELL
310 320 330 340 350
HNCDGQLKGE VAQMAAYYEH RLQLGSKAIY HLEAFVAKFM ALYKKFMEDG

LEGMMF
Length:356
Mass (Da):40,526
Last modified:June 1, 2002 - v1
Checksum:i795A37D28D475C64
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC026795 mRNA. Translation: AAH26795.1.
CCDSiCCDS39413.1.
RefSeqiNP_081285.1. NM_027009.2.
UniGeneiMm.12553.

Genome annotation databases

EnsembliENSMUST00000038131; ENSMUSP00000039621; ENSMUSG00000033970.
GeneIDi69263.
KEGGimmu:69263.
UCSCiuc009aus.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC026795 mRNA. Translation: AAH26795.1.
CCDSiCCDS39413.1.
RefSeqiNP_081285.1. NM_027009.2.
UniGeneiMm.12553.

3D structure databases

ProteinModelPortaliQ8R323.
SMRiQ8R323. Positions 4-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213324. 2 interactions.
IntActiQ8R323. 3 interactions.
STRINGi10090.ENSMUSP00000039621.

PTM databases

iPTMnetiQ8R323.
PhosphoSiteiQ8R323.

Proteomic databases

EPDiQ8R323.
MaxQBiQ8R323.
PaxDbiQ8R323.
PRIDEiQ8R323.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038131; ENSMUSP00000039621; ENSMUSG00000033970.
GeneIDi69263.
KEGGimmu:69263.
UCSCiuc009aus.1. mouse.

Organism-specific databases

CTDi5983.
MGIiMGI:1916513. Rfc3.

Phylogenomic databases

eggNOGiKOG2035. Eukaryota.
COG0470. LUCA.
GeneTreeiENSGT00550000075006.
HOGENOMiHOG000224153.
HOVERGENiHBG040509.
InParanoidiQ8R323.
KOiK10756.
OMAiQREFKVV.
OrthoDBiEOG7FXZZD.
PhylomeDBiQ8R323.
TreeFamiTF105724.

Enzyme and pathway databases

ReactomeiR-MMU-110312. Translesion synthesis by REV1.
R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-110320. Translesion Synthesis by POLH.
R-MMU-174411. Polymerase switching on the C-strand of the telomere.
R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69091. Polymerase switching.
R-MMU-69473. G2/M DNA damage checkpoint.

Miscellaneous databases

PROiQ8R323.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R323.
CleanExiMM_RFC3.
ExpressionAtlasiQ8R323. baseline and differential.
GenevisibleiQ8R323. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRFC3_MOUSE
AccessioniPrimary (citable) accession number: Q8R323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.