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Protein

Replication factor C subunit 2

Gene

Rfc2

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. This subunit binds ATP (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi71 – 788ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: InterPro
  • enzyme binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-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 2
Alternative name(s):
Activator 1 40 kDa subunit
Short name:
A1 40 kDa subunit
Activator 1 subunit 2
Replication factor C 40 kDa subunit
Short name:
RF-C 40 kDa subunit
Short name:
RFC40
Gene namesi
Name:Rfc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1341868. Rfc2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Replication factor C subunit 2PRO_0000121767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei158 – 1581N6-acetyllysineBy similarity
Modified residuei299 – 2991N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9WUK4.
MaxQBiQ9WUK4.
PaxDbiQ9WUK4.
PRIDEiQ9WUK4.

PTM databases

iPTMnetiQ9WUK4.
PhosphoSiteiQ9WUK4.
SwissPalmiQ9WUK4.

Expressioni

Gene expression databases

BgeeiQ9WUK4.
CleanExiMM_RFC2.
ExpressionAtlasiQ9WUK4. baseline and differential.
GenevisibleiQ9WUK4. 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. RFC2 also interacts with PRKAR1A; the complex may be involved in cell survival (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi202869. 3 interactions.
IntActiQ9WUK4. 1 interaction.
STRINGi10090.ENSMUSP00000023867.

Structurei

3D structure databases

ProteinModelPortaliQ9WUK4.
SMRiQ9WUK4. Positions 30-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

eggNOGiKOG0991. Eukaryota.
COG0470. LUCA.
GeneTreeiENSGT00550000075050.
HOGENOMiHOG000224155.
HOVERGENiHBG002053.
InParanoidiQ9WUK4.
KOiK10755.
OMAiTHSGFGY.
OrthoDBiEOG7SR4MP.
PhylomeDBiQ9WUK4.
TreeFamiTF300585.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WUK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVQESGCDP SESGAQEPSP VPSKTAGHYE LPWVEKYRPL KLNEIVGNED
60 70 80 90 100
TVSRLEVFAR EGNVPNIIIA GPPGTGKTTS ILCLARALLG PALKDAVLEL
110 120 130 140 150
NASNDRGIDV VRNKIKMFAQ QKVTLPKGRH KIIILDEADS MTDGAQQALR
160 170 180 190 200
RTMEIYSKTT RFALACNASD KIIEPIQSRC AVLRYTKLTD AQVLTRLMNV
210 220 230 240 250
IEKEKVPYTD DGLEAIIFTA QGDMRQALNN LQSTFSGFGY INSENVFKVC
260 270 280 290 300
DEPHPLLVKE MIQHCVDANI DEAYKILAHL WHLGYSPEDV IGNIFRVCKT
310 320 330 340
FPMAEYLKLE FIKEIGYTHM KVAEGVNSLL QMAGLLARLC QKTMAPVAS
Length:349
Mass (Da):38,725
Last modified:November 1, 1999 - v1
Checksum:i62BB552004CCA27F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF139987 Genomic DNA. Translation: AAD34861.1.
AF289664 Genomic DNA. Translation: AAF99332.1.
AK075997 mRNA. Translation: BAC36108.1.
BC023028 mRNA. Translation: AAH23028.1.
CCDSiCCDS19722.1.
RefSeqiNP_064406.1. NM_020022.2.
UniGeneiMm.332739.

Genome annotation databases

EnsembliENSMUST00000023867; ENSMUSP00000023867; ENSMUSG00000023104.
GeneIDi19718.
KEGGimmu:19718.
UCSCiuc008zwl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF139987 Genomic DNA. Translation: AAD34861.1.
AF289664 Genomic DNA. Translation: AAF99332.1.
AK075997 mRNA. Translation: BAC36108.1.
BC023028 mRNA. Translation: AAH23028.1.
CCDSiCCDS19722.1.
RefSeqiNP_064406.1. NM_020022.2.
UniGeneiMm.332739.

3D structure databases

ProteinModelPortaliQ9WUK4.
SMRiQ9WUK4. Positions 30-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202869. 3 interactions.
IntActiQ9WUK4. 1 interaction.
STRINGi10090.ENSMUSP00000023867.

PTM databases

iPTMnetiQ9WUK4.
PhosphoSiteiQ9WUK4.
SwissPalmiQ9WUK4.

Proteomic databases

EPDiQ9WUK4.
MaxQBiQ9WUK4.
PaxDbiQ9WUK4.
PRIDEiQ9WUK4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023867; ENSMUSP00000023867; ENSMUSG00000023104.
GeneIDi19718.
KEGGimmu:19718.
UCSCiuc008zwl.1. mouse.

Organism-specific databases

CTDi5982.
MGIiMGI:1341868. Rfc2.

Phylogenomic databases

eggNOGiKOG0991. Eukaryota.
COG0470. LUCA.
GeneTreeiENSGT00550000075050.
HOGENOMiHOG000224155.
HOVERGENiHBG002053.
InParanoidiQ9WUK4.
KOiK10755.
OMAiTHSGFGY.
OrthoDBiEOG7SR4MP.
PhylomeDBiQ9WUK4.
TreeFamiTF300585.

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

ChiTaRSiRfc2. mouse.
PROiQ9WUK4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WUK4.
CleanExiMM_RFC2.
ExpressionAtlasiQ9WUK4. baseline and differential.
GenevisibleiQ9WUK4. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23."
    Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X., Duronio V., Koop B.F.
    Mamm. Genome 11:890-898(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  2. Green E.D.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  4. "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].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiRFC2_MOUSE
AccessioniPrimary (citable) accession number: Q9WUK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 137 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.