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Protein

Replication factor C subunit 2

Gene

RFC2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 bindingi74 – 818ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C subunit 2
Alternative name(s):
Activator 1 subunit 2
Gene namesi
Name:RFC2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Replication factor C subunit 2PRO_0000330461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei161 – 1611N6-acetyllysineBy similarity
Modified residuei302 – 3021N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ05B83.
PRIDEiQ05B83.

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

Protein-protein interaction databases

BioGridi165290. 1 interaction.
STRINGi9913.ENSBTAP00000024740.

Structurei

3D structure databases

ProteinModelPortaliQ05B83.
SMRiQ05B83. Positions 33-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

eggNOGiKOG0991. Eukaryota.
COG0470. LUCA.
GeneTreeiENSGT00550000075050.
HOGENOMiHOG000224155.
HOVERGENiHBG002053.
InParanoidiQ05B83.
KOiK10755.
OMAiTHSGFGY.
OrthoDBiEOG7SR4MP.
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.

Q05B83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAQDSGGGT GECGAQDAAP GPSKAPGSAG HYELPWVEKY RPVKLNEIVG
60 70 80 90 100
NEDTVSRLEV FAREGNVPNI IIAGPPGTGK TTSILCLARA LLGPALKDAV
110 120 130 140 150
LELNASNDRG IDVVRNKIKM FAQQKVTLPK GRHKIIILDE ADSMTDGAQQ
160 170 180 190 200
ALRRTMEIYS KTTRFALACN ASDKIIEPIQ SRCAVLRYTK LTDMQILARL
210 220 230 240 250
LSVIEKEKVQ YTDDGLEAII FTAQGDMRQA LNNLQSTYSG FGFINSENVF
260 270 280 290 300
KVCDEPHPLL VKEMIQHCVS ADIDEAYKIL AHLWHLGYSP EDIIGNIFRV
310 320 330 340 350
CKTFQMAEYL KLEFIKEIGY THMKIAEGVN SLLQMAGLLA RLCQKTMAPV

AS
Length:352
Mass (Da):38,730
Last modified:November 14, 2006 - v1
Checksum:i6841C45B36474076
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC122635 mRNA. Translation: AAI22636.1.
RefSeqiNP_001074372.1. NM_001080903.1.
UniGeneiBt.35362.

Genome annotation databases

EnsembliENSBTAT00000024740; ENSBTAP00000024740; ENSBTAG00000018589.
GeneIDi508652.
KEGGibta:508652.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC122635 mRNA. Translation: AAI22636.1.
RefSeqiNP_001074372.1. NM_001080903.1.
UniGeneiBt.35362.

3D structure databases

ProteinModelPortaliQ05B83.
SMRiQ05B83. Positions 33-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi165290. 1 interaction.
STRINGi9913.ENSBTAP00000024740.

Proteomic databases

PaxDbiQ05B83.
PRIDEiQ05B83.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000024740; ENSBTAP00000024740; ENSBTAG00000018589.
GeneIDi508652.
KEGGibta:508652.

Organism-specific databases

CTDi5982.

Phylogenomic databases

eggNOGiKOG0991. Eukaryota.
COG0470. LUCA.
GeneTreeiENSGT00550000075050.
HOGENOMiHOG000224155.
HOVERGENiHBG002053.
InParanoidiQ05B83.
KOiK10755.
OMAiTHSGFGY.
OrthoDBiEOG7SR4MP.
TreeFamiTF300585.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20868620.

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

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Brain cortex.

Entry informationi

Entry nameiRFC2_BOVIN
AccessioniPrimary (citable) accession number: Q05B83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 14, 2006
Last modified: May 11, 2016
This is version 72 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. 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.