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Protein

Replication factor C subunit 3

Gene

RFC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

  1. DNA clamp loader activity Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: Reactome
  2. DNA replication Source: UniProtKB
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. DNA synthesis involved in DNA repair Source: UniProtKB
  5. mitotic cell cycle Source: Reactome
  6. nucleotide-excision repair Source: Reactome
  7. nucleotide-excision repair, DNA gap filling Source: Reactome
  8. response to organophosphorus Source: UniProtKB
  9. telomere maintenance Source: Reactome
  10. telomere maintenance via recombination Source: Reactome
  11. telomere maintenance via semi-conservative replication Source: Reactome
  12. transcription-coupled nucleotide-excision repair Source: Reactome
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1792. Polymerase switching.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_6769. Activation of ATR in response to replication stress.
REACT_7987. Polymerase switching on the C-strand of the telomere.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:9971. RFC3.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. DNA replication factor C complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34340.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Replication factor C subunit 3PRO_0000121761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N6-acetyllysine1 Publication
Modified residuei125 – 1251Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP40938.
PaxDbiP40938.
PeptideAtlasiP40938.
PRIDEiP40938.

PTM databases

PhosphoSiteiP40938.

Expressioni

Gene expression databases

BgeeiP40938.
CleanExiHS_RFC3.
ExpressionAtlasiP40938. baseline and differential.
GenevestigatoriP40938.

Organism-specific databases

HPAiHPA030149.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RFC4P352495EBI-1055010,EBI-476655

Protein-protein interaction databases

BioGridi111915. 32 interactions.
DIPiDIP-36432N.
IntActiP40938. 13 interactions.
MINTiMINT-3015032.
STRINGi9606.ENSP00000369411.

Structurei

3D structure databases

ProteinModelPortaliP40938.
SMRiP40938. Positions 4-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

eggNOGiCOG0470.
GeneTreeiENSGT00550000075006.
HOGENOMiHOG000224153.
HOVERGENiHBG040509.
InParanoidiP40938.
KOiK10756.
OMAiHLEAWVV.
OrthoDBiEOG7FXZZD.
PhylomeDBiP40938.
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.
IPR013748. Rep_factorC_C_dom.
[Graphical view]
PfamiPF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P40938-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSLWVDKYRP CSLGRLDYHK EQAAQLRNLV QCGDFPHLLV YGPSGAGKKT
60 70 80 90 100
RIMCILRELY GVGVEKLRIE HQTITTPSKK KIEISTIASN YHLEVNPSDA
110 120 130 140 150
GNSDRVVIQE MLKTVAQSQQ LETNSQRDFK VVLLTEVDKL TKDAQHALRR
160 170 180 190 200
TMEKYMSTCR LILCCNSTSK VIPPIRSRCL AVRVPAPSIE DICHVLSTVC
210 220 230 240 250
KKEGLNLPSQ LAHRLAEKSC RNLRKALLMC EACRVQQYPF TADQEIPETD
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):40,556
Last modified:December 15, 1998 - v2
Checksum:i820C11675A2C63A5
GO
Isoform 2 (identifier: P40938-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     294-356: GLLSELLHNCDGQLKGEVAQMAAYYEHRLQLGSKAIYHLEAFVAKFMALYKKFMEDGLEGMMF → ACKEESRSCDIF

Note: No experimental confirmation available.

Show »
Length:305
Mass (Da):34,756
Checksum:i2835F2D0A4DDF1E4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161L → V.1 Publication
Corresponds to variant rs3135533 [ dbSNP | Ensembl ].
VAR_018750

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei294 – 35663GLLSE…EGMMF → ACKEESRSCDIF in isoform 2. 1 PublicationVSP_044920Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07541 mRNA. Translation: AAB07268.1.
AF484446 Genomic DNA. Translation: AAL82505.1.
AL139081 Genomic DNA. Translation: CAH70947.1.
AL160394 Genomic DNA. No translation available.
AL161891 Genomic DNA. No translation available.
CH471075 Genomic DNA. Translation: EAX08537.1.
BC000149 mRNA. Translation: AAH00149.1.
CX786577 mRNA. No translation available.
CCDSiCCDS45025.1. [P40938-2]
CCDS9352.1. [P40938-1]
PIRiT09573.
RefSeqiNP_002906.1. NM_002915.3. [P40938-1]
NP_853536.2. NM_181558.2. [P40938-2]
UniGeneiHs.115474.

Genome annotation databases

EnsembliENST00000380071; ENSP00000369411; ENSG00000133119. [P40938-1]
ENST00000434425; ENSP00000401001; ENSG00000133119. [P40938-2]
GeneIDi5983.
KEGGihsa:5983.
UCSCiuc001uuz.3. human. [P40938-1]

Polymorphism databases

DMDMi3915601.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07541 mRNA. Translation: AAB07268.1.
AF484446 Genomic DNA. Translation: AAL82505.1.
AL139081 Genomic DNA. Translation: CAH70947.1.
AL160394 Genomic DNA. No translation available.
AL161891 Genomic DNA. No translation available.
CH471075 Genomic DNA. Translation: EAX08537.1.
BC000149 mRNA. Translation: AAH00149.1.
CX786577 mRNA. No translation available.
CCDSiCCDS45025.1. [P40938-2]
CCDS9352.1. [P40938-1]
PIRiT09573.
RefSeqiNP_002906.1. NM_002915.3. [P40938-1]
NP_853536.2. NM_181558.2. [P40938-2]
UniGeneiHs.115474.

3D structure databases

ProteinModelPortaliP40938.
SMRiP40938. Positions 4-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111915. 32 interactions.
DIPiDIP-36432N.
IntActiP40938. 13 interactions.
MINTiMINT-3015032.
STRINGi9606.ENSP00000369411.

PTM databases

PhosphoSiteiP40938.

Polymorphism databases

DMDMi3915601.

Proteomic databases

MaxQBiP40938.
PaxDbiP40938.
PeptideAtlasiP40938.
PRIDEiP40938.

Protocols and materials databases

DNASUi5983.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380071; ENSP00000369411; ENSG00000133119. [P40938-1]
ENST00000434425; ENSP00000401001; ENSG00000133119. [P40938-2]
GeneIDi5983.
KEGGihsa:5983.
UCSCiuc001uuz.3. human. [P40938-1]

Organism-specific databases

CTDi5983.
GeneCardsiGC13P034392.
HGNCiHGNC:9971. RFC3.
HPAiHPA030149.
MIMi600405. gene.
neXtProtiNX_P40938.
PharmGKBiPA34340.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0470.
GeneTreeiENSGT00550000075006.
HOGENOMiHOG000224153.
HOVERGENiHBG040509.
InParanoidiP40938.
KOiK10756.
OMAiHLEAWVV.
OrthoDBiEOG7FXZZD.
PhylomeDBiP40938.
TreeFamiTF105724.

Enzyme and pathway databases

ReactomeiREACT_1792. Polymerase switching.
REACT_1993. Repair synthesis for gap-filling by DNA polymerase in TC-NER.
REACT_378. Repair synthesis of patch ~27-30 bases long by DNA polymerase.
REACT_6769. Activation of ATR in response to replication stress.
REACT_7987. Polymerase switching on the C-strand of the telomere.

Miscellaneous databases

ChiTaRSiRFC3. human.
GeneWikiiRFC3.
GenomeRNAii5983.
NextBioi23291.
PROiP40938.
SOURCEiSearch...

Gene expression databases

BgeeiP40938.
CleanExiHS_RFC3.
ExpressionAtlasiP40938. baseline and differential.
GenevestigatoriP40938.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C_dom.
[Graphical view]
PfamiPF08542. 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. "Homology in accessory proteins of replicative polymerases -- E. coli to humans."
    O'Donnell M., Onrust R., Dean F.B., Chen M., Hurwitz J.
    Nucleic Acids Res. 21:1-3(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. NIEHS SNPs program
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-16.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-305 (ISOFORM 2).
    Tissue: Embryonic stem cell and Placenta.
  6. "The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9."
    Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M.
    J. Biol. Chem. 275:29767-29771(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD17.
  7. "Purification and characterization of human DNA damage checkpoint Rad complexes."
    Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.
    Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD17.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRFC3_HUMAN
AccessioniPrimary (citable) accession number: P40938
Secondary accession number(s): C9JU95, O15252, Q5W0E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 15, 1998
Last modified: March 4, 2015
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.