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P40938 (RFC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RFC3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.6 Ref.7

Subcellular location

Nucleus Probable.

Sequence similarities

Belongs to the activator 1 small subunits family.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 9488738. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

DNA replication

Inferred from direct assay PubMed 9488738. Source: UniProtKB

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

DNA synthesis involved in DNA repair

Traceable author statement PubMed 9488738. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA gap filling

Traceable author statement. Source: Reactome

response to organophosphorus

Inferred from expression pattern PubMed 16079077. Source: UniProtKB

telomere maintenance

Traceable author statement. Source: Reactome

telomere maintenance via recombination

Traceable author statement. Source: Reactome

telomere maintenance via semi-conservative replication

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

   Cellular_componentDNA replication factor C complex

Inferred from direct assay PubMed 9488738. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA clamp loader activity

Traceable author statement PubMed 9488738. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 9488738. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RFC4P352495EBI-1055010,EBI-476655

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P40938-1)

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.
Isoform 2 (identifier: P40938-2)

The sequence of this isoform differs from the canonical sequence as follows:
     294-356: GLLSELLHNCDGQLKGEVAQMAAYYEHRLQLGSKAIYHLEAFVAKFMALYKKFMEDGLEGMMF → ACKEESRSCDIF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Replication factor C subunit 3
PRO_0000121761

Amino acid modifications

Modified residue201N6-acetyllysine Ref.9
Modified residue1251Phosphoserine Ref.8

Natural variations

Alternative sequence294 – 35663GLLSE…EGMMF → ACKEESRSCDIF in isoform 2.
VSP_044920
Natural variant161L → V. Ref.2
Corresponds to variant rs3135533 [ dbSNP | Ensembl ].
VAR_018750

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 820C11675A2C63A5

FASTA35640,556
        10         20         30         40         50         60 
MSLWVDKYRP CSLGRLDYHK EQAAQLRNLV QCGDFPHLLV YGPSGAGKKT RIMCILRELY 

        70         80         90        100        110        120 
GVGVEKLRIE HQTITTPSKK KIEISTIASN YHLEVNPSDA GNSDRVVIQE MLKTVAQSQQ 

       130        140        150        160        170        180 
LETNSQRDFK VVLLTEVDKL TKDAQHALRR TMEKYMSTCR LILCCNSTSK VIPPIRSRCL 

       190        200        210        220        230        240 
AVRVPAPSIE DICHVLSTVC KKEGLNLPSQ LAHRLAEKSC RNLRKALLMC EACRVQQYPF 

       250        260        270        280        290        300 
TADQEIPETD WEVYLRETAN AIVSQQTPQR LLEVRGRLYE LLTHCIPPEI IMKGLLSELL 

       310        320        330        340        350 
HNCDGQLKGE VAQMAAYYEH RLQLGSKAIY HLEAFVAKFM ALYKKFMEDG LEGMMF 

« Hide

Isoform 2 [UniParc].

Checksum: 2835F2D0A4DDF1E4
Show »

FASTA30534,756

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45025.1. [P40938-2]
CCDS9352.1. [P40938-1]
PIRT09573.
RefSeqNP_002906.1. NM_002915.3. [P40938-1]
NP_853536.2. NM_181558.2. [P40938-2]
UniGeneHs.115474.

3D structure databases

ProteinModelPortalP40938.
SMRP40938. Positions 4-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111915. 29 interactions.
DIPDIP-36432N.
IntActP40938. 13 interactions.
MINTMINT-3015032.
STRING9606.ENSP00000369411.

PTM databases

PhosphoSiteP40938.

Polymorphism databases

DMDM3915601.

Proteomic databases

MaxQBP40938.
PaxDbP40938.
PeptideAtlasP40938.
PRIDEP40938.

Protocols and materials databases

DNASU5983.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380071; ENSP00000369411; ENSG00000133119. [P40938-1]
ENST00000434425; ENSP00000401001; ENSG00000133119. [P40938-2]
GeneID5983.
KEGGhsa:5983.
UCSCuc001uuz.3. human. [P40938-1]

Organism-specific databases

CTD5983.
GeneCardsGC13P034392.
HGNCHGNC:9971. RFC3.
HPAHPA030149.
MIM600405. gene.
neXtProtNX_P40938.
PharmGKBPA34340.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0470.
HOGENOMHOG000224153.
HOVERGENHBG040509.
InParanoidP40938.
KOK10756.
OMATRIMCLL.
OrthoDBEOG7FXZZD.
PhylomeDBP40938.
TreeFamTF105724.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_216. DNA Repair.
REACT_383. DNA Replication.

Gene expression databases

BgeeP40938.
CleanExHS_RFC3.
GenevestigatorP40938.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C_dom.
[Graphical view]
PfamPF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRFC3. human.
GeneWikiRFC3.
GenomeRNAi5983.
NextBio23291.
PROP40938.
SOURCESearch...

Entry information

Entry nameRFC3_HUMAN
AccessionPrimary (citable) accession number: P40938
Secondary accession number(s): C9JU95, O15252, Q5W0E8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM