P40938 (RFC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

RFC3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8
Sequence similarities	Belongs to the activator 1 small subunits family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome DNA synthesis involved in DNA repair Traceable author statement. Source: UniProtKB S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle checkpoint Traceable author statement. Source: Reactome nucleotide-excision repair, DNA gap filling Traceable author statement. Source: Reactome response to organophosphorus Inferred from expression pattern. Source: UniProtKB 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 component	DNA replication factor C complex Inferred from direct assay. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro DNA clamp loader activity Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RFC4	P35249	5	EBI-1055010,EBI-476655

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Replication factor C subunit 3		PRO_0000121761
Amino acid modifications
	Modified residue	20	1	N6-acetyllysine Ref.9
	Modified residue	125	1	Phosphoserine Ref.8
Natural variations
	Natural variant	16	1	L → V. Ref.2 Corresponds to variant rs3135533 [ dbSNP | Ensembl ].		VAR_018750

Sequences

	Sequence		Length	Mass (Da)
	P40938 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: 820C11675A2C63A5	FASTA	356	40,556
	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

References

	« Hide 'large scale' referencesShow '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: 8441605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15057823] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: 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: 10884395] [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: 11572977] [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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	L07541 mRNA. Translation: AAB07268.1. AF484446 Genomic DNA. Translation: AAL82505.1. AL139081 Genomic DNA. Translation: CAH70947.1. CH471075 Genomic DNA. Translation: EAX08537.1. BC000149 mRNA. Translation: AAH00149.1.
IPI	IPI00031521.
PIR	T09573.
RefSeq	NP_002906.1. NM_002915.3.
UniGene	Hs.115474.
3D structure databases
ProteinModelPortal	P40938.
SMR	P40938. Positions 4-343.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36432N.
IntAct	P40938. 7 interactions.
MINT	MINT-3015032.
STRING	P40938.
PTM databases
PhosphoSite	P40938.
Polymorphism databases
DMDM	3915601.
Proteomic databases
PeptideAtlas	P40938.
PRIDE	P40938.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380071; ENSP00000369411; ENSG00000133119.
GeneID	5983.
KEGG	hsa:5983.
UCSC	uc001uuz.1. human.
Organism-specific databases
CTD	5983.
GeneCards	GC13P034392.
H-InvDB	HIX0011228.
HGNC	HGNC:9971. RFC3.
HPA	HPA030149.
MIM	600405. gene.
neXtProt	NX_P40938.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09137.
HOGENOM	HBG330815.
HOVERGEN	HBG040509.
InParanoid	P40938.
OMA	TRIMCLL.
OrthoDB	EOG4T4CVP.
PhylomeDB	P40938.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_216. DNA Repair. REACT_22172. Chromosome Maintenance. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	P40938.
Bgee	P40938.
CleanEx	HS_RFC3.
Genevestigator	P40938.
GermOnline	ENSG00000133119. Homo sapiens.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR008921. DNA_pol3_clamp-load_cplx_C. IPR019483. DNA_pol3_clamp-load_cplx_suE_C. [Graphical view]
KO	K10756.
Pfam	PF00004. AAA. 1 hit. PF10424. RFC-E_C. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF48019. Pol_clamp_load_C. 1 hit.
ProtoNet	Search...
Other
NextBio	23291.
SOURCE	Search...

Entry information

Entry name

RFC3_HUMAN

Accession

Primary (citable) accession number: P40938
Secondary accession number(s): O15252, Q5W0E8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	December 15, 1998
Last modified:	January 25, 2012
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.