RFC3_HUMAN
ID RFC3_HUMAN Reviewed; 356 AA.
AC P40938; C9JU95; O15252; Q5W0E8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Replication factor C subunit 3;
DE AltName: Full=Activator 1 38 kDa subunit;
DE Short=A1 38 kDa subunit;
DE AltName: Full=Activator 1 subunit 3;
DE AltName: Full=Replication factor C 38 kDa subunit;
DE Short=RF-C 38 kDa subunit;
DE Short=RFC38;
GN Name=RFC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8441605; DOI=10.1093/nar/21.1.1;
RA O'Donnell M., Onrust R., Dean F.B., Chen M., Hurwitz J.;
RT "Homology in accessory proteins of replicative polymerases -- E. coli to
RT humans.";
RL Nucleic Acids Res. 21:1-3(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-16.
RG NIEHS SNPs program;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 51-305 (ISOFORM 2).
RC TISSUE=Embryonic stem cell, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH RAD17.
RX PubMed=10884395; DOI=10.1074/jbc.m005782200;
RA Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M.;
RT "The human checkpoint protein hRad17 interacts with the PCNA-like proteins
RT hRad1, hHus1, and hRad9.";
RL J. Biol. Chem. 275:29767-29771(2000).
RN [7]
RP INTERACTION WITH RAD17.
RX PubMed=11572977; DOI=10.1073/pnas.201373498;
RA Lindsey-Boltz L.A., Bermudez V.P., Hurwitz J., Sancar A.;
RT "Purification and characterization of human DNA damage checkpoint Rad
RT complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11236-11241(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC delta and epsilon requires the action of the accessory proteins
CC proliferating cell nuclear antigen (PCNA) and activator 1.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex either with RFC1 or with RAD17. The former interacts
CC with PCNA in the presence of ATP, while the latter has ATPase activity
CC but is not stimulated by PCNA. Interacts with CNTD1; this interaction
CC facilitates crossover formation (By similarity).
CC {ECO:0000250|UniProtKB:Q8R323, ECO:0000269|PubMed:10884395,
CC ECO:0000269|PubMed:11572977}.
CC -!- INTERACTION:
CC P40938; Q6AI12: ANKRD40; NbExp=3; IntAct=EBI-1055010, EBI-2838246;
CC P40938; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1055010, EBI-6509505;
CC P40938; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-1055010, EBI-742808;
CC P40938; O75525: KHDRBS3; NbExp=3; IntAct=EBI-1055010, EBI-722504;
CC P40938; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1055010, EBI-79165;
CC P40938; P35249: RFC4; NbExp=11; IntAct=EBI-1055010, EBI-476655;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P40938-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40938-2; Sequence=VSP_044920;
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rfc3/";
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DR EMBL; L07541; AAB07268.1; -; mRNA.
DR EMBL; AF484446; AAL82505.1; -; Genomic_DNA.
DR EMBL; AL139081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08537.1; -; Genomic_DNA.
DR EMBL; BC000149; AAH00149.1; -; mRNA.
DR EMBL; CX786577; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS45025.1; -. [P40938-2]
DR CCDS; CCDS9352.1; -. [P40938-1]
DR PIR; T09573; T09573.
DR RefSeq; NP_002906.1; NM_002915.3. [P40938-1]
DR RefSeq; NP_853536.2; NM_181558.2. [P40938-2]
DR PDB; 6VVO; EM; 3.40 A; E=1-356.
DR PDBsum; 6VVO; -.
DR AlphaFoldDB; P40938; -.
DR SMR; P40938; -.
DR BioGRID; 111915; 162.
DR ComplexPortal; CPX-415; DNA replication factor C complex.
DR CORUM; P40938; -.
DR DIP; DIP-36432N; -.
DR IntAct; P40938; 54.
DR MINT; P40938; -.
DR STRING; 9606.ENSP00000369411; -.
DR GlyGen; P40938; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40938; -.
DR MetOSite; P40938; -.
DR PhosphoSitePlus; P40938; -.
DR SwissPalm; P40938; -.
DR BioMuta; RFC3; -.
DR DMDM; 3915601; -.
DR EPD; P40938; -.
DR jPOST; P40938; -.
DR MassIVE; P40938; -.
DR MaxQB; P40938; -.
DR PaxDb; P40938; -.
DR PeptideAtlas; P40938; -.
DR PRIDE; P40938; -.
DR ProteomicsDB; 11702; -.
DR ProteomicsDB; 55391; -. [P40938-1]
DR Antibodypedia; 7909; 252 antibodies from 32 providers.
DR DNASU; 5983; -.
DR Ensembl; ENST00000380071.8; ENSP00000369411.3; ENSG00000133119.13. [P40938-1]
DR Ensembl; ENST00000434425.5; ENSP00000401001.1; ENSG00000133119.13. [P40938-2]
DR GeneID; 5983; -.
DR KEGG; hsa:5983; -.
DR MANE-Select; ENST00000380071.8; ENSP00000369411.3; NM_002915.4; NP_002906.1.
DR UCSC; uc001uuz.4; human. [P40938-1]
DR CTD; 5983; -.
DR DisGeNET; 5983; -.
DR GeneCards; RFC3; -.
DR HGNC; HGNC:9971; RFC3.
DR HPA; ENSG00000133119; Low tissue specificity.
DR MalaCards; RFC3; -.
DR MIM; 600405; gene.
DR neXtProt; NX_P40938; -.
DR OpenTargets; ENSG00000133119; -.
DR PharmGKB; PA34340; -.
DR VEuPathDB; HostDB:ENSG00000133119; -.
DR eggNOG; KOG2035; Eukaryota.
DR GeneTree; ENSGT00550000075006; -.
DR HOGENOM; CLU_042324_5_0_1; -.
DR InParanoid; P40938; -.
DR OMA; LMCEACK; -.
DR PhylomeDB; P40938; -.
DR TreeFam; TF105724; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; P40938; -.
DR Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69091; Polymerase switching.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR SignaLink; P40938; -.
DR SIGNOR; P40938; -.
DR BioGRID-ORCS; 5983; 768 hits in 1089 CRISPR screens.
DR ChiTaRS; RFC3; human.
DR GeneWiki; RFC3; -.
DR GenomeRNAi; 5983; -.
DR Pharos; P40938; Tbio.
DR PRO; PR:P40938; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P40938; protein.
DR Bgee; ENSG00000133119; Expressed in ventricular zone and 189 other tissues.
DR ExpressionAtlas; P40938; baseline and differential.
DR Genevisible; P40938; HS.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IDA:UniProtKB.
DR GO; GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003689; F:DNA clamp loader activity; TAS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:ProtInc.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:UniProtKB.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0046683; P:response to organophosphorus; IEP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; DNA replication;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..356
FT /note="Replication factor C subunit 3"
FT /id="PRO_0000121761"
FT MOD_RES 20
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 294..356
FT /note="GLLSELLHNCDGQLKGEVAQMAAYYEHRLQLGSKAIYHLEAFVAKFMALYKK
FT FMEDGLEGMMF -> ACKEESRSCDIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044920"
FT VARIANT 16
FT /note="L -> V (in dbSNP:rs3135533)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_018750"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6VVO"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:6VVO"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 308..322
FT /evidence="ECO:0007829|PDB:6VVO"
FT HELIX 328..348
FT /evidence="ECO:0007829|PDB:6VVO"
SQ SEQUENCE 356 AA; 40556 MW; 820C11675A2C63A5 CRC64;
MSLWVDKYRP CSLGRLDYHK EQAAQLRNLV QCGDFPHLLV YGPSGAGKKT RIMCILRELY
GVGVEKLRIE HQTITTPSKK KIEISTIASN YHLEVNPSDA GNSDRVVIQE MLKTVAQSQQ
LETNSQRDFK VVLLTEVDKL TKDAQHALRR TMEKYMSTCR LILCCNSTSK VIPPIRSRCL
AVRVPAPSIE DICHVLSTVC KKEGLNLPSQ LAHRLAEKSC RNLRKALLMC EACRVQQYPF
TADQEIPETD WEVYLRETAN AIVSQQTPQR LLEVRGRLYE LLTHCIPPEI IMKGLLSELL
HNCDGQLKGE VAQMAAYYEH RLQLGSKAIY HLEAFVAKFM ALYKKFMEDG LEGMMF
