CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007429
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Replication factor C subunit 3 
Protein Synonyms/Alias
 Activator 1 38 kDa subunit; A1 38 kDa subunit; Activator 1 subunit 3; Replication factor C 38 kDa subunit; RF-C 38 kDa subunit; RFC38 
Gene Name
 RFC3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MSLWVDKYRPCSLGmethylation[1]
7*MSLWVDKYRPCSLGubiquitination[2]
20LGRLDYHKEQAAQLRacetylation[3, 4]
20LGRLDYHKEQAAQLRubiquitination[2, 4, 5]
49GPSGAGKKTRIMCILubiquitination[2]
66LYGVGVEKLRIEHQTubiquitination[2, 4, 6, 7]
113VVIQEMLKTVAQSQQubiquitination[2, 5, 8]
139VLLTEVDKLTKDAQHubiquitination[5]
154ALRRTMEKYMSTCRLubiquitination[2]
170LCCNSTSKVIPPIRSubiquitination[2, 4]
201HVLSTVCKKEGLNLPubiquitination[9]
202VLSTVCKKEGLNLPSubiquitination[2, 4, 5, 6, 7, 8]
225KSCRNLRKALLMCEAubiquitination[2]
308HNCDGQLKGEVAQMAubiquitination[8]
344AKFMALYKKFMEDGLubiquitination[5]
Reference
 [1] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 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. 
Sequence Annotation
 MOD_RES 20 20 N6-acetyllysine.
 MOD_RES 125 125 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; DNA replication; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 356 AA 
Protein Sequence
MSLWVDKYRP CSLGRLDYHK EQAAQLRNLV QCGDFPHLLV YGPSGAGKKT RIMCILRELY 60
GVGVEKLRIE HQTITTPSKK KIEISTIASN YHLEVNPSDA GNSDRVVIQE MLKTVAQSQQ 120
LETNSQRDFK VVLLTEVDKL TKDAQHALRR TMEKYMSTCR LILCCNSTSK VIPPIRSRCL 180
AVRVPAPSIE DICHVLSTVC KKEGLNLPSQ LAHRLAEKSC RNLRKALLMC EACRVQQYPF 240
TADQEIPETD WEVYLRETAN AIVSQQTPQR LLEVRGRLYE LLTHCIPPEI IMKGLLSELL 300
HNCDGQLKGE VAQMAAYYEH RLQLGSKAIY HLEAFVAKFM ALYKKFMEDG LEGMMF 356 
Gene Ontology
 GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003689; F:DNA clamp loader activity; TAS:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
 GO:0000731; P:DNA synthesis involved in DNA repair; TAS:UniProtKB.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
 GO:0046683; P:response to organophosphorus; IEP:UniProtKB.
 GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
 GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
 GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR008921; DNA_pol3_clamp-load_cplx_C.
 IPR027417; P-loop_NTPase.
 IPR013748; Rep_factorC_C_dom. 
Pfam
 PF08542; Rep_fac_C 
SMART
 SM00382; AAA 
PROSITE
  
PRINTS