CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006455
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Replication factor C subunit 4 
Protein Synonyms/Alias
 Activator 1 37 kDa subunit; A1 37 kDa subunit; Activator 1 subunit 4; Replication factor C 37 kDa subunit; RF-C 37 kDa subunit; RFC37 
Gene Name
 RFC4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MQAFLKGTSISTKacetylation[1]
6**MQAFLKGTSISTKubiquitination[2]
13KGTSISTKPPLTKDRacetylation[1]
13KGTSISTKPPLTKDRubiquitination[2]
18STKPPLTKDRGVAASubiquitination[2]
36SGENKKAKPVPWVEKubiquitination[2]
64EVVAVLKKSLEGADLubiquitination[2, 3, 4, 5, 6]
84YGPPGTGKTSTILAAubiquitination[2, 4, 5]
124QVVREKVKNFAQLTVubiquitination[2]
139SGSRSDGKPCPPFKIubiquitination[2]
200RCSKFRFKPLSDKIQubiquitination[2]
205RFKPLSDKIQQQRLLubiquitination[2, 5]
216QRLLDIAKKENVKISubiquitination[2]
232EGIAYLVKVSEGDLRubiquitination[2, 4]
240VSEGDLRKAITFLQSubiquitination[2, 3, 6]
255ATRLTGGKEITEKVIubiquitination[2]
260GGKEITEKVITDIAGubiquitination[2]
288CQSGSFDKLEAVVKDubiquitination[2]
322VENNLSDKQKSIITEubiquitination[4]
324NNLSDKQKSIITEKLubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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] 
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. This subunit may be involved in the elongation of the multiprimed DNA template. 
Sequence Annotation
 NP_BIND 78 85 ATP (Potential).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 6 6 N6-acetyllysine.
 MOD_RES 13 13 N6-acetyllysine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; DNA replication; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 363 AA 
Protein Sequence
MQAFLKGTSI STKPPLTKDR GVAASAGSSG ENKKAKPVPW VEKYRPKCVD EVAFQEEVVA 60
VLKKSLEGAD LPNLLFYGPP GTGKTSTILA AARELFGPEL FRLRVLELNA SDERGIQVVR 120
EKVKNFAQLT VSGSRSDGKP CPPFKIVILD EADSMTSAAQ AALRRTMEKE SKTTRFCLIC 180
NYVSRIIEPL TSRCSKFRFK PLSDKIQQQR LLDIAKKENV KISDEGIAYL VKVSEGDLRK 240
AITFLQSATR LTGGKEITEK VITDIAGVIP AEKIDGVFAA CQSGSFDKLE AVVKDLIDEG 300
HAATQLVNQL HDVVVENNLS DKQKSIITEK LAEVDKCLAD GADEHLQLIS LCATVMQQLS 360
QNC 363 
Gene Ontology
 GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
 GO:0048015; P:phosphatidylinositol-mediated signaling; NAS: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.
 IPR003959; ATPase_AAA_core.
 IPR008921; DNA_pol3_clamp-load_cplx_C.
 IPR027417; P-loop_NTPase.
 IPR013748; Rep_factorC_C_dom. 
Pfam
 PF00004; AAA
 PF08542; Rep_fac_C 
SMART
 SM00382; AAA 
PROSITE
  
PRINTS