CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006456
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Replication factor C subunit 2 
Protein Synonyms/Alias
 Activator 1 40 kDa subunit; A1 40 kDa subunit; Activator 1 subunit 2; Replication factor C 40 kDa subunit; RF-C 40 kDa subunit; RFC40 
Gene Name
 RFC2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46VEKYRPVKLNEIVGNubiquitination[1, 2]
82AGPPGTGKTTSILCLubiquitination[2, 3, 4, 5]
99ALLGPALKDAMLELNubiquitination[1, 2]
163RTMEIYSKTTRFALAacetylation[6]
163RTMEIYSKTTRFALAubiquitination[1, 2]
176LACNASDKIIEPIQSubiquitination[2]
192CAVLRYTKLTDAQILubiquitination[1, 2, 4, 7]
208RLMNVIEKERVPYTDubiquitination[1, 2]
304GNIFRVCKTFQMAEYacetylation[6]
347LLARLCQKTMAPVASubiquitination[4]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
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 binds ATP (By similarity). 
Sequence Annotation
 NP_BIND 76 83 ATP (Potential).
 MOD_RES 163 163 N6-acetyllysine.
 MOD_RES 304 304 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; DNA replication; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Williams-Beuren syndrome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 354 AA 
Protein Sequence
MEVEAVCGGA GEVEAQDSDP APAFSKAPGS AGHYELPWVE KYRPVKLNEI VGNEDTVSRL 60
EVFAREGNVP NIIIAGPPGT GKTTSILCLA RALLGPALKD AMLELNASND RGIDVVRNKI 120
KMFAQQKVTL PKGRHKIIIL DEADSMTDGA QQALRRTMEI YSKTTRFALA CNASDKIIEP 180
IQSRCAVLRY TKLTDAQILT RLMNVIEKER VPYTDDGLEA IIFTAQGDMR QALNNLQSTF 240
SGFGFINSEN VFKVCDEPHP LLVKEMIQHC VNANIDEAYK ILAHLWHLGY SPEDIIGNIF 300
RVCKTFQMAE YLKLEFIKEI GYTHMKIAEG VNSLLQMAGL LARLCQKTMA PVAS 354 
Gene Ontology
 GO:0005663; C:DNA replication factor C complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; TAS:ProtInc.
 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: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