CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000391
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerases I and III subunit RPAC1 
Protein Synonyms/Alias
 DNA-directed RNA polymerase I subunit C; RNA polymerases I and III subunit AC1; AC40; DNA-directed RNA polymerases I and III 40 kDa polypeptide; RPA40; RPA39; RPC40 
Gene Name
 POLR1C 
Gene Synonyms/Alias
 POLR1E 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
47WDQDRFEKNFRVDVVubiquitination[1]
91VPTMAVEKVLVYNNTubiquitination[2]
154TRNPHAAKDSSDPNEubiquitination[1, 2, 3]
167NELYVNHKVYTRHMTubiquitination[1, 2]
220HCVKGIGKDHAKFSPubiquitination[2]
224GIGKDHAKFSPVATAubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
270EVQEVQGKKVARVANubiquitination[2, 5]
271VQEVQGKKVARVANPubiquitination[2]
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] 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]
 [4] 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]
 [5] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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] 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
Functional Description
 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPAC1 is part of the Pol core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 346 AA 
Protein Sequence
MAASQAVEEM RSRVVLGEFG VRNVHTTDFP GNYSGYDDAW DQDRFEKNFR VDVVHMDENS 60
LEFDMVGIDA AIANAFRRIL LAEVPTMAVE KVLVYNNTSI VQDEILAHRL GLIPIHADPR 120
LFEYRNQGDE EGTEIDTLQF RLQVRCTRNP HAAKDSSDPN ELYVNHKVYT RHMTWIPLGN 180
QADLFPEGTI RPVHDDILIA QLRPGQEIDL LMHCVKGIGK DHAKFSPVAT ASYRLLPDIT 240
LLEPVEGEAA EELSRCFSPG VIEVQEVQGK KVARVANPRL DTFSREIFRN EKLKKVVRLA 300
RVRDHYIFSV ESTGVLPPDV LVSEAIKVLM GKCRRFLDEL DAVQMD 346 
Gene Ontology
 GO:0005736; C:DNA-directed RNA polymerase I complex; TAS:ProtInc.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; TAS:ProtInc.
 GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
 GO:0006386; P:termination of RNA polymerase III transcription; TAS:Reactome.
 GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
 GO:0006385; P:transcription elongation from RNA polymerase III promoter; TAS:Reactome.
 GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome. 
Interpro
 IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
 IPR011261; DNA-dir_RNA_pol_dimersation.
 IPR011262; DNA-dir_RNA_pol_insert.
 IPR009025; DNA-dir_RNA_pol_RBP11-like.
 IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3. 
Pfam
 PF01000; RNA_pol_A_bac
 PF01193; RNA_pol_L 
SMART
 SM00662; RPOLD 
PROSITE
 PS00446; RNA_POL_D_30KD 
PRINTS