CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022243
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerase III subunit RPC2 
Protein Synonyms/Alias
 RNA polymerase III subunit C2; C128; DNA-directed RNA polymerase III 127.6 kDa polypeptide; DNA-directed RNA polymerase III subunit B 
Gene Name
 POLR3B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
35RLLPAFLKVKGLVKQubiquitination[1]
37LPAFLKVKGLVKQHIubiquitination[1]
64KIMKANEKVTSDADPubiquitination[1]
150SNCVLTGKTPAEFAKubiquitination[1]
157KTPAEFAKLNECPLDubiquitination[1, 2]
172PGGYFIVKGVEKVILubiquitination[1]
210VTSSTHEKKSRTNMAubiquitination[3]
290ALKYIGNKVRRQRMWubiquitination[1]
324ILTHVPVKEFNFRAKubiquitination[4]
360DRDYYGNKRLELAGQubiquitination[3]
404AAQFDVVKHMRQDQIubiquitination[1]
461RISSQFEKTRKVSGPubiquitination[3]
691TYQCAMGKQAMGTIGubiquitination[1, 2]
723QKPMVKTKTIELIEFubiquitination[3]
820GICSPGEKVENKQVLubiquitination[2]
824PGEKVENKQVLVNKSubiquitination[1]
830NKQVLVNKSMPTVTQubiquitination[2]
852VPQQPQYKDVPITYKubiquitination[2, 3]
859KDVPITYKGATDSYIubiquitination[1, 5]
896RRPEIGDKFSSRHGQubiquitination[1, 2, 5]
950LIELLAGKAGVLDGRubiquitination[1, 2, 3, 5, 6]
968GTAFGGSKVKDVCEDubiquitination[1, 2, 3]
970AFGGSKVKDVCEDLVubiquitination[1, 5]
1013PVYYQKLKHMVLDKMmethylation[7]
1019LKHMVLDKMHARARGubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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] 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] 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] 
Functional Description
 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. 
Sequence Annotation
 ZN_FING 1080 1095 C4-type.
 METAL 1080 1080 Zinc (By similarity).
 METAL 1083 1083 Zinc (By similarity).
 METAL 1092 1092 Zinc (By similarity).
 METAL 1095 1095 Zinc (By similarity).  
Keyword
 Alternative splicing; Antiviral defense; Complete proteome; Disease mutation; DNA-directed RNA polymerase; Immunity; Innate immunity; Leukodystrophy; Metal-binding; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Transcription; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1133 AA 
Protein Sequence
MDVLAEEFGN LTPEQLAAPI PTVEEKWRLL PAFLKVKGLV KQHIDSFNYF INVEIKKIMK 60
ANEKVTSDAD PMWYLKYLNI YVGLPDVEES FNVTRPVSPH ECRLRDMTYS APITVDIEYT 120
RGSQRIIRNA LPIGRMPIML RSSNCVLTGK TPAEFAKLNE CPLDPGGYFI VKGVEKVILI 180
QEQLSKNRII VEADRKGAVG ASVTSSTHEK KSRTNMAVKQ GRFYLRHNTL SEDIPIVIIF 240
KAMGVESDQE IVQMIGTEEH VMAAFGPSLE ECQKAQIFTQ MQALKYIGNK VRRQRMWGGG 300
PKKTKIEEAR ELLASTILTH VPVKEFNFRA KCIYTAVMVR RVILAQGDNK VDDRDYYGNK 360
RLELAGQLLS LLFEDLFKKF NSEMKKIADQ VIPKQRAAQF DVVKHMRQDQ ITNGMVNAIS 420
TGNWSLKRFK MDRQGVTQVL SRLSYISALG MMTRISSQFE KTRKVSGPRS LQPSQWGMLC 480
PSDTPEGEAC GLVKNLALMT HITTDMEDGP IVKLASNLGV EDVNLLCGEE LSYPNVFLVF 540
LNGNILGVIR DHKKLVNTFR LMRRAGYINE FVSISTNLTD RCVYISSDGG RLCRPYIIVK 600
KQKPAVTNKH MEELAQGYRN FEDFLHESLV EYLDVNEEND CNIALYEHTI NKDTTHLEIE 660
PFTLLGVCAG LIPYPHHNQS PRNTYQCAMG KQAMGTIGYN QRNRIDTLMY LLAYPQKPMV 720
KTKTIELIEF EKLPAGQNAT VAVMSYSGYD IEDALVLNKA SLDRGFGRCL VYKNAKCTLK 780
RYTNQTFDKV MGPMLDAATR KPIWRHEILD ADGICSPGEK VENKQVLVNK SMPTVTQIPL 840
EGSNVPQQPQ YKDVPITYKG ATDSYIEKVM ISSNAEDAFL IKMLLRQTRR PEIGDKFSSR 900
HGQKGVCGLI VPQEDMPFCD SGICPDIIMN PHGFPSRMTV GKLIELLAGK AGVLDGRFHY 960
GTAFGGSKVK DVCEDLVRHG YNYLGKDYVT SGITGEPLEA YIYFGPVYYQ KLKHMVLDKM 1020
HARARGPRAV LTRQPTEGRS RDGGLRLGEM ERDCLIGYGA SMLLLERLMI SSDAFEVDVC 1080
GQCGLLGYSG WCHYCKSSCH VSSLRIPYAC KLLFQELQSM NIIPRLKLSK YNE 1133 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0032549; F:ribonucleoside binding; IEA:InterPro.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
 GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
 GO:0006386; P:termination of RNA polymerase III transcription; TAS:Reactome.
 GO:0006385; P:transcription elongation from RNA polymerase III promoter; TAS:Reactome. 
Interpro
 IPR015712; DNA-dir_RNA_pol_su2.
 IPR007120; DNA-dir_RNA_pol_su2_6.
 IPR007121; RNA_pol_bsu_CS.
 IPR007644; RNA_pol_bsu_protrusion.
 IPR007642; RNA_pol_Rpb2_2.
 IPR007645; RNA_pol_Rpb2_3.
 IPR007646; RNA_pol_Rpb2_4.
 IPR007647; RNA_pol_Rpb2_5.
 IPR007641; RNA_pol_Rpb2_7.
 IPR014724; RNA_pol_RPB2_OB-fold. 
Pfam
 PF04563; RNA_pol_Rpb2_1
 PF04561; RNA_pol_Rpb2_2
 PF04565; RNA_pol_Rpb2_3
 PF04566; RNA_pol_Rpb2_4
 PF04567; RNA_pol_Rpb2_5
 PF00562; RNA_pol_Rpb2_6
 PF04560; RNA_pol_Rpb2_7 
SMART
  
PROSITE
 PS01166; RNA_POL_BETA 
PRINTS