CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004767
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerase II subunit RPB3 
Protein Synonyms/Alias
 RNA polymerase II subunit 3; RNA polymerase II subunit B3; DNA-directed RNA polymerase II 33 kDa polypeptide; RPB33; DNA-directed RNA polymerase II subunit C; RPB31 
Gene Name
 POLR2C 
Gene Synonyms/Alias
 A-152E5.7 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20ELTDENVKFIIENTDubiquitination[1, 2, 3]
81ISDDIVDKLQYSRDCubiquitination[1, 2, 3, 4]
152QDDILIVKLRKGQELubiquitination[3, 4]
175GFGKEHAKWNPTAGVubiquitination[1, 3, 4, 5]
199LRHTVYPKPEEWPKSubiquitination[3, 4, 5]
205PKPEEWPKSEYSELDubiquitination[1, 5]
225APYDPNGKPERFYYNubiquitination[1, 3, 4, 5, 6]
253LSALSGLKKKLSDLQubiquitination[5, 7]
254SALSGLKKKLSDLQTubiquitination[3]
255ALSGLKKKLSDLQTQubiquitination[1, 3]
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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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
 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft (By similarity). 
Sequence Annotation
 MOD_RES 124 124 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; DNA-directed RNA polymerase; Nucleus; Phosphoprotein; Reference proteome; Transcription. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 275 AA 
Protein Sequence
MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH 60
DEFIAHRLGL IPLISDDIVD KLQYSRDCTC EEFCPECSVE FTLDVRCNED QTRHVTSRDL 120
ISNSPRVIPV TSRNRDNDPN DYVEQDDILI VKLRKGQELR LRAYAKKGFG KEHAKWNPTA 180
GVAFEYDPDN ALRHTVYPKP EEWPKSEYSE LDEDESQAPY DPNGKPERFY YNVESCGSLR 240
PETIVLSALS GLKKKLSDLQ TQLSHEIQSD VLTIN 275 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
 GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
 GO:0022415; P:viral reproductive process; 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