CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004768
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerases I, II, and III subunit RPABC1 
Protein Synonyms/Alias
 RNA polymerases I, II, and III subunit ABC1; DNA-directed RNA polymerase II 23 kDa polypeptide; DNA-directed RNA polymerase II subunit E; RPB5 homolog; XAP4 
Gene Name
 POLR2E 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15YRLWKIRKTIMQLCHubiquitination[1]
85EEPKVGIKTIKVYCQubiquitination[2]
88KVGIKTIKVYCQRMQubiquitination[1, 3]
115QGMTPSAKQSLVDMAubiquitination[1, 4, 5, 6, 7]
186VARYFGIKRGQVVKIubiquitination[1]
192IKRGQVVKIIRPSETubiquitination[1, 2, 4, 5]
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] 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]
 [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] 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] 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]
 [7] 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
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, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process (By similarity). 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; DNA-directed RNA polymerase; Host-virus interaction; Nucleus; Polymorphism; Reference proteome; Transcription. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 210 AA 
Protein Sequence
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE GRPRRTDLTV 60
LVAHNDDPTD QMFVFFPEEP KVGIKTIKVY CQRMQEENIT RALIVVQQGM TPSAKQSLVD 120
MAPKYILEQF LQQELLINIT EHELVPEHVV MTKEEVTELL ARYKLRENQL PRIQAGDPVA 180
RYFGIKRGQV VKIIRPSETA GRYITYRLVQ 210 
Gene Ontology
 GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; TAS:ProtInc.
 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:0006386; P:termination of RNA polymerase III transcription; TAS:Reactome.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0006385; P:transcription elongation from RNA polymerase III 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.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR014381; DNA_RNA_pol_RPB5_euk/virus.
 IPR005571; RNA_pol_Rpb5_N.
 IPR000783; RNA_pol_subH/Rpb5_C.
 IPR020608; RNA_pol_subH/Rpb5_CS.
 IPR020609; RpoH/RPB5. 
Pfam
 PF01191; RNA_pol_Rpb5_C
 PF03871; RNA_pol_Rpb5_N 
SMART
  
PROSITE
 PS01110; RNA_POL_H_23KD 
PRINTS