CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021564
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA-directed RNA polymerase I subunit RPA2 
Protein Synonyms/Alias
 RNA polymerase I subunit 2; DNA-directed RNA polymerase I 135 kDa polypeptide; RPA135 
Gene Name
 POLR1B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17LPSGPSLKHLTDPSYubiquitination[1]
32GIPREQQKAALQELTubiquitination[2, 3]
94VPKGTICKEANVYPAubiquitination[3]
272FQELIKGKEDDSFLRubiquitination[2]
406AFDKKAQKTSVSMNTubiquitination[2]
784EFIDLSEKIKQGDSSubiquitination[2]
797SSLVFGIKPGDPRVLubiquitination[2]
806GDPRVLQKLDDDGLPubiquitination[2]
1009LRHMVSDKFQVRTTGubiquitination[2]
1095WSAMRNRKYNCTLCSubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [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] 
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 I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 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). 
Sequence Annotation
 ZN_FING 1070 1101 C4-type (Potential).  
Keyword
 Alternative splicing; Complete proteome; DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Transcription; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1135 AA 
Protein Sequence
MDPGSRWRNL PSGPSLKHLT DPSYGIPREQ QKAALQELTR AHVESFNYAV HEGLGLAVQA 60
IPPFEFAFKD ERISFTILDA VISPPTVPKG TICKEANVYP AECRGRRSTY RGKLTADINW 120
AVNGISKGII KQFLGYVPIM VKSKLCNLRN LPPQALIEHH EEAEEMGGYF IINGIEKVIR 180
MLIMPRRNFP IAMIRPKWKT RGPGYTQYGV SMHCVREEHS AVNMNLHYLE NGTVMLNFIY 240
RKELFFLPLG FALKALVSFS DYQIFQELIK GKEDDSFLRN SVSQMLRIVM EEGCSTQKQV 300
LNYLGECFRV KLNVPDWYPN EQAAEFLFNQ CICIHLKSNT EKFYMLCLMT RKLFALAKGE 360
CMEDNPDSLV NQEVLTPGQL FLMFLKEKLE GWLVSIKIAF DKKAQKTSVS MNTDNLMRIF 420
TMGIDLTKPF EYLFATGNLR SKTGLGLLQD SGLCVVADKL NFIRYLSHFR CVHRGADFAK 480
MRTTTVRRLL PESWGFLCPV HTPDGEPCGL MNHLTAVCEV VTQFVYTASI PALLCNLGVT 540
PIDGAPHRSY SECYPVLLDG VMVGWVDKDL APGIADSLRH FKVLREKRIP PWMEVVLIPM 600
TGKPSLYPGL FLFTTPCRLV RPVQNLALGK EELIGTMEQI FMNVAIFEDE VFAGVTTHQE 660
LFPHSLLSVI ANFIPFSDHN QSPRNMYQCQ MGKQTMGFPL LTYQDRSDNK LYRLQTPQSP 720
LVRPSMYDYY DMDNYPIGTN AIVAVISYTG YDMEDAMIVN KASWERGFAH GSVYKSEFID 780
LSEKIKQGDS SLVFGIKPGD PRVLQKLDDD GLPFIGAKLQ YGDPYYSYLN LNTGESFVMY 840
YKSKENCVVD NIKVCSNDTG SGKFKCVCIT MRVPRNPTIG DKFASRHGQK GILSRLWPAE 900
DMPFTESGMV PDILFNPHGF PSRMTIGMLI ESMAGKSAAL HGLCHDATPF IFSEENSALE 960
YFGEMLKAAG YNFYGTERLY SGISGLELEA DIFIGVVYYQ RLRHMVSDKF QVRTTGARDR 1020
VTNQPIGGRN VQGGIRFGEM ERDALLAHGT SFLLHDRLFN CSDRSVAHVC VKCGSLLSPL 1080
LEKPPPSWSA MRNRKYNCTL CSRSDTIDTV SVPYVFRYFV AELAAMNIKV KLDVV 1135 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005736; C:DNA-directed RNA polymerase I complex; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:HPA.
 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:0009790; P:embryo development; IEA:Compara.
 GO:0007566; P:embryo implantation; IEA:Compara.
 GO:0017126; P:nucleologenesis; IEA:Compara.
 GO:0009303; P:rRNA transcription; IEA:Compara.
 GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
 GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
 GO:0006361; P:transcription initiation from RNA polymerase I 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.
 IPR009674; RNA_pol_Rpa2-specific.
 IPR007642; RNA_pol_Rpb2_2.
 IPR007645; RNA_pol_Rpb2_3.
 IPR007647; RNA_pol_Rpb2_5.
 IPR007641; RNA_pol_Rpb2_7.
 IPR014724; RNA_pol_RPB2_OB-fold. 
Pfam
 PF06883; RNA_pol_Rpa2_4
 PF04563; RNA_pol_Rpb2_1
 PF04561; RNA_pol_Rpb2_2
 PF04565; RNA_pol_Rpb2_3
 PF04567; RNA_pol_Rpb2_5
 PF00562; RNA_pol_Rpb2_6
 PF04560; RNA_pol_Rpb2_7 
SMART
  
PROSITE
 PS01166; RNA_POL_BETA 
PRINTS