CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032801
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 DNA-directed RNA polymerase 
Protein Synonyms/Alias
  
Gene Name
 POLR1A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MLISKNMPWRRLubiquitination[1, 2, 3]
31ELKKLSVKSITNPRYubiquitination[2, 3]
190NVCESKSKLIALFWKubiquitination[2]
222VRKEHNSKLTITFPAubiquitination[2]
238VHRTAGQKDSEPLGIubiquitination[2, 4, 5]
252IEEAQIGKRGYLTPTubiquitination[2, 3, 4, 5, 6]
350ALMAQEQKLPEEVATubiquitination[4]
364TPTTDEEKDSLIAIDubiquitination[4]
413MDKLMMDKYPGIRQIubiquitination[7]
520TQREAVAKQLLTPATubiquitination[2, 5, 6]
536APKPQGTKIVCRHVKubiquitination[2]
543KIVCRHVKNGDILLLubiquitination[2]
573ARILPEEKVLRLHYAubiquitination[2, 3, 7]
583RLHYANCKAYNADFDubiquitination[2, 6]
664VYRGLTDKVGRVKLLubiquitination[2, 3]
669TDKVGRVKLLSPSILubiquitination[2]
677LLSPSILKPFPLWTGubiquitination[1, 2, 3, 5, 6]
714GKAKITGKAWVKETPubiquitination[2, 3]
718ITGKAWVKETPRSVPubiquitination[2, 3]
805GVEDILVKPKADVKRubiquitination[2, 4]
807EDILVKPKADVKRQRubiquitination[2]
845SYDEVRGKWQDAHLGubiquitination[2, 3]
853WQDAHLGKDQRDFNMubiquitination[2]
864DFNMIDLKFKEEVNHubiquitination[2, 4]
866NMIDLKFKEEVNHYSacetylation[3, 8]
866NMIDLKFKEEVNHYSubiquitination[2, 3]
878HYSNEINKACMPFGLubiquitination[2, 3]
933PPLMASGKSLPCFEPubiquitination[2, 3]
960GRFLTGIKPPEFFFHubiquitination[2, 3]
981GLVDTAVKTSRSGYLubiquitination[1, 2, 3, 4]
1028EDGLDIPKTQFLQPKubiquitination[4]
1078AIKKWQSKHPNTLLRubiquitination[2, 3]
1095AFLSYSQKIQEAVKAubiquitination[2]
1101QKIQEAVKALKLESEubiquitination[2, 3, 4]
1104QEAVKALKLESENRNubiquitination[1, 2, 3]
1180EWAAQTEKSYEKSELubiquitination[2, 3, 4, 5, 6]
1184QTEKSYEKSELSLDRubiquitination[2, 3, 4]
1199LRTLLQLKWQRSLCEubiquitination[2, 3, 6]
1273VPVLNTKKALKRVKSubiquitination[2]
1311CMEEKQNKFQVYQLRubiquitination[2]
1331HAYYQQEKCLRPEDIubiquitination[2]
1356LLMESIKKKNNKASAubiquitination[2]
1360SIKKKNNKASAFRNVubiquitination[2]
1510LNETTNNKNEKELVLubiquitination[6]
1513TTNNKNEKELVLNTEubiquitination[4]
1643SACLVVGKVVRGGTGubiquitination[2, 3, 7]
1655GTGLFELKQPLR***ubiquitination[2, 3, 4, 5]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1659 AA 
Protein Sequence
MLISKNMPWR RLQGISFGMY SAEELKKLSV KSITNPRYLD SLGNPSANGL YDLALGPADS 60
KEVCSTCVQD FSNCSGHLGH IELPLTVYNP LLFDKLYLLL RGSCLNCHML TCPRAVIHLL 120
LCQLRVLEVG ALQAVYELER ILNRFLEENP DPSASEIREE LEQYTTEIVQ NNLLGSQGAH 180
VKNVCESKSK LIALFWKAHM NAKRCPHCKT GRSVVRKEHN SKLTITFPAM VHRTAGQKDS 240
EPLGIEEAQI GKRGYLTPTS AREHLSALWK NEGFFLNYLF SGMDDDGMES RFNPSVFFLD 300
FLVVPPSRYR PVSRLGDQMF TNGQTVNLQA VMKDVVLIRK LLALMAQEQK LPEEVATPTT 360
DEEKDSLIAI DRSFLSTLPG QSLIDKLYNI WIRLQSHVNI VFDSEMDKLM MDKYPGIRQI 420
LEKKEGLFRK HMMGKRVDYA ARSVICPDMY INTNEIGIPM VFATKLTYPQ PVTPWNVQEL 480
RQAVINGPNV HPGASMVINE DGSRTALSAV DMTQREAVAK QLLTPATGAP KPQGTKIVCR 540
HVKNGDILLL NRQPTLHRPS IQAHRARILP EEKVLRLHYA NCKAYNADFD GDEMNAHFPQ 600
SELGRAEAYV LACTDQQYLV PKDGQPLAGL IQDHMVSGAS MTTRGCFFTR EHYMELVYRG 660
LTDKVGRVKL LSPSILKPFP LWTGKQVVST LLINIIPEDH IPLNLSGKAK ITGKAWVKET 720
PRSVPGFNPD SMCESQVIIR EGELLCGVLD KAHYGSSAYG LVHCCYEIYG GETSGKVLTC 780
LARLFTAYLQ LYRGFTLGVE DILVKPKADV KRQRIIEEST HCGPQAVRAA LNLPEAASYD 840
EVRGKWQDAH LGKDQRDFNM IDLKFKEEVN HYSNEINKAC MPFGLHRQFP ENSLQMMVQS 900
GAKGSTVNTM QISCLLGQIE LEGRRPPLMA SGKSLPCFEP YEFTPRAGGF VTGRFLTGIK 960
PPEFFFHCMA GREGLVDTAV KTSRSGYLQR CIIKHLEGLV VQYDLTVRDS DGSVVQFLYG 1020
EDGLDIPKTQ FLQPKQFPFL ASNYEVIMKS QHLHEVLSRA DPKKALHHFR AIKKWQSKHP 1080
NTLLRRGAFL SYSQKIQEAV KALKLESENR NGRSPGTQEM LRMWYELDEE SRRKYQKKAA 1140
ACPDPSLSVW RPDIYFASVS ETFETKVDDY SQEWAAQTEK SYEKSELSLD RLRTLLQLKW 1200
QRSLCEPGEA VGLLAAQSIG EPSTQMTLNT FHFAGRGEMN VTLGIPRLRE ILMVASANIK 1260
TPMMSVPVLN TKKALKRVKS LKKQLTRVCL GEVLQKIDVQ ESFCMEEKQN KFQVYQLRFQ 1320
FLPHAYYQQE KCLRPEDILR FMETRFFKLL MESIKKKNNK ASAFRNVNTR RATQRDLDNA 1380
GELGRSRGEQ EGDEEEEGHI VDAEAEEGDA DASDAKRKEK QEEEVDYESE EEEEREGEEN 1440
DDEDMQEERN PHREGARKTQ EQDEEVTVKL PLMKINFDMS SLVVSLAHGA VIYATKGITR 1500
CLLNETTNNK NEKELVLNTE GINLPELFKY AEVLDLRRLY SNDIHAIANT YGIEAALRVI 1560
EKEIKDVFAV YGIAVDPRHL SLVADYMCFE GVYKPLNRFG IRSNSSPLQQ MTFETSFQFL 1620
KQATMLGSHD ELRSPSACLV VGKVVRGGTG LFELKQPLR 1659 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006351; P:transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR009010; Asp_de-COase-like_dom.
 IPR015699; DNA-dir_RNA_pol1_lsu.
 IPR000722; RNA_pol_asu.
 IPR006592; RNA_pol_N.
 IPR007080; RNA_pol_Rpb1_1.
 IPR007066; RNA_pol_Rpb1_3.
 IPR007083; RNA_pol_Rpb1_4.
 IPR007081; RNA_pol_Rpb1_5. 
Pfam
 PF04997; RNA_pol_Rpb1_1
 PF00623; RNA_pol_Rpb1_2
 PF04983; RNA_pol_Rpb1_3
 PF05000; RNA_pol_Rpb1_4
 PF04998; RNA_pol_Rpb1_5 
SMART
 SM00663; RPOLA_N 
PROSITE
  
PRINTS