CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-033027
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 DNA-directed RNA polymerase 
Protein Synonyms/Alias
  
Gene Name
 POLR2B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
80EPPRYLLKFEQIYLSubiquitination[1, 2, 3]
88FEQIYLSKPTHWERDubiquitination[1, 2, 3, 4, 5, 6, 7]
123PLYVDITKTVIKEGEubiquitination[1, 2, 3, 5, 7]
127DITKTVIKEGEEQLQubiquitination[1, 2, 3, 5, 7]
139QLQTQHQKTFIGKIPubiquitination[1, 2, 3, 4, 5, 6, 7]
144HQKTFIGKIPIMLRSubiquitination[1, 2, 3, 4, 5, 6, 7]
192KVLIAQEKMATNTVYubiquitination[1, 2, 7]
203NTVYVFAKKDSKYAYubiquitination[1, 2, 7]
204TVYVFAKKDSKYAYTubiquitination[2, 3, 5]
207VFAKKDSKYAYTGECubiquitination[2, 3, 5]
241ARGGQGAKKSAIGQRubiquitination[1, 7]
242RGGQGAKKSAIGQRIubiquitination[1, 7]
257VATLPYIKQEVPIIIubiquitination[1, 2, 3, 5, 7]
330VTKEKRIKYAKEVLQubiquitination[3]
333EKRIKYAKEVLQKEMubiquitination[1, 2, 3, 7]
338YAKEVLQKEMLPHVGubiquitination[2, 3]
353VSDFCETKKAYFLGYubiquitination[2, 5]
354SDFCETKKAYFLGYMubiquitination[2, 3]
384DRDHYGNKRLDLAGPubiquitination[1, 2, 3, 5, 7]
406GMFKNLLKEVRIYAQubiquitination[1]
414EVRIYAQKFIDRGKDubiquitination[1, 2, 4]
420QKFIDRGKDFNLELAubiquitination[1, 2, 3, 5]
429FNLELAIKTRIISDGubiquitination[1, 5]
438RIISDGLKYSLATGNubiquitination[1, 2, 3, 7]
450TGNWGDQKKAHQARAubiquitination[1, 2, 3, 5, 6, 7]
451GNWGDQKKAHQARAGubiquitination[2, 3]
571GCWVGIHKDPEQLMNubiquitination[2, 3, 5]
623RPLLIVEKQKLLLKKubiquitination[1, 2, 3, 6, 7]
625LLIVEKQKLLLKKRHubiquitination[2, 3]
637KRHIDQLKEREYNNYubiquitination[1, 2, 5, 6, 7]
723TYQSAMGKQAMGVYIubiquitination[1, 2, 3, 5, 6, 7]
749HVLYYPQKPLVTTRSubiquitination[1, 2, 3, 4, 5, 6, 7]
808SVFYRSYKEQESKKGubiquitination[1]
814YKEQESKKGFDQEEVubiquitination[1, 2, 3, 5, 7]
824DQEEVFEKPTRETCQubiquitination[1, 2, 3, 5, 6, 7]
840MRHAIYDKLDDDGLIubiquitination[1, 2, 3, 4, 5, 7]
862GDDVIIGKTVTLPENubiquitination[1, 2, 3, 5, 6, 7]
910TLNQEGYKFCKIRVRubiquitination[2, 3, 5]
927RIPQIGDKFASRHGQubiquitination[1, 2, 3, 4, 6, 7]
935FASRHGQKGTCGIQYubiquitination[2, 3, 5]
981LIECLQGKVSANKGEubiquitination[2, 3, 5]
986QGKVSANKGEIGDATubiquitination[1, 2, 3, 5, 6, 7]
1003NDAVNVQKISNLLSDubiquitination[1, 2, 3, 5, 7]
1029YNGFTGRKITSQIFIubiquitination[1, 2, 3, 6]
1045PTYYQRLKHMVDDKImethylation[8]
1051LKHMVDDKIHSRARGubiquitination[1]
1136ECRGCRNKTQISLVRubiquitination[1, 2, 3, 6, 7]
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] 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] 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] 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]
 [8] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1167 AA 
Protein Sequence
MQYDEDDDEI TPDLWQEACW IVISSYFDEK GLVRQQLDSF DEFIQMSVQR IVEDAPPIDL 60
QAEAQHASGE VEEPPRYLLK FEQIYLSKPT HWERDGAPSP MMPNEARLRN LTYSAPLYVD 120
ITKTVIKEGE EQLQTQHQKT FIGKIPIMLR STYCLLNGLT DRDLCELNEC PLDPGGYFII 180
NGSEKVLIAQ EKMATNTVYV FAKKDSKYAY TGECRSCLEN SSRPTSTIWV SMLARGGQGA 240
KKSAIGQRIV ATLPYIKQEV PIIIVFRALG FVSDRDILEH IIYDFEDPEM MEMVKPSLDE 300
AFVIQEQNVA LNFIGSRGAK PGVTKEKRIK YAKEVLQKEM LPHVGVSDFC ETKKAYFLGY 360
MVHRLLLAAL GRRELDDRDH YGNKRLDLAG PLLAFLFRGM FKNLLKEVRI YAQKFIDRGK 420
DFNLELAIKT RIISDGLKYS LATGNWGDQK KAHQARAGVS QVLNRLTFAS TLSHLRRLNS 480
PIGRDGKLAK PRQLHNTLWG MVCPAETPEG HAVGLVKNLA LMAYISVGSQ PSPILEFLEE 540
WSMENLEEIS PAAIADATKI FVNGCWVGIH KDPEQLMNTL RKLRRQMDII VSEVSMIRDI 600
REREIRIYTD AGRICRPLLI VEKQKLLLKK RHIDQLKERE YNNYSWQDLV ASGVVEYIDT 660
LEEETVMLAM TPDDLQEKEV AYCSTYTHCE IHPSMILGVC ASIIPFPDHN QSPRNTYQSA 720
MGKQAMGVYI TNFHVRMDTL AHVLYYPQKP LVTTRSMEYL RFRELPAGIN SIVAIASYTG 780
YNQEDSVIMN RSAVDRGFFR SVFYRSYKEQ ESKKGFDQEE VFEKPTRETC QGMRHAIYDK 840
LDDDGLIAPG VRVSGDDVII GKTVTLPENE DELESTNRRY TKRDCSTFLR TSETGIVDQV 900
MVTLNQEGYK FCKIRVRSVR IPQIGDKFAS RHGQKGTCGI QYRQEDMPFT CEGITPDIII 960
NPHAIPSRMT IGHLIECLQG KVSANKGEIG DATPFNDAVN VQKISNLLSD YGYHLRGNEV 1020
LYNGFTGRKI TSQIFIGPTY YQRLKHMVDD KIHSRARGPI QILNRQPMEG RSRDGGLRFG 1080
EMERDCQIAH GAAQFLRERL FEASDPYQVH VCNLCGIMAI ANTRTHTYEC RGCRNKTQIS 1140
LVRMPYACKL LFQELMSMSI APRMMSV 1167 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
 GO:0032549; F:ribonucleoside binding; IEA:InterPro.
 GO:0006351; P:transcription, DNA-dependent; IEA:InterPro. 
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