CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031251
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mediator of RNA polymerase II transcription subunit 6 
Protein Synonyms/Alias
 Mediator complex subunit 6 
Gene Name
 MED6 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51TCNNEVVKMQRLTLEubiquitination[1, 2, 3]
150YCRYHPSKGYWWHFKubiquitination[2]
172VRPKAKRKEEPSSIFubiquitination[1, 2, 4]
203PPKFVQLKPGEKPVPubiquitination[2, 3, 4]
207VQLKPGEKPVPVDQTubiquitination[2, 5, 6]
216VPVDQTKKEAEPIPEubiquitination[4]
226EPIPETVKPEEKETTubiquitination[4]
234PEEKETTKNVQQTVSubiquitination[2, 3, 4]
243VQQTVSAKGPPEKRMacetylation[3, 7, 8]
243VQQTVSAKGPPEKRMubiquitination[4]
248SAKGPPEKRMRLQ**acetylation[3, 7, 8]
Reference
 [1] 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]
 [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] 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]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [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
 Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). 
Sequence Annotation
  
Keyword
 Activator; Complete proteome; Nucleus; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 253 AA 
Protein Sequence
MAAVDIRDNL LGISWVDSSW IPILNSGSVL DYFSERSNPF YDRTCNNEVV KMQRLTLEHL 60
NQMVGIEYIL LHAQEPILFI IRKQQRQSPA QVIPLADYYI IAGVIYQAPD LGSVINSRVS 120
LFSFYKLTAV HGIQSAFDEA MSYCRYHPSK GYWWHFKDHE EQDKVRPKAK RKEEPSSIFQ 180
RQRVDALLLD LRQKFPPKFV QLKPGEKPVP VDQTKKEAEP IPETVKPEEK ETTKNVQQTV 240
SAKGPPEKRM RLQ 253 
Gene Ontology
 GO:0016592; C:mediator complex; IEA:InterPro.
 GO:0001104; F:RNA polymerase II transcription cofactor activity; IEA:InterPro. 
Interpro
 IPR007018; Mediator_Med6.
 IPR016820; Mediator_Med6_met/pln. 
Pfam
 PF04934; Med6 
SMART
  
PROSITE
  
PRINTS