CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022198
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mediator of RNA polymerase II transcription subunit 17 
Protein Synonyms/Alias
 Activator-recruited cofactor 77 kDa component; ARC77; Cofactor required for Sp1 transcriptional activation subunit 6; CRSP complex subunit 6; Mediator complex subunit 17; Thyroid hormone receptor-associated protein complex 80 kDa component; Trap80; Transcriptional coactivator CRSP77; Vitamin D3 receptor-interacting protein complex 80 kDa component; DRIP80 
Gene Name
 MED17 
Gene Synonyms/Alias
 ARC77; CRSP6; DRIP77; DRIP80; TRAP80 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17SIESACEKQVHEVGLubiquitination[1]
123LSIVRDKKFMTLDPVubiquitination[2]
138SQDALPPKQNPQTLQubiquitination[3]
149QTLQLISKKKSLAGAubiquitination[3]
162GAAQILLKGAERLTKubiquitination[1, 3, 4]
169KGAERLTKSVTENQEubiquitination[3, 5]
178VTENQENKLQRDFNSubiquitination[1, 3, 4]
202KLRKVGDKILGDLSYubiquitination[1, 3]
226HGTFEVIKNTDLDLDubiquitination[3, 5]
234NTDLDLDKKIPEDYCubiquitination[3]
263YIKVSIQKQAPDIGDubiquitination[3, 4, 5, 6, 7]
278LGTVNLFKRPLPKSKacetylation[7]
278LGTVNLFKRPLPKSKubiquitination[1, 6]
285KRPLPKSKPGSPHWQubiquitination[1]
294GSPHWQTKLEAAQNVubiquitination[6]
305AQNVLLCKEIFAQLSubiquitination[4, 5, 6, 7]
319SREAVQIKSQVPHIVubiquitination[3]
356SNDKKSQKFATEKQCubiquitination[3]
361SQKFATEKQCPEDHLubiquitination[1]
403ASAPFGHKRMRLSGPubiquitination[3, 6]
415SGPQAFDKNEINSLQubiquitination[1, 3, 4, 5, 6, 7]
430SSEGLLEKIIKQAKHubiquitination[1, 3, 5, 6]
436EKIIKQAKHIFLRSRubiquitination[1]
591NGPESGSKIMVQFPRubiquitination[1, 3, 5]
606NQCKDLPKSDVLQDNubiquitination[1, 3]
614SDVLQDNKWSHLRGPubiquitination[1, 3, 5, 6]
623SHLRGPFKEVQWNKMubiquitination[1, 2, 3, 4, 5]
629FKEVQWNKMEGRNFVubiquitination[1, 3]
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] 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]
 [3] 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]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [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] 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] 
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. 
Sequence Annotation
  
Keyword
 Activator; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; Nucleus; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 651 AA 
Protein Sequence
MSGVRAVRIS IESACEKQVH EVGLDGTETY LPPLSMSQNL ARLAQRIDFS QGSGSEEEEA 60
AGTEGDAQEW PGAGSSADQD DEEGVVKFQP SLWPWDSVRN NLRSALTEMC VLYDVLSIVR 120
DKKFMTLDPV SQDALPPKQN PQTLQLISKK KSLAGAAQIL LKGAERLTKS VTENQENKLQ 180
RDFNSELLRL RQHWKLRKVG DKILGDLSYR SAGSLFPHHG TFEVIKNTDL DLDKKIPEDY 240
CPLDVQIPSD LEGSAYIKVS IQKQAPDIGD LGTVNLFKRP LPKSKPGSPH WQTKLEAAQN 300
VLLCKEIFAQ LSREAVQIKS QVPHIVVKNQ IISQPFPSLQ LSISLCHSSN DKKSQKFATE 360
KQCPEDHLYV LEHNLHLLIR EFHKQTLSSI MMPHPASAPF GHKRMRLSGP QAFDKNEINS 420
LQSSEGLLEK IIKQAKHIFL RSRAAATIDS LASRIEDPQI QAHWSNINDV YESSVKVLIT 480
SQGYEQICKS IQLQLNIGVE QIRVVHRDGR VITLSYQEQE LQDFLLSQMS QHQVHAVQQL 540
AKVMGWQVLS FSNHVGLGPI ESIGNASAIT VASPSGDYAI SVRNGPESGS KIMVQFPRNQ 600
CKDLPKSDVL QDNKWSHLRG PFKEVQWNKM EGRNFVYKME LLMSALSPCL L 651 
Gene Ontology
 GO:0016592; C:mediator complex; IDA:UniProtKB.
 GO:0005667; C:transcription factor complex; IDA:MGI.
 GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; NAS:UniProtKB.
 GO:0004872; F:receptor activity; IDA:UniProtKB.
 GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB.
 GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB.
 GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB.
 GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0019827; P:stem cell maintenance; IEA:Compara.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB. 
Interpro
 IPR019313; Mediator_Med17. 
Pfam
 PF10156; Med17 
SMART
  
PROSITE
  
PRINTS