MED17_HUMAN - dbPTM
MED17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED17_HUMAN
UniProt AC Q9NVC6
Protein Name Mediator of RNA polymerase II transcription subunit 17
Gene Name MED17
Organism Homo sapiens (Human).
Sequence Length 651
Subcellular Localization Nucleus .
Protein 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..
Protein Sequence MSGVRAVRISIESACEKQVHEVGLDGTETYLPPLSMSQNLARLAQRIDFSQGSGSEEEEAAGTEGDAQEWPGAGSSADQDDEEGVVKFQPSLWPWDSVRNNLRSALTEMCVLYDVLSIVRDKKFMTLDPVSQDALPPKQNPQTLQLISKKKSLAGAAQILLKGAERLTKSVTENQENKLQRDFNSELLRLRQHWKLRKVGDKILGDLSYRSAGSLFPHHGTFEVIKNTDLDLDKKIPEDYCPLDVQIPSDLEGSAYIKVSIQKQAPDIGDLGTVNLFKRPLPKSKPGSPHWQTKLEAAQNVLLCKEIFAQLSREAVQIKSQVPHIVVKNQIISQPFPSLQLSISLCHSSNDKKSQKFATEKQCPEDHLYVLEHNLHLLIREFHKQTLSSIMMPHPASAPFGHKRMRLSGPQAFDKNEINSLQSSEGLLEKIIKQAKHIFLRSRAAATIDSLASRIEDPQIQAHWSNINDVYESSVKVLITSQGYEQICKSIQLQLNIGVEQIRVVHRDGRVITLSYQEQELQDFLLSQMSQHQVHAVQQLAKVMGWQVLSFSNHVGLGPIESIGNASAITVASPSGDYAISVRNGPESGSKIMVQFPRNQCKDLPKSDVLQDNKWSHLRGPFKEVQWNKMEGRNFVYKMELLMSALSPCLL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationGVRAVRISIESACEK
CCCEEEEEHHHHHHH		15.1126657352
13PhosphorylationAVRISIESACEKQVH
EEEEEHHHHHHHCCE		36.2327251275
17UbiquitinationSIESACEKQVHEVGL
EHHHHHHHCCEECCC		58.4629967540
37PhosphorylationYLPPLSMSQNLARLA
CCCCCCHHHHHHHHH		16.7317525332
50PhosphorylationLAQRIDFSQGSGSEE
HHHHCCCCCCCCCHH		29.8622817900
53PhosphorylationRIDFSQGSGSEEEEA
HCCCCCCCCCHHHHH		31.3522817900
55PhosphorylationDFSQGSGSEEEEAAG
CCCCCCCCHHHHHCC		43.4618691976
63PhosphorylationEEEEAAGTEGDAQEW
HHHHHCCCCCCCCCC		31.8828348404
75PhosphorylationQEWPGAGSSADQDDE
CCCCCCCCCCCCCCC		23.0925841592
76PhosphorylationEWPGAGSSADQDDEE
CCCCCCCCCCCCCCC		34.6425841592
117PhosphorylationCVLYDVLSIVRDKKF
HHHHHHHHHHCCCCC		20.9124719451
122UbiquitinationVLSIVRDKKFMTLDP
HHHHHCCCCCCCCCC		37.0322817900
123 (in isoform 2)Ubiquitination-44.6621890473
123UbiquitinationLSIVRDKKFMTLDPV
HHHHCCCCCCCCCCC		44.6622817900
123 (in isoform 1)Ubiquitination-44.6621890473
138UbiquitinationSQDALPPKQNPQTLQ
CCCCCCCCCCHHHHH		61.85-
143PhosphorylationPPKQNPQTLQLISKK
CCCCCHHHHHHHHHH		20.0917192257
148PhosphorylationPQTLQLISKKKSLAG
HHHHHHHHHHCCHHH		47.1924719451
149UbiquitinationQTLQLISKKKSLAGA
HHHHHHHHHCCHHHH		58.1721906983
149 (in isoform 1)Ubiquitination-58.1721890473
150UbiquitinationTLQLISKKKSLAGAA
HHHHHHHHCCHHHHH		40.5822817900
151UbiquitinationLQLISKKKSLAGAAQ
HHHHHHHCCHHHHHH		55.2122817900
162UbiquitinationGAAQILLKGAERLTK
HHHHHHHHHHHHHHH		53.2621906983
162 (in isoform 1)Ubiquitination-53.2621890473
169UbiquitinationKGAERLTKSVTENQE
HHHHHHHHHCCHHHH		47.7421906983
169 (in isoform 1)Ubiquitination-47.7421890473
170PhosphorylationGAERLTKSVTENQEN
HHHHHHHHCCHHHHH		29.0921406692
172PhosphorylationERLTKSVTENQENKL
HHHHHHCCHHHHHHH		35.9921406692
178 (in isoform 1)Ubiquitination-45.2921890473
178UbiquitinationVTENQENKLQRDFNS
CCHHHHHHHHHHHHH		45.2921906983
185PhosphorylationKLQRDFNSELLRLRQ
HHHHHHHHHHHHHHH		29.6122817900
198AcetylationRQHWKLRKVGDKILG
HHHHHHHHHCHHHCC		62.0925953088
198UbiquitinationRQHWKLRKVGDKILG
HHHHHHHHHCHHHCC		62.0922817900
202AcetylationKLRKVGDKILGDLSY
HHHHHCHHHCCCCCC		33.6225953088
202UbiquitinationKLRKVGDKILGDLSY
HHHHHCHHHCCCCCC		33.6221906983
202 (in isoform 1)Ubiquitination-33.6221890473
226UbiquitinationHGTFEVIKNTDLDLD
CCCEEEEECCCCCCC		60.0021906983
226 (in isoform 1)Ubiquitination-60.0021890473
234UbiquitinationNTDLDLDKKIPEDYC
CCCCCCCCCCCCCCC		60.9621906983
234 (in isoform 1)Ubiquitination-60.9621890473
235UbiquitinationTDLDLDKKIPEDYCP
CCCCCCCCCCCCCCC		64.2622817900
256PhosphorylationSDLEGSAYIKVSIQK
CCCCCCEEEEEEEEE		11.72-
258UbiquitinationLEGSAYIKVSIQKQA
CCCCEEEEEEEEECC		19.7722817900
263 (in isoform 1)Ubiquitination-46.9221890473
263UbiquitinationYIKVSIQKQAPDIGD
EEEEEEEECCCCCCC		46.9221906983
263AcetylationYIKVSIQKQAPDIGD
EEEEEEEECCCCCCC		46.9225953088
278AcetylationLGTVNLFKRPLPKSK
CCCEECCCCCCCCCC		57.1623749302
278UbiquitinationLGTVNLFKRPLPKSK
CCCEECCCCCCCCCC		57.1621963094
283UbiquitinationLFKRPLPKSKPGSPH
CCCCCCCCCCCCCCC		77.9622817900
284PhosphorylationFKRPLPKSKPGSPHW
CCCCCCCCCCCCCCH		41.99-
285UbiquitinationKRPLPKSKPGSPHWQ
CCCCCCCCCCCCCHH		60.5727667366
288PhosphorylationLPKSKPGSPHWQTKL
CCCCCCCCCCHHHHH		23.32-
294UbiquitinationGSPHWQTKLEAAQNV
CCCCHHHHHHHHHHH		29.2721963094
305UbiquitinationAQNVLLCKEIFAQLS
HHHHHHHHHHHHHHC		54.5421963094
319 (in isoform 1)Ubiquitination-20.1121890473
319UbiquitinationSREAVQIKSQVPHIV
CHHHHHHHHCCCEEE		20.1121906983
352UbiquitinationLCHSSNDKKSQKFAT
ECCCCCCHHCHHCCH		59.5822817900
353AcetylationCHSSNDKKSQKFATE
CCCCCCHHCHHCCHH		62.077465895
353UbiquitinationCHSSNDKKSQKFATE
CCCCCCHHCHHCCHH		62.0722817900
356UbiquitinationSNDKKSQKFATEKQC
CCCHHCHHCCHHHCC		44.0221906983
356AcetylationSNDKKSQKFATEKQC
CCCHHCHHCCHHHCC		44.027465905
356 (in isoform 1)Ubiquitination-44.0221890473
361UbiquitinationSQKFATEKQCPEDHL
CHHCCHHHCCCCHHH		53.5022817900
361AcetylationSQKFATEKQCPEDHL
CHHCCHHHCCCCHHH		53.5025953088
403UbiquitinationASAPFGHKRMRLSGP
CCCCCCCCCCCCCCC		48.5521906983
403 (in isoform 1)Ubiquitination-48.5521890473
403AcetylationASAPFGHKRMRLSGP
CCCCCCCCCCCCCCC		48.5525953088
408PhosphorylationGHKRMRLSGPQAFDK
CCCCCCCCCCCCCCH		37.7525159151
415UbiquitinationSGPQAFDKNEINSLQ
CCCCCCCHHHHHHHH		50.4521906983
415 (in isoform 1)Ubiquitination-50.4521890473
415AcetylationSGPQAFDKNEINSLQ
CCCCCCCHHHHHHHH		50.4526051181
430UbiquitinationSSEGLLEKIIKQAKH
CCHHHHHHHHHHHHH		50.1021906983
430 (in isoform 1)Ubiquitination-50.1021890473
433UbiquitinationGLLEKIIKQAKHIFL
HHHHHHHHHHHHHHH		47.9122817900
436UbiquitinationEKIIKQAKHIFLRSR
HHHHHHHHHHHHHHH		34.4423503661
490PhosphorylationGYEQICKSIQLQLNI
CHHHHHHHHHHHCCC		15.9122210691
550PhosphorylationVMGWQVLSFSNHVGL
HHCCEEEEEECCCCC		27.9822210691
567PhosphorylationIESIGNASAITVASP
HHHCCCEEEEEEECC		24.9722210691
590PhosphorylationRNGPESGSKIMVQFP
ECCCCCCCEEEEECC		28.4322210691
591UbiquitinationNGPESGSKIMVQFPR
CCCCCCCEEEEECCH		38.0421906983
591 (in isoform 1)Ubiquitination-38.0421890473
602UbiquitinationQFPRNQCKDLPKSDV
ECCHHHCCCCCHHHH		53.1622817900
606AcetylationNQCKDLPKSDVLQDN
HHCCCCCHHHHCCCC		67.5926051181
606UbiquitinationNQCKDLPKSDVLQDN
HHCCCCCHHHHCCCC		67.5921906983
606 (in isoform 1)Ubiquitination-67.5921890473
614UbiquitinationSDVLQDNKWSHLRGP
HHHCCCCCCHHHCCC		59.3621906983
614 (in isoform 1)Ubiquitination-59.3621890473
623UbiquitinationSHLRGPFKEVQWNKM
HHHCCCCHHCCCCCC		61.1722817900
623AcetylationSHLRGPFKEVQWNKM
HHHCCCCHHCCCCCC		61.1725953088
623 (in isoform 1)Ubiquitination-61.1721890473
629UbiquitinationFKEVQWNKMEGRNFV
CHHCCCCCCCCCCHH		35.0621906983
629 (in isoform 1)Ubiquitination-35.0621890473
629AcetylationFKEVQWNKMEGRNFV
CHHCCCCCCCCCCHH		35.0626051181
637PhosphorylationMEGRNFVYKMELLMS
CCCCCHHHHHHHHHH		10.65-
647PhosphorylationELLMSALSPCLL---
HHHHHHHHCCCC---		17.1824719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MED17_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED17_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MED17_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRCA1_HUMANBRCA1physical
12154023
BARD1_HUMANBARD1physical
12154023
SMCA4_HUMANSMARCA4physical
12154023
P53_HUMANTP53physical
10198638
MED28_HUMANMED28physical
22939629
MED24_HUMANMED24physical
22939629
MED21_HUMANMED21physical
22939629
TFP11_HUMANTFIP11physical
22939629
WDR33_HUMANWDR33physical
22939629
MED12_HUMANMED12physical
26344197
MED13_HUMANMED13physical
26344197
MED16_HUMANMED16physical
26344197
MED22_HUMANMED22physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613668Microcephaly, postnatal progressive, with seizures and brain atrophy (MCPHSBA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MED17_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-53; SER-55;SER-75 AND SER-76, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory