MED2_YEAST - dbPTM
MED2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED2_YEAST
UniProt AC Q12124
Protein Name Mediator of RNA polymerase II transcription subunit 2
Gene Name MED2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 431
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. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins..
Protein Sequence MVVQNSPVSSVHTANFSERGSNTRTMTYKNKLTVCFDDILKVGAEMMMQQQLKNVQLDSYLVNGFSQSQQKLLKEKVKLFHGILDDLETSLSQSSSYLETLTALGKEKEKEREEAEKKRAEQENMRKVREQEELKKRQELEEASQQQQLQQNSKEKNGLGLNFSTTAPANTTDANGSKENYQELGSLQSSSQTQLENANAANNGAAFSPLTTTRIQSQQAQPSDVMFNDLNSMDISMFSGLDSTGFDSTAFNATVDETKGFDDNDSGNNYNDINISSIENNINNNINSTKNGKDNNNESNKNNNGDEKNKNNNEDNENNNNSSEKNNNNNNNNNNNNDDNGNNNNNNSGNDNNNTTNNDSNNKNNSITTGNDNENIVNNDLPTTVVSNPGDNPPPADNGEEYLTLNDFNDLNIDWSTTGDNGELDLSGFNI
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
6Phosphorylation--MVVQNSPVSSVHT
--CCCCCCCCCEEEE		15.0222369663
9PhosphorylationVVQNSPVSSVHTANF
CCCCCCCCEEEECCC		29.9922369663
10PhosphorylationVQNSPVSSVHTANFS
CCCCCCCEEEECCCC		20.3922369663
13PhosphorylationSPVSSVHTANFSERG
CCCCEEEECCCCCCC		22.5722369663
17PhosphorylationSVHTANFSERGSNTR
EEEECCCCCCCCCCC		26.6222369663
33PhosphorylationMTYKNKLTVCFDDIL
EEEECCEEEEHHHHH		19.4828889911
68PhosphorylationLVNGFSQSQQKLLKE
HHCCCCHHHHHHHHH		33.1223749301
71UbiquitinationGFSQSQQKLLKEKVK
CCCHHHHHHHHHHHH		48.4224961812
172PhosphorylationTTAPANTTDANGSKE
CCCCCCCCCCCCCCH		32.6827017623
177PhosphorylationNTTDANGSKENYQEL
CCCCCCCCCHHHHHH		36.2827017623
181PhosphorylationANGSKENYQELGSLQ
CCCCCHHHHHHHHCC		12.4022369663
186PhosphorylationENYQELGSLQSSSQT
HHHHHHHHCCCCCHH		35.5422369663
189PhosphorylationQELGSLQSSSQTQLE
HHHHHCCCCCHHHHH		36.9322369663
190PhosphorylationELGSLQSSSQTQLEN
HHHHCCCCCHHHHHH		17.3222369663
191PhosphorylationLGSLQSSSQTQLENA
HHHCCCCCHHHHHHH		42.3622369663
193PhosphorylationSLQSSSQTQLENANA
HCCCCCHHHHHHHHH		36.7522369663
208PhosphorylationANNGAAFSPLTTTRI
HCCCCCCCCCCHHHH		17.8014988503
211PhosphorylationGAAFSPLTTTRIQSQ
CCCCCCCCHHHHHHC		29.5222369663
212PhosphorylationAAFSPLTTTRIQSQQ
CCCCCCCHHHHHHCC		23.0422369663
213PhosphorylationAFSPLTTTRIQSQQA
CCCCCCHHHHHHCCC		22.1222369663
266PhosphorylationKGFDDNDSGNNYNDI
CCCCCCCCCCCCCCC		50.0722369663
270PhosphorylationDNDSGNNYNDINISS
CCCCCCCCCCCCHHH		20.4322369663
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
208SPhosphorylationKinaseCDK8P39073
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED2_YEAST !!
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 MED2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED9_YEASTCSE2physical
11805826
MED15_YEASTGAL11physical
11805826
MED1_YEASTMED1physical
11805826
MED11_YEASTMED11physical
11805826
MED4_YEASTMED4physical
11805826
MED6_YEASTMED6physical
11805826
MED7_YEASTMED7physical
11805826
MED8_YEASTMED8physical
11805826
MED5_YEASTNUT1physical
11805826
MED10_YEASTNUT2physical
11805826
MED3_YEASTPGD1physical
11805826
MED14_YEASTRGR1physical
11805826
EIF3A_YEASTRPG1physical
11805826
COG3_YEASTCOG3physical
11805826
MED16_YEASTSIN4physical
11805826
MED20_YEASTSRB2physical
11805826
MED17_YEASTSRB4physical
11805826
MED18_YEASTSRB5physical
11805826
MED22_YEASTSRB6physical
11805826
SRB8_YEASTSRB8physical
11805826
SSN2_YEASTSSN2physical
11805826
IMA1_YEASTSRP1physical
11805826
HSP79_YEASTSSE2physical
11805826
SSN3_YEASTSSN3physical
11805826
AP1_YEASTYAP1physical
11805826
MED3_YEASTPGD1physical
9420330
MED4_YEASTMED4physical
9420330
MED7_YEASTMED7physical
9420330
MED8_YEASTMED8physical
9420330
RPB3_YEASTRPB3physical
9420330
MED17_YEASTSRB4physical
9420330
MED3_YEASTPGD1physical
9874773
MED4_YEASTMED4physical
9874773
MED7_YEASTMED7physical
9874773
PDC1_YEASTPDC1genetic
12468546
PDC2_YEASTPDC2genetic
12468546
ZDS1_YEASTZDS1genetic
12468546
T2EA_YEASTTFA1genetic
10973956
GCN5_YEASTGCN5genetic
16581789
MED3_YEASTPGD1physical
16230344
SWD1_YEASTSWD1genetic
17314980
SNF5_YEASTSNF5genetic
17314980
AIM4_YEASTAIM4genetic
17314980
SWD3_YEASTSWD3genetic
17314980
UBX1_YEASTSHP1genetic
17314980
OAF1_YEASTOAF1genetic
17314980
UBC4_YEASTUBC4genetic
17314980
HTL1_YEASTHTL1genetic
17314980
ECM33_YEASTECM33genetic
20093466
HXKB_YEASTHXK2genetic
20093466
CTU1_YEASTNCS6genetic
20093466
YG34_YEASTYGR122Wgenetic
20093466
PACC_YEASTRIM101genetic
20093466
MUD2_YEASTMUD2genetic
20093466
PDC1_YEASTPDC1genetic
20093466
THI7_YEASTTHI7genetic
20093466
VPS9_YEASTVPS9genetic
20093466
BRE5_YEASTBRE5genetic
20093466
IES4_YEASTIES4genetic
20093466
MTHR1_YEASTMET12genetic
20093466
TKT1_YEASTTKL1genetic
20093466
ADR1_YEASTADR1genetic
20139423
MED15_YEASTGAL11physical
19940160
RPB3_YEASTRPB3physical
19940160
XRN1_YEASTXRN1genetic
21738494
MED3_YEASTPGD1physical
21498544
SIR2_YEASTSIR2genetic
21930512
MED20_YEASTSRB2physical
26240385
MED14_YEASTRGR1physical
26240385
DED1_YEASTDED1genetic
27708008
YP191_YEASTYPL191Cgenetic
27708008
ECM33_YEASTECM33genetic
27708008
CTU1_YEASTNCS6genetic
27708008
HXKB_YEASTHXK2genetic
27708008
RPA34_YEASTRPA34genetic
27708008
MUD2_YEASTMUD2genetic
27708008
PDC1_YEASTPDC1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
THI7_YEASTTHI7genetic
27708008
VPS9_YEASTVPS9genetic
27708008
RIM13_YEASTRIM13genetic
27708008
SCS7_YEASTSCS7genetic
27708008
BRE5_YEASTBRE5genetic
27708008
IES4_YEASTIES4genetic
27708008
MTHR1_YEASTMET12genetic
27708008
TKT1_YEASTTKL1genetic
27708008
MED3_YEASTPGD1genetic
25645928
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MED2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-190; SER-191 ANDTHR-193, AND MASS SPECTROMETRY.
"Mediator expression profiling epistasis reveals a signal transductionpathway with antagonistic submodules and highly specific downstreamtargets.";
van de Peppel J., Kettelarij N., van Bakel H., Kockelkorn T.T.J.P.,van Leenen D., Holstege F.C.P.;
Mol. Cell 19:511-522(2005).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-208, AND MUTAGENESIS OF SER-208.
"Site-specific Srb10-dependent phosphorylation of the yeast Mediatorsubunit Med2 regulates gene expression from the 2-micrometerplasmid.";
Hallberg M., Polozkov G.V., Hu G.-Z., Beve J., Gustafsson C.M.,Ronne H., Bjoerklund S.;
Proc. Natl. Acad. Sci. U.S.A. 101:3370-3375(2004).
Cited for: INTERACTION WITH PDG1, PHOSPHORYLATION AT SER-208, AND MUTAGENESIS OFSER-208.

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