Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Mediator of RNA polymerase II transcription subunit 31  

UniProtKB / Swiss-Prot ID :  MED31_HUMAN

Gene Name (Synonyms) : 
MED31, SOH1 CGI-125  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (Probable). 

Protein Function :  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 MAAAVAMETDDAGNRLRFQLELEFVQCLANPNYLNFLAQRGYFKDKAFVNYLKYLLYWKDPEYAKYLKYP...
Predicted Secondary Structure CCCCCCCCCCCCCCCEEHHHHHHHHHHHCCCHHHHHHHHCCCCCCHHHHHHHHHHHHHCCCCHHHEECCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
129PhosphoserineQNNTSGK
HCCCCCC
46.86HPRD
Link-
129PhosphoserineQNNTSGK
HCCCCCC
46.86Phosphositeplus
Link-
129PhosphoserineQNNTSGK
HCCCCCC
46.86SysPTM
Link-
129Phosphoserine.QNNTSGK
HCCCCCC
46.86UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MAFG_HUMANphysical interactionMINT-63108MINT16169070
LEU1_HUMANphysical interactionMINT-63131MINT16169070
PQBP1_HUMANphysical interactionMINT-63184MINT16169070
PFD1_HUMANphysical interactionMINT-63199MINT16169070
HNRL1_HUMANphysical interactionMINT-65539MINT16169070
CBPE_HUMANphysical interactionMINT-63495MINT16169070
SAT1_HUMANphysical interactionMINT-63592MINT16169070
HMOX2_HUMANphysical interactionMINT-63652MINT16169070
RFC5_HUMANphysical interactionMINT-63726MINT16169070
SPB9_HUMANphysical interactionMINT-63834MINT16169070
UBE2B_HUMANphysical interactionMINT-63985MINT16169070
GSTM4_HUMANphysical interactionMINT-64048MINT16169070
TGIF1_HUMANphysical interactionMINT-64253MINT16169070
Q4JM47_HUMANphysical interactionMINT-64310MINT16169070
Q5QPQ3_HUMANphysical interactionMINT-64462MINT16169070
CACB4_HUMANphysical interactionMINT-64583MINT16169070
Q6P3T6_HUMANphysical interactionMINT-64671MINT16169070
RBM23_HUMANphysical interactionMINT-64814MINT16169070
TCPH_HUMANphysical interactionMINT-65294MINT16169070
BRP16_HUMANphysical interactionMINT-65347MINT16169070
CB044_HUMANphysical interactionMINT-65502MINT16169070
ORA2P_HUMANphysical interactionMINT-65530MINT16169070
PMF1_HUMANphysical interactionMINT-65682MINT16169070
MOBL3_HUMANphysical interactionMINT-65842MINT16169070
EPN1_HUMANphysical interactionMINT-65867MINT16169070
HSPB1_HUMANphysical interactionEBI-730180
intact16169070
HD_HUMANin vitroHPRD:14382HPRD15383276
PABP4_HUMANyeast 2-hybridHPRD:14382HPRD15383276
GA45G_HUMANin vitro
yeast 2-hybrid
HPRD:14382HPRD15383276
RAB25_HUMANin vivoHPRD:14382HPRD11591653
MED8_HUMANin vitroHPRD:14382HPRD12149480
RBM23_HUMANyeast 2-hybridHPRD:14382HPRD16169070
ZBT45_HUMANyeast 2-hybridHPRD:14382HPRD16169070
ASCC2_HUMANyeast 2-hybridHPRD:14382HPRD16169070
BRP16_HUMANyeast 2-hybridHPRD:14382HPRD16169070
TINAL_HUMANyeast 2-hybridHPRD:14382HPRD16169070
ORAI2_HUMANyeast 2-hybridHPRD:14382HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-129, AND MASSSPECTROMETRY.
"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-129, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures