MED31_HUMAN - dbPTM
MED31_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED31_HUMAN
UniProt AC Q9Y3C7
Protein Name Mediator of RNA polymerase II transcription subunit 31
Gene Name MED31
Organism Homo sapiens (Human).
Sequence Length 131
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 MAAAVAMETDDAGNRLRFQLELEFVQCLANPNYLNFLAQRGYFKDKAFVNYLKYLLYWKDPEYAKYLKYPQCLHMLELLQYEHFRKELVNAQCAKFIDEQQILHWQHYSRKRMRLQQALAEQQQQNNTSGK
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
2Acetylation------MAAAVAMET
------CCCEEEEEC
12.2522814378
9PhosphorylationAAAVAMETDDAGNRL
CCEEEEECCCCCCCE
26.54-
65UbiquitinationWKDPEYAKYLKYPQC
CCCHHHHHHCCCHHH
50.6529967540
69PhosphorylationEYAKYLKYPQCLHML
HHHHHCCCHHHHHHH
8.92-
95UbiquitinationLVNAQCAKFIDEQQI
HHHHHHHHHCCHHHH
50.9429967540
128PhosphorylationEQQQQNNTSGK----
HHHHHHCCCCC----
46.5428555341
129PhosphorylationQQQQNNTSGK-----
HHHHHCCCCC-----
46.8617192257
131AcetylationQQNNTSGK-------
HHHCCCCC-------
57.8630590379
131UbiquitinationQQNNTSGK-------
HHHCCCCC-------
57.8624816145

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 MED31_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED31_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 MED31_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED19_HUMANMED19physical
12584197
ZSCA1_HUMANZSCAN1physical
20211142
HD_HUMANHTTphysical
15383276

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MED31_HUMAN

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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-129, 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 SER-129, AND MASSSPECTROMETRY.

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