MED7_HUMAN - dbPTM
MED7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED7_HUMAN
UniProt AC O43513
Protein Name Mediator of RNA polymerase II transcription subunit 7
Gene Name MED7
Organism Homo sapiens (Human).
Sequence Length 233
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 MGEPQQVSALPPPPMQYIKEYTDENIQEGLAPKPPPPIKDSYMMFGNQFQCDDLIIRPLESQGIERLHPMQFDHKKELRKLNMSILINFLDLLDILIRSPGSIKREEKLEDLKLLFVHVHHLINEYRPHQARETLRVMMEVQKRQRLETAERFQKHLERVIEMIQNCLASLPDDLPHSEAGMRVKTEPMDADDSNNCTGQNEHQRENSGHRRDQIIEKDAALCVLIDEMNERP
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
33UbiquitinationIQEGLAPKPPPPIKD
HHHCCCCCCCCCCCC
65.63-
155UbiquitinationETAERFQKHLERVIE
HHHHHHHHHHHHHHH
47.6621890473
185SumoylationSEAGMRVKTEPMDAD
CCCCCCEECCCCCCC
36.48-
185SumoylationSEAGMRVKTEPMDAD
CCCCCCEECCCCCCC
36.4825114211
185UbiquitinationSEAGMRVKTEPMDAD
CCCCCCEECCCCCCC
36.48-
185AcetylationSEAGMRVKTEPMDAD
CCCCCCEECCCCCCC
36.4826051181
186PhosphorylationEAGMRVKTEPMDADD
CCCCCEECCCCCCCC
42.3327251275
194PhosphorylationEPMDADDSNNCTGQN
CCCCCCCCCCCCCCC
30.4125218447
198PhosphorylationADDSNNCTGQNEHQR
CCCCCCCCCCCHHHH
43.8827251275

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 MED7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED7_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 MED7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBAC1_HUMANUBAC1physical
17353931
BARH1_HUMANBARHL1physical
17353931
FXR2_HUMANFXR2physical
17353931
RFOX2_HUMANRBFOX2physical
20211142
TRI29_HUMANTRIM29physical
20211142
MED31_HUMANMED31physical
20211142
PHS2_HUMANPCBD2physical
20211142
RHXF2_HUMANRHOXF2physical
20211142
TRI15_HUMANTRIM15physical
20211142
ZSCA1_HUMANZSCAN1physical
20211142
HAUS1_HUMANHAUS1physical
25416956
MED13_HUMANMED13physical
26186194
MED1_HUMANMED1physical
26186194
MED27_HUMANMED27physical
26186194
MED31_HUMANMED31physical
26186194
MED26_HUMANMED26physical
26186194
MD13L_HUMANMED13Lphysical
26186194
MED16_HUMANMED16physical
26186194
MED14_HUMANMED14physical
26186194
MED12_HUMANMED12physical
26186194
MD12L_HUMANMED12Lphysical
26186194
MED21_HUMANMED21physical
26186194
MED23_HUMANMED23physical
26186194
MED15_HUMANMED15physical
26186194
MED9_HUMANMED9physical
26186194
MED6_HUMANMED6physical
26186194
MED4_HUMANMED4physical
26186194
MED28_HUMANMED28physical
26186194
MED17_HUMANMED17physical
26186194
CCNC_HUMANCCNCphysical
26186194
MED29_HUMANMED29physical
26186194
MED22_HUMANMED22physical
26186194
MED24_HUMANMED24physical
26186194
MED10_HUMANMED10physical
26186194
PRDC1_HUMANPRTFDC1physical
26186194
MED20_HUMANMED20physical
26186194
CDK19_HUMANCDK19physical
26186194
CDK8_HUMANCDK8physical
26186194
MED19_HUMANMED19physical
26186194
MED18_HUMANMED18physical
26186194
MED30_HUMANMED30physical
26186194
MED8_HUMANMED8physical
26186194
MED11_HUMANMED11physical
26186194
MED1_HUMANMED1physical
28514442
MED19_HUMANMED19physical
28514442
CCNC_HUMANCCNCphysical
28514442
MED31_HUMANMED31physical
28514442
MED6_HUMANMED6physical
28514442
MED27_HUMANMED27physical
28514442
MED13_HUMANMED13physical
28514442
MED9_HUMANMED9physical
28514442
MED22_HUMANMED22physical
28514442
MED17_HUMANMED17physical
28514442
MED20_HUMANMED20physical
28514442
MD13L_HUMANMED13Lphysical
28514442
MED26_HUMANMED26physical
28514442
MED4_HUMANMED4physical
28514442
MED14_HUMANMED14physical
28514442
MED8_HUMANMED8physical
28514442
MD12L_HUMANMED12Lphysical
28514442
MED10_HUMANMED10physical
28514442
MED30_HUMANMED30physical
28514442
MED12_HUMANMED12physical
28514442
MED28_HUMANMED28physical
28514442
MED24_HUMANMED24physical
28514442
CDK8_HUMANCDK8physical
28514442
MED11_HUMANMED11physical
28514442
MED23_HUMANMED23physical
28514442
MED15_HUMANMED15physical
28514442
MED16_HUMANMED16physical
28514442
MED29_HUMANMED29physical
28514442
CDK19_HUMANCDK19physical
28514442
PRDC1_HUMANPRTFDC1physical
28514442

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 MED7_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-194, AND MASSSPECTROMETRY.

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