MED10_HUMAN - dbPTM
MED10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED10_HUMAN
UniProt AC Q9BTT4
Protein Name Mediator of RNA polymerase II transcription subunit 10
Gene Name MED10
Organism Homo sapiens (Human).
Sequence Length 135
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 MAEKFDHLEEHLEKFVENIRQLGIIVSDFQPSSQAGLNQKLNFIVTGLQDIDKCRQQLHDITVPLEVFEYIDQGRNPQLYTKECLERALAKNEQVKGKIDTMKKFKSLLIQELSKVFPEDMAKYRSIRGEDHPPS
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------MAEKFDHLE
------CHHHHHHHH
28.78-
4Acetylation----MAEKFDHLEEH
----CHHHHHHHHHH
46.7025953088
4Ubiquitination----MAEKFDHLEEH
----CHHHHHHHHHH
46.7033845483
14UbiquitinationHLEEHLEKFVENIRQ
HHHHHHHHHHHHHHH
62.1632015554
53UbiquitinationTGLQDIDKCRQQLHD
HCHHHHHHHHHHHCC
31.4829967540
82UbiquitinationRNPQLYTKECLERAL
CCCHHCCHHHHHHHH
32.6427667366
91UbiquitinationCLERALAKNEQVKGK
HHHHHHHHCCHHCCC
62.9627667366
98AcetylationKNEQVKGKIDTMKKF
HCCHHCCCHHHHHHH
31.5230590367
98UbiquitinationKNEQVKGKIDTMKKF
HCCHHCCCHHHHHHH
31.52-
106UbiquitinationIDTMKKFKSLLIQEL
HHHHHHHHHHHHHHH
49.4229967540
115UbiquitinationLLIQELSKVFPEDMA
HHHHHHHHHCHHHHH
61.5922817900
123UbiquitinationVFPEDMAKYRSIRGE
HCHHHHHHHHHHCCC
34.2629967540
135PhosphorylationRGEDHPPS-------
CCCCCCCC-------
58.2522617229

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 MED10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED10_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 MED10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MD13L_HUMANMED13Lphysical
15175163
MED13_HUMANMED13physical
15175163
MED12_HUMANMED12physical
15175163
MED14_HUMANMED14physical
15175163
MED23_HUMANMED23physical
15175163
MED15_HUMANMED15physical
15175163
MED16_HUMANMED16physical
15175163
MED17_HUMANMED17physical
15175163
MED26_HUMANMED26physical
15175163
CCNC_HUMANCCNCphysical
15175163
CDK8_HUMANCDK8physical
15175163
CDK19_HUMANCDK19physical
15175163
MED27_HUMANMED27physical
15175163
MED4_HUMANMED4physical
15175163
MED19_HUMANMED19physical
15175163
MED6_HUMANMED6physical
15175163
MED7_HUMANMED7physical
15175163
MED8_HUMANMED8physical
15175163
MED18_HUMANMED18physical
15175163
MED20_HUMANMED20physical
15175163
MED9_HUMANMED9physical
15175163
MED29_HUMANMED29physical
15175163
MED30_HUMANMED30physical
15175163
MED28_HUMANMED28physical
15175163
MED21_HUMANMED21physical
15175163
MED11_HUMANMED11physical
15175163
MED31_HUMANMED31physical
15175163
MED1_HUMANMED1physical
15175163
MED24_HUMANMED24physical
15175163
MED25_HUMANMED25physical
15175163
MED22_HUMANMED22physical
15175163
RPB1_HUMANPOLR2Aphysical
15175163
RPB2_HUMANPOLR2Bphysical
15175163
RPB3_HUMANPOLR2Cphysical
15175163
RPAB1_HUMANPOLR2Ephysical
15175163
RPAB2_HUMANPOLR2Fphysical
15175163
RPB7_HUMANPOLR2Gphysical
15175163
RPAB3_HUMANPOLR2Hphysical
15175163
RPB9_HUMANPOLR2Iphysical
15175163
RPAB5_HUMANPOLR2Lphysical
15175163
RPAB4_HUMANPOLR2Kphysical
15175163
RPB4_HUMANPOLR2Dphysical
15175163
RPB11_HUMANPOLR2Jphysical
15175163
MED1_HUMANMED1physical
14638676
MED19_HUMANMED19physical
14638676
MED4_HUMANMED4physical
14638676
MED8_HUMANMED8physical
14638676
MED18_HUMANMED18physical
14638676
MED11_HUMANMED11physical
14638676
MED29_HUMANMED29physical
14638676
MED17_HUMANMED17physical
14638676
MED17_HUMANMED17physical
14576168
MED6_HUMANMED6physical
14576168
MED8_HUMANMED8physical
14576168
MED20_HUMANMED20physical
14576168
MED29_HUMANMED29physical
14576168
MED31_HUMANMED31physical
14576168
MED18_HUMANMED18physical
14576168
MED11_HUMANMED11physical
14576168
MED17_HUMANMED17physical
12584197
MED6_HUMANMED6physical
12584197
MED8_HUMANMED8physical
12584197
MED19_HUMANMED19physical
12584197
MED18_HUMANMED18physical
12584197
MED22_HUMANMED22physical
12584197
MED11_HUMANMED11physical
12584197
MED13_HUMANMED13physical
15989967
MED6_HUMANMED6physical
15989967
MED16_HUMANMED16physical
15989967
MED17_HUMANMED17physical
15989967
MED20_HUMANMED20physical
15989967
MED1_HUMANMED1physical
15989967
MED14_HUMANMED14physical
15989967
MED12_HUMANMED12physical
15989967
MED23_HUMANMED23physical
15989967
MED24_HUMANMED24physical
15989967
CDK8_HUMANCDK8physical
15989967
MED27_HUMANMED27physical
15989967
MED4_HUMANMED4physical
15989967
MED7_HUMANMED7physical
15989967
MED8_HUMANMED8physical
15989967
MED30_HUMANMED30physical
15989967
MED22_HUMANMED22physical
15989967
MED31_HUMANMED31physical
15989967
MED25_HUMANMED25physical
15989967
MED15_HUMANMED15physical
15989967
MED19_HUMANMED19physical
15989967
MED18_HUMANMED18physical
15989967
MED11_HUMANMED11physical
15989967
MED13_HUMANMED13physical
10882111
MED12_HUMANMED12physical
10882111
MED1_HUMANMED1physical
10882111
MED14_HUMANMED14physical
10882111
MED24_HUMANMED24physical
10882111
MED16_HUMANMED16physical
10882111
MED17_HUMANMED17physical
10882111
MED7_HUMANMED7physical
10882111
MED20_HUMANMED20physical
10882111
CCNC_HUMANCCNCphysical
10882111
MED21_HUMANMED21physical
10882111
MED8_HUMANMED8physical
12149480
MED17_HUMANMED17physical
12149480
MED11_HUMANMED11physical
22939629
MED6_HUMANMED6physical
22939629
MED4_HUMANMED4physical
22939629
MED11_HUMANMED11physical
26344197
MED12_HUMANMED12physical
26344197
MED16_HUMANMED16physical
26344197
MED17_HUMANMED17physical
26344197
MED22_HUMANMED22physical
26344197
MED27_HUMANMED27physical
26344197
RPB1_HUMANPOLR2Aphysical
26344197

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 MED10_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

TOP