MED6_HUMAN - dbPTM
MED6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED6_HUMAN
UniProt AC O75586
Protein Name Mediator of RNA polymerase II transcription subunit 6
Gene Name MED6
Organism Homo sapiens (Human).
Sequence Length 246
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 MAAVDIRDNLLGISWVDSSWIPILNSGSVLDYFSERSNPFYDRTCNNEVVKMQRLTLEHLNQMVGIEYILLHAQEPILFIIRKQQRQSPAQVIPLADYYIIAGVIYQAPDLGSVINSRVLTAVHGIQSAFDEAMSYCRYHPSKGYWWHFKDHEEQDKVRPKAKRKEEPSSIFQRQRVDALLLDLRQKFPPKFVQLKPGEKPVPVDQTKKEAEPIPETVKPEEKETTKNVQQTVSAKGPPEKRMRLQ
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
44PhosphorylationSNPFYDRTCNNEVVK
CCCCCCCCCCHHHHH		19.3825332170
51UbiquitinationTCNNEVVKMQRLTLE
CCCHHHHHHHHHCHH		34.19-
51UbiquitinationTCNNEVVKMQRLTLE
CCCHHHHHHHHHCHH		34.19-
136PhosphorylationAFDEAMSYCRYHPSK
HHHHHHHHHHCCCCC		2.82-
139PhosphorylationEAMSYCRYHPSKGYW
HHHHHHHCCCCCCCE		17.96-
143UbiquitinationYCRYHPSKGYWWHFK
HHHCCCCCCCEEEEC		61.54-
145PhosphorylationRYHPSKGYWWHFKDH
HCCCCCCCEEEECCH		14.73-
150UbiquitinationKGYWWHFKDHEEQDK
CCCEEEECCHHHHHC		45.34-
157UbiquitinationKDHEEQDKVRPKAKR
CCHHHHHCCCCCHHC		39.58-
164 (in isoform 3)Phosphorylation-57.3822210691
165 (in isoform 3)Phosphorylation-66.7722210691
165UbiquitinationVRPKAKRKEEPSSIF
CCCCHHCCCCCCHHH		66.7721906983
167 (in isoform 3)Phosphorylation-54.2222210691
172UbiquitinationKEEPSSIFQRQRVDA
CCCCCHHHHHHHHHH		5.45-
196UbiquitinationPPKFVQLKPGEKPVP
CCCCCCCCCCCCCCC		33.6121906983
200UbiquitinationVQLKPGEKPVPVDQT
CCCCCCCCCCCCCCC		58.1721890473
200AcetylationVQLKPGEKPVPVDQT
CCCCCCCCCCCCCCC		58.1725953088
203UbiquitinationKPGEKPVPVDQTKKE
CCCCCCCCCCCCCCC		32.28-
207UbiquitinationKPVPVDQTKKEAEPI
CCCCCCCCCCCCCCC		39.3521890473
208SumoylationPVPVDQTKKEAEPIP
CCCCCCCCCCCCCCC		42.8828112733
216UbiquitinationKEAEPIPETVKPEEK
CCCCCCCCCCCHHHH		67.94-
219SumoylationEPIPETVKPEEKETT
CCCCCCCCHHHHHCC		54.88-
219SumoylationEPIPETVKPEEKETT
CCCCCCCCHHHHHCC		54.88-
219AcetylationEPIPETVKPEEKETT
CCCCCCCCHHHHHCC		54.8826051181
226UbiquitinationKPEEKETTKNVQQTV
CHHHHHCCCCHHHHH		23.01-
227UbiquitinationPEEKETTKNVQQTVS
HHHHHCCCCHHHHHH		63.6421906983
234UbiquitinationKNVQQTVSAKGPPEK
CCHHHHHHCCCCHHH		27.87-
234PhosphorylationKNVQQTVSAKGPPEK
CCHHHHHHCCCCHHH		27.8725159151
236UbiquitinationVQQTVSAKGPPEKRM
HHHHHHCCCCHHHHH		65.5319608861
236AcetylationVQQTVSAKGPPEKRM
HHHHHHCCCCHHHHH		65.5319608861
241AcetylationSAKGPPEKRMRLQ--
HCCCCHHHHHCCC--		58.2119608861
243UbiquitinationKGPPEKRMRLQ----
CCCHHHHHCCC----		8.10-
243AcetylationKGPPEKRMRLQ----
CCCHHHHHCCC----		8.10-
243AcetylationKGPPEKRMRLQ----
CCCHHHHHCCC----		8.1019608861
243UbiquitinationKGPPEKRMRLQ----
CCCHHHHHCCC----		8.1019608861
248AcetylationKRMRLQ---------
HHHCCC---------		-
248AcetylationKRMRLQ---------
HHHCCC---------		19608861
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 MED6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED6_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 MED6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED15_HUMANMED15physical
14983011
CDK8_HUMANCDK8physical
14983011
MED14_HUMANMED14physical
9734358
MED21_HUMANMED21physical
9734358
CUL1_HUMANCUL1physical
22479149
MED7_HUMANMED7physical
22939629
MED23_HUMANMED23physical
10993082
CCNC_HUMANCCNCphysical
10993082
MED10_HUMANMED10physical
10993082
MED10_HUMANMED10physical
26344197
MED11_HUMANMED11physical
26344197
MED12_HUMANMED12physical
26344197
MED14_HUMANMED14physical
26344197
MED15_HUMANMED15physical
26344197
MED16_HUMANMED16physical
26344197
MED17_HUMANMED17physical
26344197
MED18_HUMANMED18physical
26344197
MED19_HUMANMED19physical
26344197
MED24_HUMANMED24physical
26344197
MED27_HUMANMED27physical
26344197
MED4_HUMANMED4physical
26344197
MED8_HUMANMED8physical
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 MED6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-236 AND LYS-241, AND MASSSPECTROMETRY.

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