MED8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MED8_HUMAN
• UniProt AC: Q96G25
• Protein Name: Mediator of RNA polymerase II transcription subunit 8
• Gene Name: MED8
• Organism: Homo sapiens (Human).
• Sequence Length: 268
• 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. May play a role as a target recruitment subunit in E3 ubiquitin-protein ligase complexes and thus in ubiquitination and subsequent proteasomal degradation of target proteins..
• Protein Sequence: MQREEKQLEASLDALLSQVADLKNSLGSFICKLENEYGRLTWPSVLDSFALLSGQLNTLNKVLKHEKTPLFRNQVIIPLVLSPDRDEDLMRQTEGRVPVFSHEVVPDHLRTKPDPEVEEQEKQLTTDAARIGADAAQKQIQSLNKMCSNLLEKISKEERESESGGLRPNKQTFNPTDTNALVAAVAFGKGLSNWRPSGSSGPGQAGQPGAGTILAGTSGLQQVQMAGAPSQQQPMLSGVQMAQAGQPGKMPSGIKTNIKSASMHPYQR

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
6	Ubiquitination	--MQREEKQLEASLD --CCHHHHHHHHHHH	56.27	29967540
33	Ubiquitination	LGSFICKLENEYGRL HHHHHHHHHCCCCCC	8.08	29967540
56	Ubiquitination	FALLSGQLNTLNKVL HHHHHCHHHHHHHHH	6.36	29967540
67	Ubiquitination	NKVLKHEKTPLFRNQ HHHHHCCCCCCCCCC	55.98	29967540
82	Phosphorylation	VIIPLVLSPDRDEDL EEEEEEECCCCCHHH	19.78	30266825
82 (in isoform 2)	Phosphorylation	-	19.78	27251275
111	Phosphorylation	VVPDHLRTKPDPEVE CCCCHHCCCCCHHHH	53.97	22985185
112	Sumoylation	VPDHLRTKPDPEVEE CCCHHCCCCCHHHHH	40.78	-
112	Sumoylation	VPDHLRTKPDPEVEE CCCHHCCCCCHHHHH	40.78	-
122	Ubiquitination	PEVEEQEKQLTTDAA HHHHHHHHHHHHHHH	50.75	29967540
138	Acetylation	IGADAAQKQIQSLNK HCHHHHHHHHHHHHH	44.64	25953088
145	Ubiquitination	KQIQSLNKMCSNLLE HHHHHHHHHHHHHHH	46.72	29967540
170	Ubiquitination	SGGLRPNKQTFNPTD CCCCCCCCCCCCCCC	54.09	29967540
252	Phosphorylation	GQPGKMPSGIKTNIK CCCCCCCCCCCCCCC	50.04	23532336
255	Acetylation	GKMPSGIKTNIKSAS CCCCCCCCCCCCCCC	38.76	25953088
256	Phosphorylation	KMPSGIKTNIKSASM CCCCCCCCCCCCCCC	40.01	22985185
259	Ubiquitination	SGIKTNIKSASMHPY CCCCCCCCCCCCCCC	41.88	29967540
259	Acetylation	SGIKTNIKSASMHPY CCCCCCCCCCCCCCC	41.88	25953088
259	Methylation	SGIKTNIKSASMHPY CCCCCCCCCCCCCCC	41.88	3755571
260	Phosphorylation	GIKTNIKSASMHPYQ CCCCCCCCCCCCCCC	23.06	29083192
262	Phosphorylation	KTNIKSASMHPYQR- CCCCCCCCCCCCCC-	25.39	29083192
266	Phosphorylation	KSASMHPYQR----- CCCCCCCCCC-----	11.40	29083192

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MED8_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MED8_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MED8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THOC7_HUMAN	THOC7	physical	12584197
ELOB_HUMAN	TCEB2	physical	12149480
ELOC_HUMAN	TCEB1	physical	12149480
RBX1_HUMAN	RBX1	physical	12149480
A4_HUMAN	APP	physical	21832049
K1C40_HUMAN	KRT40	physical	25416956
MED1_HUMAN	MED1	physical	26344197
MED10_HUMAN	MED10	physical	26344197
MED11_HUMAN	MED11	physical	26344197
MED12_HUMAN	MED12	physical	26344197
MED14_HUMAN	MED14	physical	26344197
MED16_HUMAN	MED16	physical	26344197
MED17_HUMAN	MED17	physical	26344197
MED19_HUMAN	MED19	physical	26344197
MED24_HUMAN	MED24	physical	26344197
MED27_HUMAN	MED27	physical	26344197
MED4_HUMAN	MED4	physical	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-82, AND MASSSPECTROMETRY.
PubMed: 19369195