MED9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MED9_HUMAN
• UniProt AC: Q9NWA0
• Protein Name: Mediator of RNA polymerase II transcription subunit 9
• Gene Name: MED9
• Organism: Homo sapiens (Human).
• Sequence Length: 146
• 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: MASAGVAAGRQAEDVLPPTSDQPLPDTKPLPPPQPPPVPAPQPQQSPAPRPQSPARAREEENYSFLPLVHNIIKCMDKDSPEVHQDLNALKSKFQEMRKLISTMPGIHLSPEQQQQQLQSLREQVRTKNELLQKYKSLCMFEIPKE

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
2	Acetylation	------MASAGVAAG ------CCCCCCCCC	14.21	22814378
3	Phosphorylation	-----MASAGVAAGR -----CCCCCCCCCC	25.02	25159151
19	Phosphorylation	AEDVLPPTSDQPLPD HHHCCCCCCCCCCCC	42.89	18691976
19	O-linked_Glycosylation	AEDVLPPTSDQPLPD HHHCCCCCCCCCCCC	42.89	23301498
20	Phosphorylation	EDVLPPTSDQPLPDT HHCCCCCCCCCCCCC	39.77	30206219
20	O-linked_Glycosylation	EDVLPPTSDQPLPDT HHCCCCCCCCCCCCC	39.77	23301498
27	Phosphorylation	SDQPLPDTKPLPPPQ CCCCCCCCCCCCCCC	32.40	20873877
46	Phosphorylation	PAPQPQQSPAPRPQS CCCCCCCCCCCCCCC	20.13	29255136
53	Phosphorylation	SPAPRPQSPARAREE CCCCCCCCCCHHCHH	24.18	30278072
63	Phosphorylation	RAREEENYSFLPLVH HHCHHHHCCHHHHHH	12.22	22817900
64	Phosphorylation	AREEENYSFLPLVHN HCHHHHCCHHHHHHH	31.71	-
80	Phosphorylation	IKCMDKDSPEVHQDL HHHCCCCCHHHHHHH	28.80	25159151
91	Ubiquitination	HQDLNALKSKFQEMR HHHHHHHHHHHHHHH	49.54	29967540
99	Ubiquitination	SKFQEMRKLISTMPG HHHHHHHHHHHCCCC	49.19	29967540
110	Phosphorylation	TMPGIHLSPEQQQQQ CCCCCCCCHHHHHHH	16.54	20068231
128	Sumoylation	LREQVRTKNELLQKY HHHHHHHHHHHHHHH	37.55	-
128	Sumoylation	LREQVRTKNELLQKY HHHHHHHHHHHHHHH	37.55	-
134	Ubiquitination	TKNELLQKYKSLCMF HHHHHHHHHHHHHCC	55.40	22817900
135	Phosphorylation	KNELLQKYKSLCMFE HHHHHHHHHHHHCCC	7.89	22817900
136	Ubiquitination	NELLQKYKSLCMFEI HHHHHHHHHHHCCCC	43.94	22817900
145	Ubiquitination	LCMFEIPKE------ HHCCCCCCC------	80.06	-

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

Oops, there are no upstream regulatory protein records of MED9_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MED9_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 MED9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MD13L_HUMAN	MED13L	physical	15175163
MED13_HUMAN	MED13	physical	15175163
MED12_HUMAN	MED12	physical	15175163
MED14_HUMAN	MED14	physical	15175163
MED23_HUMAN	MED23	physical	15175163
MED15_HUMAN	MED15	physical	15175163
MED24_HUMAN	MED24	physical	15175163
MED16_HUMAN	MED16	physical	15175163
MED25_HUMAN	MED25	physical	15175163
MED17_HUMAN	MED17	physical	15175163
MED26_HUMAN	MED26	physical	15175163
CDK8_HUMAN	CDK8	physical	15175163
CDK19_HUMAN	CDK19	physical	15175163
MED27_HUMAN	MED27	physical	15175163
MED4_HUMAN	MED4	physical	15175163
MED19_HUMAN	MED19	physical	15175163
MED6_HUMAN	MED6	physical	15175163
MED7_HUMAN	MED7	physical	15175163
MED8_HUMAN	MED8	physical	15175163
MED18_HUMAN	MED18	physical	15175163
MED20_HUMAN	MED20	physical	15175163
MED29_HUMAN	MED29	physical	15175163
MED30_HUMAN	MED30	physical	15175163
MED28_HUMAN	MED28	physical	15175163
MED21_HUMAN	MED21	physical	15175163
MED22_HUMAN	MED22	physical	15175163
MED11_HUMAN	MED11	physical	15175163
MED31_HUMAN	MED31	physical	15175163
MED10_HUMAN	MED10	physical	15175163
MED1_HUMAN	MED1	physical	15175163
RPB1_HUMAN	POLR2A	physical	15175163
RPB2_HUMAN	POLR2B	physical	15175163
RPB3_HUMAN	POLR2C	physical	15175163
RPB4_HUMAN	POLR2D	physical	15175163
RPAB1_HUMAN	POLR2E	physical	15175163
RPAB2_HUMAN	POLR2F	physical	15175163
RPB7_HUMAN	POLR2G	physical	15175163
RPB11_HUMAN	POLR2J	physical	15175163
A4_HUMAN	APP	physical	21832049
MED29_HUMAN	MED29	physical	14638676
MED17_HUMAN	MED17	physical	14638676
MED1_HUMAN	MED1	physical	14638676
MED19_HUMAN	MED19	physical	14638676
MED4_HUMAN	MED4	physical	14638676
MED8_HUMAN	MED8	physical	14638676
MED18_HUMAN	MED18	physical	14638676
MED22_HUMAN	MED22	physical	14638676
MED11_HUMAN	MED11	physical	14638676
NEUG_HUMAN	NRGN	physical	28514442
JIP4_HUMAN	SPAG9	physical	28514442
CARM1_HUMAN	CARM1	physical	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.

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 THR-19, AND MASSSPECTROMETRY.
PubMed: 19369195