MED1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MED1_DROME
• UniProt AC: Q9VP05
• Protein Name: Mediator of RNA polymerase II transcription subunit 1
• Gene Name: MED1
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1475
• 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 (By similarity). Required for activated transcription of the MtnA, MtnB and MtnD genes..
• Protein Sequence: MSGSNAKSSGTGFGSHIPSIEEKNKQIQQETMMEKLRAKYRNKPKSYEEIKKSVRMYFIEKHYPLDPLCKATLQSALDKLQHYIKVTSRHGLVERLESLSRQLGLKFMEDQQLLFISTDMFYVEILLDAAGSLSDVKVHHECKIEQQSSELVACLKSGDFADFTVQLEGLSSIYQLNAEPKVKKKAFVALQAMETDIQSLYQLHLQGHSGDSYSLMTSSSVGLVLPRRGGHPMRLTYFCPPLHLPEGDPKLASGDFTIDQVMRSSYGLSATINLEGSSANKLQTLPTVTLVRDAQTGLEVPTYAQLNQNNSLLMPATFVLRLNKPMPVCLESLKALGLPGLDSVATPPGPPTTVLNLIVQTASKQAIKNTQRGLYVNLPKETHCYFFTDNRKLQGTLVSSLPFTEPAQVPRIVAFLKKQALFYTLLASCVREQQKQYNDMDSTVILEVTAVSFNQITVELQHPYEESLATVDFLLEDGQPTCSVYCLTNEYELLSQKLTRTARKVVSIPMVIYKLLKCWDEEHEFKLHGAIGPGSGSGAIGGGGMSGGGPVSGVGNNFSQFSMDTPTPSDGSLPGGGFANINNLKMDAKSRSLADAFAASTSAAAAIAGLINLKRETDPQSGSSASGTTVSGSSSSSGSAKTSDHDIADKYKNIWKDKTPNLKHCVSITPIPGDGKSGSAGGVSGVEVQRTGGIEIIPLNAQAAIAGGGVTASSSATPTTITITPITGKDPSKDSTKKSTAASAGVGVAAKRPHESSTSSSSTSGCSGSGSSMSSSASSGSSDTQKEKKRKKKRDDSPMGPPEKIYSRQNSPAGGADASATGGVVRKFSSPSSSPKAGGGGQGLMAGVPTARPSPKHSPVYSSPKHNTASNSPKSPFGTHSPKHGSSGKPSMSTLKSAATAATILSPKGDKSSSAVGNTSSGPSASSGSSGATGLVRSFASVGAPPPPPPIPPLASSSGSISSSQSLKKEKTSSASGSSSTSSSATAGVASGGGISPASVAAAVAALKSSQQQMKSVASLSHLAAGGGLGSYAAPSGAGASGAAAVVVGAGAGAGAGASGLELSALRKGMAGGAVSLMTSTAALAPTIPAPTTTVAAGSAASLVSPVSAVVGQGQETAGAAAAATLATATILQQQPQPGAAPTSSCLTTSGGSSDSAGSINPAGASTEYMVKPSSQEGLKLTINKTGSSKSSGTGSGSSSSSGLQAKAKSSSSGATSFAGSTGSTKKQHTGLKPGVNSGPASKKATAAVSSATASSSKHFFQKANSSGNLSSKLSGSGSGGGIPLTKSNSTNSFQEHNAPRRRPSMGALASGSSGGGSGQRKLGSASGGGSGSSGSVSPALSGSMSQPPPRFDHHTDMMTILQYASPTMAASMEGFIKGLHNKFQIPKLSQRGSGGNTTSGRSTPSGSSEPALAGTSSSILGPIASSTGLTEPEAKPPVPPSQSGNEGLLNLSSTAGTPSADGIDEELLASLAGE

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
650	Acetylation	SDHDIADKYKNIWKD CCCCHHHHHHHHHCC	49.45	21791702
667	Phosphorylation	PNLKHCVSITPIPGD CCCCCEEEEEECCCC	26.58	21082442
797	Phosphorylation	RKKKRDDSPMGPPEK HHHCCCCCCCCCHHH	22.52	19429919
811	Phosphorylation	KIYSRQNSPAGGADA HHHCCCCCCCCCCCC	14.05	27794539
830	Phosphorylation	GVVRKFSSPSSSPKA CCEEECCCCCCCCCC	31.75	25749252
832	Phosphorylation	VRKFSSPSSSPKAGG EEECCCCCCCCCCCC	45.45	30478224
834	Phosphorylation	KFSSPSSSPKAGGGG ECCCCCCCCCCCCCC	34.45	22817900
850	Phosphorylation	GLMAGVPTARPSPKH CCCCCCCCCCCCCCC	32.65	19429919
854	Phosphorylation	GVPTARPSPKHSPVY CCCCCCCCCCCCCCC	40.81	19429919
858	Phosphorylation	ARPSPKHSPVYSSPK CCCCCCCCCCCCCCC	23.37	19429919
861	Phosphorylation	SPKHSPVYSSPKHNT CCCCCCCCCCCCCCC	13.55	19429919
862	Phosphorylation	PKHSPVYSSPKHNTA CCCCCCCCCCCCCCC	40.16	19429919
863	Phosphorylation	KHSPVYSSPKHNTAS CCCCCCCCCCCCCCC	21.93	19429919
868	Phosphorylation	YSSPKHNTASNSPKS CCCCCCCCCCCCCCC	31.05	19429919
870	Phosphorylation	SPKHNTASNSPKSPF CCCCCCCCCCCCCCC	35.48	19429919
872	Phosphorylation	KHNTASNSPKSPFGT CCCCCCCCCCCCCCC	31.07	19429919
875	Phosphorylation	TASNSPKSPFGTHSP CCCCCCCCCCCCCCC	28.92	19429919
879	Phosphorylation	SPKSPFGTHSPKHGS CCCCCCCCCCCCCCC	21.40	19429919
881	Phosphorylation	KSPFGTHSPKHGSSG CCCCCCCCCCCCCCC	35.17	19429919
889	Acetylation	PKHGSSGKPSMSTLK CCCCCCCCCCHHHHH	35.55	21791702
903	Phosphorylation	KSAATAATILSPKGD HHHHHHHHHHCCCCC	21.71	29892262
906	Phosphorylation	ATAATILSPKGDKSS HHHHHHHCCCCCCCC	22.25	22817900
1233	Acetylation	KKQHTGLKPGVNSGP CCCCCCCCCCCCCCC	40.86	21791702
1266	Phosphorylation	HFFQKANSSGNLSSK HHHHHCCCCCCCCHH	44.47	29892262
1267	Phosphorylation	FFQKANSSGNLSSKL HHHHCCCCCCCCHHC	31.35	29892262
1290	Phosphorylation	IPLTKSNSTNSFQEH CCCCCCCCCCCCHHC	35.74	29892262
1291	Phosphorylation	PLTKSNSTNSFQEHN CCCCCCCCCCCHHCC	38.85	29892262
1305	Phosphorylation	NAPRRRPSMGALASG CCCCCCCCCCCCCCC	28.21	22817900

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

Oops, there are no upstream regulatory protein records of MED1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MED1_DROME !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MED1_DROME !!

Protein-Protein Interaction

Oops, there are no PPI records of MED1_DROME !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830; SER-834; SER-854AND SER-858, AND MASS SPECTROMETRY.
PubMed: 18327897