MED13_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MED13_DROME
• UniProt AC: Q7KTX8
• Protein Name: Mediator of RNA polymerase II transcription subunit 13
• Gene Name: skd
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 2618
• 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 leg and eye development and macrochaete specification or differentiation. Negatively regulates sex comb development. Required for activated transcription of the MtnB and MtnD genes..
• Protein Sequence: MTHQNHQTNGASLEDCHTNFYALTDLCGIKWRKFVNGERPNASSDPLADPILRSYSRCIQADMLCVWRRVQSTKTDHADPNALTFEMTTSTKVHPPLSLAAAKELWIFWYGEEPDLSELVDAELLRVAANQALWNGTWKGALTYECRSLLFKALHNLMERFVLTKDIVRFGKWFVQPCTSSDRLFGRSSQHLSFSFTFFVHGDTVCASIDLREHPAVRPLTKEHLTEAAAAFAAASSPPGSNGSAASAGGAVPNPGQDPNGASMDGLDGGEGAAKAAPPPHARKVMLAPFGIAGILTGNSYKASDPIAEKILEDWASFFPLCNKDNTDVPPVVEVVSGGHKMYHPTNYVLVTDLDDMEHMEFVEMQKMQSSVAGAAAESAVLASLSCPPGAASAPSSMGAAPSATAVPLGPASLNAPALAGAGVGATASSAAKEISRKAAPQAVSALERLAFQPYYDQRPTSGFTFNTNNTHIPASAAVEMPERTWQDCVMNTLHVDAAAAAAAVASSTPASGTGSLSADGDENEQNKPPQDSKQLVQQQIQQQQQRQKLWNFVDPMQKAPCICTKHLGNTPHGTPHGGASTYSRNSLGGDSSMPVASVESPATPAPSPHPNSAHSQPTSVPPAEQLLNMSPHAPTSVSNLQQPPTPIDHLLDKNTPAPTPTDQHDSKSITASPYVHQTPSVEPPSYTDHAAGGGPAGGQGLGTGPGSVPAQQPATPTAATSAGGAGSGGPSNAIGANAVGTISVKKLEMQQQTPSAAMAIKQEPGAQGRGVGGVTSTTEALNNFKRLYNPPKLTLKDPDSFYDEEWLKEVIYDFQYQEYWDYSTVKRPKMEKQRRPRYAKNLYEGQNHVKPVMPSPGSVYGSQLLSLDESASQAGGRGGGGQAAGSSGGGLVGIANSTASGSDVEADGSSFFQGLNIKTEPGLHSPSCKETSKSSGGNSSGGGSGSGGNLFTAEGLNPSLNDLEQLFETSSNDECSSVQIHTPPDSNNPSNGGCSAVTNTIEDLKRSTAVASAAVAAAAAAAASGAGNIQAEDLTKMFPTPPSHEQQHPNSSPCQTDVVMTDLSVDTTTTIITSSITTTCNTTITSSINTTTTACSNPSNSIMLAAAQAPVTVVAIQTVSKMVKQEYNLELGSPMEEPINDWDYVYRPPQQEKFVGSTRYAPLTNLPSQTQPPLTLPTGCFYQPTWSSHKSRAATLAKAAAAQQQQHQKHQALQQRIQLHQQKLQQLQLQNQQQQQAAAAAAAAASGGVGHQKHQHQHLHDLLSAAPRTPLTPSTVPQPLSSGGSQYLLNQLNCPQAPPGASMQQLMHRAGMSPISPGPGMGPYAARSSPMSRATPTHPPPPYPYDLAVASPATSTSSYLNRPLHSQEHPHMHGLGGGATGVVGHGTGGGGHMGMVAYTGDAGIVSGGTAMAAGSSSLLQELPEVNSVLVNILLYDTALNVFRDHNFDSSSVCVCNADTQKIGNIRGADSGVYVPLPGVSFNPFPSGAGGALAGQRMLNGPSSAGFGGMRMISAFGGSPASASMPGAGSGHGHGPNGGSNSSSCTPPSSNPHITGYVDDDPVECTCGFSAVVNRRLSHRAGLFYEDEVEITGIADDPGRNKQPTLLSIIQSLSRKNQNKQGPGETSSALDKIGAGGLPNGQLEQLGHAVFDLLLDQCSIIQTSSSSVHRALQSHRRRMSRQRRIFGNNGAPTASLASIANVLEFMDAHDVISLALEQSRLAFENQRMDNMMDFHGNGSSSSHQQQQLTAFHAPPPALRHKLAGIGAGRLTVHKWPYLPVGFTRSNKEIVRTMNAIQPMLQNAFHCKSRGGSGSKDASSYNTVSGPLTWRQFHRLAGRASGQCEPQPIPSVVVGYEKDWISVAPHSIHYWDKFLLEPYSYARDVVYVVVCPDNEHVVNCTRSYFRELSSTYEMCKLGKHTPIRGWDGFLQVGAARNNVPADRETTPLDDWLRTLEHAALAEQIRRYAVAFIHQLAPYLSRVPNDKTLLNPPDGSGNSHSKGGSSCSSNSSSVSGLPGGDLPTDNIKLEPGTEPQVQPMETNEIKQEPGVGKGGTAAGETKPTLILGDPLGMGETLEDINPSAIVLYVVNPFTFASDSCELERLALIALLRCYAELLKAVPDSVRSQMNIQIISLESVMELGPCGNRKRFSDEIRCLALNIFSQCRRHLVHAQSVKSLTGFGTAANMEAFLKTKDEPNRRAYKMYTAPFVLAPMHERNDKTDFSRSAGSMHGQNEHRYSVMYCNYCLSEDQAWLLATATDERGEMLEKICINIDVPNRARRRKAPARYVALKKLMDFIMGIISQTSQMWRLVIGRIGRIGHSELKSWSFLLSKQQLQKASKQFKDMCKQCTLMYPPTILSACLVTLEPDAKLRVMPDQFTPDERFSQISMQNPLATPQDVTCTHILVFPTSAVCAPFTRQFQNEPQVDDDFLTFEEEGNEDFSDADIGDLFWDTHMDRVSNHGSPGRMDDNRSWQSAGGNNFKCTPPQEVEEVGSLNQQPISVGYMVSTAPTGRMPAWFWSACPHLEDVCPVFLKTALHLHVPSIQSADDILNSTNAHQSGNDHPLDSNLTADVLRFVLEGYNALSWLALDSNTHDRLSCLPINVQTLMDLYYLTAAIA

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
571	Phosphorylation	CTKHLGNTPHGTPHG EECCCCCCCCCCCCC	18.18	19429919
575	Phosphorylation	LGNTPHGTPHGGAST CCCCCCCCCCCCCCC	14.74	19429919
581	Phosphorylation	GTPHGGASTYSRNSL CCCCCCCCCCCCCCC	31.02	19429919
582	Phosphorylation	TPHGGASTYSRNSLG CCCCCCCCCCCCCCC	25.61	19429919
584	Phosphorylation	HGGASTYSRNSLGGD CCCCCCCCCCCCCCC	25.69	19429919
926	Phosphorylation	KTEPGLHSPSCKETS CCCCCCCCCCCCCCC	24.45	22817900
1314	Phosphorylation	LMHRAGMSPISPGPG HHHHCCCCCCCCCCC	20.40	19429919
1317	Phosphorylation	RAGMSPISPGPGMGP HCCCCCCCCCCCCCC	27.47	19429919
1815	Acetylation	SRGGSGSKDASSYNT CCCCCCCCCCCCCCC	61.92	21791702
2463	Phosphorylation	DRVSNHGSPGRMDDN HHHCCCCCCCCCCCC	19.34	19429919
2472	Phosphorylation	GRMDDNRSWQSAGGN CCCCCCCCCCCCCCC	35.40	22817900
2475	Phosphorylation	DDNRSWQSAGGNNFK CCCCCCCCCCCCCCC	23.71	25749252

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

Oops, there are no upstream regulatory protein records of MED13_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MED13_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 MED13_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MED14_DROME	MED14	physical	22036573
CDK8_DROME	Cdk8	physical	22036573
MED23_DROME	MED23	physical	22036573
MED18_DROME	MED18	physical	22036573
MED15_DROME	MED15	physical	22036573
MED17_DROME	MED17	physical	22036573
EBI_DROME	ebi	physical	22036573
MED4_DROME	MED4	physical	22036573
MED8_DROME	MED8	physical	22036573
MED7_DROME	MED7	physical	22036573
MED16_DROME	MED16	physical	22036573
MED30_DROME	MED30	physical	22036573
CPSF6_DROME	CG7185	physical	22036573
MED11_DROME	MED11	physical	22036573
MED12_DROME	kto	genetic	12835386
SUH_DROME	Su(H)	physical	21793099
CI_DROME	ci	physical	24962581
MED12_DROME	kto	physical	24962581

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 THR-571; THR-575; SER-2472AND SER-2475, AND MASS SPECTROMETRY.
PubMed: 18327897