MED12_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MED12_DROME
• UniProt AC: Q9VW47
• Protein Name: Mediator of RNA polymerase II transcription subunit 12
• Gene Name: kto
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 2531
• Subcellular Localization: Nucleus .
• Protein Description: Component of the Mediator complex, a coactivator involved in regulated gene 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. Required for leg and eye development and macrochaete specification or differentiation..
• Protein Sequence: MLSMLQEKRPLKRTRLGPPDIYPQDAKQREDELTPTNVKHGFTTTPPLSDEFGTAHNSNVNASKVSAFFSGVLAKKEELMTLPDTGRKKQQINCKDNFWPVSPRRKCTVDAWFKDLAGNKPLLSLAKRAPSFNKKEEIFITLCENQVNMQRATWFIKLSAAYTLSFTESKNKKRSIYDPAAEWTGNMIKFMKELLPKLQEYYQQNHDKSSSNGTTSGSLTAAGNGPASNGSTGTSSINSVTGSSASTNVIPVPSMASPLPPIHSPANGQQAAPGGGVNAGSVMPTTGSLGGVVGGPGSSVVGGAAGAGAAVPPGSTISGIGSQFEDSRNALKYWKYCHQLSKYMYEESLLDRQEFLNWILDLLDKMRTQASFDEPLKKLVLSFALQYMHDFVQSERLCRKMAYIVSKKLAQLLNTVVEQQTIKELDEPKLQQDPYELALQEQMSCPHHRDIVLYLSTILQIITIECPTALVWSGIAAHRAPSSLLGSPLDHLPLAPSVLPMPTRCPRTNHEIRRQLRAAESDIVLRTQHAEQRWFAAKWLSAGKNQYTSVLATLDHLDTHCFDRMEHNNSIDTLYAQIFPSPTVSRRREEDQVEPRPPYEPKQDKDTVRILCEWAVSGQRWGEHRAMVVAILLDKRQIDVTSTPADQQSSDKDDKDSLASGAGLIDGLPVFQHVLMHFLDHDAPVLDEHVSSPQQRTEFTNLVQLFSALIRHDVFSHNAYMHTLISRGDLLLESVLVIKSGTTATKTSPPPPAPPPTTTHGFDDDGFGGGLDFKHNEFDDSNVDDDLDKLVQNIKEKGQQHEAPDSPKIGPPGDGETNPGGSISRHYVYTKHFPIPQDDPSMSSYSSESNQRYILLFGVGKERDEKKHAVKKMSKEIGKLFTKKFSIDVAAAGHVKKHSRNEFNFEATTSKCQQMAYFDQHVVTAQCAANVLEQLNGFALGNNNYLPVQEHVAFLFDLMELALNIYSLLELCDSLLKELPEVEHQLQLKKSNLVRSYTTSLALYIVSILRRYHSCLLLSPEQTLSVFEGVCRTIRHVSNPSECTSAERCIIAYLSDLHESCVLLQGKEQSTEYYQQLQCIKRFKDIFNTPEQLDLPPQGYNPLLLQELFMAPRRGGKLDPHWLGTLHESPANVYSFVSNALIAVCRETDNERLNDVALACAELTASCNVLSEEWIYALQSLCSGSKSPRYPHLGGQVDIGQLKTHNALAVFVCILVARHCFSLADFVSKFALPTLARSVSAGGAELSVDAEAGARLTCHLVLKLFKTLEIPQPGMYSVSTSPNPLHAVGNDFSIRLSCDRHLLVGAHKTIPIAAVLAVLKAILIVVDNAALKTPLASGSGTSSGGLGGAFGSGKRSGFNTPVHPGSTPKSNEQRPADLSQILGTSDLQLGSSLTSEPEALQQPSVGGMEQISLLEFAQAVLKQICAQEHVLERCLKNAEQLCDMIIDEMLTAKQAQRVLHMICYPEPEFNIISELDQRSMIVRILENLGQWTLRISWLDLQLMYRQSLSNNAELNVWLDTVARAAIDVFHMEEVVLPGAVKATHKPKPSTWLVAPLIAKLTPAVQGRILRVAGQVLESMNYFSKVSKSDCNSSGSGDEREKSNSCHSSNSYGLGGVPARNKKMPLDYQPFLGLILTCLKGQDEYKENLLVSLYAQLSQCLQSFAELDTIGGIDEPQAREEILDALQLRFSLVGGMFEAIQKNSTPTTDWAILLAQLVCQGVVDLSCNRELFTTVVDMLATLVHSTLVSDDERHYMNLMKKLKKEIGEKNNASIRVIRQLLPLYKQPTEVIACEHSGMDTKGNKICDIDKKQLRISDKQRISVWDILEGHKNPAPLSWVWFGAVKLERKPLTYEEAHRNLKYHTHSLVKPSSYYYEPLPLPPEDIEPVPEKICIKDEMKADTPSSVDQSPSAVVGGTGRGRGKGTTTRKRKPKNPKTPPVVNTQQQQPQLAQQPQQPQNVQQQQLQQQQQQQQHMQQQHMQQQQMQPNQMGQMPMNMPMNMQQFAPNPNNMMQQNAMLQQQQQQQMQQMGNNPMQQQLNVGGGNGQPNPQMNFMQQGPGGGGAGPQGMPGQQQQWHNAPQQQQPPQPYHNQYAPHQQNMQSNRIERPPLNANSKQALSQMLRQRQPFQQQAQQGPGGGFNPMQQQPQASQQQPGPQQQMNPNQMRQQQMNPQQNPQSVAAFNAMQQQPQQNAQQQQMNPNQQQQQQFMRGGNMRPGMAPNQMNQMNMGGQGMSQNPMMQQQIPQNMVGMVNPNANQMMQSGGAQGGNGVGVGVGVGVGGAGNNPNMGMGGMPQQGMIQQQPQQQPQQQVQFQNFQNQYQQQQQQGMQQQGGGAGVGVGVGMAPNQQQQQQANMMGNFNPQMQQGNRNNPDFMAAAAVAQQQQQQQQQQRVVPGGMMAGNRNQYMNQAPNVTMSTMMGPGPGGVVGQVPPYARQQSAGGGKPGVLNTQQQFQQQQQQQQQLRHQMMQLQGMGGGAGGGMGAGPQQGGGAVGGGAGGGMVPQQQSMNQQQTPNLVAQLQRQNMMGQQQYQPPPY

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
102	Phosphorylation	KDNFWPVSPRRKCTV CCCCCCCCCCCCCCH	14.49	19429919
745	Phosphorylation	IKSGTTATKTSPPPP EECCCCCCCCCCCCC	32.53	18327897
748	Phosphorylation	GTTATKTSPPPPAPP CCCCCCCCCCCCCCC	36.64	18327897
781	Phosphorylation	KHNEFDDSNVDDDLD CCCCCCCCCCCHHHH	40.37	19429919
806	Phosphorylation	QQHEAPDSPKIGPPG CCCCCCCCCCCCCCC	27.34	19429919
1281	Phosphorylation	GMYSVSTSPNPLHAV CCEEEECCCCCCCCC	18.38	21082442
1356	Phosphorylation	AFGSGKRSGFNTPVH CCCCCCCCCCCCCCC	51.74	19429919
1360	Phosphorylation	GKRSGFNTPVHPGST CCCCCCCCCCCCCCC	25.15	19429919
1366	Phosphorylation	NTPVHPGSTPKSNEQ CCCCCCCCCCCCCCC	46.09	19429919
1367	Phosphorylation	TPVHPGSTPKSNEQR CCCCCCCCCCCCCCC	40.42	19429919
1592	Phosphorylation	VSKSDCNSSGSGDER CCHHHHCCCCCCCHH	42.27	19429919
1593	Phosphorylation	SKSDCNSSGSGDERE CHHHHCCCCCCCHHH	24.00	19429919
1595	Phosphorylation	SDCNSSGSGDEREKS HHHCCCCCCCHHHHC	45.05	19429919
1908	Phosphorylation	TPSSVDQSPSAVVGG CCCCCCCCCCCEECC	19.16	19429919
2439	Acetylation	QQSAGGGKPGVLNTQ CCCCCCCCCCCCHHH	41.70	21791702

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

Oops, there are no upstream regulatory protein records of MED12_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MED12_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 MED12_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MED14_DROME	MED14	physical	22036573
MED13_DROME	skd	physical	22036573
MED13_DROME	skd	genetic	12835386
SUH_DROME	Su(H)	physical	21793099
CI_DROME	ci	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-745; SER-748; SER-806;SER-1356 AND THR-1360, AND MASS SPECTROMETRY.
PubMed: 18327897

"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781, AND MASSSPECTROMETRY.
PubMed: 17372656