MED14_DROME - dbPTM
MED14_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED14_DROME
UniProt AC Q9W0P8
Protein Name Mediator of RNA polymerase II transcription subunit 14
Gene Name MED14
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1553
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 pre-initiation complex with RNA polymerase II and the general transcription factors. Required for activated transcription of the MtnA, MtnB and MtnD genes..
Protein Sequence MAPTPLPLEQMPGVGGGGGGYLPAAQEGGPRINTMSMSVLIDFIIQRTYHELTVLAELLPRKTDMERKVEIYNYAARTRHLFTRLNALVKWGNSVSKVDKSSQIMSFLDKQNMLFVETADMLARMSRETLVRARLPNFHIPAAVEVLTTGTYNRLPTCIRERIVPADAITPAEKRQTLLRLNQVIQHRLVTGKLLPQMREFRIRNGRVTFEVKHEFSVSLTVMGDNPTVPWRLLDIDVLVEDKETGDGKSLVHPLQVNYIHQLIQARLVENPNALSEVYNCLHYFCQSLQLEVLYTQTLRLNYERLDDNNITVEEYVPGVKLTVSYWRDLKSELGYRLTVQSDPSEIGRPLAVVHVPSLGAKESAEVADRAVRSEHLSMERLIVHTVYIRSVSRLSDLKLEFQAFLKDVDFNLQGTPAILTVPVLSPCLRAEQIHITIDTHTGMFRCHVPKHLDCPIMEEMQDCLNGDRSKLPALLSELRFWITHRRCDKTLQHLPATATETLPFLVQPDQEILQPGRHKIYVKLHRHPNIVLVVQLKEKTTMPNEMEYTFHLGFVAYQKDELDVIDDSAMQLVSIVAQPHSDIPKCYTKLMRLIEFDTFVATHGPGTEVDAEVSPHKRKSNGDLLAPPAKQQKTIFPAYFIPELAHVVAMCDEKIPFMNLAQTLSKHNIPHSGLQVEANATSLVLKILALPQPGKTTFATQQQQQQGAPAVAGENKPSGTSGLPKIDSHVWDDLMRRVLSISIRSQTNKNSQVRIWVVEFVFYSTPLQSSHPKEQGSRRTVYLTYEQANYDFSKTVEDLLNDWSKIVYLYTLVYDFAEQLLNKRLSLCDMLVVKSYSYMNLLLGYGPKKEVSCNIYWSVQSHGFRLTFVGGMSAVNGHSMMRDQLAQHLNQQHSITQIAQILHETYNPLSSIAKLPVLPFLGIPRPQVPVLSFCVLAQSPCLIRLTYQAVYCLELRFRANRLVSIRDGASSRFERNVVEEFTPIQGLKAFLSKYVDESAVYRGRASHEDDNPLSPMGMEDNFGGPSSVAGVSAGGSSPFLGTGMRGPQSPRDSGLRFPAPHTPPSSSNPHTPASPHPSAGAGGGSGPQGHGNFNLTSPPAPHMPHPSPSGLMPSSPLNPQPSPHMVHSPGPNTLYMQSHQDSPFTAMSPANNNWPGSPSMPRPSPRPGQSPDHKSTGGGAGVAGGTDRGGSRGTLNRPWAGAVPTLLTHEALETLCRPSPYPNKDINVPDMSPLERFLGCVYMRRQLHRNIQSEETLTALNSTEPGVVLFKVDGLQCQVVLNQMHMQTLHLKVSQLPPMPDKHPPPFQLSQDDLLVIEQYFDTRVAAPPYRPNSLHSICRLLNLPAQVLKDFVQIMRLDLKPELGGDQLKWTVQICLRMPPSAVPIVPSGNACVVMGRMKILFFLQITRIPYGAVIGVGKDWKDSPSLVLPIVYDIQTNVTQLAERTGQVISPTMTAASTLLRRFAEFNAQQNQCTLFPAITDLLTNLQLAAEMPQPPPNQSIGPPVGVGVGVGSSPNPMMPMQQLPQQVGPQGPVGPGGYPQMGPNPGGPQ
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 Orthologous
Protein Cluster
615PhosphorylationTEVDAEVSPHKRKSN
CEECEECCCCCCCCC
16.8822817900
1007PhosphorylationAVYRGRASHEDDNPL
HHHCCCCCCCCCCCC
26.5023607784
1015PhosphorylationHEDDNPLSPMGMEDN
CCCCCCCCCCCCCCC
17.6923607784
1027PhosphorylationEDNFGGPSSVAGVSA
CCCCCCCCCCCCCCC
40.4923607784
1028PhosphorylationDNFGGPSSVAGVSAG
CCCCCCCCCCCCCCC
21.0823607784
1038PhosphorylationGVSAGGSSPFLGTGM
CCCCCCCCCCCCCCC
23.9722817900
1171PhosphorylationPSPRPGQSPDHKSTG
CCCCCCCCCCCCCCC
37.9019429919

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MED14_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED14_DROME !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MED14_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED17_DROMEMED17physical
22036573
CPSF6_DROMECG7185physical
22036573
MED11_DROMEMED11physical
22036573
MED7_DROMEMED7physical
22036573
MED30_DROMEMED30physical
22036573
MED27_DROMEMED27physical
22036573
MED4_DROMEMED4physical
22036573
MED10_DROMEMED10physical
22036573
Y1505_DROMECG11505physical
22036573
MED25_DROMEMED25physical
22036573
MED24_DROMEMED24physical
22036573
MED31_DROMEMED31physical
22036573
Y2199_DROMECG2199physical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MED14_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-615 AND SER-1015, ANDMASS SPECTROMETRY.

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