ELP1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELP1_DROME
• UniProt AC: Q9VGK7
• Protein Name: Putative elongator complex protein 1
• Gene Name: Elp1
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1252
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: May act as a scaffold protein that may assemble active IKK complexes.; Acts as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation..
• Protein Sequence: MRNLKLRYCKELNAVAHPQHLLLQPELNGGASDIYFVVADNKIYAVQESGDVRLKVIADLPDIVGVEFLQLDNAICVASGAGEVILVDPQTGATSEGTFCDVGIESMAWSPNQEVVAFVTRTHNVVLMTSTFDVIAEQPLDAELDPDQQFVNVGWGKKETQFHGSEGKQAAKQKESDSTFIRDEQELNQDVSISWRGDGEFFVVSYVAAQLGRTFKVYDSEGKLNHTAEKSANLKDSVVWRPTGNWIAVPQQFPNKSTIALFEKNGLRHRELVLPFDLQEEPVVQLRWSEDSDILAIRTCAKEEQRVYLYTIGNYHWYLKQVLIFEQADPLALLHWDTRCGAEHTLHVLKESGKHLVYRWAFAVDRNNSIVGVIDGKRLLLTDFDEAIVPPPMSKIVLKFETYINAFISHGTSLWVYTCDRKIYLNEHIHTLGKELQKPIMLMPDAELSGLHLANLTHFSPHYLLATHSSAGSTRLLLLSYKDNDNKPGEWFYRVHSSVRINGLVNAVAVAPYAMNEFYVQTVNNGHTYEVSLKADKTLKVERSYVQLHEPADQIDWVIVKGCIWDGYTGALVTLRNQHLLHIDGYRIGEDVTSFCVVTNYLVYTQLNAMHFVQLDDRRQVASRNIERGAKIVTAVARKARVVLQLPRGNLEAICPRVLVLELVGDLLERGKYQKAIEMSRKQRINLNIIFDHDVKRFVSSVGAFLNDINEPQWLCLFLSELQNEDFTKGMYSSNYDASKQTYPSDYRVDQKVEYVCRLLEQQMNRFVSRFRLPLITAYVKLGCLEMALQVIWKEQQEDASLADQLLQHLLYLVDVNDLYNVALGTYDFGLVLFVAQKSQKDPKEFLPYLNDLKALPIDYRKFRIDDHLKRYTSALSHLAACGEQHYEEALEYIRKHGLYTDGLAFYREHIEFQKNIYVAYADHLRAIAKLDNASLMYERGGQLQQALLSAKHTLDWQRVLVLAKKLSEPLDQVAQSLVGPLQQQGRHMEAYELVKEHCQDRKRQFDVLLEGHLYSRAIYEAGLEDDDVSEKIAPALLAYGVQLESSLQADLQLFLDYKQRLLDIRRNQAKSGEGYIDTDVNLKEVDLLSDTTSLHSSQYSGTSRRTGKTFRSSKNRRKHERKLFSLKPGNPFEDIALIDALHNHVTKIAQQQQPVRDTCKALLQLANAADADPLAAALQREFKTLLQAVDAALDEIWTPELRGNGLMADHLTGPNVDYLALQKEQRYALLSPLKRFKPQLIMMDWQHEILQ

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
227	Phosphorylation	SEGKLNHTAEKSANL CCCCCCCCCCCCCCC	35.12	22817900
257	Phosphorylation	PQQFPNKSTIALFEK CCCCCCCCEEEEEEC	31.52	27626673
258	Phosphorylation	QQFPNKSTIALFEKN CCCCCCCEEEEEECC	16.33	27626673
369	Phosphorylation	FAVDRNNSIVGVIDG EEECCCCCEEEEECC	23.38	19429919
1094	Phosphorylation	DLLSDTTSLHSSQYS ECCCCCCCCCCCCCC	26.61	22817900
1232	Phosphorylation	EQRYALLSPLKRFKP HHHHHHHCHHHHHCC	29.09	22817900

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

Oops, there are no upstream regulatory protein records of ELP1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ELP1_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 ELP1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AGO2_DROME	AGO2	physical	19805217
DCR1_DROME	Dcr-1	physical	19805217

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-1094, AND MASSSPECTROMETRY.
PubMed: 18327897