ELP4_DROME - dbPTM
ELP4_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELP4_DROME
UniProt AC Q9VMQ7
Protein Name Putative elongator complex protein 4
Gene Name CG6907
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 437
Subcellular Localization Nucleus.
Protein Description 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 MTSFRKRTVQKPIRGTRTSPHTAQVITSSGNPYLDVVIGGGLPMGSICLIEEDRFMTHAKVLAKYFLAEGVISKQEIFLGSLDDIPAEMLRRLPRPLTDQESMEQSEVQALGDAGAENGLRIAWRYNDLPLVNSEHATAKIGHHFNLMEQMDSMMLYNVKTTLWDDSPKHLDIVIDEEFSKSSSPTTPSLEQQPVEDAPPIPGTETAPQEKMPAQEEENSANNNNNNNNNSSSVTSSTKTGSQDSPLQVFHNPRYKGLLNDIQQLLRNESFVAGTKNNLCRVCLTSLGSPLWYDEHFGEDLIKFLTLLMASVRNCNSVCLITMPMHLIAKYDASLVPKIRQLVDYAIELESFAGSERETHPAFKEYSGLLHLHKMSAINTLAVHMPETPDLAFKLRRKKFIIEKFHLPPELQESSAKPDNCISGLLSNSNATASLDF
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
182PhosphorylationIDEEFSKSSSPTTPS
ECHHHHCCCCCCCCC
34.5519429919
183PhosphorylationDEEFSKSSSPTTPSL
CHHHHCCCCCCCCCH
44.0419429919
184PhosphorylationEEFSKSSSPTTPSLE
HHHHCCCCCCCCCHH
33.1019429919
186PhosphorylationFSKSSSPTTPSLEQQ
HHCCCCCCCCCHHCC
53.9722668510
187PhosphorylationSKSSSPTTPSLEQQP
HCCCCCCCCCHHCCC
17.7919429919
189PhosphorylationSSSPTTPSLEQQPVE
CCCCCCCCHHCCCCC
42.3119429919
232PhosphorylationNNNNNNSSSVTSSTK
CCCCCCCCCCCCCCC
30.8330478224
240PhosphorylationSVTSSTKTGSQDSPL
CCCCCCCCCCCCCCE
42.0021082442
242PhosphorylationTSSTKTGSQDSPLQV
CCCCCCCCCCCCEEE
35.7322817900
245PhosphorylationTKTGSQDSPLQVFHN
CCCCCCCCCEEECCC
21.6322817900
399AcetylationAFKLRRKKFIIEKFH
HHHHHHCCEEEECCC
39.7321791702

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 ELP4_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELP4_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 ELP4_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ELP4_DROME !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELP4_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-183 AND SER-242, ANDMASS SPECTROMETRY.

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