TOPRS_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TOPRS_DROME
• UniProt AC: Q9V8P9
• Protein Name: E3 ubiquitin-protein ligase Topors
• Gene Name: Topors
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1038
• Subcellular Localization: Nucleus . Chromosome . Colocalizes with the gypsy chromatin insulator complex on polytene chromosomes and to nuclear insulator bodies. Also localizes to the nuclear lamina.
• Protein Description: Functions as a ubiquitin-protein E3 ligase. Negatively regulates the transcriptional repressor h/hairy by promoting its ubiquitination and subsequent degradation. Also directs the nuclear organization of the gypsy chromatin insulator. Chromatin insulators are regulatory elements which establish independent domains of transcriptional activity within eukaryotic genomes. Insulators have two defining properties; they can block the communication between an enhancer and a promoter when placed between them, and can also buffer transgenes from position effect variegation (PEV). Insulators are proposed to structure the chromatin fiber into independent domains of differing transcriptional potential by promoting the formation of distinct chromatin loops. This chromatin looping may require the formation of insulator bodies, where homotypic interactions between individual subunits of the insulator complex could promote the clustering of widely spaced insulators at the nuclear periphery. Within the gypsy insulator complex, this protein may promote formation of nuclear insulator bodies by recruiting individual insulator complexes to the nuclear lamina..
• Protein Sequence: MAEENPGALAANVPYLGVDELGASVIVEPGLEGSNAGGRTLPAAAIKFADLTESGSESGDNEAEEPVSAGPDNANAIGEPGTSASAAEENGTVERNSPPPNCAICLSRCRRKCFTDSCMHQFCFKCLCEWSKIKPECPLCKQPFRTIIHNVRTLDDYDRYPVQTTSPVPTENPSLRYHIVRRPRYTPLVQNQAVIVNDIEAAIAAGAAGEDVLSAAEVAAGRRSYSRFEPYRSELMNYYQHDQDASTSGSLSQLWRRYVYDRKLYALPVSDSVTGHFREWSARFYRNNPAQIHRLMPWIHRDIMCLLRNAAHSVNTVMTLMSDLLPMTSLLGPTFRRRLSPYLGERTSHFIHELFNFARSPYDINGYDHVVQYSARVAEEVEVDLLDMVETQSSNGDDLNLEVGDSDADAINAGFSPDWSPPRVRPSTSVIVTNPGATHSFSVTMASDGSELPGISIRRTTNVGSQTVAINLSMRRPAAVASEEPEVIEIDDGDAAANAEVAAINDGSNTSRRHAGATLPVTAHIELESSSSSGDEDECVFVLELKPPHMRTPEQVSLDSNSDSDVVFVNEQHEAAPDAIAENRSTQSPLDLASRDQGLFMGPSTSGAAANRGKNWKLVMAQTRRLDQLRTLRSIRSKKSRRSSMPARSDSGSSPSSCSSSSFHFSSSSDEDSSDSSTTNSEPPKKKSRKRVANNKRSKKESIGKRTSRKRKAKDQNMEMLEQQQISQKKPQRQPESSSDSPSSSDDESGGDSSESSGQPNTNNNKSSSDSDDDSAVNMQLSALRATLKAEATLEDRKPVKLELQLPDDDQAGPLHSRMTPSPREDNEPGCSAPKRRRSCSHSNQSSQSASLASSSTATSSSAPLSSFAWGAAGFSGDPLMRGHPAMEEHDIANSLIELSTLTQPVNIGLFNEHYNSAENSMGMLSNTLCDSPQTLAADDANLENYFDTDADPEASRERDAYSLEAAIDVVGESELQIAEDTATATEEQDEEDEEDEDQEEDDQEEEKAAEEEEEEEEDDDDSDNHDENDENQGLLPY

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
585	Phosphorylation	DAIAENRSTQSPLDL CHHHHCCCCCCCCHH	42.24	29892262
588	Phosphorylation	AENRSTQSPLDLASR HHCCCCCCCCHHHCC	27.76	22817900
820	Phosphorylation	GPLHSRMTPSPREDN CCCCCCCCCCCCCCC	21.36	22817900
822	Phosphorylation	LHSRMTPSPREDNEP CCCCCCCCCCCCCCC	27.67	14871887
839	Phosphorylation	SAPKRRRSCSHSNQS CCCCCHHCCCCCCCC	20.40	22817900
841	Phosphorylation	PKRRRSCSHSNQSSQ CCCHHCCCCCCCCCC	31.06	22817900
843	Phosphorylation	RRRSCSHSNQSSQSA CHHCCCCCCCCCCCH	21.92	22817900

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TOPRS_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 TOPRS_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LAM0_DROME	Lam	physical	16209949
HAIR_DROME	h	physical	14871887
SUHW_DROME	su(Hw)	physical	16209949
CP190_DROME	Cp190	physical	16209949
MMD4_DROME	mod(mdg4)	physical	16209949

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-820 AND SER-822, ANDMASS SPECTROMETRY.
PubMed: 18327897