RING1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RING1_DROME
• UniProt AC: Q9VB08
• Protein Name: E3 ubiquitin-protein ligase RING1
• Gene Name: Sce
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 435
• Subcellular Localization: Nucleus. Chromosome. Colocalizes with ubiquitinated histone H2A. Colocalizes with Pc, Pcl, Psc, ph at many sites on polytene chromosomes. Colocalizes with ORD on the chromatin of primary spermatocytes during G2 of meiosis.
• Protein Description: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-118' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-118' ubiquitination gives a specific tag for epigenetic transcriptional repression. Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. PcG complexes act via modification of histones, such as methylation, deacetylation, ubiquitination rendering chromatin heritably changed in its expressibility. May play a role in meiotic sister chromatid cohesion..
• Protein Sequence: MTSLDPAPNKTWELSLYELQRKPQEVITDSTEIAVSPRSLHSELMCPICLDMLKKTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRADPNFDLLISKIYPSREEYEAIQEKVMAKFNQTQSQQALVNSINEGIKLQSQNRPQRFRTKGGGGGGGGGGNGNGAANVAAPPAPGAPTAVGRNASNQMHVHDTASNDSNSNTNSIDRENRDPGHSGTSAASAITSASNAAPSSSANSGASTSATRMQVDDASNPPSVRSTPSPVPSNSSSSKPKRAMSVLTSERSEESESDSQMDCRTEGDSNIDTEGEGNGELGINDEIELVFKPHPTEMSADNQLIRALKENCVRYIKTTANATVDHLSKYLAMRLTLDLGADLPEACRVLNFCIYVAPQPQQLVILNGNQTLHQVNDKFWKVNKPMEMYYSWKKT

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
36	Phosphorylation	DSTEIAVSPRSLHSE CCCCEECCCCHHCHH	12.94	22817900
129	Phosphorylation	VMAKFNQTQSQQALV HHHHHCCHHHHHHHH	31.15	21082442
131	Phosphorylation	AKFNQTQSQQALVNS HHHCCHHHHHHHHHH	27.87	21082442
202	Phosphorylation	MHVHDTASNDSNSNT CEEECCCCCCCCCCC	43.17	22817900
263	Phosphorylation	DDASNPPSVRSTPSP CCCCCCCCCCCCCCC	31.27	22817900
266	Phosphorylation	SNPPSVRSTPSPVPS CCCCCCCCCCCCCCC	42.38	22817900
267	Phosphorylation	NPPSVRSTPSPVPSN CCCCCCCCCCCCCCC	19.74	22817900
269	Phosphorylation	PSVRSTPSPVPSNSS CCCCCCCCCCCCCCC	38.32	22817900
285	Phosphorylation	SKPKRAMSVLTSERS CCCCCHHHHHHCCCC	17.00	19429919
288	Phosphorylation	KRAMSVLTSERSEES CCHHHHHHCCCCCCC	26.79	19429919
289	Phosphorylation	RAMSVLTSERSEESE CHHHHHHCCCCCCCC	27.18	19429919

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

Oops, there are no upstream regulatory protein records of RING1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RING1_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 RING1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPC2_DROME	RpIII128	physical	14605208
ORD_DROME	ord	physical	14669021
DOME_DROME	dome	genetic	19749759
PSC_DROME	Psc	genetic	1806331
DOT1L_DROME	gpp	genetic	15371351
PHP_DROME	ph-p	physical	18923078
PHP_DROME	ph-p	physical	25415640
TPR_DROME	Mtor	physical	18923078
PSC_DROME	Psc	physical	18923078
PSC_DROME	Psc	physical	25415640
ELF1_DROME	grh	physical	25242320
ELF1_DROME	grh	physical	11865070
PC_DROME	Pc	physical	18923078
PC_DROME	Pc	physical	25415640
JHD1_DROME	Kdm2	physical	18923078
JHD1_DROME	Kdm2	physical	25415640

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-202; SER-266; THR-267AND SER-269, AND MASS SPECTROMETRY.
PubMed: 18327897