ORC2_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ORC2_DROME
• UniProt AC: Q24168
• Protein Name: Origin recognition complex subunit 2
• Gene Name: Orc2
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 618
• Subcellular Localization: Nucleus . Chromosome . Chromosome, centromere . Centromeres of metaphase and anaphase chromosomes of early syncytial embryos. Later in development, found in pericentric regions of late anaphase and telophase chromosomes.
• Protein Description: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication..
• Protein Sequence: MSASNKGGYKTPRKENLMSIENLTNSEEESEDLNTAMVGNAVESQPKVTSRRSTRRPSPTKKYQAYQKESNGKGQEERIVVNYVEMSDERSSDAEDQEEEESIEESENAARPAAKDLHLIQSEYNVAGTSMFGFNTPKKRDAMALAALNATPCTPKTPKTPRLGVKTPDTKRKKSMDQPKTPAHVRTRVKKQIAKIVADSDEDFSGDESDFRPSDEESSSSSSSSDAGNSSDNDAADDEPKTPSRARRAIVVPVLPKTPSAARLRQSARAKKSNEFVPESDGYFHSHASSKILTSDHTLDRLKNPRLAADRVFSLLSEIKTSAEHEGSINAIMEEYRSYFPKWMCILNEGFNILLYGLGSKHQLLQSFHREVLHKQTVLVVNGFFPSLTIKDMLDSITSDILDAGISPANPHEAVDMIEEEFALIPETHLFLIVHNLDGAMLRNVKAQAILSRLARIPNIHLLASIDHINTPLLWDQGKLCSFNFSWWDCTTMLPYTNETAFENSLLVQNSGELALSSMRSVFSSLTTNSRGIYMLIVKYQLKNKGNATYQGMPFRDLYSSCREAFLVSSDLALRAQLTEFLDHKLVKSKRSVDGSEQLTIPIDGALLQQFLEEQEKK

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
24	Phosphorylation	LMSIENLTNSEEESE CCCHHHCCCCHHHHH	48.56	22817900
26	Phosphorylation	SIENLTNSEEESEDL CHHHCCCCHHHHHHH	40.94	22817900
30	Phosphorylation	LTNSEEESEDLNTAM CCCCHHHHHHHHHHH	39.42	22817900
58	Phosphorylation	RRSTRRPSPTKKYQA CCCCCCCCCCHHHHE	43.31	22817900
87	Phosphorylation	VVNYVEMSDERSSDA EEEEEECCCCCCCCC	23.86	22817900
91	Phosphorylation	VEMSDERSSDAEDQE EECCCCCCCCCCCHH	30.44	22817900
92	Phosphorylation	EMSDERSSDAEDQEE ECCCCCCCCCCCHHH	47.24	22817900
151	Phosphorylation	ALAALNATPCTPKTP HHHHHCCCCCCCCCC	20.16	25749252
154	Phosphorylation	ALNATPCTPKTPKTP HHCCCCCCCCCCCCC	29.08	25749252
157	Phosphorylation	ATPCTPKTPKTPRLG CCCCCCCCCCCCCCC	31.08	22817900
160	Phosphorylation	CTPKTPKTPRLGVKT CCCCCCCCCCCCCCC	18.16	22817900
167	Phosphorylation	TPRLGVKTPDTKRKK CCCCCCCCCCCCCCC	24.80	25749252
170	Phosphorylation	LGVKTPDTKRKKSMD CCCCCCCCCCCCCCC	33.67	22817900
175	Phosphorylation	PDTKRKKSMDQPKTP CCCCCCCCCCCCCCH	30.54	25749252
181	Phosphorylation	KSMDQPKTPAHVRTR CCCCCCCCHHHHHHH	32.18	25749252
258	Phosphorylation	VVPVLPKTPSAARLR EEEECCCCCCHHHHH	22.12	22817900
260	Phosphorylation	PVLPKTPSAARLRQS EECCCCCCHHHHHHH	39.53	22817900
273	Phosphorylation	QSARAKKSNEFVPES HHHHHHHHCCCCCCC	40.67	19429919
314	Phosphorylation	LAADRVFSLLSEIKT HHHHHHHHHHHHHHC	26.08	21082442

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

Oops, there are no upstream regulatory protein records of ORC2_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ORC2_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 ORC2_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBF_DROME	Rbf	physical	11231579
RBF_DROME	Rbf	physical	18665226
HP1_DROME	Su(var)205	physical	9363940
ORC5_DROME	Orc5	physical	24137536
ORC5_DROME	Orc5	physical	26139588
ORC5_DROME	Orc5	physical	27016737
ORC5_DROME	Orc5	physical	9363940
MCM10_DROME	Mcm10	physical	20498296
ORC1_DROME	Orc1	physical	12490953
ORC6_DROME	Orc6	physical	12490953
ORC6_DROME	Orc6	physical	24137536
ORC6_DROME	Orc6	physical	26139588
ORC6_DROME	Orc6	physical	27016737
ORC6_DROME	Orc6	physical	9363940
E2F1_DROME	E2f	physical	11231579
XMAS2_DROME	xmas-2	physical	27016737
ENY2_DROME	e(y)2	physical	27016737

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-24; SER-26; SER-30;SER-87; SER-91; SER-92; THR-151; THR-154; THR-157; THR-160; THR-167;THR-170; THR-181; THR-258 AND SER-260, AND MASS SPECTROMETRY.
PubMed: 18327897