ORC1_DROME - dbPTM
ORC1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ORC1_DROME
UniProt AC O16810
Protein Name Origin recognition complex subunit 1
Gene Name Orc1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 924
Subcellular Localization Nucleus.
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 MVNKENARSVGQQVKWIGSQDELPPVKNLEHKNVYFYQKCIYGPLTLSVGDFILVSNADAAEPDTVSGCDVARILHMYELRELTDREPCRAIVQWYSWPKAIPHNKYDDDEVAIDFSLEVIEEHRPYDNDVALGAIYRKCIVLEGTSKTSAEEILKRHANKLKSTACPMFVSRYRFVKVKRSYRLIPLEIHLEQPEDNARPTRSSRKSLTAHRESKRSISARHDDTAGNKGSSVEKRRRASMAASSSVEFIDVNSFICENKVSPIKIVGGRSVVRLSEKKNAPEINANYLPASPLTEKNAKVETPKSRASAARRNLNLSLDRGADTTADSDCLNYSIVQQTPDPKTPSNDMKIKLRLSERRRSVRLASMDVDPLSLEEAVQEPNAQGRKRLGVANGDIYHTPTKKSKEPLESAAATEQTPSTRRKSILKSATSRLAEGTPRRSIHLSNIVEQRVFEDDEIISTPKRGRSKKTVQDNDEDYSPKKSVQKTPTRTRRSSTTTKTATTPSKGITTATATPMTPSQKMKKIRAGELSPSMQQRTDLPAKDSSKSELQLAREQLHVSVVPKSLPCREREFENIYAFLEGKIQDQCGGCMYVSGVPGTGKTATVTGVIRTLQRMAKQNELPAFEYLEINGMRLTEPRQAYVQIYKQLTGKTVSWEQAHALLEKRFTTPAPRRVTTVLLVDELDILCNRRQDVVYNLLDWPTKSAAKLVVVTIANTMDLPERLLMGKVTSRLGLTRLTFQPYSHKQLQEIVTARLGGSETFKGEAVQLVARKVAAVSGDARRALDICRRATEIADTAAVKCVTMLHVQQALAEMIASAKVQAIRNCSRMEQIFLQAIAAEVTRTGVEETTFMGVYQQVETIAAFMGVTFPPPGRALRLCSKLGAERLIISEHSRNDLFQKILLNVSADDIHYALRVEEMVN
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
218PhosphorylationAHRESKRSISARHDD
HCHHHHHCHHHCCCC		25.3219429919
220PhosphorylationRESKRSISARHDDTA
HHHHHCHHHCCCCCC		22.0919429919
277PhosphorylationGRSVVRLSEKKNAPE
CEEEEEHHHCCCCCC		36.4822817900
293PhosphorylationNANYLPASPLTEKNA
CCCCCCCCCCCCCCC		20.6428490779
296PhosphorylationYLPASPLTEKNAKVE
CCCCCCCCCCCCCCC		48.5828490779
319PhosphorylationARRNLNLSLDRGADT
HHHHCCCCCCCCCCC		27.4419429919
368PhosphorylationRRSVRLASMDVDPLS
HHHHHEEECCCCCCC		21.8023607784
401PhosphorylationANGDIYHTPTKKSKE
CCCCCCCCCCCCCCC		18.7127626673
403PhosphorylationGDIYHTPTKKSKEPL
CCCCCCCCCCCCCCH		52.8621082442
419PhosphorylationSAAATEQTPSTRRKS
HHHCCCCCCCHHHHH		16.9928490779
422PhosphorylationATEQTPSTRRKSILK
CCCCCCCHHHHHHHH		35.3822817900
426PhosphorylationTPSTRRKSILKSATS
CCCHHHHHHHHHHHH		31.2022817900
430PhosphorylationRRKSILKSATSRLAE
HHHHHHHHHHHHHHC		33.0822817900
439PhosphorylationTSRLAEGTPRRSIHL
HHHHHCCCCCCEEEH		12.7225749252
443PhosphorylationAEGTPRRSIHLSNIV
HCCCCCCEEEHHHHH		18.6822817900
463PhosphorylationEDDEIISTPKRGRSK
CCCCCCCCCCCCCCC		23.5625749252
480PhosphorylationVQDNDEDYSPKKSVQ
CCCCCCCCCCCCCCC		25.4829892262
481PhosphorylationQDNDEDYSPKKSVQK
CCCCCCCCCCCCCCC		42.4322817900
511PhosphorylationTTPSKGITTATATPM
ECCCCCCEEEECCCC		21.0319429919
512PhosphorylationTPSKGITTATATPMT
CCCCCCEEEECCCCC		21.7919429919
514PhosphorylationSKGITTATATPMTPS
CCCCEEEECCCCCHH		29.0419429919
516PhosphorylationGITTATATPMTPSQK
CCEEEECCCCCHHHH		14.8319429919
533PhosphorylationKIRAGELSPSMQQRT
HHHCCCCCHHHHHCC		15.6125749252
535PhosphorylationRAGELSPSMQQRTDL
HCCCCCHHHHHCCCC		26.3327626673
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
-KUbiquitinationE3 ubiquitin ligasefzrO18402
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ORC1_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 ORC1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ORC2_DROMEOrc2physical
16188887
RBF_DROMERbfphysical
11231579
ORC5_DROMEOrc5physical
24137536
ORC6_DROMEOrc6physical
24137536
ORC2_DROMEOrc2physical
12490953
ORC2_DROMEOrc2physical
24137536
E2F1_DROMEE2fphysical
11231579
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ORC1_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-293; THR-419; SER-426;SER-430 AND SER-533, AND MASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND MASSSPECTROMETRY.

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