dbPTM

MCM3_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM3_DROME
UniProt AC	Q9XYU1
Protein Name	DNA replication licensing factor Mcm3
Gene Name	Mcm3
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	819
Subcellular Localization	Nucleus .
Protein Description	Acts as component of the Mcm2-7 complex (Mcm complex) (Mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the Mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity..
Protein Sequence	MAHEGEQFIKDIQREYVDFLDDEEDQGIYAGHVKDMIAEKSKRLIVNVNDLKRKNPQRALGLLSNAADEQLAFGRALKEYASTVDPGYAKMHEDLFVGFEGCFGNRHVTPRSLTSIYLGNMVCVEGIVTKVSLIRPKVVRSVHYCPNTRKVMERKYTDLTSFEAVPSGAAYPTKDEDGNLLETEYGLSVYKDHQTLTIQEMPEKAPAGQLPRSVDIVCDDDLVDRCKPGDRVQIVGSYRCLPGKRGGYTSGTFRTVLLANNISLLSKESNLDISREDIMLCKKLAKNNDIFELLSKSLAPSIHGHAYVKQAILCLLLGGVEKILPNGTRLRGDINVLLIGDPSVAKSQLLRYVLNTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDIDRTAIHEVMEQGRVTISKAGIHASLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFVMLDVIDSDVDQMISDHVVRMHRYRNPKEADGEPLSMGSSYADSLSFVSSSEEKKDTEVYEKYDALLHGKSRQRHEKILSVEFMRKYIHIAKCMKPKLGEQACEAIANEYSRLRSQEAVETDVARTQPITARTLETLIRLSTAHARARMSKSVTIDDAHAAIELVQFAYFKKVLDKDRPSKRRRNSGSDAEDDNGEASSQRSPSRRSKRTRTATVGADSDEEDIEPPQPDAGDLTRRETRRSLPARSVAMLMASPSSEEQSVATSTTEPAIISDARLGEFKNNLQRLFREAREQSLALARITTAINVGSQEPFTAGEIEAAVHRMTEDNQIMVADDIVFLI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
522	Phosphorylation	MGSSYADSLSFVSSS CCCCHHHHCCCCCCC	20.10	18327897
538	Phosphorylation	EKKDTEVYEKYDALL CCCCCHHHHHHHHHH	10.64	18327897
548	Acetylation	YDALLHGKSRQRHEK HHHHHCCCCHHHHHH	31.55	21791702
664	Phosphorylation	PSKRRRNSGSDAEDD CCCCCCCCCCCCCCC	37.55	19429919
666	Phosphorylation	KRRRNSGSDAEDDNG CCCCCCCCCCCCCCC	33.21	19429919
676	Phosphorylation	EDDNGEASSQRSPSR CCCCCCCCCCCCCCH	23.77	19429919
677	Phosphorylation	DDNGEASSQRSPSRR CCCCCCCCCCCCCHH	36.34	19429919
680	Phosphorylation	GEASSQRSPSRRSKR CCCCCCCCCCHHCCC	21.42	19429919
682	Phosphorylation	ASSQRSPSRRSKRTR CCCCCCCCHHCCCEE	41.39	19429919
690	Phosphorylation	RRSKRTRTATVGADS HHCCCEEEEEECCCC	26.52	19429919
692	Phosphorylation	SKRTRTATVGADSDE CCCEEEEEECCCCCC	20.89	19429919
697	Phosphorylation	TATVGADSDEEDIEP EEEECCCCCCCCCCC	46.52	21082442
732	Phosphorylation	SVAMLMASPSSEEQS HHHHHHCCCCHHHCC	16.02	21082442
735	Phosphorylation	MLMASPSSEEQSVAT HHHCCCCHHHCCCCC	48.84	22817900
739	Phosphorylation	SPSSEEQSVATSTTE CCCHHHCCCCCCCCC	19.59	19060867
787	Phosphorylation	TTAINVGSQEPFTAG HHCCCCCCCCCCCHH	27.39	22817900

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 MCM3_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM3_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 MCM3_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MCMBP_DROME	CG3430	physical	22036573

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MCM3_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-522; TYR-538; SER-664;SER-666; SER-680; SER-682; THR-690; THR-692 AND SER-697, AND MASSSPECTROMETRY.	18327897 [Abstract]
"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-697; SER-735 ANDSER-739, AND MASS SPECTROMETRY.	17372656 [Abstract]