dbPTM

MCM4_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM4_DROME
UniProt AC	Q26454
Protein Name	DNA replication licensing factor MCM4
Gene Name	dpa
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	866
Subcellular Localization	Nucleus.
Protein Description	Acts as component of the Mcm2-7 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. Required for DNA replication and cell proliferation. Essential role in mitotic DNA replication but not in endoreplication..
Protein Sequence	MSSPARSPSVGGATPKQGARTPTRGIASQDVETPMRMGPGRAVRPSDNISLPPTSPGNISLPATSPARGLGANMSEIDLSSPLNYGTPSSMGSIRTPRSGIRGTPLRARPDIRTDKRIRQVAIGGGSGLEPIPEKGSETTDPVSESSQAPQLVVWGTNVVVSQCKSKFKSFIMRFIDPSAEQDEISENIDVNQPLYLQKLEEIHTLEEPYLNLNCAHLKTFDQDLYRQLICYPQEVIPGFDMAINEMFFERYPAALLEHQIQVRPFNADKTRNMRSLNPEDMDQLISISGMVIRSSNVIPEMREAFFSCNICSFSTTVEVDRGRINQPTLCTNCNTNHCFRLIHNRSEFTDKQLVKLQESPDDMAAGQTPHNVLLYAHNDLVDKVQPGDRVTVTGIYRATPLKTGGLSSSVKSVYKTHVDVVHFRKVDNKRLYEDEEGKDHIFPPERVELLQLLAKKPDIYDRLARAIAPSIYENDDIKKGILLQLFGGTKKKHATLGRQNFRSEIHLLLCGDPGTSKSQMLQYVFNLVPRSQYTSGRGSSAVGLTAYVTKDPETRQLVLQTGALVLADNGVCCIDEFDKMNDSTRSVLHEVMEQQTLSIAKAGIICQLNARTSILAAANPAESQWNKRKNIIDNVQLPHTLLSRFDLIFLVLDPQDEIFDKRLASHLVSLYYVTRHEEEDTMFDMSVLRDYIAYAREHLSPTLSDEAQQRLIQAYVDMRKVGAGRGQISAYPRQLESLIRLSEAHAKVRLSNQVELLDVEEAWRLHREALKQSATDPLSGKIDVGILTTGLSTAARKKRADLVAAIKENLKKKGKVLTVPYQKLFSDIKEGSQIMITREQFEDALKEVQDEGAIVVMGKNTIRIC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSPARSPS ------CCCCCCCCC	45.06	19429919
3	Phosphorylation	-----MSSPARSPSV -----CCCCCCCCCC	22.68	19429919
7	Phosphorylation	-MSSPARSPSVGGAT -CCCCCCCCCCCCCC	24.51	19429919
9	Phosphorylation	SSPARSPSVGGATPK CCCCCCCCCCCCCCC	34.34	19429919
14	Phosphorylation	SPSVGGATPKQGART CCCCCCCCCCCCCCC	34.00	19429919
21	Phosphorylation	TPKQGARTPTRGIAS CCCCCCCCCCCCCCC	28.60	27626673
28	Phosphorylation	TPTRGIASQDVETPM CCCCCCCCCCCCCCH	25.62	27626673
33	Phosphorylation	IASQDVETPMRMGPG CCCCCCCCCHHCCCC	23.41	25749252
54	Phosphorylation	DNISLPPTSPGNISL CCCCCCCCCCCCCCC	45.68	25749252
55	Phosphorylation	NISLPPTSPGNISLP CCCCCCCCCCCCCCC	36.26	28490779
60	Phosphorylation	PTSPGNISLPATSPA CCCCCCCCCCCCCCC	32.09	28490779
64	Phosphorylation	GNISLPATSPARGLG CCCCCCCCCCCCCCC	33.05	28490779
65	Phosphorylation	NISLPATSPARGLGA CCCCCCCCCCCCCCC	20.76	22817900
75	Phosphorylation	RGLGANMSEIDLSSP CCCCCCCCCCCCCCC	31.07	19429919
80	Phosphorylation	NMSEIDLSSPLNYGT CCCCCCCCCCCCCCC	26.60	19429919
81	Phosphorylation	MSEIDLSSPLNYGTP CCCCCCCCCCCCCCC	40.48	19429919
85	Phosphorylation	DLSSPLNYGTPSSMG CCCCCCCCCCCCCCC	30.02	19429919
87	Phosphorylation	SSPLNYGTPSSMGSI CCCCCCCCCCCCCCC	15.05	19429919
89	Phosphorylation	PLNYGTPSSMGSIRT CCCCCCCCCCCCCCC	32.56	19429919
90	Phosphorylation	LNYGTPSSMGSIRTP CCCCCCCCCCCCCCC	28.50	21082442
104	Phosphorylation	PRSGIRGTPLRARPD CCCCCCCCCCCCCCC	14.86	27626673
614	Phosphorylation	CQLNARTSILAAANP EECCCCHHHHHHCCC	15.28	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 MCM4_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM4_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 MCM4_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM7_DROME	Mcm7	physical	22036573
MCM6_DROME	Mcm6	physical	22036573
MCM5_DROME	Mcm5	physical	22036573

Drug and Disease Associations

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

Regulatory Network of MCM4_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-55; SER-81 AND THR-87,AND MASS SPECTROMETRY.	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-55, AND MASSSPECTROMETRY.	17372656 [Abstract]