dbPTM

MCM2_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM2_DROME
UniProt AC	P49735
Protein Name	DNA replication licensing factor Mcm2
Gene Name	Mcm2
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	887
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..
Protein Sequence	MDNPSSPPPNTPSDAAERRDLRAAMTSPVGDFEPFENEDEILGDQTVRDEAEEEDGEELFGDNMENDYRPMPELDHYDPALLDDEDDFSEMSQGDRFAAESEMRRRDRAAGIHRDDRDLGFGQSDDEDDVGPRAKRRAGEKAAVGEVEDTEMVESIENLEDTKGHSTKEWVSMLGPRTEIANRFQSFLRTFVDERGAYTYRDRIRRMCEQNMSSFVVSYTDLANKEHVLAYFLPEAPFQMLEIFDKVAKDMVLSIFPTYERVTTEIHVRISELPLIEELRTFRKLHLNQLVRTLGVVTATTGVLPQLSVIKYDCVKCGYVLGPFVQSQNTEIKPGSCPECQSTGPFSINMEQTLYRNYQKITLQESPGRIPAGRIPRSKDVILLADLCDQCKPGDELEVTGIYTNNYDGSLNTDQGFPVFATVIIANHVVVKDSKQVVQSLTDEDIATIQKLSKDPRIVERVVASMAPSIYGHDYIKRALALALFGGESKNPGEKHKVRGDINLLICGDPGTAKSQFLKYTEKVAPRAVFTTGQGASAVGLTAYVRRNPVSREWTLEAGALVLADQGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSMTFSENVNLSEPILSRFDVLCVVKDEFDPMQDQQLAKFVVHSHMKHHPSEEEQPELEEPQLKTVDEIPQDLLRQYIVYAKENIRPKLTNIDEDKIAKMYAQLRQESFATGSLPITVRHIESVIRMSEAHARMHLRENVMEADVSMAIRMMLESFIEAQKFSVMKKMRSTFQKYLSFQKDHSELLFFILRQLTLDQLAYIRCKDGPGATHVEIMERDLIERAKQLDIVNLKPFYESDLFRTNGFSYDPKRRIILQIVVDGNTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MDNPSSPPPNTP ---CCCCCCCCCCCC	62.83	19429919
6	Phosphorylation	--MDNPSSPPPNTPS --CCCCCCCCCCCCC	42.56	19429919
11	Phosphorylation	PSSPPPNTPSDAAER CCCCCCCCCCHHHHH	29.91	19429919
13	Phosphorylation	SPPPNTPSDAAERRD CCCCCCCCHHHHHHH	37.53	19429919
26	Phosphorylation	RDLRAAMTSPVGDFE HHHHHHHCCCCCCCC	25.75	19429919
27	Phosphorylation	DLRAAMTSPVGDFEP HHHHHHCCCCCCCCC	12.42	19429919
89	Phosphorylation	LDDEDDFSEMSQGDR CCCCCCHHHCCHHCH	39.11	22817900
92	Phosphorylation	EDDFSEMSQGDRFAA CCCHHHCCHHCHHHH	27.28	19429919
124	Phosphorylation	RDLGFGQSDDEDDVG CCCCCCCCCCCCCCC	47.62	21082442
150	Phosphorylation	AVGEVEDTEMVESIE CCCCCCCHHHHHHHH	16.69	22817900
593	Phosphorylation	HEAMEQQSISISKAG HHHHHHHCCCEEHHC	20.28	22668510
595	Phosphorylation	AMEQQSISISKAGIV HHHHHCCCEEHHCHH	26.51	22668510
597	Phosphorylation	EQQSISISKAGIVTS HHHCCCEEHHCHHHH	15.06	22668510

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 MCM2_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM2_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 MCM2_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM6_DROME	Mcm6	physical	22036573
MCM5_DROME	Mcm5	physical	22036573
MCM10_DROME	Mcm10	physical	20498296

Drug and Disease Associations

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

Regulatory Network of MCM2_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-89 AND SER-92, 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 THR-26; SER-27 AND SER-124,AND MASS SPECTROMETRY.	17372656 [Abstract]