dbPTM

MCM2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM2_MOUSE
UniProt AC	P97310
Protein Name	DNA replication licensing factor MCM2
Gene Name	Mcm2
Organism	Mus musculus (Mouse).
Sequence Length	904
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 the entry in S phase and for cell division. Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis..
Protein Sequence	MAESSESLSASSPARQRRRISDPLTSSPGRSSRRADALTSSPGRDLPPFEDESEGLLGTEGPMEEEEDGEELIGDGMERDYRPIPELDVYEAEGLALDDEDVEELTASQREAAERTMRQRDREAGRGLGRMRRGLLYDSSEEDEERPARKRRHVERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLPQLSMVKYNCSKCNFVLGPFCQSQNQEVKPGSCPECQSAGPFEINMEETIYQNYQRIRIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTANGFPVFATIILANHVAKKDNKVAVGELTDEDVKMITGLSKDQQIGEKIFASIAPSIYGHEDIKRGLALALFGGEPKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYIEKVSSRAIFTTGQGASAVGLTAYVQRHPVSREWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSLTFSENVDLTEPIISRFDVLCVVRDTVDPVQDEMLARFVVGSHVRHHPSNKKDEGLTNGGTLEPAMPNTYGVEPLPQEVLKKYIIYAKERVRPKLNQMDQDKVARMYSDLRKESMATGSIPITVRHIESMIRMAEAHARMHLRDYVMEDDVNMAIRVMMESFIDTQKFSVMRSMRKTFARYLSFRRDNNDLLLFILKQLVAEQVTYQRNRFGAQQDTIEIPEKDLMDKARQINIHNLSAFYDSDLFKFNKFSRDLKRKLILQQF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAESSESLS ------CCCCCCCCC	25.94	19131326
4	Phosphorylation	----MAESSESLSAS ----CCCCCCCCCCC	29.84	27566939
5	Phosphorylation	---MAESSESLSASS ---CCCCCCCCCCCC	23.78	27566939
7	Phosphorylation	-MAESSESLSASSPA -CCCCCCCCCCCCHH	29.58	25168779
9	Phosphorylation	AESSESLSASSPARQ CCCCCCCCCCCHHHH	35.07	27566939
11	Phosphorylation	SSESLSASSPARQRR CCCCCCCCCHHHHHH	33.22	23527152
12	Phosphorylation	SESLSASSPARQRRR CCCCCCCCHHHHHHC	23.46	23527152
21	Phosphorylation	ARQRRRISDPLTSSP HHHHHCCCCCCCCCC	31.22	27087446
25	Phosphorylation	RRISDPLTSSPGRSS HCCCCCCCCCCCCHH	32.33	27087446
26	Phosphorylation	RISDPLTSSPGRSSR CCCCCCCCCCCCHHH	42.07	27087446
27	Phosphorylation	ISDPLTSSPGRSSRR CCCCCCCCCCCHHHH	26.58	27087446
31	Phosphorylation	LTSSPGRSSRRADAL CCCCCCCHHHHHHHC	33.83	22942356
32	Phosphorylation	TSSPGRSSRRADALT CCCCCCHHHHHHHCC	25.15	27600695
39	Phosphorylation	SRRADALTSSPGRDL HHHHHHCCCCCCCCC	28.95	22942356
40	Phosphorylation	RRADALTSSPGRDLP HHHHHCCCCCCCCCC	35.07	26824392
41	Phosphorylation	RADALTSSPGRDLPP HHHHCCCCCCCCCCC	26.58	27087446
53	Phosphorylation	LPPFEDESEGLLGTE CCCCCCCCCCCCCCC	49.65	21149613
59	Phosphorylation	ESEGLLGTEGPMEEE CCCCCCCCCCCCCCC	37.42	21149613
90	Phosphorylation	PIPELDVYEAEGLAL CCCCCCEEEECCCCC	14.75	30635358
106	Phosphorylation	DEDVEELTASQREAA HHHHHHHHHHHHHHH	27.78	26239621
108	Phosphorylation	DVEELTASQREAAER HHHHHHHHHHHHHHH	25.24	27087446
108	O-linked_Glycosylation	DVEELTASQREAAER HHHHHHHHHHHHHHH	25.24	29562282
137	Phosphorylation	RMRRGLLYDSSEEDE HHHCCCCCCCCHHHC	20.87	27149854
139	Phosphorylation	RRGLLYDSSEEDEER HCCCCCCCCHHHCCC	26.54	27087446
140	Phosphorylation	RGLLYDSSEEDEERP CCCCCCCCHHHCCCC	41.95	27087446
158	Phosphorylation	RRHVERATEDGEEDE HHHHHHHCCCCCHHH	40.61	25619855
170	Phosphorylation	EDEEMIESIENLEDL HHHHHHHHHHCHHHH	25.03	25619855
209	Phosphorylation	FLRTHVDSHGHNVFK HHHHHHHHCCCHHHH	30.22	27841257
216	Acetylation	SHGHNVFKERISDMC HCCCHHHHHHHHHHH	41.63	-
229	Phosphorylation	MCKENRESLVVNYED HHHHCHHHEECCHHH	24.19	22817900
308	Phosphorylation	HLNQLIRTSGVVTSC HHHHHHHHHCCCCCC	23.88	30635358
309	Phosphorylation	LNQLIRTSGVVTSCT HHHHHHHHCCCCCCC	21.53	30635358
313	Phosphorylation	IRTSGVVTSCTGVLP HHHHCCCCCCCCCHH	18.71	30635358
314	Phosphorylation	RTSGVVTSCTGVLPQ HHHCCCCCCCCCHHH	9.70	30635358
316	Phosphorylation	SGVVTSCTGVLPQLS HCCCCCCCCCHHHHH	30.05	30635358
323	Phosphorylation	TGVLPQLSMVKYNCS CCCHHHHHCEEECCC	19.11	30635358
327	Phosphorylation	PQLSMVKYNCSKCNF HHHHCEEECCCCCCE	15.25	30635358
330	Phosphorylation	SMVKYNCSKCNFVLG HCEEECCCCCCEEEC	36.28	30635358
381	Phosphorylation	QRIRIQESPGKVAAG HEEEEECCCCCCCCC	23.68	27600695
457	Phosphorylation	KVAVGELTDEDVKMI CEEEEECCHHHHHHH	32.80	26525534
462	Acetylation	ELTDEDVKMITGLSK ECCHHHHHHHHCCCC	36.59	23236377
480	Phosphorylation	IGEKIFASIAPSIYG HHHHHHHHHCHHHHC	14.45	26239621
484	Phosphorylation	IFASIAPSIYGHEDI HHHHHCHHHHCCHHH	21.30	26239621
534	Acetylation	TAKSQFLKYIEKVSS CHHHHHHHHHHHHCC	45.53	22826441
538	Acetylation	QFLKYIEKVSSRAIF HHHHHHHHHCCCEEE	37.55	22826441
546	Phosphorylation	VSSRAIFTTGQGASA HCCCEEEECCCCCCC	24.73	20531401
547	Phosphorylation	SSRAIFTTGQGASAV CCCEEEECCCCCCCE	19.43	20531401
552	Phosphorylation	FTTGQGASAVGLTAY EECCCCCCCEECEEH	30.25	20531401
591	Acetylation	CLIDEFDKMNDQDRT EEECCHHHCCCCCCH	44.94	22826441
599	Phosphorylation	MNDQDRTSIHEAMEQ CCCCCCHHHHHHHHH	23.88	25338131
757	Phosphorylation	LRKESMATGSIPITV HHHHHHHCCCCCEEH	23.87	29895711
759	Phosphorylation	KESMATGSIPITVRH HHHHHCCCCCEEHHH	22.34	29895711
763	Phosphorylation	ATGSIPITVRHIESM HCCCCCEEHHHHHHH	13.21	29895711
857	Phosphorylation	RFGAQQDTIEIPEKD CCCCCCCCEECCHHH	19.03	29514104

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
40	S	Phosphorylation	Kinase	CDC7	Q9Z0H0	Uniprot
53	S	Phosphorylation	Kinase	CDC7	Q9Z0H0	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
40	S	Phosphorylation	-
Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex.
53	S	Phosphorylation	-
Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex.
108	S	Phosphorylation	21183079
Phosphorylated on Ser-108 by ATR in proliferating cells.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM10_HUMAN	MCM10	physical	11095689
TIM_MOUSE	Timeless	physical	17141802
MCM3_HUMAN	MCM3	physical	26496610
MCM4_HUMAN	MCM4	physical	26496610
MCM5_HUMAN	MCM5	physical	26496610
MCM6_HUMAN	MCM6	physical	26496610
MCM7_HUMAN	MCM7	physical	26496610
ECD_HUMAN	ECD	physical	26496610
HSPB8_HUMAN	HSPB8	physical	26496610

Drug and Disease Associations

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

Regulatory Network of MCM2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-21; SER-27;SER-139 AND SER-140, AND MASS SPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-27; SER-41;SER-139 AND SER-140, AND MASS SPECTROMETRY.	17242355 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-25; SER-27;SER-139 AND SER-140, AND MASS SPECTROMETRY.	17622165 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-139 AND SER-140,AND MASS SPECTROMETRY.	15345747 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-26 AND SER-27,AND MASS SPECTROMETRY.	14729942 [Abstract]

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