Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  DNA replication licensing factor MCM2  

UniProtKB / Swiss-Prot ID :  MCM2_MOUSE

Gene Name (Synonyms) : 
Mcm2, Bm28, Cdcl1, Kiaa0030, Mcmd2  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus (Probable). 

Protein Function :  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. 

Protein Sequence MAESSESLSASSPARQRRRISDPLTSSPGRSSRRADALTSSPGRDLPPFEDESEGLLGTEGPMEEEEDGE...
Predicted Secondary Structure CCCCCCCCCCCCCHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCHH...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
12PhosphoserineLSASSPARQ
CCCCCCHHH
23.46Phosphositeplus
Link-
12Phosphoserine.LSASSPARQ
CCCCCCHHH
23.46UniProtKB
Link-
21PhosphoserineRRRISDPLT
CCCCCCCCC
31.22PhosphoELM
Link-
21PhosphoserineRRRISDPLT
CCCCCCCCC
31.22Phosphositeplus
Link-
21PhosphoserineRRRISDPLT
CCCCCCCCC
31.22SysPTM
Link-
21Phosphoserine.RRRISDPLT
CCCCCCCCC
31.22UniProtKB
Link-
25PhosphothreonineSDPLTSSPG
CCCCCCCCC
32.33Phosphositeplus
Link-
25PhosphothreonineSDPLTSSPG
CCCCCCCCC
32.33SysPTM
Link-
25Phosphothreonine.SDPLTSSPG
CCCCCCCCC
32.33UniProtKB
Link-
26PhosphoserineDPLTSSPGR
CCCCCCCCC
42.07Phosphositeplus
Link-
26PhosphoserineDPLTSSPGR
CCCCCCCCC
42.07SysPTM
Link-
26Phosphoserine.DPLTSSPGR
CCCCCCCCC
42.07UniProtKB
Link-
27PhosphoserinePLTSSPGRS
CCCCCCCCC
26.58PhosphoELM
Link-
27PhosphoserinePLTSSPGRS
CCCCCCCCC
26.58Phosphositeplus
Link-
27PhosphoserinePLTSSPGRS
CCCCCCCCC
26.58SysPTM
Link-
27Phosphoserine.PLTSSPGRS
CCCCCCCCC
26.58UniProtKB
Link-
31PhosphoserineSPGRSSRRA
CCCCCCCCC
33.83Phosphositeplus
Link-
39PhosphothreonineADALTSSPG
CCCCCCCCC
28.95Phosphositeplus
Link-
39PhosphothreonineADALTSSPG
CCCCCCCCC
28.95SysPTM
Link-
40PhosphoserineDALTSSPGR
CCCCCCCCC
35.07Phosphositeplus
Link-
41PhosphoserineALTSSPGRD
CCCCCCCCC
26.58PhosphoELM
Link-
41PhosphoserineALTSSPGRD
CCCCCCCCC
26.58Phosphositeplus
Link-
41PhosphoserineALTSSPGRD
CCCCCCCCC
26.58SysPTM
Link-
41Phosphoserine.ALTSSPGRD
CCCCCCCCC
26.58UniProtKB
Link-
108PhosphoserineELTASQREA
HHHHHHHHH
25.24Phosphositeplus
Link-
137PhosphotyrosineRGLLYDSSE
CCCCCCCCC
20.87Phosphositeplus
Link-
139PhosphoserineLLYDSSEED
CCCCCCCHH
26.54PhosphoELM
Link-
139PhosphoserineLLYDSSEED
CCCCCCCHH
26.54Phosphositeplus
Link-
139PhosphoserineLLYDSSEED
CCCCCCCHH
26.54SysPTM
Link-
139Phosphoserine.LLYDSSEED
CCCCCCCHH
26.54UniProtKB
Link-
140PhosphoserineLYDSSEEDE
CCCCCCHHH
41.95PhosphoELM
Link-
140PhosphoserineLYDSSEEDE
CCCCCCHHH
41.95Phosphositeplus
Link-
140PhosphoserineLYDSSEEDE
CCCCCCHHH
41.95SysPTM
Link-
140Phosphoserine.LYDSSEEDE
CCCCCCHHH
41.95UniProtKB
Link-
229PhosphoserineENRESLVVN
CCCCEEEEE
24.19Phosphositeplus
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Drug Reference
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
"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.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures