MCM3_MOUSE - dbPTM
MCM3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCM3_MOUSE
UniProt AC P25206
Protein Name DNA replication licensing factor MCM3
Gene Name Mcm3
Organism Mus musculus (Mouse).
Sequence Length 812
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 MAGTVVLDDVELREAQRDYLDFLDDEEDQGIYQNKVRELISDNQYRLIVSVNDLRRKNEKRANRLLNNAFEELVAFQRALKDFVASIDATYAKQYEEFYIGLEGSFGSKHVSPRTLTSCFLSCVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERRYSDLTTLVAFPSSSVYPTKDEENNPLETEYGLSVYKDHQTITIQEMPEKAPAGQLPRSVDVILDDDLVDKVKPGDRIQVVGTYRCLPGKKGCYTSGTFRTVLIACNVKQMSKDIQPAFSADDIAKIKKFSKTRSKDVFEQLARSLAPSIHGHDYVKKAILCLLLGGVERELENGSHIRGDINILLIGDPSVAKSQLLRYVLCTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEQDREISDHVLRMHQYRAPGEQDGDALPLGSSVDILATDDPDFTQDDQQDTRIYEKHDSLLHGTKKKKEKMVSAAFMKKYIHVAKIIKPTLTQESAAYIAEEYSRLRSQDSMSSDTARTSPVTARTLETLIRLATAHAKARMSKTVDLQDAEEAVELVQYAYFKKVLEKEKKRKKASEDESDLEDEEEKSQEDTEQKRKRRKTHAKDGESYDPYDFSEAETQMPQVHTPKTDDSQEKTDDSQETQDSQKVELSEPRLKAFKAALLEVFQEAHEQSVGMLHLTESINRNREEPFSSEEIQACLSRMQDDNQVMVSEGIVFLI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAGTVVLDD
------CCCEEEECH		23.51-
4Phosphorylation----MAGTVVLDDVE
----CCCEEEECHHH		9.6328066266
91PhosphorylationVASIDATYAKQYEEF
HHHCCHHHHHHCCEE		17.3321183079
112PhosphorylationSFGSKHVSPRTLTSC
CCCCCCCCHHHHHHH		14.3722817900
135PhosphorylationEGIVTKCSLVRPKVV
HCHHHHCCCCCCCCE		31.3024719451
148GlutathionylationVVRSVHYCPATKKTI
CEEEEEECCCCHHHH		0.8224333276
154PhosphorylationYCPATKKTIERRYSD
ECCCCHHHHHHHHCC		29.6226643407
159PhosphorylationKKTIERRYSDLTTLV
HHHHHHHHCCCCEEE		16.8626239621
160PhosphorylationKTIERRYSDLTTLVA
HHHHHHHCCCCEEEE		25.0821082442
163PhosphorylationERRYSDLTTLVAFPS
HHHHCCCCEEEECCC		24.0726239621
164PhosphorylationRRYSDLTTLVAFPSS
HHHCCCCEEEECCCC		26.9126239621
170PhosphorylationTTLVAFPSSSVYPTK
CEEEECCCCCCCCCC		28.8825777480
171PhosphorylationTLVAFPSSSVYPTKD
EEEECCCCCCCCCCC		24.8625777480
172PhosphorylationLVAFPSSSVYPTKDE
EEECCCCCCCCCCCC		29.9725293948
174PhosphorylationAFPSSSVYPTKDEEN
ECCCCCCCCCCCCCC		13.7225293948
176PhosphorylationPSSSVYPTKDEENNP
CCCCCCCCCCCCCCC		33.1825293948
234MethylationDKVKPGDRIQVVGTY
CCCCCCCEEEEEEEE		27.4416188069
242MethylationIQVVGTYRCLPGKKG
EEEEEEEEECCCCCC		18.4816188077
252PhosphorylationPGKKGCYTSGTFRTV
CCCCCCCCCCCHHEE		25.4229176673
253PhosphorylationGKKGCYTSGTFRTVL
CCCCCCCCCCHHEEE		14.9025266776
255PhosphorylationKGCYTSGTFRTVLIA
CCCCCCCCHHEEEEE		15.0929176673
258PhosphorylationYTSGTFRTVLIACNV
CCCCCHHEEEEECCH		18.5722817900
269PhosphorylationACNVKQMSKDIQPAF
ECCHHHCCCCCCCCC		25.36-
277PhosphorylationKDIQPAFSADDIAKI
CCCCCCCCHHHHHHH		32.6626525534
293AcetylationKFSKTRSKDVFEQLA
HHCCCCCHHHHHHHH		55.4023806337
352PhosphorylationGDPSVAKSQLLRYVL
CCHHHHHHHHHHHHH		19.1425777480
357PhosphorylationAKSQLLRYVLCTAPR
HHHHHHHHHHHCCCC		9.5725777480
360GlutathionylationQLLRYVLCTAPRAIP
HHHHHHHHCCCCCCC		1.8624333276
361PhosphorylationLLRYVLCTAPRAIPT
HHHHHHHCCCCCCCC		35.2225777480
413AcetylationVCIDEFDKMSDMDRT
EEECCCCCCCCCCHH		45.7022826441
415PhosphorylationIDEFDKMSDMDRTAI
ECCCCCCCCCCHHHH		35.2126525534
420PhosphorylationKMSDMDRTAIHEVME
CCCCCCHHHHHHHHH		26.2128059163
435AcetylationQGRVTIAKAGIHARL
CCCEEEEECCHHHHH		43.2122826441
435UbiquitinationQGRVTIAKAGIHARL
CCCEEEEECCHHHHH		43.21-
474PhosphorylationENIGLQDSLLSRFDL
HHCCCCHHHHHHHHH		20.4628973931
522PhosphorylationGDALPLGSSVDILAT
CCCCCCCCCEEEEEC		34.5726525534
523PhosphorylationDALPLGSSVDILATD
CCCCCCCCEEEEECC		23.2430635358
529PhosphorylationSSVDILATDDPDFTQ
CCEEEEECCCCCCCC		37.1730635358
535PhosphorylationATDDPDFTQDDQQDT
ECCCCCCCCCHHHCC		38.1726525534
547AcetylationQDTRIYEKHDSLLHG
HCCHHHHHHHHHHCC		35.4223806337
550PhosphorylationRIYEKHDSLLHGTKK
HHHHHHHHHHCCCHH		32.3325266776
611PhosphorylationSSDTARTSPVTARTL
CCCCCCCCCCHHHHH		16.3022817900
614PhosphorylationTARTSPVTARTLETL
CCCCCCCHHHHHHHH		17.5125338131
668PhosphorylationEKKRKKASEDESDLE
HHHHHHCCCCCCCCC		55.2325521595
672PhosphorylationKKASEDESDLEDEEE
HHCCCCCCCCCHHHH		60.8727087446
681PhosphorylationLEDEEEKSQEDTEQK
CCHHHHHHHHHHHHH		41.9227087446
685PhosphorylationEEKSQEDTEQKRKRR
HHHHHHHHHHHHHHH		39.2925619855
697AcetylationKRRKTHAKDGESYDP
HHHHHHCCCCCCCCC		59.6723806337
701PhosphorylationTHAKDGESYDPYDFS
HHCCCCCCCCCCCCC		40.1225168779
702PhosphorylationHAKDGESYDPYDFSE
HCCCCCCCCCCCCCH		19.3525619855
705PhosphorylationDGESYDPYDFSEAET
CCCCCCCCCCCHHHH		27.0727742792
708PhosphorylationSYDPYDFSEAETQMP
CCCCCCCCHHHHCCC		32.7627087446
712PhosphorylationYDFSEAETQMPQVHT
CCCCHHHHCCCCCCC		36.9027087446
719PhosphorylationTQMPQVHTPKTDDSQ
HCCCCCCCCCCCCCC		27.8527087446
722PhosphorylationPQVHTPKTDDSQEKT
CCCCCCCCCCCCCCC		46.3627087446
725PhosphorylationHTPKTDDSQEKTDDS
CCCCCCCCCCCCCCC		42.9522942356
729PhosphorylationTDDSQEKTDDSQETQ
CCCCCCCCCCCCCCH		44.2627087446
732PhosphorylationSQEKTDDSQETQDSQ
CCCCCCCCCCCHHHH		32.5027087446
735PhosphorylationKTDDSQETQDSQKVE
CCCCCCCCHHHHHCC		30.0021082442
738PhosphorylationDSQETQDSQKVELSE
CCCCCHHHHHCCCCH		23.2927087446
740UbiquitinationQETQDSQKVELSEPR
CCCHHHHHCCCCHHH		41.45-
744PhosphorylationDSQKVELSEPRLKAF
HHHHCCCCHHHHHHH		31.8625619855
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
112SPhosphorylationKinaseCDK1P06493
PSP
112SPhosphorylationKinaseCDK1P11440
PSP
611SPhosphorylationKinaseCDK1P06493
PSP
611SPhosphorylationKinaseCDK2P24941
PSP
719TPhosphorylationKinaseCDK1P06493
PSP
719TPhosphorylationKinaseCDK1P11440
PSP
725SPhosphorylationKinaseATMQ13315
PSP
725SPhosphorylationKinaseATMQ62388
PSP
725SPhosphorylationKinaseATRQ9JKK8
PSP
732SPhosphorylationKinaseATMQ13315
PSP
732SPhosphorylationKinaseATMQ62388
PSP
732SPhosphorylationKinaseATRQ9JKK8
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCM3_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2B2B_MOUSEHist2h2bbphysical
18635963
AP2A1_HUMANAP2A1physical
26496610
FMNL1_HUMANFMNL1physical
26496610
EI2BA_HUMANEIF2B1physical
26496610
MCM2_HUMANMCM2physical
26496610
MCM4_HUMANMCM4physical
26496610
MCM5_HUMANMCM5physical
26496610
MCM6_HUMANMCM6physical
26496610
MCM7_HUMANMCM7physical
26496610
PMS2_HUMANPMS2physical
26496610
RCN1_HUMANRCN1physical
26496610
RL40_HUMANUBA52physical
26496610
OGT1_HUMANOGTphysical
26496610
GCC2_HUMANGCC2physical
26496610
TIF1B_HUMANTRIM28physical
26496610
RPP38_HUMANRPP38physical
26496610
SPAG5_HUMANSPAG5physical
26496610
ELL2_HUMANELL2physical
26496610
UBR5_HUMANUBR5physical
26496610
SCLY_HUMANSCLYphysical
26496610
CN166_HUMANC14orf166physical
26496610
GAR1_HUMANGAR1physical
26496610
DGCR8_HUMANDGCR8physical
26496610
GPAT1_HUMANGPAMphysical
26496610
MCMBP_HUMANMCMBPphysical
26496610
PCGF5_HUMANPCGF5physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCM3_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-672, AND MASSSPECTROMETRY.
"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-668 AND SER-672, ANDMASS 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-668; SER-672 ANDTHR-719, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory