MCMBP_HUMAN - dbPTM
MCMBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCMBP_HUMAN
UniProt AC Q9BTE3
Protein Name Mini-chromosome maintenance complex-binding protein
Gene Name MCMBP
Organism Homo sapiens (Human).
Sequence Length 642
Subcellular Localization Nucleus . Associates with chromatin. Highly associated with chromatin in G1/S and S phases, reduced binding to chromatin in G2, and further decreased binding in early M phase. It then reassociates with chromatin in late M phase. Dissociates from chro
Protein Description Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion..
Protein Sequence MPCGEDWLSHPLGIVQGFFAQNGVNPDWEKKVIEYFKEKLKENNAPKWVPSLNEVPLHYLKPNSFVKFRCMIQDMFDPEFYMGVYETVNQNTKAHVLHFGKYRDVAECGPQQELDLNSPRNTTLERQTFYCVPVPGESTWVKEAYVNANQARVSPSTSYTPSRHKRSYEDDDDMDLQPNKQKDQHAGARQAGSVGGLQWCGEPKRLETEASTGQQLNSLNLSSPFDLNFPLPGEKGPACLVKVYEDWDCFKVNDILELYGILSVDPVLSILNNDERDASALLDPMECTDTAEEQRVHSPPASLVPRIHVILAQKLQHINPLLPACLNKEESKTCKFVSSFMSELSPVRAELLGFLTHALLGDSLAAEYLILHLISTVYTRRDVLPLGKFTVNLSGCPRNSTFTEHLYRIIQHLVPASFRLQMTIENMNHLKFIPHKDYTANRLVSGLLQLPSNTSLVIDETLLEQGQLDTPGVHNVTALSNLITWQKVDYDFSYHQMEFPCNINVFITSEGRSLLPADCQIHLQPQLIPPNMEEYMNSLLSAVLPSVLNKFRIYLTLLRFLEYSISDEITKAVEDDFVEMRKNDPQSITADDLHQLLVVARCLSLSAGQTTLSRERWLRAKQLESLRRTRLQQQKCVNGNEL
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
31UbiquitinationVNPDWEKKVIEYFKE
CCCHHHHHHHHHHHH		36.61-
37UbiquitinationKKVIEYFKEKLKENN
HHHHHHHHHHHHHCC		53.70-
39AcetylationVIEYFKEKLKENNAP
HHHHHHHHHHHCCCC		66.5025953088
47UbiquitinationLKENNAPKWVPSLNE
HHHCCCCCCCCCCCC		59.4121890473
47 (in isoform 2)Ubiquitination-59.4121890473
47 (in isoform 1)Ubiquitination-59.4121890473
47UbiquitinationLKENNAPKWVPSLNE
HHHCCCCCCCCCCCC		59.4121890473
61UbiquitinationEVPLHYLKPNSFVKF
CCCCHHCCCCCEEEE		34.6821890473
61 (in isoform 2)Ubiquitination-34.6821890473
61 (in isoform 1)Ubiquitination-34.6821890473
61UbiquitinationEVPLHYLKPNSFVKF
CCCCHHCCCCCEEEE		34.6821890473
61AcetylationEVPLHYLKPNSFVKF
CCCCHHCCCCCEEEE		34.6823954790
67UbiquitinationLKPNSFVKFRCMIQD
CCCCCEEEEEEEHHH		25.69-
101UbiquitinationAHVLHFGKYRDVAEC
EEEEEEECCCCHHHH		35.85-
102PhosphorylationHVLHFGKYRDVAECG
EEEEEECCCCHHHHC		16.66-
108GlutathionylationKYRDVAECGPQQELD
CCCCHHHHCCCCCCC		7.5022555962
118PhosphorylationQQELDLNSPRNTTLE
CCCCCCCCCCCCCCE		32.3128985074
142UbiquitinationPGESTWVKEAYVNAN
CCCCCEEEEEEECCC		28.34-
145PhosphorylationSTWVKEAYVNANQAR
CCEEEEEEECCCCCC		8.7023927012
154PhosphorylationNANQARVSPSTSYTP
CCCCCCCCCCCCCCC		13.9519664994
156PhosphorylationNQARVSPSTSYTPSR
CCCCCCCCCCCCCCC		23.6030266825
157PhosphorylationQARVSPSTSYTPSRH
CCCCCCCCCCCCCCC		29.1829255136
158PhosphorylationARVSPSTSYTPSRHK
CCCCCCCCCCCCCCC		31.2029255136
158O-linked_GlycosylationARVSPSTSYTPSRHK
CCCCCCCCCCCCCCC		31.2023301498
159PhosphorylationRVSPSTSYTPSRHKR
CCCCCCCCCCCCCCC		23.8223927012
160 (in isoform 3)Phosphorylation-17.9821406692
160PhosphorylationVSPSTSYTPSRHKRS
CCCCCCCCCCCCCCC		17.9819664994
162PhosphorylationPSTSYTPSRHKRSYE
CCCCCCCCCCCCCCC		38.9429255136
163 (in isoform 3)Phosphorylation-40.3221406692
164 (in isoform 3)Phosphorylation-33.9321406692
165UbiquitinationSYTPSRHKRSYEDDD
CCCCCCCCCCCCCCC		41.76-
166MethylationYTPSRHKRSYEDDDD
CCCCCCCCCCCCCCC		38.04115483037
167 (in isoform 3)Phosphorylation-37.3621406692
167PhosphorylationTPSRHKRSYEDDDDM
CCCCCCCCCCCCCCC		37.3628355574
168PhosphorylationPSRHKRSYEDDDDMD
CCCCCCCCCCCCCCC		27.6628796482
170 (in isoform 3)Phosphorylation-57.3021406692
180UbiquitinationDMDLQPNKQKDQHAG
CCCCCCCCHHCCCHH		66.4621906983
180 (in isoform 2)Ubiquitination-66.4621890473
180 (in isoform 1)Ubiquitination-66.4621890473
182UbiquitinationDLQPNKQKDQHAGAR
CCCCCCHHCCCHHCC		62.05-
193PhosphorylationAGARQAGSVGGLQWC
HHCCCCCCCCCCCCC		22.1721815630
204AcetylationLQWCGEPKRLETEAS
CCCCCCCCCCCCCCC		66.3726051181
204UbiquitinationLQWCGEPKRLETEAS
CCCCCCCCCCCCCCC		66.3721906983
204 (in isoform 1)Ubiquitination-66.3721890473
204 (in isoform 2)Ubiquitination-66.3721890473
212PhosphorylationRLETEASTGQQLNSL
CCCCCCCCCCCHHCC		46.1624173317
218PhosphorylationSTGQQLNSLNLSSPF
CCCCCHHCCCCCCCC		27.5125159151
222PhosphorylationQLNSLNLSSPFDLNF
CHHCCCCCCCCCCCC		34.5925159151
223PhosphorylationLNSLNLSSPFDLNFP
HHCCCCCCCCCCCCC		32.5225627689
235UbiquitinationNFPLPGEKGPACLVK
CCCCCCCCCCEEEEE		75.90-
235AcetylationNFPLPGEKGPACLVK
CCCCCCCCCCEEEEE		75.9026051181
242UbiquitinationKGPACLVKVYEDWDC
CCCEEEEEEECCCCC		26.59-
244PhosphorylationPACLVKVYEDWDCFK
CEEEEEEECCCCCEE		11.4928152594
269O-linked_GlycosylationLSVDPVLSILNNDER
CCCCCHHHHHCCCCC		25.8423301498
279PhosphorylationNNDERDASALLDPME
CCCCCCHHHHCCCCC		24.6029978859
288PhosphorylationLLDPMECTDTAEEQR
HCCCCCCCCCHHHHC		24.0723401153
290PhosphorylationDPMECTDTAEEQRVH
CCCCCCCCHHHHCCC		20.1623401153
298PhosphorylationAEEQRVHSPPASLVP
HHHHCCCCCCHHHHC		29.7129255136
302PhosphorylationRVHSPPASLVPRIHV
CCCCCCHHHHCHHHH		35.3623401153
314AcetylationIHVILAQKLQHINPL
HHHHHHHHHHHHCCC		44.5025953088
314UbiquitinationIHVILAQKLQHINPL
HHHHHHHHHHHHCCC		44.50-
328UbiquitinationLLPACLNKEESKTCK
CHHHHCCHHHHHHHH		50.3219608861
328AcetylationLLPACLNKEESKTCK
CHHHHCCHHHHHHHH		50.3223954790
332 (in isoform 2)Ubiquitination-62.3121890473
332UbiquitinationCLNKEESKTCKFVSS
HCCHHHHHHHHHHHH		62.3121906983
332UbiquitinationCLNKEESKTCKFVSS
HCCHHHHHHHHHHHH		62.3121890473
333 (in isoform 2)Phosphorylation-30.1521406692
336 (in isoform 2)Phosphorylation-7.5821406692
337 (in isoform 2)Phosphorylation-2.6121406692
340 (in isoform 2)Phosphorylation-4.9421406692
343 (in isoform 2)Phosphorylation-41.2921406692
386 (in isoform 2)Ubiquitination-11.5821890473
386UbiquitinationTRRDVLPLGKFTVNL
CCCCCCCCCEEEEEC		11.5821890473
388 (in isoform 1)Ubiquitination-45.6121890473
388UbiquitinationRDVLPLGKFTVNLSG
CCCCCCCEEEEECCC		45.6121890473
407PhosphorylationSTFTEHLYRIIQHLV
CCHHHHHHHHHHHHH		11.1524927040
431UbiquitinationIENMNHLKFIPHKDY
EECCCCCEECCCCCC		33.43-
436UbiquitinationHLKFIPHKDYTANRL
CCEECCCCCCCHHHH		47.26-
571UbiquitinationSISDEITKAVEDDFV
HCCHHHHHHHHHCHH		56.97-
580SulfoxidationVEDDFVEMRKNDPQS
HHHCHHHHHHCCCCC		6.5921406390
580 (in isoform 2)Ubiquitination-6.5921890473
582 (in isoform 1)Ubiquitination-65.4821890473
582UbiquitinationDDFVEMRKNDPQSIT
HCHHHHHHCCCCCCC		65.4822053931
604PhosphorylationLVVARCLSLSAGQTT
HHHHHHHHCCCCCCC		24.7321406692
606PhosphorylationVARCLSLSAGQTTLS
HHHHHHCCCCCCCCC		27.2921406692
610PhosphorylationLSLSAGQTTLSRERW
HHCCCCCCCCCHHHH		28.8721406692
611PhosphorylationSLSAGQTTLSRERWL
HCCCCCCCCCHHHHH		18.1721406692
613PhosphorylationSAGQTTLSRERWLRA
CCCCCCCCHHHHHHH		29.9721406692
621UbiquitinationRERWLRAKQLESLRR
HHHHHHHHHHHHHHH		49.32-
633 (in isoform 2)Ubiquitination-49.6621890473
635 (in isoform 1)Ubiquitination-35.4921890473
635AcetylationRTRLQQQKCVNGNEL
HHHHHHHHCCCCCCC		35.4926051181
635UbiquitinationRTRLQQQKCVNGNEL
HHHHHHHHCCCCCCC		35.492190698
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 MCMBP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCMBP_HUMAN !!
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 MCMBP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCM6_HUMANMCM6physical
24190967
UBP7_HUMANUSP7physical
24190967
MCM3_HUMANMCM3physical
24190967
RPR1A_HUMANRPRD1Aphysical
22863883
XPOT_HUMANXPOTphysical
22863883
FKBP5_HUMANFKBP5physical
25036637
KEAP1_HUMANKEAP1physical
25036637
MCM2_HUMANMCM2physical
25036637
MCM3_HUMANMCM3physical
25036637
MCM4_HUMANMCM4physical
25036637
MCM5_HUMANMCM5physical
25036637
MCM6_HUMANMCM6physical
25036637
MCM7_HUMANMCM7physical
25036637
MCM8_HUMANMCM8physical
25036637
MCM9_HUMANMCM9physical
25036637
PEPL1_HUMANNPEPL1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCMBP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND THR-160, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; THR-160 ANDSER-298, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND THR-160, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND THR-160, ANDMASS SPECTROMETRY.

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