DBF4A_HUMAN - dbPTM
DBF4A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DBF4A_HUMAN
UniProt AC Q9UBU7
Protein Name Protein DBF4 homolog A
Gene Name DBF4
Organism Homo sapiens (Human).
Sequence Length 674
Subcellular Localization Nucleus .
Protein Description Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle..
Protein Sequence MNSGAMRIHSKGHFQGGIQVKNEKNRPSLKSLKTDNRPEKSKCKPLWGKVFYLDLPSVTISEKLQKDIKDLGGRVEEFLSKDISYLISNKKEAKFAQTLGRISPVPSPESAYTAETTSPHPSHDGSSFKSPDTVCLSRGKLLVEKAIKDHDFIPSNSILSNALSWGVKILHIDDIRYYIEQKKKELYLLKKSSTSVRDGGKRVGSGAQKTRTGRLKKPFVKVEDMSQLYRPFYLQLTNMPFINYSIQKPCSPFDVDKPSSMQKQTQVKLRIQTDGDKYGGTSIQLQLKEKKKKGYCECCLQKYEDLETHLLSEQHRNFAQSNQYQVVDDIVSKLVFDFVEYEKDTPKKKRIKYSVGSLSPVSASVLKKTEQKEKVELQHISQKDCQEDDTTVKEQNFLYKETQETEKKLLFISEPIPHPSNELRGLNEKMSNKCSMLSTAEDDIRQNFTQLPLHKNKQECILDISEHTLSENDLEELRVDHYKCNIQASVHVSDFSTDNSGSQPKQKSDTVLFPAKDLKEKDLHSIFTHDSGLITINSSQEHLTVQAKAPFHTPPEEPNECDFKNMDSLPSGKIHRKVKIILGRNRKENLEPNAEFDKRTEFITQEENRICSSPVQSLLDLFQTSEEKSEFLGFTSYTEKSGICNVLDIWEEENSDNLLTAFFSSPSTSTFTGF
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
10PhosphorylationSGAMRIHSKGHFQGG
CCCEEEECCCCCCCC
37.6524719451
21SumoylationFQGGIQVKNEKNRPS
CCCCEEECCCCCCCC
42.91-
21SumoylationFQGGIQVKNEKNRPS
CCCCEEECCCCCCCC
42.91-
28PhosphorylationKNEKNRPSLKSLKTD
CCCCCCCCHHHCCCC
45.2329978859
30AcetylationEKNRPSLKSLKTDNR
CCCCCCHHHCCCCCC
59.0725953088
34PhosphorylationPSLKSLKTDNRPEKS
CCHHHCCCCCCCCCC
43.7422210691
52PhosphorylationPLWGKVFYLDLPSVT
CCCCEEEEEECCCCC
11.4229083192
57PhosphorylationVFYLDLPSVTISEKL
EEEEECCCCCHHHHH
38.9120873877
59PhosphorylationYLDLPSVTISEKLQK
EEECCCCCHHHHHHH
24.1120873877
61PhosphorylationDLPSVTISEKLQKDI
ECCCCCHHHHHHHHH
21.2229083192
81UbiquitinationRVEEFLSKDISYLIS
HHHHHHCCCHHHHHC
62.32-
84PhosphorylationEFLSKDISYLISNKK
HHHCCCHHHHHCCCH
24.8227135362
88PhosphorylationKDISYLISNKKEAKF
CCHHHHHCCCHHHHH
39.7527135362
98PhosphorylationKEAKFAQTLGRISPV
HHHHHHHHHCCCCCC
27.9623186163
103PhosphorylationAQTLGRISPVPSPES
HHHHCCCCCCCCHHH
20.6325849741
107PhosphorylationGRISPVPSPESAYTA
CCCCCCCCHHHCCCC
41.3520873877
110PhosphorylationSPVPSPESAYTAETT
CCCCCHHHCCCCCCC
29.9320873877
112PhosphorylationVPSPESAYTAETTSP
CCCHHHCCCCCCCCC
18.7620873877
113PhosphorylationPSPESAYTAETTSPH
CCHHHCCCCCCCCCC
20.1020873877
116PhosphorylationESAYTAETTSPHPSH
HHCCCCCCCCCCCCC
30.0620873877
117PhosphorylationSAYTAETTSPHPSHD
HCCCCCCCCCCCCCC
31.5920873877
118PhosphorylationAYTAETTSPHPSHDG
CCCCCCCCCCCCCCC
28.7320873877
122PhosphorylationETTSPHPSHDGSSFK
CCCCCCCCCCCCCCC
31.0420873877
126PhosphorylationPHPSHDGSSFKSPDT
CCCCCCCCCCCCCCE
38.3620873877
127PhosphorylationHPSHDGSSFKSPDTV
CCCCCCCCCCCCCEE
42.0720873877
130PhosphorylationHDGSSFKSPDTVCLS
CCCCCCCCCCEEEEC
26.4625159151
140UbiquitinationTVCLSRGKLLVEKAI
EEEECCCCEEHHHHH
37.22-
177PhosphorylationLHIDDIRYYIEQKKK
EEHHHHHHHHHHHHC
14.77-
187PhosphorylationEQKKKELYLLKKSST
HHHHCEEEEEECCCC
15.8730108239
194PhosphorylationYLLKKSSTSVRDGGK
EEEECCCCCCEECCE
38.0322817900
195PhosphorylationLLKKSSTSVRDGGKR
EEECCCCCCEECCEE
19.6622817900
201UbiquitinationTSVRDGGKRVGSGAQ
CCCEECCEECCCCCC
49.82-
205PhosphorylationDGGKRVGSGAQKTRT
ECCEECCCCCCCCCC
28.2629496963
210O-linked_GlycosylationVGSGAQKTRTGRLKK
CCCCCCCCCCCCCCC
22.7630379171
212O-linked_GlycosylationSGAQKTRTGRLKKPF
CCCCCCCCCCCCCCE
31.7030379171
259PhosphorylationPFDVDKPSSMQKQTQ
CCCCCCCCHHCCCCE
44.1525627689
260PhosphorylationFDVDKPSSMQKQTQV
CCCCCCCHHCCCCEE
33.4925159151
273PhosphorylationQVKLRIQTDGDKYGG
EEEEEEECCCCCCCC
39.3125159151
278PhosphorylationIQTDGDKYGGTSIQL
EECCCCCCCCEEEEE
26.0620873877
281PhosphorylationDGDKYGGTSIQLQLK
CCCCCCCEEEEEEEH
20.4920873877
282PhosphorylationGDKYGGTSIQLQLKE
CCCCCCEEEEEEEHH
16.1820873877
303PhosphorylationCECCLQKYEDLETHL
HHHHHHHHHHHHHHH
11.17-
312PhosphorylationDLETHLLSEQHRNFA
HHHHHHHCHHHHHHH
41.3825849741
341PhosphorylationLVFDFVEYEKDTPKK
HHHHHHHCCCCCCCC
23.9928450419
345PhosphorylationFVEYEKDTPKKKRIK
HHHCCCCCCCCCCEE
48.3430266825
353PhosphorylationPKKKRIKYSVGSLSP
CCCCCEEEECCCCCC
13.2528176443
354PhosphorylationKKKRIKYSVGSLSPV
CCCCEEEECCCCCCC
18.2625159151
357PhosphorylationRIKYSVGSLSPVSAS
CEEEECCCCCCCCHH
24.4230266825
359PhosphorylationKYSVGSLSPVSASVL
EEECCCCCCCCHHHH
25.5929255136
362PhosphorylationVGSLSPVSASVLKKT
CCCCCCCCHHHHHHH
20.4330266825
364PhosphorylationSLSPVSASVLKKTEQ
CCCCCCHHHHHHHHC
22.0730266825
381PhosphorylationKVELQHISQKDCQED
HEEEEECCHHHCCCC
29.1123401153
393UbiquitinationQEDDTTVKEQNFLYK
CCCCCCHHHHCCEEC
52.03-
408SumoylationETQETEKKLLFISEP
CCHHHHHEEEEEECC
44.16-
408SumoylationETQETEKKLLFISEP
CCHHHHHEEEEEECC
44.16-
413PhosphorylationEKKLLFISEPIPHPS
HHEEEEEECCCCCCC
29.9529255136
420PhosphorylationSEPIPHPSNELRGLN
ECCCCCCCHHHHCHH
39.6425159151
429UbiquitinationELRGLNEKMSNKCSM
HHHCHHHHHCCHHHH
46.70-
431PhosphorylationRGLNEKMSNKCSMLS
HCHHHHHCCHHHHHH
44.1827732954
435PhosphorylationEKMSNKCSMLSTAED
HHHCCHHHHHHCCHH
25.1121815630
438PhosphorylationSNKCSMLSTAEDDIR
CCHHHHHHCCHHHHH
19.5528165663
439PhosphorylationNKCSMLSTAEDDIRQ
CHHHHHHCCHHHHHH
30.0621815630
449PhosphorylationDDIRQNFTQLPLHKN
HHHHHHCCCCCCCCC
36.4222123827
455UbiquitinationFTQLPLHKNKQECIL
CCCCCCCCCHHEEEE
73.79-
465PhosphorylationQECILDISEHTLSEN
HEEEEECCCCCCCHH
24.0027422710
468PhosphorylationILDISEHTLSENDLE
EEECCCCCCCHHHHH
28.1120873877
470PhosphorylationDISEHTLSENDLEEL
ECCCCCCCHHHHHHH
35.1927422710
502PhosphorylationFSTDNSGSQPKQKSD
CCCCCCCCCCCCCCC
43.0322123827
508PhosphorylationGSQPKQKSDTVLFPA
CCCCCCCCCEEEEEH
35.7030266825
510PhosphorylationQPKQKSDTVLFPAKD
CCCCCCCEEEEEHHH
26.6330266825
535PhosphorylationTHDSGLITINSSQEH
ECCCCEEEECCCCCE
21.1017525332
538PhosphorylationSGLITINSSQEHLTV
CCEEEECCCCCEEEE
29.5529523821
539PhosphorylationGLITINSSQEHLTVQ
CEEEECCCCCEEEEE
34.7917525332
544PhosphorylationNSSQEHLTVQAKAPF
CCCCCEEEEEEECCC
16.6929523821
553PhosphorylationQAKAPFHTPPEEPNE
EEECCCCCCCCCCCC
40.7023401153
568PhosphorylationCDFKNMDSLPSGKIH
CCCCCCCCCCCCCHH
31.2625159151
571PhosphorylationKNMDSLPSGKIHRKV
CCCCCCCCCCHHCEE
58.9929255136
573AcetylationMDSLPSGKIHRKVKI
CCCCCCCCHHCEEEE
39.4125953088
579SumoylationGKIHRKVKIILGRNR
CCHHCEEEEEECCCH
27.37-
579SumoylationGKIHRKVKIILGRNR
CCHHCEEEEEECCCH
27.37-
612PhosphorylationQEENRICSSPVQSLL
HHHHCCCCCHHHHHH
34.9920873877
613PhosphorylationEENRICSSPVQSLLD
HHHCCCCCHHHHHHH
25.3620873877
617PhosphorylationICSSPVQSLLDLFQT
CCCCHHHHHHHHHCC
31.0027732954
624PhosphorylationSLLDLFQTSEEKSEF
HHHHHHCCCHHHHHH
30.6730177828
625PhosphorylationLLDLFQTSEEKSEFL
HHHHHCCCHHHHHHC
32.7320873877
629PhosphorylationFQTSEEKSEFLGFTS
HCCCHHHHHHCCCCC
36.5422777824
635PhosphorylationKSEFLGFTSYTEKSG
HHHHCCCCCCCCCCC
21.0128450419
636PhosphorylationSEFLGFTSYTEKSGI
HHHCCCCCCCCCCCC
28.0021815630
637PhosphorylationEFLGFTSYTEKSGIC
HHCCCCCCCCCCCCC
18.8328450419
638PhosphorylationFLGFTSYTEKSGICN
HCCCCCCCCCCCCCE
36.3828450419
664PhosphorylationNLLTAFFSSPSTSTF
CCCHHHHCCCCCCCC
34.58-
665PhosphorylationLLTAFFSSPSTSTFT
CCHHHHCCCCCCCCC
20.08-
667PhosphorylationTAFFSSPSTSTFTGF
HHHHCCCCCCCCCCC
36.6229997176
669PhosphorylationFFSSPSTSTFTGF--
HHCCCCCCCCCCC--
26.3429997176

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
273TPhosphorylationKinaseCDC7O00311
PSP
281TPhosphorylationKinaseCDC7O00311
PSP
312SPhosphorylationKinaseCDC7O00311
PSP
449TPhosphorylationKinaseATMQ13315
PSP
449TPhosphorylationKinaseATRQ13535
PSP
502SPhosphorylationKinaseATMQ13315
PSP
502SPhosphorylationKinaseATRQ13535
PSP
539SPhosphorylationKinaseATMQ13315
PSP
539SPhosphorylationKinaseATRQ13535
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DBF4A_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 DBF4A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCM2_HUMANMCM2physical
12614612
ORC1_HUMANORC1physical
12614612
ORC2_HUMANORC2physical
12614612
ORC5_HUMANORC5physical
12614612
ORC6_HUMANORC6physical
12614612
MCM3_HUMANMCM3physical
12614612
MCM4_HUMANMCM4physical
12614612
MCM7_HUMANMCM7physical
12614612
ORC4_HUMANORC4physical
12614612
CDC7_HUMANCDC7physical
10523313
CDC7_HUMANCDC7physical
10373557
CDC7_HUMANCDC7physical
16912045
DBF4A_HUMANDBF4physical
12968034
DAXX_HUMANDAXXphysical
12968034
MCM2_HUMANMCM2physical
10846177
CDC7_HUMANCDC7physical
10846177
DBF4A_HUMANDBF4physical
10846177
MCM4_HUMANMCM4physical
10846177
MCM6_HUMANMCM6physical
10846177
MCM7_HUMANMCM7physical
10846177
RAD18_HUMANRAD18physical
24240236
HDGR2_HUMANHDGFRP2physical
28514442
CDC7_HUMANCDC7physical
28514442
NDK6_HUMANNME6physical
28514442
EF1A2_HUMANEEF1A2physical
28514442

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 DBF4A_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-359, 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 THR-273; THR-345; SER-359;SER-381; SER-413 AND SER-508, AND MASS SPECTROMETRY.
"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-359, AND MASSSPECTROMETRY.
"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-354 AND SER-359, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359 AND SER-381, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; THR-535 ANDSER-539, AND MASS SPECTROMETRY.

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