DBF4B_HUMAN - dbPTM
DBF4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DBF4B_HUMAN
UniProt AC Q8NFT6
Protein Name Protein DBF4 homolog B
Gene Name DBF4B
Organism Homo sapiens (Human).
Sequence Length 615
Subcellular Localization Nucleus . Predominantly found in soluble fraction but not in the chromatin-bound fraction.
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 and M phases. The complex CDC7-DBF4B selectively phosphorylates MCM2 subunit at 'Ser-40' and then is involved in regulating the initiation of DNA replication during cell cycle..
Protein Sequence MSEPGKGDDCLELESSMAESRLRAPDLGVSRCLGKCQKNSPGARKHPFSGKSFYLDLPAGKNLQFLTGAIQQLGGVIEGFLSKEVSYIVSSRREVKAESSGKSHRGCPSPSPSEVRVETSAMVDPKGSHPRPSRKPVDSVPLSRGKELLQKAIRNQGSISGGGSGGSSSLLTNARSWGVRILHVDEMMMHVQQLSLASLCVKKQQPKKPEGTCPAAESRTRKVARLKAPFLKIEDESRKFRPFHHQFKSFPEISFLGPKDASPFEAPTTLGSMHHTRESKDGEPSPRSAAHTMPRRKKGYCECCQEAFEELHVHLQSAQHRSFALEAHLYAEVDRIIAQLSHSFADIPFQAGLPRWSGSPASDCDPLCPETLHPHQPSHPRAASPRIRKEDSCQASVTQGRAAGQQRWTESLDGVMGPPASHTCVSATTLLPALPKGSREQGCLCPCPASFTQSHLVTSLALLPGEWSPAEDMPLHPSQENSFAPADIPVKGPLLFPEARPWLMSARCWVRPFPFVTWGCLIPHDTTPLHEEVSPCPCLRLGYLYLLLTQSLWCRVRVPSLSTAGPIPRTSHPCTLAFPSYLNDHDLGHLCQAKPQGWNTPQPFLHCGFLAVDSG
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
49PhosphorylationGARKHPFSGKSFYLD
CCCCCCCCCCEEEEE		50.16-
133UbiquitinationKGSHPRPSRKPVDSV
CCCCCCCCCCCCCCC		54.9721963094
135AcetylationSHPRPSRKPVDSVPL
CCCCCCCCCCCCCCC		54.4519608861
135UbiquitinationSHPRPSRKPVDSVPL
CCCCCCCCCCCCCCC		54.4519608861
139PhosphorylationPSRKPVDSVPLSRGK
CCCCCCCCCCCHHHH		26.3528634120
143PhosphorylationPVDSVPLSRGKELLQ
CCCCCCCHHHHHHHH		32.6828634120
146UbiquitinationSVPLSRGKELLQKAI
CCCCHHHHHHHHHHH		44.0429967540
151UbiquitinationRGKELLQKAIRNQGS
HHHHHHHHHHHHCCC		45.83-
158PhosphorylationKAIRNQGSISGGGSG
HHHHHCCCCCCCCCC		12.1022210691
160PhosphorylationIRNQGSISGGGSGGS
HHHCCCCCCCCCCCC		32.8422210691
164PhosphorylationGSISGGGSGGSSSLL
CCCCCCCCCCCHHHH		43.1622210691
164UbiquitinationGSISGGGSGGSSSLL
CCCCCCCCCCCHHHH		43.1621963094
168PhosphorylationGGGSGGSSSLLTNAR
CCCCCCCHHHHHCHH		28.42-
169PhosphorylationGGSGGSSSLLTNARS
CCCCCCHHHHHCHHH		29.15-
172PhosphorylationGGSSSLLTNARSWGV
CCCHHHHHCHHHHCE		31.93-
198PhosphorylationVQQLSLASLCVKKQQ
HHHHHHHHHHHHCCC		27.8227050516
203 (in isoform 3)Ubiquitination-33.49-
203UbiquitinationLASLCVKKQQPKKPE
HHHHHHHCCCCCCCC		33.4921963094
208UbiquitinationVKKQQPKKPEGTCPA
HHCCCCCCCCCCCCH		55.79-
272PhosphorylationEAPTTLGSMHHTRES
CCCCCCCCCCCCCCC		20.3229759185
276PhosphorylationTLGSMHHTRESKDGE
CCCCCCCCCCCCCCC		22.8125627689
279PhosphorylationSMHHTRESKDGEPSP
CCCCCCCCCCCCCCC		32.5325159151
288PhosphorylationDGEPSPRSAAHTMPR
CCCCCCCCCCCCCCC		32.9428348404
292PhosphorylationSPRSAAHTMPRRKKG
CCCCCCCCCCCCCCC		24.9329449344
296 (in isoform 3)Phosphorylation-38.8822673903
298 (in isoform 3)Phosphorylation-53.9922673903
333 (in isoform 3)Phosphorylation-4.5728450419
337 (in isoform 3)Phosphorylation-1.7628634298
341 (in isoform 3)Phosphorylation-12.6628634298
389UbiquitinationAASPRIRKEDSCQAS
CCCCCCCCCCCCCCE		64.6021963094
397UbiquitinationEDSCQASVTQGRAAG
CCCCCCEEHHHHHCH		5.3321963094
415UbiquitinationWTESLDGVMGPPASH
CHHCCCCCCCCCCCC		3.9121963094
420UbiquitinationDGVMGPPASHTCVSA
CCCCCCCCCCCCEEH		19.6521963094
436UbiquitinationTLLPALPKGSREQGC
HHCCCCCCCCHHCCC		71.0721963094
500 (in isoform 3)Phosphorylation-22.6722115753
501 (in isoform 3)Phosphorylation-35.2822115753
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 DBF4B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DBF4B_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 DBF4B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
16189514
CDC7_HUMANCDC7physical
12065429
MDFI_HUMANMDFIphysical
19060904
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
MAP1B_HUMANMAP1Bphysical
26186194
MAP1S_HUMANMAP1Sphysical
26186194
CDC7_HUMANCDC7physical
26186194
EVA1C_HUMANEVA1Cphysical
26186194
MAP1S_HUMANMAP1Sphysical
28514442
CDC7_HUMANCDC7physical
28514442
MAP1B_HUMANMAP1Bphysical
28514442
EVA1C_HUMANEVA1Cphysical
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 DBF4B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135, AND MASS SPECTROMETRY.

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