CDC7_HUMAN - dbPTM
CDC7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDC7_HUMAN
UniProt AC O00311
Protein Name Cell division cycle 7-related protein kinase
Gene Name CDC7
Organism Homo sapiens (Human).
Sequence Length 574
Subcellular Localization Nucleus.
Protein Description Seems to phosphorylate critical substrates that regulate the G1/S phase transition and/or DNA replication. Can phosphorylates MCM2 and MCM3..
Protein Sequence MEASLGIQMDEPMAFSPQRDRFQAEGSLKKNEQNFKLAGVKKDIEKLYEAVPQLSNVFKIEDKIGEGTFSSVYLATAQLQVGPEEKIALKHLIPTSHPIRIAAELQCLTVAGGQDNVMGVKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVREYMLNLFKALKRIHQFGIVHRDVKPSNFLYNRRLKKYALVDFGLAQGTHDTKIELLKFVQSEAQQERCSQNKSHIITGNKIPLSGPVPKELDQQSTTKASVKRPYTNAQIQIKQGKDGKEGSVGLSVQRSVFGERNFNIHSSISHESPAVKLMKQSKTVDVLSRKLATKKKAISTKVMNSAVMRKTASSCPASLTCDCYATDKVCSICLSRRQQVAPRAGTPGFRAPEVLTKCPNQTTAIDMWSAGVIFLSLLSGRYPFYKASDDLTALAQIMTIRGSRETIQAAKTFGKSILCSKEVPAQDLRKLCERLRGMDSSTPKLTSDIQGHASHQPAISEKTDHKASCLVQTPPGQYSGNSFKKGDSNSCEHCFDEYNTNLEGWNEVPDEAYDLLDKLLDLNPASRITAEEALLHPFFKDMSL
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
4Phosphorylation----MEASLGIQMDE
----CCCCCCCCCCC		17.5226074081
16PhosphorylationMDEPMAFSPQRDRFQ
CCCCCCCCCCHHHHH		15.5817192257
27PhosphorylationDRFQAEGSLKKNEQN
HHHHHHCCCHHCHHC		28.6425159151
29UbiquitinationFQAEGSLKKNEQNFK
HHHHCCCHHCHHCCE		56.07-
30UbiquitinationQAEGSLKKNEQNFKL
HHHCCCHHCHHCCEE		71.64-
36SumoylationKKNEQNFKLAGVKKD
HHCHHCCEECCHHHH		45.00-
36SumoylationKKNEQNFKLAGVKKD
HHCHHCCEECCHHHH		45.00-
36UbiquitinationKKNEQNFKLAGVKKD
HHCHHCCEECCHHHH		45.00-
48PhosphorylationKKDIEKLYEAVPQLS
HHHHHHHHHHHHHHH		16.9527642862
59SumoylationPQLSNVFKIEDKIGE
HHHHCCEEEECCCCC		40.69-
59SumoylationPQLSNVFKIEDKIGE
HHHHCCEEEECCCCC		40.69-
59UbiquitinationPQLSNVFKIEDKIGE
HHHHCCEEEECCCCC		40.69-
90UbiquitinationPEEKIALKHLIPTSH
CHHHHHHHHHCCCCC		27.61-
179UbiquitinationGIVHRDVKPSNFLYN
CCCCCCCCCHHHCCC		47.20-
179SumoylationGIVHRDVKPSNFLYN
CCCCCCCCCHHHCCC		47.20-
179SumoylationGIVHRDVKPSNFLYN
CCCCCCCCCHHHCCC		47.20-
181PhosphorylationVHRDVKPSNFLYNRR
CCCCCCCHHHCCCCC		34.2019664994
191UbiquitinationLYNRRLKKYALVDFG
CCCCCCCEEEEECCC		40.11-
192PhosphorylationYNRRLKKYALVDFGL
CCCCCCEEEEECCCC		11.9929496907
207UbiquitinationAQGTHDTKIELLKFV
CCCCCHHHHHHHHHH		39.99-
212UbiquitinationDTKIELLKFVQSEAQ
HHHHHHHHHHHHHHH		56.992190698
216PhosphorylationELLKFVQSEAQQERC
HHHHHHHHHHHHHHH		29.60-
227UbiquitinationQERCSQNKSHIITGN
HHHHHCCCCCEECCC		35.46-
235SumoylationSHIITGNKIPLSGPV
CCEECCCCCCCCCCC		47.23-
235SumoylationSHIITGNKIPLSGPV
CCEECCCCCCCCCCC		47.23-
235UbiquitinationSHIITGNKIPLSGPV
CCEECCCCCCCCCCC		47.23-
239PhosphorylationTGNKIPLSGPVPKEL
CCCCCCCCCCCCCCC		35.3823312004
244SumoylationPLSGPVPKELDQQST
CCCCCCCCCCCCCCC		71.75-
244SumoylationPLSGPVPKELDQQST
CCCCCCCCCCCCCCC		71.75-
244UbiquitinationPLSGPVPKELDQQST
CCCCCCCCCCCCCCC		71.75-
253UbiquitinationLDQQSTTKASVKRPY
CCCCCCCCCCCCCCC		38.46-
255PhosphorylationQQSTTKASVKRPYTN
CCCCCCCCCCCCCCC		29.72-
257UbiquitinationSTTKASVKRPYTNAQ
CCCCCCCCCCCCCEE		45.20-
260PhosphorylationKASVKRPYTNAQIQI
CCCCCCCCCCEEEEE		19.3625690035
261PhosphorylationASVKRPYTNAQIQIK
CCCCCCCCCEEEEEE		27.1025690035
268SumoylationTNAQIQIKQGKDGKE
CCEEEEEEECCCCCC		36.30-
268SumoylationTNAQIQIKQGKDGKE
CCEEEEEEECCCCCC		36.3028112733
268UbiquitinationTNAQIQIKQGKDGKE
CCEEEEEEECCCCCC		36.30-
274UbiquitinationIKQGKDGKEGSVGLS
EEECCCCCCCCEEEE		69.87-
274SumoylationIKQGKDGKEGSVGLS
EEECCCCCCCCEEEE		69.87-
274SumoylationIKQGKDGKEGSVGLS
EEECCCCCCCCEEEE		69.87-
277PhosphorylationGKDGKEGSVGLSVQR
CCCCCCCCEEEEEEE		17.6920873877
281PhosphorylationKEGSVGLSVQRSVFG
CCCCEEEEEEEHHHC		15.4120873877
285PhosphorylationVGLSVQRSVFGERNF
EEEEEEEHHHCCCCE		12.52-
296PhosphorylationERNFNIHSSISHESP
CCCEECCCCCCCCCH		26.1020873877
297PhosphorylationRNFNIHSSISHESPA
CCEECCCCCCCCCHH		17.5920873877
299PhosphorylationFNIHSSISHESPAVK
EECCCCCCCCCHHHH		24.1321712546
302PhosphorylationHSSISHESPAVKLMK
CCCCCCCCHHHHHHH		16.8525159151
306UbiquitinationSHESPAVKLMKQSKT
CCCCHHHHHHHCCCH		44.99-
312UbiquitinationVKLMKQSKTVDVLSR
HHHHHCCCHHHHHHH		50.50-
318PhosphorylationSKTVDVLSRKLATKK
CCHHHHHHHHHHHHH		27.50-
331SumoylationKKKAISTKVMNSAVM
HHHHHHHHHHCHHHH		32.47-
331SumoylationKKKAISTKVMNSAVM
HHHHHHHHHHCHHHH		32.47-
331AcetylationKKKAISTKVMNSAVM
HHHHHHHHHHCHHHH		32.4730587557
331UbiquitinationKKKAISTKVMNSAVM
HHHHHHHHHHCHHHH		32.47-
340UbiquitinationMNSAVMRKTASSCPA
HCHHHHHHCCCCCCC		30.28-
348PhosphorylationTASSCPASLTCDCYA
CCCCCCCCEECCEEE		14.8919690332
356PhosphorylationLTCDCYATDKVCSIC
EECCEEECCCHHHHH		15.1819690332
358UbiquitinationCDCYATDKVCSICLS
CCEEECCCHHHHHHH		40.56-
361PhosphorylationYATDKVCSICLSRRQ
EECCCHHHHHHHCCC		21.2330631047
365PhosphorylationKVCSICLSRRQQVAP
CHHHHHHHCCCCCCC		22.4730631047
376PhosphorylationQVAPRAGTPGFRAPE
CCCCCCCCCCCCCHH		21.1810846177
386PhosphorylationFRAPEVLTKCPNQTT
CCCHHHHHCCCCCCC		35.46-
406PhosphorylationSAGVIFLSLLSGRYP
HHHHHHHHHHHCCCC		19.2628355574
415PhosphorylationLSGRYPFYKASDDLT
HHCCCCCEECCHHHH		10.92-
441UbiquitinationRETIQAAKTFGKSIL
HHHHHHHHHHCCHHH		47.61-
445AcetylationQAAKTFGKSILCSKE
HHHHHHCCHHHCCCC		30.0826051181
445UbiquitinationQAAKTFGKSILCSKE
HHHHHHCCHHHCCCC		30.08-
451UbiquitinationGKSILCSKEVPAQDL
CCHHHCCCCCCHHHH		62.83-
451AcetylationGKSILCSKEVPAQDL
CCHHHCCCCCCHHHH		62.8323749302
472PhosphorylationLRGMDSSTPKLTSDI
HCCCCCCCCCCCCCC		28.5228985074
474UbiquitinationGMDSSTPKLTSDIQG
CCCCCCCCCCCCCCC		65.57-
484PhosphorylationSDIQGHASHQPAISE
CCCCCCCCCCCCCCC		19.58-
490PhosphorylationASHQPAISEKTDHKA
CCCCCCCCCCCCCCC		34.8425159151
492UbiquitinationHQPAISEKTDHKASC
CCCCCCCCCCCCCEE		53.08-
493PhosphorylationQPAISEKTDHKASCL
CCCCCCCCCCCCEEE		39.0128555341
498PhosphorylationEKTDHKASCLVQTPP
CCCCCCCEEEEECCC		16.88-
503PhosphorylationKASCLVQTPPGQYSG
CCEEEEECCCCCCCC		24.7925159151
508PhosphorylationVQTPPGQYSGNSFKK
EECCCCCCCCCCCCC		25.1826074081
509PhosphorylationQTPPGQYSGNSFKKG
ECCCCCCCCCCCCCC		24.5025159151
512PhosphorylationPGQYSGNSFKKGDSN
CCCCCCCCCCCCCCC		41.8028985074
556PhosphorylationLLDLNPASRITAEEA
HHCCCHHHCCCHHHH		26.02-
559PhosphorylationLNPASRITAEEALLH
CCHHHCCCHHHHHHC		27.23-
570UbiquitinationALLHPFFKDMSL---
HHHCHHHHCCCC---		53.56-
573PhosphorylationHPFFKDMSL------
CHHHHCCCC------		40.85-
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
216SPhosphorylationKinaseCDC7O00311
PSP
239SPhosphorylationKinaseCDC7O00311
PSP
277SPhosphorylationKinaseCDC7O00311
PSP
285SPhosphorylationKinaseCDC7O00311
PSP
296SPhosphorylationKinaseCDC7O00311
PSP
297SPhosphorylationKinaseCDC7O00311
PSP
318SPhosphorylationKinaseCDC7O00311
PSP
376TPhosphorylationKinaseCDK1P06493
PSP
376TPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDC7_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 CDC7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCM2_HUMANMCM2physical
12614612
DBF4A_HUMANDBF4physical
12614612
DBF4A_HUMANDBF4physical
10373557
ORC1_HUMANORC1physical
12614612
ORC6_HUMANORC6physical
12614612
MCM4_HUMANMCM4physical
12614612
MCM5_HUMANMCM5physical
12614612
MCM7_HUMANMCM7physical
12614612
MCM2_XENLAmcm2physical
9250678
MCM3_HUMANMCM3physical
9250678
DBF4A_HUMANDBF4physical
10523313
CAF1A_HUMANCHAF1Aphysical
16826239
MCM2_HUMANMCM2physical
16826239
MCM2_MOUSEMcm2physical
20421204
MCM4_MOUSEMcm4physical
20421204
MCM6_MOUSEMcm6physical
20421204
RAD18_HUMANRAD18physical
21098111
MCM2_HUMANMCM2physical
17927916
CDK2_HUMANCDK2physical
17927916
MCM2_HUMANMCM2physical
16446360
TOB1_HUMANTOB1physical
23066029
MCM2_HUMANMCM2physical
23066029
A4_HUMANAPPphysical
21832049
MCM2_HUMANMCM2physical
10846177
CDC7_HUMANCDC7physical
10846177
DBF4A_HUMANDBF4physical
10846177
MCM4_HUMANMCM4physical
10846177
MCM6_HUMANMCM6physical
10846177
MCM7_HUMANMCM7physical
10846177
ORC6_HUMANORC6physical
15232106
MCM10_HUMANMCM10physical
15232106
CDN1A_HUMANCDKN1Aphysical
15232106
CDN2A_HUMANCDKN2Aphysical
15232106
ARF_HUMANCDKN2Aphysical
15232106
MCM3_HUMANMCM3physical
15232106
GRHPR_HUMANGRHPRphysical
21988832
CDK9_HUMANCDK9physical
21988832
ALAT1_HUMANGPTphysical
21988832
IF122_HUMANIFT122physical
27173435
BRD4_HUMANBRD4genetic
27453043
RS11_HUMANRPS11genetic
27453043
ING5_HUMANING5genetic
27453043
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 CDC7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-27; TYR-508 AND SER-509,AND MASS 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-16 AND SER-27, 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 THR-503, AND MASSSPECTROMETRY.

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