CDK17_HUMAN - dbPTM
CDK17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDK17_HUMAN
UniProt AC Q00537
Protein Name Cyclin-dependent kinase 17
Gene Name CDK17
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization
Protein Description May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 (By similarity)..
Protein Sequence MKKFKRRLSLTLRGSQTIDESLSELAEQMTIEENSSKDNEPIVKNGRPPTSHSMHSFLHQYTGSFKKPPLRRPHSVIGGSLGSFMAMPRNGSRLDIVHENLKMGSDGESDQASGTSSDEVQSPTGVCLRNRIHRRISMEDLNKRLSLPADIRIPDGYLEKLQINSPPFDQPMSRRSRRASLSEIGFGKMETYIKLEKLGEGTYATVYKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKDLKQYMDDCGNIMSMHNVKLFLYQILRGLAYCHRRKVLHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPSQETWPGISSNEEFKNYNFPKYKPQPLINHAPRLDSEGIELITKFLQYESKKRVSAEEAMKHVYFRSLGPRIHALPESVSIFSLKEIQLQKDPGFRNSSYPETGHGKNRRQSMLF
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
9 (in isoform 2)Phosphorylation-19.9324719451
9PhosphorylationKKFKRRLSLTLRGSQ
CHHHHHHHHHHCCCH		19.9330266825
11PhosphorylationFKRRLSLTLRGSQTI
HHHHHHHHHCCCHHH		15.8429255136
37UbiquitinationTIEENSSKDNEPIVK
CCCCCCCCCCCCCCC		65.48-
64PhosphorylationFLHQYTGSFKKPPLR
HHHHHHCCCCCCCCC		26.54-
75PhosphorylationPPLRRPHSVIGGSLG
CCCCCCCCEECCCHH		20.3629255136
75 (in isoform 2)Phosphorylation-20.3624719451
80 (in isoform 2)Phosphorylation-25.0924719451
80PhosphorylationPHSVIGGSLGSFMAM
CCCEECCCHHHHHCC		25.0929255136
83PhosphorylationVIGGSLGSFMAMPRN
EECCCHHHHHCCCCC		19.6929255136
92 (in isoform 2)Phosphorylation-32.9724719451
92PhosphorylationMAMPRNGSRLDIVHE
HCCCCCCCCCEEEEC		32.9723401153
105 (in isoform 2)Phosphorylation-38.6624719451
105PhosphorylationHENLKMGSDGESDQA
ECCCCCCCCCCCCCC		38.6623927012
109PhosphorylationKMGSDGESDQASGTS
CCCCCCCCCCCCCCC		40.3223403867
113PhosphorylationDGESDQASGTSSDEV
CCCCCCCCCCCCCCC		36.6529255136
115PhosphorylationESDQASGTSSDEVQS
CCCCCCCCCCCCCCC		23.6729255136
116PhosphorylationSDQASGTSSDEVQSP
CCCCCCCCCCCCCCC		39.0429255136
117PhosphorylationDQASGTSSDEVQSPT
CCCCCCCCCCCCCCC		37.3129255136
122PhosphorylationTSSDEVQSPTGVCLR
CCCCCCCCCCCCHHH		29.6123401153
122 (in isoform 2)Phosphorylation-29.6124719451
124PhosphorylationSDEVQSPTGVCLRNR
CCCCCCCCCCHHHHH		47.7129255136
137 (in isoform 2)Phosphorylation-17.8224719451
137PhosphorylationNRIHRRISMEDLNKR
HHHHCCCCHHHHHHH		17.8229255136
143UbiquitinationISMEDLNKRLSLPAD
CCHHHHHHHHCCCCC		63.11-
146 (in isoform 2)Phosphorylation-36.0224719451
146PhosphorylationEDLNKRLSLPADIRI
HHHHHHHCCCCCCCC		36.0229255136
157PhosphorylationDIRIPDGYLEKLQIN
CCCCCCCHHHHCCCC		21.0421406692
160UbiquitinationIPDGYLEKLQINSPP
CCCCHHHHCCCCCCC		43.0021890473
165 (in isoform 2)Phosphorylation-35.2624719451
165PhosphorylationLEKLQINSPPFDQPM
HHHCCCCCCCCCCCC		35.2630266825
173PhosphorylationPPFDQPMSRRSRRAS
CCCCCCCCHHHHCCC		31.0930266825
176PhosphorylationDQPMSRRSRRASLSE
CCCCCHHHHCCCHHH		25.6323403867
180 (in isoform 2)Phosphorylation-30.5324719451
180PhosphorylationSRRSRRASLSEIGFG
CHHHHCCCHHHHCCC		30.5329255136
182PhosphorylationRSRRASLSEIGFGKM
HHHCCCHHHHCCCHH		25.3630266825
188UbiquitinationLSEIGFGKMETYIKL
HHHHCCCHHHEEEEE		31.16-
191PhosphorylationIGFGKMETYIKLEKL
HCCCHHHEEEEEEEC		27.3523927012
192PhosphorylationGFGKMETYIKLEKLG
CCCHHHEEEEEEECC		5.2423927012
194UbiquitinationGKMETYIKLEKLGEG
CHHHEEEEEEECCCC		39.9321890473
197UbiquitinationETYIKLEKLGEGTYA
HEEEEEEECCCCEEE		72.7021906983
202PhosphorylationLEKLGEGTYATVYKG
EEECCCCEEEEEEEC		12.9929255136
203PhosphorylationEKLGEGTYATVYKGR
EECCCCEEEEEEECC		15.9027273156
205PhosphorylationLGEGTYATVYKGRSK
CCCCEEEEEEECCCH		17.6029255136
207PhosphorylationEGTYATVYKGRSKLT
CCEEEEEEECCCHHH		11.9029255136
208UbiquitinationGTYATVYKGRSKLTE
CEEEEEEECCCHHHH		43.44-
212UbiquitinationTVYKGRSKLTENLVA
EEEECCCHHHHHHHH		59.05-
221UbiquitinationTENLVALKEIRLEHE
HHHHHHHHHHHCCCC		41.1621890473
234PhosphorylationHEEGAPCTAIREVSL
CCCCCCCCHHHHHHH		24.8628857561
240PhosphorylationCTAIREVSLLKDLKH
CCHHHHHHHHHHHHC		24.1924719451
243UbiquitinationIREVSLLKDLKHANI
HHHHHHHHHHHCCCE		67.33-
246UbiquitinationVSLLKDLKHANIVTL
HHHHHHHHCCCEEEH		51.29-
275UbiquitinationEYLDKDLKQYMDDCG
HHHCHHHHHHHHHHC		49.90-
315UbiquitinationKVLHRDLKPQNLLIN
CHHCCCCCHHCEEEC		49.17-
324UbiquitinationQNLLINEKGELKLAD
HCEEECCCCCEEEHH		53.87-
328UbiquitinationINEKGELKLADFGLA
ECCCCCEEEHHHHCC		37.0121890473
328MethylationINEKGELKLADFGLA
ECCCCCEEEHHHHCC		37.0123644510
338UbiquitinationDFGLARAKSVPTKTY
HHHCCCCCCCCCCCC		46.57-
339PhosphorylationFGLARAKSVPTKTYS
HHCCCCCCCCCCCCC		32.1426074081
342PhosphorylationARAKSVPTKTYSNEV
CCCCCCCCCCCCCCE		33.5926074081
344PhosphorylationAKSVPTKTYSNEVVT
CCCCCCCCCCCCEEE		34.3626074081
345PhosphorylationKSVPTKTYSNEVVTL
CCCCCCCCCCCEEEE		15.8526074081
346PhosphorylationSVPTKTYSNEVVTLW
CCCCCCCCCCEEEEE		31.5726074081
423UbiquitinationISSNEEFKNYNFPKY
CCCCHHHHCCCCCCC		62.90-
425PhosphorylationSNEEFKNYNFPKYKP
CCHHHHCCCCCCCCC		20.8329496907
430PhosphorylationKNYNFPKYKPQPLIN
HCCCCCCCCCCCCCC		28.3029496907
431UbiquitinationNYNFPKYKPQPLINH
CCCCCCCCCCCCCCC		43.21-
444PhosphorylationNHAPRLDSEGIELIT
CCCCCCCHHHHHHHH		42.1722817900
452UbiquitinationEGIELITKFLQYESK
HHHHHHHHHHHHHHH		36.76-
456PhosphorylationLITKFLQYESKKRVS
HHHHHHHHHHHCCCC		25.0729496907
458PhosphorylationTKFLQYESKKRVSAE
HHHHHHHHHCCCCHH		38.2429496907
459UbiquitinationKFLQYESKKRVSAEE
HHHHHHHHCCCCHHH		32.43-
469AcetylationVSAEEAMKHVYFRSL
CCHHHHHHHHHHHHC		36.6530591183
469UbiquitinationVSAEEAMKHVYFRSL
CCHHHHHHHHHHHHC		36.65-
486PhosphorylationRIHALPESVSIFSLK
HHCCCCCCEEEEEEC		21.1620071362
488PhosphorylationHALPESVSIFSLKEI
CCCCCCEEEEEECEE		27.4820873877
491PhosphorylationPESVSIFSLKEIQLQ
CCCEEEEEECEEECC		36.5420873877
493UbiquitinationSVSIFSLKEIQLQKD
CEEEEEECEEECCCC		52.1221890473
493UbiquitinationSVSIFSLKEIQLQKD
CEEEEEECEEECCCC		52.1221890473
499UbiquitinationLKEIQLQKDPGFRNS
ECEEECCCCCCCCCC		74.59-
506PhosphorylationKDPGFRNSSYPETGH
CCCCCCCCCCCCCCC		27.3028348404
506 (in isoform 2)Phosphorylation-27.3029083192
507PhosphorylationDPGFRNSSYPETGHG
CCCCCCCCCCCCCCC		48.5328348404
507 (in isoform 2)Phosphorylation-48.5329083192
508 (in isoform 2)Phosphorylation-12.6129083192
511 (in isoform 2)Phosphorylation-29.9428450419
515UbiquitinationYPETGHGKNRRQSML
CCCCCCCCCCCCCCC		41.42-
520PhosphorylationHGKNRRQSMLF----
CCCCCCCCCCC----		18.6821712546
520 (in isoform 2)Phosphorylation-18.6825849741
523 (in isoform 2)Phosphorylation-7.6325159151
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 CDK17_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDK17_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 CDK17_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
KAPCG_HUMANPRKACGphysical
21988832
PTMA_HUMANPTMAphysical
23602568
2ABA_HUMANPPP2R2Aphysical
23602568
PP2AB_HUMANPPP2CBphysical
23602568
G3P_HUMANGAPDHphysical
23602568
NOP10_HUMANNOP10physical
23602568
P2R3A_HUMANPPP2R3Aphysical
26186194
TDRD7_HUMANTDRD7physical
26186194
SUGP1_HUMANSUGP1physical
26186194
DHYS_HUMANDHPSphysical
26186194
2A5E_HUMANPPP2R5Ephysical
26186194
CL043_HUMANC12orf43physical
26186194
FEM1A_HUMANFEM1Aphysical
26186194
P2R3A_HUMANPPP2R3Aphysical
28514442
TDRD7_HUMANTDRD7physical
28514442
2A5E_HUMANPPP2R5Ephysical
28514442
FEM1A_HUMANFEM1Aphysical
28514442
SUGP1_HUMANSUGP1physical
28514442
HDGR3_HUMANHDGFRP3physical
28514442
CL043_HUMANC12orf43physical
28514442
DHYS_HUMANDHPSphysical
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 CDK17_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-165 AND SER-180, ANDMASS SPECTROMETRY.
"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-9; SER-75; SER-80;SER-105; THR-115; SER-116; SER-122; SER-137; SER-146; SER-165; SER-180AND THR-202, 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-165, 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-146; SER-165 ANDSER-180, 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-9; SER-105; SER-122;SER-137; SER-146; SER-165; SER-180; THR-205 AND SER-520, AND MASSSPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-137 AND SER-180,AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, AND MASSSPECTROMETRY.

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