CDK18_HUMAN - dbPTM
CDK18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDK18_HUMAN
UniProt AC Q07002
Protein Name Cyclin-dependent kinase 18
Gene Name CDK18
Organism Homo sapiens (Human).
Sequence Length 474
Subcellular Localization
Protein Description May play a role in signal transduction cascades in terminally differentiated cells..
Protein Sequence MIMNKMKNFKRRFSLSVPRTETIEESLAEFTEQFNQLHNRRNENLQLGPLGRDPPQECSTFSPTDSGEEPGQLSPGVQFQRRQNQRRFSMEDVSKRLSLPMDIRLPQEFLQKLQMESPDLPKPLSRMSRRASLSDIGFGKLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDLIHTDRSLTLVFEYLDSDLKQYLDHCGNLMSMHNVKIFMFQLLRGLAYCHHRKILHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCIHYEMATGRPLFPGSTVKEELHLIFRLLGTPTEETWPGVTAFSEFRTYSFPCYLPQPLINHAPRLDTDGIHLLSSLLLYESKSRMSAEAALSHSYFRSLGERVHQLEDTASIFSLKEIQLQKDPGYRGLAFQQPGRGKNRRQSIF
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
12PhosphorylationKMKNFKRRFSLSVPR
HCCCCHHHHCCCCCC
20.2330266825
14PhosphorylationKNFKRRFSLSVPRTE
CCCHHHHCCCCCCCH
28.9523927012
20PhosphorylationFSLSVPRTETIEESL
HCCCCCCCHHHHHHH
32.8328348404
57PhosphorylationLGRDPPQECSTFSPT
CCCCCCCCCCCCCCC
31.5623927012
58PhosphorylationGRDPPQECSTFSPTD
CCCCCCCCCCCCCCC
39.5328857561
60PhosphorylationDPPQECSTFSPTDSG
CCCCCCCCCCCCCCC
27.2918691976
62PhosphorylationPQECSTFSPTDSGEE
CCCCCCCCCCCCCCC
41.4118691976
64PhosphorylationECSTFSPTDSGEEPG
CCCCCCCCCCCCCCC
51.0523927012
72PhosphorylationDSGEEPGQLSPGVQF
CCCCCCCCCCCCHHH
16.2430278072
74PhosphorylationGEEPGQLSPGVQFQR
CCCCCCCCCCHHHHH
23.6019369195
87PhosphorylationQRRQNQRRFSMEDVS
HHHHHCCCCCHHHHH
21.3223401153
89PhosphorylationRQNQRRFSMEDVSKR
HHHCCCCCHHHHHHH
54.8018691976
89 (in isoform 3)Phosphorylation-54.8028978645
92PhosphorylationQRRFSMEDVSKRLSL
CCCCCHHHHHHHHCC
25.1223927012
93AcetylationRRFSMEDVSKRLSLP
CCCCHHHHHHHHCCC
58.15-
95 (in isoform 3)Phosphorylation-7.6822210691
96PhosphorylationSMEDVSKRLSLPMDI
CHHHHHHHHCCCCCC
34.1630266825
98PhosphorylationEDVSKRLSLPMDIRL
HHHHHHHCCCCCCCC
18.2819369195
115PhosphorylationEFLQKLQMESPDLPK
HHHHHHHHCCCCCCC
20.5528355574
117PhosphorylationLQKLQMESPDLPKPL
HHHHHHCCCCCCCCH
82.1619369195
123PhosphorylationESPDLPKPLSRMSRR
CCCCCCCCHHHHHHH
34.1723927012
126PhosphorylationDLPKPLSRMSRRASL
CCCCCHHHHHHHHCH
19.9429514088
128 (in isoform 3)Phosphorylation-22.6318691976
128PhosphorylationPKPLSRMSRRASLSD
CCCHHHHHHHHCHHH
22.6318691976
130PhosphorylationPLSRMSRRASLSDIG
CHHHHHHHHCHHHCC
26.9629255136
132PhosphorylationSRMSRRASLSDIGFG
HHHHHHHCHHHCCCC
25.3722167270
134PhosphorylationMSRRASLSDIGFGKL
HHHHHCHHHCCCCHH
4.4118669648
141PhosphorylationSDIGFGKLETYVKLD
HHCCCCHHHEEEEEE
44.0123927012
142PhosphorylationDIGFGKLETYVKLDK
HCCCCHHHEEEEEEE
6.0423927012
144UbiquitinationGFGKLETYVKLDKLG
CCCHHHEEEEEEECC
40.322189047
146 (in isoform 2)Ubiquitination-38.1121890473
147PhosphorylationKLETYVKLDKLGEGT
HHHEEEEEEECCCCE
69.6818691976
152PhosphorylationVKLDKLGEGTYATVF
EEEEECCCCEEEEEE
12.9917192257
153PhosphorylationKLDKLGEGTYATVFK
EEEECCCCEEEEEEE
15.9023927012
155PhosphorylationDKLGEGTYATVFKGR
EECCCCEEEEEEECC
18.9627273156
157PhosphorylationLGEGTYATVFKGRSK
CCCCEEEEEEECCCH
6.3618691976
162PhosphorylationYATVFKGRSKLTENL
EEEEEECCCHHHHHH
59.0520068231
164PhosphorylationTVFKGRSKLTENLVA
EEEECCCHHHHHHHH
26.9417924679
171UbiquitinationKLTENLVALKEIRLE
HHHHHHHHHHHHHCC
41.16-
173 (in isoform 2)Ubiquitination-6.1121890473
176 (in isoform 3)Ubiquitination-39.1321890473
184PhosphorylationLEHEEGAPCTAIREV
CCCCCCCCCCHHHHH
24.8628857561
185PhosphorylationEHEEGAPCTAIREVS
CCCCCCCCCHHHHHH
12.9318691976
187PhosphorylationEEGAPCTAIREVSLL
CCCCCCCHHHHHHHH
35.4818691976
190PhosphorylationAPCTAIREVSLLKNL
CCCCHHHHHHHHHCC
24.1924719451
203 (in isoform 3)Ubiquitination-1.7321890473
278UbiquitinationLLINERGELKLADFG
EEECCCCCEEEHHHC
37.01-
280 (in isoform 2)Ubiquitination-14.4321890473
289PhosphorylationADFGLARAKSVPTKT
HHHCCCCCCCCCCCC
32.1426074081
292PhosphorylationGLARAKSVPTKTYSN
CCCCCCCCCCCCCCC
33.5926074081
294PhosphorylationARAKSVPTKTYSNEV
CCCCCCCCCCCCCCE
34.3626074081
295PhosphorylationRAKSVPTKTYSNEVV
CCCCCCCCCCCCCEE
15.8526074081
296PhosphorylationAKSVPTKTYSNEVVT
CCCCCCCCCCCCEEE
31.5726074081
304PhosphorylationYSNEVVTLWYRPPDV
CCCCEEEEEECCCCE
19.1622817900
310 (in isoform 3)Ubiquitination-6.1321890473
376PhosphorylationTAFSEFRTYSFPCYL
EECCCCEEECCCEEC
23.3128857561
410PhosphorylationSSLLLYESKSRMSAE
HHHHHHCCCCCCCHH
42.3630206219
413PhosphorylationLLYESKSRMSAEAAL
HHHCCCCCCCHHHHH
23.1130206219
419PhosphorylationSRMSAEAALSHSYFR
CCCCHHHHHCHHHHH
12.9830206219
421PhosphorylationMSAEAALSHSYFRSL
CCHHHHHCHHHHHHH
23.6928857561
422PhosphorylationSAEAALSHSYFRSLG
CHHHHHCHHHHHHHH
9.5130206219
425PhosphorylationAALSHSYFRSLGERV
HHHCHHHHHHHHHHH
30.7230206219
436PhosphorylationGERVHQLEDTASIFS
HHHHHHHHHHHHEEE
16.9628857561
438PhosphorylationRVHQLEDTASIFSLK
HHHHHHHHHHEEEEE
26.6828857561
440PhosphorylationHQLEDTASIFSLKEI
HHHHHHHHEEEEEEE
6.92-
441PhosphorylationQLEDTASIFSLKEIQ
HHHHHHHEEEEEEEE
36.5420873877
443PhosphorylationEDTASIFSLKEIQLQ
HHHHHEEEEEEEECC
52.12-
463MethylationRGLAFQQPGRGKNRR
CCCCCCCCCCCCCCC
60.64-
470PhosphorylationPGRGKNRRQSIF---
CCCCCCCCCCCC---
24.9317192257
472PhosphorylationRGKNRRQSIF-----
CCCCCCCCCC-----
11.2418691976
502Phosphorylation-----------------------------------
-----------------------------------
18691976

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 CDK18_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDK18_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 CDK18_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
CCNK_HUMANCCNKphysical
16189514
A4_HUMANAPPphysical
21832049
PPP5_HUMANPPP5Cphysical
23602568
EF2_HUMANEEF2physical
23602568
MAGD2_HUMANMAGED2physical
23602568
BAG6_HUMANBAG6physical
23602568
PP2AB_HUMANPPP2CBphysical
23602568
NSRP1_HUMANNSRP1physical
23602568
LAR4B_HUMANLARP4Bphysical
23602568
GBB4_HUMANGNB4physical
23602568
METH_HUMANMTRphysical
23602568
EIF3I_HUMANEIF3Iphysical
23602568
CATB_HUMANCTSBphysical
23602568
UBL4A_HUMANUBL4Aphysical
23602568
CHIP_HUMANSTUB1physical
23602568
TRI27_HUMANTRIM27physical
25416956
PNMA1_HUMANPNMA1physical
25416956
MTUS2_HUMANMTUS2physical
25416956
CCDB1_HUMANCCNDBP1physical
25416956
TRI54_HUMANTRIM54physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
TSG10_HUMANTSGA10physical
25416956
LZTS2_HUMANLZTS2physical
25416956
K1C40_HUMANKRT40physical
25416956
MIPO1_HUMANMIPOL1physical
25416956
HS90A_HUMANHSP90AA1physical
26186194
HS90B_HUMANHSP90AB1physical
26186194
MTA2_HUMANMTA2physical
26186194
FKBP5_HUMANFKBP5physical
26186194
CDC37_HUMANCDC37physical
26186194
FGR_HUMANFGRphysical
26186194
CDK15_HUMANCDK15physical
26186194
DNLZ_HUMANDNLZphysical
26186194
RBM4_HUMANRBM4physical
26496610
RL37A_HUMANRPL37Aphysical
26496610
TRPS1_HUMANTRPS1physical
26496610
BAG6_HUMANBAG6physical
26496610
FXR1_HUMANFXR1physical
26496610
UBL4A_HUMANUBL4Aphysical
26496610
FUBP3_HUMANFUBP3physical
26496610
P3H1_HUMANP3H1physical
26496610
FP100_HUMANC17orf70physical
26496610
FKBP5_HUMANFKBP5physical
28514442
CDK15_HUMANCDK15physical
28514442
DNLZ_HUMANDNLZphysical
28514442
HS90A_HUMANHSP90AA1physical
28514442
FGR_HUMANFGRphysical
28514442
MTA2_HUMANMTA2physical
28514442
HS90B_HUMANHSP90AB1physical
28514442
RAB3I_HUMANRAB3IPphysical
27173435
CBY1_HUMANCBY1physical
27173435

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 CDK18_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-12; SER-14; SER-57;SER-72; SER-87; SER-96; SER-115; SER-130 AND THR-141, PHOSPHORYLATION[LARGE SCALE ANALYSIS] AT SER-89 (ISOFORM 3), AND MASS 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-12; SER-87 AND SER-130,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-12; SER-72; SER-87;SER-96; SER-115; SER-130; THR-155 AND SER-470, AND MASS SPECTROMETRY.
"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-12; SER-87 AND SER-130,AND MASS SPECTROMETRY.

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