CDK14_HUMAN - dbPTM
CDK14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDK14_HUMAN
UniProt AC O94921
Protein Name Cyclin-dependent kinase 14
Gene Name CDK14
Organism Homo sapiens (Human).
Sequence Length 469
Subcellular Localization Cell membrane
Peripheral membrane protein. Cytoplasm. Nucleus. Recruited to the cell membrane by CCNY.
Protein Description Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport..
Protein Sequence MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDEICVTKMSTRNCQGMDSVIKPLDTIPEDKKVRVQRTQSTFDPFEKPANQVKRVHSENNACINFKTSSTGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTLYSSKNLRQAWNKLSYVNHAEDLASKLLQCSPKNRLSAQAALSHEYFSDLPPRLWELTDMSSIFTVPNVRLQPEAGESMRAFGKNNSYGKSLSNSKH
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
22PhosphorylationKMKKLRRTLSESFSR
HHHHHHHHHHHHHHH		28.3629255136
24PhosphorylationKKLRRTLSESFSRIA
HHHHHHHHHHHHHHH		30.4923401153
26PhosphorylationLRRTLSESFSRIALK
HHHHHHHHHHHHHCC		25.7529255136
28PhosphorylationRTLSESFSRIALKKD
HHHHHHHHHHHCCCC		31.8623403867
45PhosphorylationTFDEICVTKMSTRNC
CHHHHHEEECCCCCC		19.3329083192
48PhosphorylationEICVTKMSTRNCQGM
HHHEEECCCCCCCCC		26.2729083192
49PhosphorylationICVTKMSTRNCQGMD
HHEEECCCCCCCCCC		23.5429083192
60PhosphorylationQGMDSVIKPLDTIPE
CCCCCCCCCCCCCCC		37.0524719451
76PhosphorylationKKVRVQRTQSTFDPF
CCEEEEEECCCCCCC		15.1330266825
77PhosphorylationKVRVQRTQSTFDPFE
CEEEEEECCCCCCCC		42.5424719451
78PhosphorylationVRVQRTQSTFDPFEK
EEEEEECCCCCCCCC		30.3523401153
79PhosphorylationRVQRTQSTFDPFEKP
EEEEECCCCCCCCCC		23.4130266825
85UbiquitinationSTFDPFEKPANQVKR
CCCCCCCCCHHHCEE		50.22-
94PhosphorylationANQVKRVHSENNACI
HHHCEEECCCCCEEE		33.1724719451
95PhosphorylationNQVKRVHSENNACIN
HHCEEECCCCCEEEE		38.8823401153
101PhosphorylationHSENNACINFKTSST
CCCCCEEEEEECCCC		6.7124719451
104PhosphorylationNNACINFKTSSTGKE
CCEEEEEECCCCCCC		42.9027251275
105PhosphorylationNACINFKTSSTGKES
CEEEEEECCCCCCCC		24.6327251275
106PhosphorylationACINFKTSSTGKESP
EEEEEECCCCCCCCC		26.8826699800
107PhosphorylationCINFKTSSTGKESPK
EEEEECCCCCCCCCC		46.5426699800
108PhosphorylationINFKTSSTGKESPKV
EEEECCCCCCCCCCC		52.6326699800
112PhosphorylationTSSTGKESPKVRRHS
CCCCCCCCCCCCCCC		33.2428985074
116PhosphorylationGKESPKVRRHSSPSS
CCCCCCCCCCCCCCC		36.4024719451
119PhosphorylationSPKVRRHSSPSSPTS
CCCCCCCCCCCCCCC		41.9823927012
120PhosphorylationPKVRRHSSPSSPTSP
CCCCCCCCCCCCCCC		23.7523927012
122PhosphorylationVRRHSSPSSPTSPKF
CCCCCCCCCCCCCCC		51.3923927012
123PhosphorylationRRHSSPSSPTSPKFG
CCCCCCCCCCCCCCC		35.2623927012
125PhosphorylationHSSPSSPTSPKFGKA
CCCCCCCCCCCCCCC		60.6623927012
126PhosphorylationSSPSSPTSPKFGKAD
CCCCCCCCCCCCCCC		29.4923927012
134PhosphorylationPKFGKADSYEKLEKL
CCCCCCCCHHHHHHH		39.8023401153
135PhosphorylationKFGKADSYEKLEKLG
CCCCCCCHHHHHHHC		20.0323403867
140UbiquitinationDSYEKLEKLGEGSYA
CCHHHHHHHCCCCCE		72.70-
145PhosphorylationLEKLGEGSYATVYKG
HHHHCCCCCEEEEEC		13.8027155012
146PhosphorylationEKLGEGSYATVYKGK
HHHCCCCCEEEEECC		19.6925884760
148PhosphorylationLGEGSYATVYKGKSK
HCCCCCEEEEECCCC		19.0127155012
154PhosphorylationATVYKGKSKVNGKLV
EEEEECCCCCCCEEE		50.9723909892
183PhosphorylationFTAIREASLLKGLKH
CHHHHHHHHHHCCHH		29.4924719451
202PhosphorylationLLHDIIHTKETLTLV
EEEEHHCCHHHHHHH		21.84-
271UbiquitinationISDTGELKLADFGLA
ECCCCCEEEHHHCCC		37.01-
297PhosphorylationNEVVTLWYRPPDVLL
CCEEEEEECCCCEEC		19.1622817900
387PhosphorylationRQAWNKLSYVNHAED
HHHHHHHHCCCHHHH		28.7529083192
388PhosphorylationQAWNKLSYVNHAEDL
HHHHHHHCCCHHHHH		18.7329083192
397PhosphorylationNHAEDLASKLLQCSP
CHHHHHHHHHHCCCC		31.0029083192
403PhosphorylationASKLLQCSPKNRLSA
HHHHHCCCCCCCHHH		26.4229083192
450PhosphorylationLQPEAGESMRAFGKN
ECCCCHHHHHHHCCC		16.7923403867
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 CDK14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDK14_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 CDK14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEPT8_HUMANSEPT8physical
12098780
CCND3_HUMANCCND3physical
17517622
CDN1A_HUMANCDKN1Aphysical
17517622
CCNY_HUMANCCNYphysical
19524571
CDK14_HUMANCDK14physical
19524571
RB_HUMANRB1physical
19524571
RB_HUMANRB1physical
17517622
CDK14_HUMANCDK14physical
23602568
CDN1A_HUMANCDKN1Aphysical
23602568
RBM14_HUMANRBM14physical
23602568
KCC1A_HUMANCAMK1physical
23602568
TOP1_HUMANTOP1physical
23602568
CCNY_HUMANCCNYphysical
24794231
CDK17_HUMANCDK17physical
26186194
ICK_HUMANICKphysical
26186194
CDN1A_HUMANCDKN1Aphysical
26186194
ICK_HUMANICKphysical
28514442
FGR_HUMANFGRphysical
28514442
CDN1A_HUMANCDKN1Aphysical
28514442
CDK17_HUMANCDK17physical
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 CDK14_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 THR-22; SER-24; THR-76;SER-95; SER-119; SER-120; SER-122; SER-123 AND SER-134, AND MASSSPECTROMETRY.
"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-24; SER-95 AND SER-134,AND MASS SPECTROMETRY.

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