dbPTM

CDK10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDK10_HUMAN
UniProt AC	Q15131
Protein Name	Cyclin-dependent kinase 10
Gene Name	CDK10
Organism	Homo sapiens (Human).
Sequence Length	360
Subcellular Localization	Cytoplasm, cytoskeleton, cilium basal body .
Protein Description	Cyclin-dependent kinase that phosphorylates the transcription factor ETS2 (in vitro) and positively controls its proteasomal degradation (in cells). [PubMed: 24218572 Involved in the regulation of actin cytoskeleton organization through the phosphorylation of actin dynamics regulators such as PKN2. Is a negative regulator of ciliogenesis through phosphorylation of PKN2 and promotion of RhoA signaling]
Protein Sequence	MAEPDLECEQIRLKCIRKEGFFTVPPEHRLGRCRSVKEFEKLNRIGEGTYGIVYRARDTQTDEIVALKKVRMDKEKDGIPISSLREITLLLRLRHPNIVELKEVVVGNHLESIFLVMGYCEQDLASLLENMPTPFSEAQVKCIVLQVLRGLQYLHRNFIIHRDLKVSNLLMTDKGCVKTADFGLARAYGVPVKPMTPKVVTLWYRAPELLLGTTTQTTSIDMWAVGCILAELLAHRPLLPGTSEIHQIDLIVQLLGTPSENIWPGFSKLPLVGQYSLRKQPYNNLKHKFPWLSEAGLRLLHFLFMYDPKKRATAGDCLESSYFKEKPLPCEPELMPTFPHHRNKRAAPATSEGQSKRCKP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Ubiquitination	RSVKEFEKLNRIGEG CCHHHHHHHHCCCCC	57.28	-
49	Phosphorylation	LNRIGEGTYGIVYRA HHCCCCCCEEEEEEE	17.80	26074081
50	Phosphorylation	NRIGEGTYGIVYRAR HCCCCCCEEEEEEEE	18.73	25159151
54	Phosphorylation	EGTYGIVYRARDTQT CCCEEEEEEEECCCC	9.16	26074081
61	Phosphorylation	YRARDTQTDEIVALK EEEECCCCCEEEEEE	37.38	20071362
68	Ubiquitination	TDEIVALKKVRMDKE CCEEEEEEECCCCCC	39.21	21906983
68 (in isoform 1)	Ubiquitination	-	39.21	21890473
68	Ubiquitination	TDEIVALKKVRMDKE CCEEEEEEECCCCCC	39.21	21890473
69	Ubiquitination	DEIVALKKVRMDKEK CEEEEEEECCCCCCC	35.60	-
70	Ubiquitination	EIVALKKVRMDKEKD EEEEEEECCCCCCCC	6.15	21890473
76	Ubiquitination	KVRMDKEKDGIPISS ECCCCCCCCCCCHHH	67.98	21890473
76 (in isoform 1)	Ubiquitination	-	67.98	21890473
76	Ubiquitination	KVRMDKEKDGIPISS ECCCCCCCCCCCHHH	67.98	21890473
76	Ubiquitination	KVRMDKEKDGIPISS ECCCCCCCCCCCHHH	67.98	21890473
82	Phosphorylation	EKDGIPISSLREITL CCCCCCHHHHHHHHH	20.26	24719451
83	Phosphorylation	KDGIPISSLREITLL CCCCCHHHHHHHHHH	31.97	25954137
133	Phosphorylation	SLLENMPTPFSEAQV HHHHCCCCCCCHHHH	26.63	-
178	Ubiquitination	MTDKGCVKTADFGLA ECCCCCCCCCCCCHH	41.91	-
178	Acetylation	MTDKGCVKTADFGLA ECCCCCCCCCCCCHH	41.91	25953088
188	Phosphorylation	DFGLARAYGVPVKPM CCCHHHHHCCCCCCC	17.07	23403867
193	Ubiquitination	RAYGVPVKPMTPKVV HHHCCCCCCCCCCEE	24.01	-
196	Phosphorylation	GVPVKPMTPKVVTLW CCCCCCCCCCEEEEE	28.60	30266825
204	Phosphorylation	PKVVTLWYRAPELLL CCEEEEEEECCHHHC	10.46	24719451
249 (in isoform 4)	Phosphorylation	-	24.63	-
250 (in isoform 4)	Phosphorylation	-	4.40	-
251 (in isoform 4)	Phosphorylation	-	1.32	-
276	Phosphorylation	LPLVGQYSLRKQPYN CCCCEECCCCCCCCC	17.51	24719451
320	Phosphorylation	TAGDCLESSYFKEKP CHHHHCCCHHCCCCC	19.86	-
321	Phosphorylation	AGDCLESSYFKEKPL HHHHCCCHHCCCCCC	25.80	-
322	Phosphorylation	GDCLESSYFKEKPLP HHHCCCHHCCCCCCC	28.13	-
350	Phosphorylation	NKRAAPATSEGQSKR CCCCCCCCCCCCCCC	26.67	28985074

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 CDK10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CDK10_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 CDK10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ETS2_HUMAN	ETS2	physical	11313931
PIN1_HUMAN	PIN1	physical	22158035
SEMG2_HUMAN	SEMG2	physical	23602568
PLSI_HUMAN	PLS1	physical	26186194
RNH2A_HUMAN	RNASEH2A	physical	26186194
FA84B_HUMAN	FAM84B	physical	26186194
ACTBL_HUMAN	ACTBL2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
TCPB_HUMAN	CCT2	physical	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 CDK10_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-196, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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 THR-196, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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 THR-196, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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 THR-196, AND MASSSPECTROMETRY.	17192257 [Abstract]