CDK9_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CDK9_SCHPO
• UniProt AC: Q96WV9
• Protein Name: Probable cyclin-dependent kinase 9
• Gene Name: cdk9
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 591
• Subcellular Localization: Nucleus.
• Protein Description: Component of the positive transcription elongation factor b (P-TEFb) which consists of cdk9 and pch1, and which phosphorylates the C-terminal domain (CTD) of RNA polymerase II and spt5..
• Protein Sequence: MKRSSSVSVEDEKSARRKLDVVPKLHFVGCSHLTDYHLMEKLGEGTFGEVYKSQRRKDGKVYALKRILMHTEKEGFPITAIREIKILKSIKHENIIPLSDMTVVRADKKHRRRGSIYMVTPYMDHDLSGLLENPSVKFTEPQIKCYMKQLFAGTKYLHDQLILHRDLKAANLLIDNHGILKIADFGLARVITEESYANKNPGLPPPNRREYTGCVVTRWYRSPELLLGERRYTTAIDMWSVGCIMAEMYKGRPILQGSSDLDQLDKIFRLCGSPTQATMPNWEKLPGCEGVRSFPSHPRTLETAFFTFGKEMTSLCGAILTLNPDERLSASMALEHEYFTTPPYPANPSELQSYSASHEYDKRRKREQRDANSHAFEQTANGKRQFRFMTRGPSDPWYGIRRPNYNSQPQYQRGSYNREGGNMDRSRNVNYQPKRQQNFKPLTSDLPQKNSEFSETNAMNQTSNHSHADGQRYYRPEQDRSQRLRNPSDYGRQGRQSSQSQQPAWNVSSRYQNNSKVQTTSRASENADTNKTQHNIKYIDSYVPEYSIARQSANQKTNEQHPSSTSLHQQSTSDLKSPSFHENSNVDDTPK

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
4	Phosphorylation	----MKRSSSVSVED ----CCCCCCCCCCC	22.80	21712547
5	Phosphorylation	---MKRSSSVSVEDE ---CCCCCCCCCCCH	38.50	24763107
6	Phosphorylation	--MKRSSSVSVEDEK --CCCCCCCCCCCHH	21.47	29996109
8	Phosphorylation	MKRSSSVSVEDEKSA CCCCCCCCCCCHHHH	23.03	24763107
53	Phosphorylation	TFGEVYKSQRRKDGK CCHHHHHHHCCCCCC	15.95	21712547
211	Phosphorylation	PPPNRREYTGCVVTR CCCCCCCCCCEEEEE	13.45	28889911
212	Phosphorylation	PPNRREYTGCVVTRW CCCCCCCCCEEEEEE	21.25	28889911
557	Phosphorylation	RQSANQKTNEQHPSS HHHHCCCCCCCCCCC	33.94	29996109
565	Phosphorylation	NEQHPSSTSLHQQST CCCCCCCHHHCCCCC	39.38	28889911
572	Phosphorylation	TSLHQQSTSDLKSPS HHHCCCCCCCCCCCC	23.17	29996109
573	Phosphorylation	SLHQQSTSDLKSPSF HHCCCCCCCCCCCCC	46.31	21712547
577	Phosphorylation	QSTSDLKSPSFHENS CCCCCCCCCCCCCCC	32.83	28889911
579	Phosphorylation	TSDLKSPSFHENSNV CCCCCCCCCCCCCCC	46.45	28889911
584	Phosphorylation	SPSFHENSNVDDTPK CCCCCCCCCCCCCCC	34.93	29996109
589	Phosphorylation	ENSNVDDTPK----- CCCCCCCCCC-----	28.63	24763107

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CDK9_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CDK9_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CDK9_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CG1C_SCHPO	pch1	physical	12475973
CG1C_SCHPO	pch1	physical	16428435
MCES_SCHPO	pcm1	physical	16428435
SPT5_SCHPO	spt5	physical	12904290
CDK9_SCHPO	cdk9	physical	12904290
RPB1_SCHPO	rpb1	physical	20605454
SPT5_SCHPO	spt5	physical	22508988
SPB1_SCHPO	spb1	physical	22508988
IMA3_SCHPO	SPCC550.11	genetic	22681890
RIA1_SCHPO	ria1	genetic	22681890
YH04_SCHPO	SPBC1685.04	genetic	22681890
YO88_SCHPO	SPBC21D10.08c	genetic	22681890
RPB1_SCHPO	rpb1	physical	25691663

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211; THR-212; THR-565AND SER-577, AND MASS SPECTROMETRY.
PubMed: 18257517