CCNO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCNO_HUMAN
• UniProt AC: P22674
• Protein Name: Cyclin-O
• Gene Name: CCNO
• Organism: Homo sapiens (Human).
• Sequence Length: 350
• Subcellular Localization: Cytoplasm . Localizes to the apical part of cytoplasm.
• Protein Description: Specifically required for generation of multiciliated cells, possibly by promoting a cell cycle state compatible with centriole amplification and maturation. Acts downstream of MCIDAS to promote mother centriole amplification and maturation in preparation for apical docking..
• Protein Sequence: MVTPCPTSPSSPAARAGRRDNDQNLRAPVKKSRRPRLRRKQPLHPLNPCPLPGDSGICDLFESPSSGSDGAESPSAARGGSPLPGPAQPVAQLDLQTFRDYGQSCYAFRKAQESHFHPREALARQPQVTAESRCKLLSWLIPVHRQFGLSFESLCLTVNTLDRFLTTTPVAADCFQLLGVTSLLIACKQVEVHPPRVKQLLALCCGAFSRQQLCNLECIVLHKLHFTLGAPTISFFLEHFTHARVEAGQAEASEALEAQALARGVAELSLADYAFTSYSPSLLAICCLALADRMLRVSRPVDLRLGDHPEAALEDCMGKLQLLVAINSTSLTHMLPVQICEKCSLPPSSK

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
3	Phosphorylation	-----MVTPCPTSPS -----CCCCCCCCCC	20.20	30266825
7	Phosphorylation	-MVTPCPTSPSSPAA -CCCCCCCCCCCHHH	61.05	30266825
8	Phosphorylation	MVTPCPTSPSSPAAR CCCCCCCCCCCHHHH	14.13	30266825
10	Phosphorylation	TPCPTSPSSPAARAG CCCCCCCCCHHHHCC	49.04	30266825
11	Phosphorylation	PCPTSPSSPAARAGR CCCCCCCCHHHHCCC	23.18	30266825
81	Phosphorylation	PSAARGGSPLPGPAQ CCHHCCCCCCCCCCC	26.53	30278072
110	Ubiquitination	QSCYAFRKAQESHFH HHHHHHHHHHHHCCC	48.22	29967540
129	Phosphorylation	LARQPQVTAESRCKL HHCCCCCCHHHHHHH	21.33	28634120
298	Phosphorylation	ADRMLRVSRPVDLRL HHHHHHCCCCCCCCC	25.16	-

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
81	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of CCNO_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 615872: Ciliary dyskinesia, primary, 29 (CILD29)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-3; THR-7; SER-8; SER-11AND SER-81, AND MASS SPECTROMETRY.
PubMed: 19369195

"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-8 AND SER-11, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-81, AND MASSSPECTROMETRY.
PubMed: 18691976