CCND3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCND3_MOUSE
• UniProt AC: P30282
• Protein Name: G1/S-specific cyclin-D3
• Gene Name: Ccnd3
• Organism: Mus musculus (Mouse).
• Sequence Length: 292
• Subcellular Localization: Nucleus. Cytoplasm. Membrane. Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated to the nucleus through interaction with KIP/CIP family members..
• Protein Description: Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex..
• Protein Sequence: MELLCCEGTRHAPRAGPDPRLLGDQRVLQSLLRLEERYVPRASYFQCVQKEIKPHMRKMLAYWMLEVCEEQRCEEDVFPLAMNYLDRYLSCVPTRKAQLQLLGTVCLLLASKLRETTPLTIEKLCIYTDQAVAPWQLREWEVLVLGKLKWDLAAVIAHDFLALILHRLSLPSDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVLGLGACSMSADELTELLAGITGTEVDCLRACQEQIEAALRESLREAAQTAPSPVPKAPRGSSSQGPSQTSTPTDVTAIHL

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
30	Phosphorylation	GDQRVLQSLLRLEER CCHHHHHHHHHHHHH	25.80	21743459
254	Phosphorylation	IEAALRESLREAAQT HHHHHHHHHHHHHHH	26.71	26060331
261	Phosphorylation	SLREAAQTAPSPVPK HHHHHHHHCCCCCCC	35.49	28833060
264	Phosphorylation	EAAQTAPSPVPKAPR HHHHHCCCCCCCCCC	35.74	25521595
273	Phosphorylation	VPKAPRGSSSQGPSQ CCCCCCCCCCCCCCC	28.26	25619855
274	Phosphorylation	PKAPRGSSSQGPSQT CCCCCCCCCCCCCCC	29.51	25619855
275	Phosphorylation	KAPRGSSSQGPSQTS CCCCCCCCCCCCCCC	40.63	25619855
279	Phosphorylation	GSSSQGPSQTSTPTD CCCCCCCCCCCCCCC	53.57	25619855
281	Phosphorylation	SSQGPSQTSTPTDVT CCCCCCCCCCCCCCE	38.62	25619855
282	Phosphorylation	SQGPSQTSTPTDVTA CCCCCCCCCCCCCEE	25.42	25619855
283	Phosphorylation	QGPSQTSTPTDVTAI CCCCCCCCCCCCEEE	33.33	25293948
285	Phosphorylation	PSQTSTPTDVTAIHL CCCCCCCCCCEEECC	43.09	25619855
288	Phosphorylation	TSTPTDVTAIHL--- CCCCCCCEEECC---	23.78	25619855

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
283	T	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
283	T	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CCND3_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CCND3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD11B_MOUSE	Cdk11b	physical	22024926
PLK4_MOUSE	Plk4	physical	22024926
AURKA_MOUSE	Aurka	physical	22024926

Drug and Disease Associations

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