CYBP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYBP_MOUSE
• UniProt AC: Q9CXW3
• Protein Name: Calcyclin-binding protein
• Gene Name: Cacybp
• Organism: Mus musculus (Mouse).
• Sequence Length: 229
• Subcellular Localization: Nucleus . Cytoplasm . Cytoplasmic in unstimulated cultured neurons. Upon increase of calcium, it localizes to a ring around the nucleus. In neuroblastoma cells, after a Retinoic acid (RA) induction and calcium increase, it localizes in both the nucle
• Protein Description: May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1) (By similarity)..
• Protein Sequence: MASVLEELQKDLEEVKVLLEKSTRKRLRDTLTSEKSKIETELKNKMQQKSQKKPELDNEKPAAVVAPLTTGYTVKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKNYSMIVNNLLKPISVESSSKKVKTDTVIILCRKKAENTRWDYLTQVEKECKEKEKPSYDTEADPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAREDTEF

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
2	Acetylation	------MASVLEELQ ------CHHHHHHHH	14.35	-
3	Phosphorylation	-----MASVLEELQK -----CHHHHHHHHH	26.41	29514104
10	Acetylation	SVLEELQKDLEEVKV HHHHHHHHHHHHHHH	76.53	-
16	Sumoylation	QKDLEEVKVLLEKST HHHHHHHHHHHHHHH	30.37	-
16	Ubiquitination	QKDLEEVKVLLEKST HHHHHHHHHHHHHHH	30.37	22790023
21	Ubiquitination	EVKVLLEKSTRKRLR HHHHHHHHHHHHHHH	58.03	27667366
21	Acetylation	EVKVLLEKSTRKRLR HHHHHHHHHHHHHHH	58.03	-
36	Phosphorylation	DTLTSEKSKIETELK HHHHHHHHHHHHHHH	34.51	-
72	Phosphorylation	VAPLTTGYTVKISNY EEECCCCCEEEEECC	13.28	29514104
86	Acetylation	YGWDQSDKFVKIYIT CCCCCCCCEEEEEEE	58.25	22826441
119	Acetylation	RSFDLLVKNLNGKNY HHHHEEEECCCCCCE	56.54	23236377
144	Ubiquitination	ISVESSSKKVKTDTV CCCCCCCCCCCCCEE	64.63	22790023
147	Ubiquitination	ESSSKKVKTDTVIIL CCCCCCCCCCEEEEE	49.95	-
172	Acetylation	DYLTQVEKECKEKEK HHHHHHHHHHHHCCC	70.34	22826441
181	Phosphorylation	CKEKEKPSYDTEADP HHHCCCCCCCCCCCC	46.86	25338131
184	Phosphorylation	KEKPSYDTEADPSEG CCCCCCCCCCCCCCH	25.49	26525534
198	Ubiquitination	GLMNVLKKIYEDGDD HHHHHHHHHHCCCCH	46.49	-
200	Phosphorylation	MNVLKKIYEDGDDDM HHHHHHHHCCCCHHH	19.49	25159016
213	Ubiquitination	DMKRTINKAWVESRE HHHHHHHHHHHHHHH	39.51	22790023

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
184	T	Phosphorylation	Kinase	CK2A1	Q60737	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CYBP_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 CYBP_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIA1A_MOUSE	Siah1a	physical	15996101
SKP1_MOUSE	Skp1a	physical	15996101
S10A6_MOUSE	S100a6	physical	12042313
S10A1_MOUSE	S100a1	physical	12042313
S10A1_RAT	S100a1	physical	12042313
S10A6_RAT	S100a6	physical	12042313
S100B_RAT	S100b	physical	12042313
S100P_HUMAN	S100P	physical	12042313
S100B_MOUSE	S100b	physical	12042313

Drug and Disease Associations

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