FBX5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FBX5_MOUSE
• UniProt AC: Q7TSG3
• Protein Name: F-box only protein 5
• Gene Name: Fbxo5 {ECO:0000312|MGI:MGI:1914391}
• Organism: Mus musculus (Mouse).
• Sequence Length: 421
• Subcellular Localization: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration. In mitotic cells, localizes throughout the cell, particularly at the spindle (By sim
• Protein Description: Regulates progression through early mitosis by inhibiting the anaphase promoting complex/cyclosome (APC). Binds to the APC activators CDC20 and FZR1/CDH1 to prevent APC activation. Can also bind directly to the APC to inhibit substrate-binding..
• Protein Sequence: MSRRTCSDLRRPSSCPCRLGARTTVDGCKEESPVLSVTMKCFNCNPDLSELEVVKPEDSGIEASYSPVCLEPSCNDCVRNHERLSFIDSPIVGHDNKENQRVQNTLDSSNETEELEASRLYEDSGYSSFTQSDRDDGILILENFRNSPQARLLPSQSPDQHPNKTLLPVLHFERVVCSTLKKNGKRNPKVDREMLKEVIASGNFRLQNIIGKKMGLEHLDILAELSRRGFVHLLANILTKLSGMDLVNLSKVSRIWKKILENNKGAFQLYSKTMQRVIESSKLSLHATTRGYVVGRAALTCVQKSSTWAPPKKDVQIKSSSQRGQRVSTYSRHNEFVEVAKTLKNNESLKACVRCNFPAKYDHYLERAVCKRESCQFEYCTKCLCAYHNNKDCLNGKILKASCKVGPLPGTKKSKKNLQRL

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
13	Phosphorylation	CSDLRRPSSCPCRLG HHHCCCCCCCCCCCC	42.64	-
85	Phosphorylation	VRNHERLSFIDSPIV HHCCHHHCCCCCCCC	26.78	22817900
89	Phosphorylation	ERLSFIDSPIVGHDN HHHCCCCCCCCCCCC	16.23	22817900
108	Phosphorylation	RVQNTLDSSNETEEL HHHHHHCCCCCCHHH	37.87	28066266
109	Phosphorylation	VQNTLDSSNETEELE HHHHHCCCCCCHHHH	38.05	28066266
112	Phosphorylation	TLDSSNETEELEASR HHCCCCCCHHHHHHH	38.72	26643407
124	Phosphorylation	ASRLYEDSGYSSFTQ HHHHHCCCCCCCCCC	27.91	-
128	Phosphorylation	YEDSGYSSFTQSDRD HCCCCCCCCCCCCCC	24.67	-
155	Phosphorylation	PQARLLPSQSPDQHP CCCCCCCCCCCCCCC	43.17	26745281
157	Phosphorylation	ARLLPSQSPDQHPNK CCCCCCCCCCCCCCC	34.48	25266776
226	Phosphorylation	LDILAELSRRGFVHL HHHHHHHHHHHHHHH	16.07	28059163
374	Phosphorylation	RAVCKRESCQFEYCT HHHHCCCCCCHHHCC	19.77	-
379	Phosphorylation	RESCQFEYCTKCLCA CCCCCHHHCCHHHHH	13.50	-
381	Phosphorylation	SCQFEYCTKCLCAYH CCCHHHCCHHHHHHC	24.72	-
387	Phosphorylation	CTKCLCAYHNNKDCL CCHHHHHHCCCCCCC	12.23	-
415	Ubiquitination	LPGTKKSKKNLQRL- CCCCHHHHHHHHCC-	55.34	-

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
124	S	Phosphorylation	Kinase	PLK1	P53350	PSP
128	S	Phosphorylation	Kinase	PLK1	P53350	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Btrc	Q3ULA2	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
11	K	ubiquitylation	Undergoes both 'Lys-11' and 'Lys-48'-linked polyubiquitination by APC-FZR1 complex leading to degradation during G1 phase by the proteasome (By similarity).	17190794

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FBX5_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of FBX5_MOUSE !!

Drug and Disease Associations

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