FBSP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FBSP1_HUMAN
• UniProt AC: P0C2W1
• Protein Name: F-box/SPRY domain-containing protein 1
• Gene Name: FBXO45
• Organism: Homo sapiens (Human).
• Sequence Length: 286
• Subcellular Localization: Cell junction, synapse, postsynaptic cell membrane. Cell junction, synapse, presynaptic cell membrane.
• Protein Description: Component of E3 ubiquitin ligase complexes. Required for normal neuromuscular synaptogenesis, axon pathfinding and neuronal migration (By similarity). Plays a role in the regulation of neurotransmission at mature neurons (By similarity). May control synaptic activity by controlling UNC13A via ubiquitin dependent pathway (By similarity). Specifically recognizes TP73, promoting its ubiquitination and degradation..
• Protein Sequence: MAAPAPGAGAASGGAGCSGGGAGAGAGSGSGAAGAGGRLPSRVLELVFSYLELSELRSCALVCKHWYRCLHGDENSEVWRSLCARSLAEEALRTDILCNLPSYKAKIRAFQHAFSTNDCSRNVYIKKNGFTLHRNPIAQSTDGARTKIGFSEGRHAWEVWWEGPLGTVAVIGIATKRAPMQCQGYVALLGSDDQSWGWNLVDNNLLHNGEVNGSFPQCNNAPKYQIGERIRVILDMEDKTLAFERGYEFLGVAFRGLPKVCLYPAVSAVYGNTEVTLVYLGKPLDG

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	------MAAPAPGAG ------CCCCCCCCC	23.35	19413330
28	Phosphorylation	GAGAGAGSGSGAAGA CCCCCCCCCCCCCCC	29.29	28857561
41	Phosphorylation	GAGGRLPSRVLELVF CCCCCCCHHHHHHHH	39.34	28857561
64	Ubiquitination	RSCALVCKHWYRCLH HHHHHHHHHHHHHHC	29.68	-
81	Phosphorylation	ENSEVWRSLCARSLA CCHHHHHHHHHHHHH	16.46	24719451
104	Ubiquitination	LCNLPSYKAKIRAFQ CCCCHHHHHHHHHHH	47.76	22505724
106	Ubiquitination	NLPSYKAKIRAFQHA CCHHHHHHHHHHHHH	28.68	-
126	Ubiquitination	CSRNVYIKKNGFTLH CCCCEEEEECCEEEE	23.62	27667366
127	Ubiquitination	SRNVYIKKNGFTLHR CCCEEEEECCEEEEC	53.39	29967540
147	Ubiquitination	STDGARTKIGFSEGR CCCCCCCEECCCCCC	34.97	21906983
239	Ubiquitination	VILDMEDKTLAFERG EEEECCCCCCHHHCC	31.93	24816145

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

Oops, there are no upstream regulatory protein records of FBSP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FBSP1_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 FBSP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P73_HUMAN	TP73	physical	19581926
SKP1_HUMAN	SKP1	physical	19398581
MYCB2_HUMAN	MYCBP2	physical	19398581
NOS2_HUMAN	NOS2	physical	23438482
PAWR_HUMAN	PAWR	physical	24992930
SKP1_HUMAN	SKP1	physical	24992930
MYCB2_HUMAN	MYCBP2	physical	24992930
CADH2_HUMAN	CDH2	physical	25143387
SKP1_HUMAN	SKP1	physical	25143387
MYCB2_HUMAN	MYCBP2	physical	25143387
CTNB1_HUMAN	CTNNB1	physical	25143387
ESR1_HUMAN	ESR1	physical	26487511
NEUL4_HUMAN	NEURL4	physical	27173435
MYCB2_HUMAN	MYCBP2	physical	27173435
RFC4_HUMAN	RFC4	physical	27173435
GALC_HUMAN	GALC	physical	27173435
PAWR_HUMAN	PAWR	physical	28625975

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• 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

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330