dbPTM

FBX43_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FBX43_HUMAN
UniProt AC	Q4G163
Protein Name	F-box only protein 43
Gene Name	FBXO43
Organism	Homo sapiens (Human).
Sequence Length	708
Subcellular Localization
Protein Description	Required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. Probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation (Probable)..
Protein Sequence	MSFKDKDERISCLEAYVTLTSKSSRFTDETEILKMSQRHSGQAGTEAGNGADSPPIVNSKYSTFRDFCSTSSFQDSGYNELKSCSFDNIDKEYLGKKEKGPTLLYEHPETSGLGLTHPLESPTQKKKCILPRKEKDKTPELCETPKISGKKCLPRRRLNVSFALLKGDFESQNSSLESSISQVINLEKNIPSSASGFSRANNFSPLVTSTLKTEEVTSCSQKLRLNFSQQKTSTIDDSKDDCSLFEVECISPIQGNNFKDSITHDFSDSSLCINDENACPELLGSSVSGTTCGTDEDIFVTPISNLVANIRFNASQILSPSPEVRGSISTPEDSGFNSLSLEKSEDSLSDQEGSFQELLQKHKGTPKVGDTIRKTRHLGRSRRLSTLREQSSQSETEEEKQIVHPDSEKRAAAASAISEGQLSSDESGDLTFSLKNLSKTPALQLVHELFMKSKRKRLQENSGHEFLEQGDGEKIAVLQCILAGLIGKKMGIEKLDILTELKYRNLKHILAMVLESLTAESLCSVWKVSRNWREIVVQDKNANRRRKFYITQLKTDSEGAVLNVEDAATRLQLLNRSALRSVQAQARIPGSQREQGSTLSPWGEVLTPLASSSVTHLSSKQEEYVKVAKTLFTDEALKPCPRCQSPAKYQPYKKRGLCSRTACGFDFCVLCLCAYHGSEECSRGAAKPRNRKDALPGSAQSKRNLKRL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	SCLEAYVTLTSKSSR HEEEEEHHHHCCCCC	16.19	28555341
20	Phosphorylation	LEAYVTLTSKSSRFT EEEEHHHHCCCCCCC	25.41	28555341
53	Phosphorylation	EAGNGADSPPIVNSK CCCCCCCCCCCCCCC	31.85	25159151
76	Phosphorylation	STSSFQDSGYNELKS CCCCCCCCCCHHHHC	32.18	15753281
121	Phosphorylation	GLTHPLESPTQKKKC CCCCCCCCCCCCCCC	40.71	25159151
138	O-linked_Glycosylation	PRKEKDKTPELCETP CCCCCCCCCCCCCCC	31.93	29237092
198	Phosphorylation	PSSASGFSRANNFSP CCCCCCCCCCCCCCC	33.73	-
234	Phosphorylation	FSQQKTSTIDDSKDD CCCCCCCCCCCCCCC	33.39	16407128
334	Phosphorylation	SISTPEDSGFNSLSL CCCCCCCCCCCCCCC	43.55	15753281
344	Phosphorylation	NSLSLEKSEDSLSDQ CCCCCCCCCCCCCCC	36.94	24850871
347	Phosphorylation	SLEKSEDSLSDQEGS CCCCCCCCCCCCCCH	26.22	29083192
349	Phosphorylation	EKSEDSLSDQEGSFQ CCCCCCCCCCCCHHH	41.00	25159151
385	Phosphorylation	LGRSRRLSTLREQSS HCHHHHHHHHHHHHC	24.47	23532336
499	Phosphorylation	IEKLDILTELKYRNL CCHHHHHHHHHHCCH	39.34	23403867
503	Phosphorylation	DILTELKYRNLKHIL HHHHHHHHCCHHHHH	19.84	23403867
507	Ubiquitination	ELKYRNLKHILAMVL HHHHCCHHHHHHHHH	31.95	-
551	Phosphorylation	RRRKFYITQLKTDSE CCEEEEEEEEECCCC	19.23	-
607	Phosphorylation	SPWGEVLTPLASSSV CCCHHHHHHHHHCCC	22.79	-
618	Phosphorylation	SSSVTHLSSKQEEYV HCCCCCCCCCHHHHH	28.08	-
619	Phosphorylation	SSVTHLSSKQEEYVK CCCCCCCCCHHHHHH	44.72	-
698	Phosphorylation	RKDALPGSAQSKRNL HHCCCCCCHHHHHHH	22.61	29083192
701	Phosphorylation	ALPGSAQSKRNLKRL CCCCCHHHHHHHHCC	33.04	29083192

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
234	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
76	S	Phosphorylation	15753281
Phosphorylated on Ser-76, Thr-234 and Ser-334 in response to calcium, which is a prerequisite for ubiquitination and proteasomal degradation.
76	S	ubiquitylation	15753281
Phosphorylated on Ser-76, Thr-234 and Ser-334 in response to calcium, which is a prerequisite for ubiquitination and proteasomal degradation.
234	T	Phosphorylation	16407128
Phosphorylated on Ser-76, Thr-234 and Ser-334 in response to calcium, which is a prerequisite for ubiquitination and proteasomal degradation.
234	T	ubiquitylation	16407128
Phosphorylated on Ser-76, Thr-234 and Ser-334 in response to calcium, which is a prerequisite for ubiquitination and proteasomal degradation.
334	S	Phosphorylation	15753281
Phosphorylated on Ser-76, Thr-234 and Ser-334 in response to calcium, which is a prerequisite for ubiquitination and proteasomal degradation.
334	S	ubiquitylation	15753281
Phosphorylated on Ser-76, Thr-234 and Ser-334 in response to calcium, which is a prerequisite for ubiquitination and proteasomal degradation.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of FBX43_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CDC27_HUMAN	CDC27	physical	25161877

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.

Regulatory Network of FBX43_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"CaMKII and polo-like kinase 1 sequentially phosphorylate thecytostatic factor Emi2/XErp1 to trigger its destruction and meioticexit."; Hansen D.V., Tung J.J., Jackson P.K.; Proc. Natl. Acad. Sci. U.S.A. 103:608-613(2006). Cited for: PHOSPHORYLATION AT THR-234.	16407128 [Abstract]