dbPTM

FBX22_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FBX22_HUMAN
UniProt AC	Q8NEZ5
Protein Name	F-box only protein 22
Gene Name	FBXO22
Organism	Homo sapiens (Human).
Sequence Length	403
Subcellular Localization	Cytoplasm, myofibril, sarcomere, Z line.
Protein Description	Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function..
Protein Sequence	MEPVGCCGECRGSSVDPRSTFVLSNLAEVVERVLTFLPAKALLRVACVCRLWRECVRRVLRTHRSVTWISAGLAEAGHLEGHCLVRVVAEELENVRILPHTVLYMADSETFISLEECRGHKRARKRTSMETALALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFPQIEGIKIQPFHFIKDPKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLQQVVSTFSDMNIILAGGQVDNLSSLTSEKNPLDIDASGVVGLSFSGHRIQSATVLLNEDVSDEKTAEAAMQRLKAANIPEHNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGNGEIGCDRIVTGNFILRKCNEVKDDDLFHSYTTIMALIHLGSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEPVGCCG -------CCCCCCCC	13.66	22223895
40	Acetylation	VLTFLPAKALLRVAC HHHHCCHHHHHHHHH	37.31	25953088
40	Ubiquitination	VLTFLPAKALLRVAC HHHHCCHHHHHHHHH	37.31	23000965
40 (in isoform 1)	Ubiquitination	-	37.31	21890473
40 (in isoform 3)	Ubiquitination	-	37.31	21890473
104	Phosphorylation	ILPHTVLYMADSETF ECCCEEEEEECCCCE	5.97	18452278
108	Phosphorylation	TVLYMADSETFISLE EEEEEECCCCEECHH	29.06	28122231
110	Phosphorylation	LYMADSETFISLEEC EEEECCCCEECHHHH	30.16	28122231
113	Phosphorylation	ADSETFISLEECRGH ECCCCEECHHHHCCC	26.07	28122231
127	Phosphorylation	HKRARKRTSMETALA CCHHHHHCCHHHHHH	35.15	25159151
128	Phosphorylation	KRARKRTSMETALAL CHHHHHCCHHHHHHH	20.75	21815630
129	Sulfoxidation	RARKRTSMETALALE HHHHHCCHHHHHHHH	5.40	21406390
131	Phosphorylation	RKRTSMETALALEKL HHHCCHHHHHHHHHH	20.52	27251275
137	Ubiquitination	ETALALEKLFPKQCQ HHHHHHHHHCHHHCC	57.17	29967540
194	Ubiquitination	IQPFHFIKDPKNLTL EECEEEECCCCCCEE	68.01	19608861
194	Acetylation	IQPFHFIKDPKNLTL EECEEEECCCCCCEE	68.01	19608861
196	Ubiquitination	PFHFIKDPKNLTLER CEEEECCCCCCEEEE	23.56	22817900
196 (in isoform 2)	Ubiquitination	-	23.56	21906983
197	Ubiquitination	FHFIKDPKNLTLERH EEEECCCCCCEEEEE	74.79	33845483
233	Ubiquitination	NCCKVGASNYLQQVV CHHHCCHHHHHHHHH	21.78	24816145
300	Ubiquitination	NEDVSDEKTAEAAMQ CCCCCCHHHHHHHHH	59.01	22817900
300 (in isoform 1)	Ubiquitination	-	59.01	21890473
337	Ubiquitination	GFQYYRAKGNVEADA CCHHEEECCCCCHHH	41.86	33845483

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
Oops, there are no upstream regulatory protein records of FBX22_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FBX22_HUMAN !!

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 FBX22_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL1_HUMAN	CUL1	physical	22268729
SKP1_HUMAN	SKP1	physical	17463251
SKP1_HUMAN	SKP1	physical	26496610
NCOR2_HUMAN	NCOR2	physical	26496610
KLF4_HUMAN	KLF4	physical	26087183
SKP1_HUMAN	SKP1	physical	26087183

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 FBX22_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND MASS SPECTROMETRY.	19608861 [Abstract]