FRDA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FRDA_HUMAN
• UniProt AC: Q16595
• Protein Name: Frataxin, mitochondrial
• Gene Name: FXN
• Organism: Homo sapiens (Human).
• Sequence Length: 210
• Subcellular Localization: Mitochondrion . Cytoplasm, cytosol . PubMed:18725397 reports localization exclusively in mitochondria.
• Protein Description: Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1..
• Protein Sequence: MWTLGRRAVAGLLASPSPAQAQTLTRVPRPAELAPLCGRRGLRTDIDATCTPRRASSNQRGLNQIWNVKKQSVYLMNLRKSGTLGHPGSLDETTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSGKDA

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
44	Phosphorylation	CGRRGLRTDIDATCT CCCCCCCCCCCCCCC	42.20	28258704
49	Phosphorylation	LRTDIDATCTPRRAS CCCCCCCCCCCCCCC	17.11	30177828
51	Phosphorylation	TDIDATCTPRRASSN CCCCCCCCCCCCCCC	18.57	28258704
56	Phosphorylation	TCTPRRASSNQRGLN CCCCCCCCCCCCCHH	28.19	30177828
57	Phosphorylation	CTPRRASSNQRGLNQ CCCCCCCCCCCCHHH	35.68	30177828
81	Phosphorylation	YLMNLRKSGTLGHPG EEEECCCCCCCCCCC	30.49	25159151
83	Phosphorylation	MNLRKSGTLGHPGSL EECCCCCCCCCCCCC	36.34	25627689
94	Phosphorylation	PGSLDETTYERLAEE CCCCCHHHHHHHHHH	22.72	-
118	Phosphorylation	EDLADKPYTFEDYDV HHHCCCCCCCCCCEE	29.78	-
143	Nitration	LGGDLGTYVINKQTP ECCCCEEEEEECCCC	9.49	-
143	Phosphorylation	LGGDLGTYVINKQTP ECCCCEEEEEECCCC	9.49	-
157	Phosphorylation	PNKQIWLSSPSSGPK CCCEEEEECCCCCCC	25.80	25278378
158	Phosphorylation	NKQIWLSSPSSGPKR CCEEEEECCCCCCCC	26.99	25278378
160	Phosphorylation	QIWLSSPSSGPKRYD EEEEECCCCCCCCCC	50.29	25278378
161	Phosphorylation	IWLSSPSSGPKRYDW EEEECCCCCCCCCCC	63.60	25278378
175	Nitration	WTGKNWVYSHDGVSL CCCCCCEECCCCCCH	7.60	-
175 (in isoform 3)	Phosphorylation	-	7.60	-
178 (in isoform 3)	Phosphorylation	-	53.93	-
187 (in isoform 3)	Phosphorylation	-	16.12	-
197 (in isoform 1)	Ubiquitination	-	38.12	21890473
197	Acetylation	LTKALKTKLDLSSLA HHHHHHHHHCHHHHH	38.12	23954790
197	Ubiquitination	LTKALKTKLDLSSLA HHHHHHHHHCHHHHH	38.12	21890473
205	Nitration	LDLSSLAYSGKDA-- HCHHHHHHCCCCC--	24.21	-
205	Phosphorylation	LDLSSLAYSGKDA-- HCHHHHHHCCCCC--	24.21	-
208	Acetylation	SSLAYSGKDA----- HHHHHCCCCC-----	44.54	25038526

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
118	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FRDA_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 FRDA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACTN1_HUMAN	ACTN1	physical	16713569
PICK1_HUMAN	PICK1	physical	16713569
RN126_HUMAN	RNF126	physical	28228265

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 229300: Friedreich ataxia (FRDA)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.