dbPTM

FNRL1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FNRL1_ARATH
UniProt AC	Q9FKW6
Protein Name	Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
Gene Name	LFNR1 {ECO:0000303\|Ref.7}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	360
Subcellular Localization	Plastid, chloroplast stroma . Plastid, chloroplast thylakoid membrane Peripheral membrane protein Stromal side . More abundant in the membrane fraction.
Protein Description	Plays a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power..
Protein Sequence	MAAAISAAVSLPSSKSSSLLTKISSVSPQRIFLKKSTVCYRRVVSVKAQVTTDTTEAPPVKVVKESKKQEEGIVVNKFKPKNPYTGRCLLNTKITGDDAPGETWHIVFTTEGEVPYREGQSIGVIPEGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDGGEIVKGVCSNFLCDLKPGDEAKITGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEEHEDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKNPDNFRLDFAVSREQTNEKGEKMYIQTRMAEYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWLEYKKQLKRSEQWNVEVY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	Phosphorylation	SSLLTKISSVSPQRI HHHHHHHHCCCCCEE	26.66	19880383
25	Phosphorylation	SLLTKISSVSPQRIF HHHHHHHCCCCCEEE	30.04	19880383
27	Phosphorylation	LTKISSVSPQRIFLK HHHHHCCCCCEEEEE	19.77	19880383
51	Phosphorylation	VSVKAQVTTDTTEAP EEEEEEEECCCCCCC	13.58	30291188
84	Nitration	KFKPKNPYTGRCLLN CCCCCCCCCCCEEEE	31.08	-
121	Phosphorylation	VPYREGQSIGVIPEG CCCCCCCEEEEECCC	31.97	22092075
141	Phosphorylation	KPHKLRLYSIASSAI CCCEEEEEEEHHHHH	7.50	22092075
141	Nitration	KPHKLRLYSIASSAI CCCEEEEEEEHHHHH	7.50	-
166	Phosphorylation	LCVKRLVYTNDGGEI EEEEEEEEECCCCCE	12.38	28295753
166	Nitration	LCVKRLVYTNDGGEI EEEEEEEEECCCCCE	12.38	-
167	Phosphorylation	CVKRLVYTNDGGEIV EEEEEEEECCCCCEE	21.25	30291188
179	Phosphorylation	EIVKGVCSNFLCDLK CEEEEHHHHCCCCCC	28.36	22092075
210	Phosphorylation	MPKDPNATIIMLGTG CCCCCCCEEEEECCC	20.06	22092075
292	Nitration	NEKGEKMYIQTRMAE CHHHCCEEHHHHHHH	10.84	-
300	Nitration	IQTRMAEYAEELWEL HHHHHHHHHHHHHHH	15.13	-
345	Nitration	DGIDWLEYKKQLKRS CCCCHHHHHHHHHHH	22.70	-

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 FNRL1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FNRL1_ARATH !!

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 FNRL1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TIC62_ARATH	AT3G18890	physical	24043709
STR4_ARATH	TROL	physical	24043709
TIC62_ARATH	AT3G18890	physical	21071627

Drug and Disease Associations

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

Regulatory Network of FNRL1_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51, AND MASSSPECTROMETRY.	19376835 [Abstract]