dbPTM

FRIL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FRIL_HUMAN
UniProt AC	P02792
Protein Name	Ferritin light chain
Gene Name	FTL
Organism	Homo sapiens (Human).
Sequence Length	175
Subcellular Localization
Protein Description	Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity)..
Protein Sequence	MSSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSQIRQNY ------CCHHHHHHC	30.83	6653779
3	Phosphorylation	-----MSSQIRQNYS -----CCHHHHHHCH	28.47	24719451
59	Ubiquitination	FRELAEEKREGYERL HHHHHHHHHHHHHHH	47.45	-
68	Ubiquitination	EGYERLLKMQNQRGG HHHHHHHHHHHHHCC	42.93	21906983
83	Ubiquitination	RALFQDIKKPAEDEW HHCHHHCCCCCCCCC	62.08	83
84	Ubiquitination	ALFQDIKKPAEDEWG HCHHHCCCCCCCCCC	50.20	21906983
92	Ubiquitination	PAEDEWGKTPDAMKA CCCCCCCCCHHHHHH	58.94	21906983
98	Acetylation	GKTPDAMKAAMALEK CCCHHHHHHHHHHHH	34.41	19608861
98	Ubiquitination	GKTPDAMKAAMALEK CCCHHHHHHHHHHHH	34.41	19608861
105	Ubiquitination	KAAMALEKKLNQALL HHHHHHHHHHHHHHH	64.51	21906983
106	Ubiquitination	AAMALEKKLNQALLD HHHHHHHHHHHHHHH	43.21	-
106	Malonylation	AAMALEKKLNQALLD HHHHHHHHHHHHHHH	43.21	26320211
119	Phosphorylation	LDLHALGSARTDPHL HHHHHHCCCCCCHHH	18.54	-
127	S-nitrosylation	ARTDPHLCDFLETHF CCCCHHHHHHHHHHC	2.94	22178444
140	Ubiquitination	HFLDEEVKLIKKMGD HCCHHHHHHHHHHHH	48.01	-
144	Ubiquitination	EEVKLIKKMGDHLTN HHHHHHHHHHHHHHH	40.91	-
150	Phosphorylation	KKMGDHLTNLHRLGG HHHHHHHHHHHHCCC	32.11	20068231
165	Phosphorylation	PEAGLGEYLFERLTL CCCCHHHHHHHHHHC	18.20	22817900
173	Acetylation	LFERLTLKHD----- HHHHHHCCCC-----	40.26	27178108

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 FRIL_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FRIL_HUMAN	FTL	physical	16189514
M3K12_HUMAN	MAP3K12	physical	16169070
TAF10_HUMAN	TAF10	physical	16169070
FRIH_HUMAN	FTH1	physical	16169070
PTN_HUMAN	PTN	physical	16169070
FRIL_HUMAN	FTL	physical	16169070
FRIL_HUMAN	FTL	physical	20159981
TOX4_HUMAN	TOX4	physical	22939629
RPB4_HUMAN	POLR2D	physical	22939629
IF4G1_HUMAN	EIF4G1	physical	22939629
NAMPT_HUMAN	NAMPT	physical	18486613
C43BP_HUMAN	COL4A3BP	physical	22863883
PACN2_HUMAN	PACSIN2	physical	22863883
FRIL_HUMAN	FTL	physical	25416956
IMA4_HUMAN	KPNA3	physical	25416956
MYOG_HUMAN	MYOG	physical	25416956
SDCB1_HUMAN	SDCBP	physical	25416956
USBP1_HUMAN	USHBP1	physical	25416956

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600886	Hereditary hyperferritinemia-cataract syndrome (HHCS)
606159	Neurodegeneration with brain iron accumulation 3 (NBIA3)
615604	L-ferritin deficiency (LFTD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00893	Iron Dextran

Regulatory Network of FRIL_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"The amino acid sequence of human liver apoferritin."; Addison J.M., Fitton J.E., Lewis W.G., May K., Harrison P.M.; FEBS Lett. 164:139-144(1983). Cited for: PROTEIN SEQUENCE OF 2-36 AND 41-175.	6653779 [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-98, AND MASS SPECTROMETRY.	19608861 [Abstract]