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HMDB Protein ID HMDBP02077
Secondary Accession Numbers
  • 7558
Name Ferritin light chain
  1. Ferritin L subunit
Gene Name FTL
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function 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
Pathways Not Available
Reactions Not Available
GO Classification
ion binding
cation binding
metal ion binding
catalytic activity
transition metal ion binding
iron ion binding
oxidoreductase activity
ferric iron binding
metabolic process
establishment of localization
biological regulation
oxidation reduction
ion transport
cation transport
metal ion transport
transition metal ion transport
iron ion transport
regulation of biological quality
homeostatic process
chemical homeostasis
ion homeostasis
cellular ion homeostasis
cellular cation homeostasis
cellular di-, tri-valent inorganic cation homeostasis
cellular iron ion homeostasis
Cellular Location Not Available
Gene Properties
Chromosome Location Chromosome:1
Locus 19q13.33
Gene Sequence
>528 bp
Protein Properties
Number of Residues 175
Molecular Weight 20019.5
Theoretical pI 5.59
Pfam Domain Function
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ferritin light chain
GenBank ID Protein 182514
UniProtKB/Swiss-Prot ID P02792
UniProtKB/Swiss-Prot Entry Name FRIL_HUMAN
PDB IDs Not Available
GenBank Gene ID M11147
GeneCard ID FTL
GenAtlas ID FTL
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  4. Boyd D, Vecoli C, Belcher DM, Jain SK, Drysdale JW: Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. J Biol Chem. 1985 Sep 25;260(21):11755-61. [PubMed:3840162 ]
  5. Dorner MH, Salfeld J, Will H, Leibold EA, Vass JK, Munro HN: Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications. Proc Natl Acad Sci U S A. 1985 May;82(10):3139-43. [PubMed:3858810 ]
  6. Santoro C, Marone M, Ferrone M, Costanzo F, Colombo M, Minganti C, Cortese R, Silengo L: Cloning of the gene coding for human L apoferritin. Nucleic Acids Res. 1986 Apr 11;14(7):2863-76. [PubMed:3754330 ]
  7. Chou CC, Gatti RA, Fuller ML, Concannon P, Wong A, Chada S, Davis RC, Salser WA: Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro. Mol Cell Biol. 1986 Feb;6(2):566-73. [PubMed:3023856 ]
  8. Addison JM, Fitton JE, Lewis WG, May K, Harrison PM: The amino acid sequence of human liver apoferritin. FEBS Lett. 1983 Nov 28;164(1):139-44. [PubMed:6653779 ]
  9. Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A: Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. Eur J Biochem. 1996 Jul 1;239(1):144-9. [PubMed:8706699 ]
  10. Maciel P, Cruz VT, Constante M, Iniesta I, Costa MC, Gallati S, Sousa N, Sequeiros J, Coutinho P, Santos MM: Neuroferritinopathy: missense mutation in FTL causing early-onset bilateral pallidal involvement. Neurology. 2005 Aug 23;65(4):603-5. [PubMed:16116125 ]