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Identification
HMDB Protein ID HMDBP08672
Secondary Accession Numbers
  • 14391
Name Ferritin heavy chain
Synonyms
  1. Cell proliferation-inducing gene 15 protein
  2. Ferritin H subunit
Gene Name FTH1
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. Has ferroxidase activity. 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).
Pathways
  • Mineral absorption
  • Porphyrin and chlorophyll metabolism
Reactions
Fe2+ + Hydrogen Ion + Oxygen → Iron + Water details
GO Classification
Biological Process
intracellular sequestering of iron ion
iron ion transport
negative regulation of fibroblast proliferation
immune response
cellular membrane organization
post-Golgi vesicle-mediated transport
transmembrane transport
Cellular Component
cytosol
intracellular ferritin complex
mitochondrion
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
iron ion binding
oxidoreductase activity
ferric iron binding
Molecular Function
ferric iron binding
ferroxidase activity
iron ion binding
Process
metabolic process
establishment of localization
transport
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 11
Locus 11q13
SNPs FTH1
Gene Sequence
>552 bp
ATGACGACCGCGTCCACCTCGCAGGTGCGCCAGAACTACCACCAGGACTCAGAGGCCGCC
ATCAACCGCCAGATCAACCTGGAGCTCTACGCCTCCTACGTTTACCTGTCCATGTCTTAC
TACTTTGACCGCGATGATGTGGCTTTGAAGAACTTTGCCAAATACTTTCTTCACCAATCT
CATGAGGAGAGGGAACATGCTGAGAAACTGATGAAGCTGCAGAACCAACGAGGTGGCCGA
ATCTTTCTTCAGGATATCAAGAAACCAGACTGTGATGACTGGGAGAGCGGGCTGAATGCA
ATGGAGTGTGCATTACATTTGGAAAAAAATGTGAATCAGTCACTACTGGAACTGCACAAA
CTGGCCACTGACAAAAATGACCCCCATTTGTGTGACTTCATTGAGACACATTACCTGAAT
GAGCAGGTGAAAGCCATCAAAGAATTGGGTGACCACGTGACCAACTTGCGCAAGATGGGA
GCGCCCGAATCTGGCTTGGCGGAATATCTCTTTGACAAGCACACCCTGGGAGACAGTGAT
AATGAAAGCTAA
Protein Properties
Number of Residues 183
Molecular Weight 21225.47
Theoretical pI 5.556
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ferritin heavy chain
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQS
HEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHK
LATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSD
NES
GenBank ID Protein 21104438
UniProtKB/Swiss-Prot ID P02794
UniProtKB/Swiss-Prot Entry Name FRIH_HUMAN
PDB IDs
GenBank Gene ID AB062402
GeneCard ID FTH1
GenAtlas ID FTH1
HGNC ID HGNC:3976
References
General References
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  2. 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 ]
  3. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  4. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  7. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  8. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. doi: 10.1002/pmic.200700884. [PubMed:18318008 ]
  9. 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 ]
  10. 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 ]
  11. Costanzo F, Santoro C, Colantuoni V, Bensi G, Raugei G, Romano V, Cortese R: Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family. EMBO J. 1984 Jan;3(1):23-7. [PubMed:6323167 ]
  12. Costanzo F, Colombo M, Staempfli S, Santoro C, Marone M, Frank R, Delius H, Cortese R: Structure of gene and pseudogenes of human apoferritin H. Nucleic Acids Res. 1986 Jan 24;14(2):721-36. [PubMed:3003694 ]
  13. Hentze MW, Keim S, Papadopoulos P, O'Brien S, Modi W, Drysdale J, Leonard WJ, Harford JB, Klausner RD: Cloning, characterization, expression, and chromosomal localization of a human ferritin heavy-chain gene. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7226-30. [PubMed:3020541 ]
  14. Dhar M, Chauthaiwale V, Joshi JG: Sequence of a cDNA encoding the ferritin H-chain from an 11-week-old human fetal brain. Gene. 1993 Apr 30;126(2):275-8. [PubMed:7916709 ]
  15. Boyd D, Jain SK, Crampton J, Barrett KJ, Drysdale J: Isolation and characterization of a cDNA clone for human ferritin heavy chain. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4751-5. [PubMed:6589621 ]
  16. Lawson DM, Artymiuk PJ, Yewdall SJ, Smith JM, Livingstone JC, Treffry A, Luzzago A, Levi S, Arosio P, Cesareni G, et al.: Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature. 1991 Feb 7;349(6309):541-4. [PubMed:1992356 ]
  17. Hempstead PD, Yewdall SJ, Fernie AR, Lawson DM, Artymiuk PJ, Rice DW, Ford GC, Harrison PM: Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution. J Mol Biol. 1997 May 2;268(2):424-48. [PubMed:9159481 ]