FTH1

From Wikipedia, the free encyclopedia

Ferritin, heavy polypeptide 1

PDB rendering based on 1fha.

Available structures: 1fha, 2cei, 2chi, 2cih, 2clu, 2cn6, 2cn7, 2fha, 2iu2

Identifiers

Symbol(s)

FTH1; FTH; FTHL6; MGC104426; PIG15; PLIF

External IDs

OMIM: 134770 MGI: 95588 HomoloGene: 74295

Gene ontology
Molecular Function:	• ferroxidase activity • binding • protein binding • ferric iron binding • oxidoreductase activity • kinase binding
Cellular Component:	• plasma membrane • ferritin complex
Biological Process:	• iron ion transport • cellular iron ion homeostasis • intracellular sequestering of iron ion • immune response • cell proliferation • negative regulation of cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002032 (mRNA)
NP_002023 (protein)

NM_010239 (mRNA)
NP_034369 (protein)

Location

Chr 11: 61.49 - 61.49 Mb

Chr 19: 10.05 - 10.05 Mb

Pubmed search

[1]

[2]

Ferritin, heavy polypeptide 1, also known as FTH1, is a human gene.^[1]

This gene encodes the heavy subunit of ferritin, the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in ferritin proteins are associated with several neurodegenerative diseases. This gene has multiple pseudogenes. Several alternatively spliced transcript variants have been observed, but their biological validity has not been determined.^[1]

[edit] See also

Ferritin

[edit] References

^ ^a ^b Entrez Gene: FTH1 ferritin, heavy polypeptide 1.

[edit] Further reading

Percy ME, Wong S, Bauer S, et al. (1998). "Iron metabolism and human ferritin heavy chain cDNA from adult brain with an elongated untranslated region: new findings and insights.". The Analyst 123 (1): 41-50. PMID 9581019.
Arosio P, Adelman TG, Drysdale JW (1978). "On ferritin heterogeneity. Further evidence for heteropolymers.". J. Biol. Chem. 253 (12): 4451-8. PMID 659425.
Lawson DM, Artymiuk PJ, Yewdall SJ, et al. (1991). "Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts.". Nature 349 (6309): 541-4. doi:10.1038/349541a0. PMID 1992356.
Costanzo F, Colombo M, Staempfli S, et al. (1986). "Structure of gene and pseudogenes of human apoferritin H.". Nucleic Acids Res. 14 (2): 721-36. PMID 3003694.
Hentze MW, Keim S, Papadopoulos P, et al. (1986). "Cloning, characterization, expression, and chromosomal localization of a human ferritin heavy-chain gene.". Proc. Natl. Acad. Sci. U.S.A. 83 (19): 7226-30. PMID 3020541.
Chou CC, Gatti RA, Fuller ML, et al. (1987). "Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro.". Mol. Cell. Biol. 6 (2): 566-73. PMID 3023856.
Hentze MW, Caughman SW, Rouault TA, et al. (1988). "Identification of the iron-responsive element for the translational regulation of human ferritin mRNA.". Science 238 (4833): 1570-3. PMID 3685996.
Boyd D, Vecoli C, Belcher DM, et al. (1985). "Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones.". J. Biol. Chem. 260 (21): 11755-61. PMID 3840162.
Worwood M, Brook JD, Cragg SJ, et al. (1985). "Assignment of human ferritin genes to chromosomes 11 and 19q13.3----19qter.". Hum. Genet. 69 (4): 371-4. PMID 3857215.
Dörner MH, Salfeld J, Will H, et al. (1985). "Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications.". Proc. Natl. Acad. Sci. U.S.A. 82 (10): 3139-43. PMID 3858810.
Costanzo F, Santoro C, Colantuoni V, et al. (1984). "Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family.". EMBO J. 3 (1): 23-7. PMID 6323167.
Boyd D, Jain SK, Crampton J, et al. (1984). "Isolation and characterization of a cDNA clone for human ferritin heavy chain.". Proc. Natl. Acad. Sci. U.S.A. 81 (15): 4751-5. PMID 6589621.
Addison JM, Fitton JE, Lewis WG, et al. (1984). "The amino acid sequence of human liver apoferritin.". FEBS Lett. 164 (1): 139-44. PMID 6653779.
Dhar MS, Joshi JG (1993). "Differential processing of the ferritin heavy chain mRNA in human liver and adult human brain.". J. Neurochem. 61 (6): 2140-6. PMID 7504084.
Connor JR, Snyder BS, Arosio P, et al. (1995). "A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains.". J. Neurochem. 65 (2): 717-24. PMID 7616228.
Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank.". Gene 150 (2): 243-50. PMID 7821789.
Dhar M, Chauthaiwale V, Joshi JG (1993). "Sequence of a cDNA encoding the ferritin H-chain from an 11-week-old human fetal brain.". Gene 126 (2): 275-8. PMID 7916709.
Qi Y, Dawson G (1994). "Hypoxia specifically and reversibly induces the synthesis of ferritin in oligodendrocytes and human oligodendrogliomas.". J. Neurochem. 63 (4): 1485-90. PMID 7931301.
Rogers JT (1996). "Ferritin translation by interleukin-1and interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes.". Blood 87 (6): 2525-37. PMID 8630420.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791-806. PMID 8889548.