FTH1

Protein-coding gene in the species Homo sapiens

FTH1

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1FHA, 2CEI, 2CHI, 2CIH, 2CLU, 2CN6, 2CN7, 2FHA, 2IU2, 2Z6M, 3AJO, 3AJP, 3AJQ, 3ERZ, 3ES3, 4DYX, 4DYY, 4DYZ, 4DZ0, 4OYN, 4Y08, 4YKH, 4ZJK, 5CMQ, 5CMR

Identifiers

Aliases

FTH1, FHC, FTH, FTHL6, HFE5, PIG15, PLIF, ferritin, heavy polypeptide 1, ferritin heavy chain 1

External IDs

OMIM: 134770; MGI: 95588; HomoloGene: 74295; GeneCards: FTH1; OMA:FTH1 - orthologs

Gene location (Human)

Chr.	Chromosome 11 (human)^[1]

Band	11q12.3	Start	61,959,718 bp^[1]
Band	11q12.3	End	61,967,634 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 19 (mouse)^[2]

Band	19 A\|19 6.23 cM	Start	9,957,962 bp^[2]
Band	19 A\|19 6.23 cM	End	9,962,462 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

stromal cell of endometrium

upper lobe of left lung

tibial nerve

right lung

gastric mucosa

Descending thoracic aorta

mucosa of transverse colon

left coronary artery

C1 segment

right adrenal cortex

Top expressed in

globus pallidus

deep cerebellar nuclei

pontine nuclei

fetal liver hematopoietic progenitor cell

right kidney

lateral geniculate nucleus

endothelial cell of lymphatic vessel

lateral hypothalamus

dentate gyrus of hippocampal formation granule cell

gastrula

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	ferric iron binding metal ion binding ferroxidase activity protein binding oxidoreductase activity iron ion binding ferrous iron binding identical protein binding
Cellular component	cytosol intracellular ferritin complex extracellular exosome nucleus extracellular region autolysosome tertiary granule lumen ficolin-1-rich granule lumen cytoplasm
Biological process	intracellular sequestering of iron ion iron ion transport immune response negative regulation of fibroblast proliferation negative regulation of cell population proliferation cellular iron ion homeostasis neutrophil degranulation negative regulation of necrotic cell death
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


2495


14319

Ensembl


ENSG00000167996


ENSMUSG00000024661

UniProt


P02794


P09528

RefSeq (mRNA)


NM_002032


NM_010239

RefSeq (protein)


NP_002023


NP_034369

Location (UCSC)

Chr 11: 61.96 – 61.97 Mb

Chr 19: 9.96 – 9.96 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Ferritin heavy chain is a ferroxidase enzyme that in humans is encoded by the FTH1 gene.^[5]^[6] FTH1 gene is located on chromosome 11, and its mutation causes Hemochromatosis type 5.^[7]

Function

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.^[6]

Interactions

FTH1 has been shown to interact with ferritin light chain.^[8]^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000167996 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000024661 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Hentze MW, Keim S, Papadopoulos P, O'Brien S, Modi W, Drysdale J, Leonard WJ, Harford JB, Klausner RD (October 1986). "Cloning, characterization, expression, and chromosomal localization of a human ferritin heavy-chain gene". Proceedings of the National Academy of Sciences of the United States of America. 83 (19): 7226–30. Bibcode:1986PNAS...83.7226H. doi:10.1073/pnas.83.19.7226. PMC 386688. PMID 3020541.
^ ^a ^b "Entrez Gene: FTH1 ferritin, heavy polypeptide 1".
^ "Hemochromatosis type 5 - About the Disease - Genetic and Rare Diseases Information Center".
^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.

Percy ME, Wong S, Bauer S, Liaghati-Nasseri N, Perry MD, Chauthaiwale VM, Dhar M, Joshi JG (January 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. doi:10.1039/a706355e. hdl:1807/16984. PMID 9581019.
Arosio P, Adelman TG, Drysdale JW (June 1978). "On ferritin heterogeneity. Further evidence for heteropolymers". The Journal of Biological Chemistry. 253 (12): 4451–8. doi:10.1016/S0021-9258(17)34741-5. PMID 659425.
Lawson DM, Artymiuk PJ, Yewdall SJ, Smith JM, Livingstone JC, Treffry A, Luzzago A, Levi S, Arosio P, Cesareni G (February 1991). "Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts". Nature. 349 (6309): 541–4. Bibcode:1991Natur.349..541L. doi:10.1038/349541a0. PMID 1992356. S2CID 4366895.
Costanzo F, Colombo M, Staempfli S, Santoro C, Marone M, Frank R, Delius H, Cortese R (January 1986). "Structure of gene and pseudogenes of human apoferritin H". Nucleic Acids Research. 14 (2): 721–36. doi:10.1093/nar/14.2.721. PMC 339460. PMID 3003694.
Chou CC, Gatti RA, Fuller ML, Concannon P, Wong A, Chada S, Davis RC, Salser WA (February 1986). "Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro". Molecular and Cellular Biology. 6 (2): 566–73. doi:10.1128/mcb.6.2.566. PMC 367547. PMID 3023856.
Hentze MW, Caughman SW, Rouault TA, Barriocanal JG, Dancis A, Harford JB, Klausner RD (December 1987). "Identification of the iron-responsive element for the translational regulation of human ferritin mRNA". Science. 238 (4833): 1570–3. Bibcode:1987Sci...238.1570H. doi:10.1126/science.3685996. PMID 3685996.
Boyd D, Vecoli C, Belcher DM, Jain SK, Drysdale JW (September 1985). "Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones". The Journal of Biological Chemistry. 260 (21): 11755–61. doi:10.1016/S0021-9258(17)39094-4. PMID 3840162.
Worwood M, Brook JD, Cragg SJ, Hellkuhl B, Jones BM, Perera P, Roberts SH, Shaw DJ (1985). "Assignment of human ferritin genes to chromosomes 11 and 19q13.3----19qter". Human Genetics. 69 (4): 371–4. doi:10.1007/BF00291657. PMID 3857215. S2CID 23574066.
Dörner MH, Salfeld J, Will H, Leibold EA, Vass JK, Munro HN (May 1985). "Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications". Proceedings of the National Academy of Sciences of the United States of America. 82 (10): 3139–43. Bibcode:1985PNAS...82.3139D. doi:10.1073/pnas.82.10.3139. PMC 397730. PMID 3858810.
Costanzo F, Santoro C, Colantuoni V, Bensi G, Raugei G, Romano V, Cortese R (January 1984). "Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family". The EMBO Journal. 3 (1): 23–7. doi:10.1002/j.1460-2075.1984.tb01756.x. PMC 557292. PMID 6323167.
Boyd D, Jain SK, Crampton J, Barrett KJ, Drysdale J (August 1984). "Isolation and characterization of a cDNA clone for human ferritin heavy chain". Proceedings of the National Academy of Sciences of the United States of America. 81 (15): 4751–5. Bibcode:1984PNAS...81.4751B. doi:10.1073/pnas.81.15.4751. PMC 391568. PMID 6589621.
Addison JM, Fitton JE, Lewis WG, May K, Harrison PM (November 1983). "The amino acid sequence of human liver apoferritin". FEBS Letters. 164 (1): 139–44. doi:10.1016/0014-5793(83)80037-4. PMID 6653779. S2CID 21144293.
Dhar MS, Joshi JG (December 1993). "Differential processing of the ferritin heavy chain mRNA in human liver and adult human brain". Journal of Neurochemistry. 61 (6): 2140–6. doi:10.1111/j.1471-4159.1993.tb07452.x. PMID 7504084. S2CID 21229082.
Connor JR, Snyder BS, Arosio P, Loeffler DA, LeWitt P (August 1995). "A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains". Journal of Neurochemistry. 65 (2): 717–24. doi:10.1046/j.1471-4159.1995.65020717.x. PMID 7616228. S2CID 930869.
Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (December 1994). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
Dhar M, Chauthaiwale V, Joshi JG (April 1993). "Sequence of a cDNA encoding the ferritin H-chain from an 11-week-old human fetal brain". Gene. 126 (2): 275–8. doi:10.1016/0378-1119(93)90380-L. PMID 7916709.
Qi Y, Dawson G (October 1994). "Hypoxia specifically and reversibly induces the synthesis of ferritin in oligodendrocytes and human oligodendrogliomas". Journal of Neurochemistry. 63 (4): 1485–90. doi:10.1046/j.1471-4159.1994.63041485.x. PMID 7931301. S2CID 22225445.
Rogers JT (March 1996). "Ferritin translation by interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes". Blood. 87 (6): 2525–37. doi:10.1182/blood.V87.6.2525.bloodjournal8762525. PMID 8630420.
Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

PDB gallery

1fha: SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS
2cei: RECOMBINANT HUMAN H FERRITIN, K86Q MUTANT, SOAKED WITH ZN
2chi: RECOMBINANT HUMAN H FERRITIN, K86Q AND E27D MUTANT
2cih: RECOMBINANT HUMAN H FERRITIN, K86Q AND E27D MUTANT, SOAKED WITH ZN
2clu: RECOMBINANT HUMAN H FERRITIN, K86Q AND E107D MUTANT
2cn6: RECOMBINANT HUMAN H FERRITIN, K86Q AND E107D MUTANT, SOAKED WITH ZN IONS
2cn7: RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT
2fha: HUMAN H CHAIN FERRITIN
2iu2: RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT, SOAKED WITH ZN IONS

v t e Other oxidoreductases (EC 1.15–1.21)
1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3
1.16: Oxidizing metal ions	Ceruloplasmin (Methionine synthase) reductase
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase 7-Hydroxymethyl chlorophyll a reductase
1.18: Acting on iron–sulfur proteins as donors	Nitrogenase
1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)
1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5
1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)