ID FRIH_HUMAN Reviewed; 183 AA. AC P02794; B3KNR5; Q3KRA8; Q3SWW1; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 253. DE RecName: Full=Ferritin heavy chain; DE Short=Ferritin H subunit; DE EC=1.16.3.1 {ECO:0000269|PubMed:9003196}; DE AltName: Full=Cell proliferation-inducing gene 15 protein; DE Contains: DE RecName: Full=Ferritin heavy chain, N-terminally processed; GN Name=FTH1; Synonyms=FTH, FTHL6; ORFNames=OK/SW-cl.84, PIG15; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Hepatocyte; RX PubMed=6323167; DOI=10.1002/j.1460-2075.1984.tb01756.x; RA Costanzo F., Santoro C., Colantuoni V., Bensi G., Raugei G., Romano V., RA Cortese R.; RT "Cloning and sequencing of a full length cDNA coding for a human RT apoferritin H chain: evidence for a multigene family."; RL EMBO J. 3:23-27(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3840162; DOI=10.1016/s0021-9258(17)39094-4; RA Boyd D., Vecoli C., Belcher D.M., Jain S.K., Drysdale J.W.; RT "Structural and functional relationships of human ferritin H and L chains RT deduced from cDNA clones."; RL J. Biol. Chem. 260:11755-11761(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3023856; DOI=10.1128/mcb.6.2.566-573.1986; RA Chou C.-C., Gatti R.A., Fuller M.L., Concannon P., Wong A., Chada S., RA Davis R.C., Salser W.A.; RT "Structure and expression of ferritin genes in a human promyelocytic cell RT line that differentiates in vitro."; RL Mol. Cell. Biol. 6:566-573(1986). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3003694; DOI=10.1093/nar/14.2.721; RA Costanzo F., Colombo M., Staempfli S., Santoro C., Marone M., Frank R., RA Delius H., Cortese R.; RT "Structure of gene and pseudogenes of human apoferritin H."; RL Nucleic Acids Res. 14:721-736(1986). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3020541; DOI=10.1073/pnas.83.19.7226; RA Hentze M.W., Keim S., Papadopoulos P., O'Brien S., Modi W., Drysdale J.W., RA Leonard W.J., Harford J.B., Klausner R.D.; RT "Cloning, characterization, expression, and chromosomal localization of a RT human ferritin heavy-chain gene."; RL Proc. Natl. Acad. Sci. U.S.A. 83:7226-7230(1986). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=7916709; DOI=10.1016/0378-1119(93)90380-l; RA Dhar M., Chauthaiwale V.M., Joshi J.G.; RT "Sequence of a cDNA encoding the ferritin H-chain from an 11-week-old human RT fetal brain."; RL Gene 126:275-278(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Chauthaiwale V.M., Dhar M., McLachlan D.R., Joshi J.G.; RT "Cloning of a novel full length cDNA for ferritin heavy chain from normal RT adult human and Alzheimer's brain."; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Franco A.V., Gray C.P., Myers K., Hersey P.; RT "Detection of ferritin heavy chain by SEREX: a multifunctional molecule in RT malignant tumour cells."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kim J.W.; RT "Identification of a human cell proliferation gene 15."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Cervix, Colon, Lung, Ovary, Prostate, and Salivary RC gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 128-183. RX PubMed=6589621; DOI=10.1073/pnas.81.15.4751; RA Boyd D., Jain S.K., Crampton J., Barrett K.J., Drysdale J.; RT "Isolation and characterization of a cDNA clone for human ferritin heavy RT chain."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4751-4755(1984). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-28; LYS-87 AND RP GLU-108. RX PubMed=9003196; DOI=10.1021/bi961830l; RA Treffry A., Zhao Z., Quail M.A., Guest J.R., Harrison P.M.; RT "Dinuclear center of ferritin: studies of iron binding and oxidation show RT differences in the two iron sites."; RL Biochemistry 36:432-441(1997). RN [17] RP TISSUE SPECIFICITY, AND INVOLVEMENT IN HFE5. RX PubMed=11389486; DOI=10.1086/321261; RA Kato J., Fujikawa K., Kanda M., Fukuda N., Sasaki K., Takayama T., RA Kobune M., Takada K., Takimoto R., Hamada H., Ikeda T., Niitsu Y.; RT "A mutation, in the iron-responsive element of H ferritin mRNA, causing RT autosomal dominant iron overload."; RL Am. J. Hum. Genet. 69:191-197(2001). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-183, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [27] {ECO:0007744|PDB:1FHA} RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON. RX PubMed=1992356; DOI=10.1038/349541a0; RA Lawson D.M., Artymiuk P.J., Yewdall S.J., Smith J.M.A., Livingstone J.C., RA Treffry A., Luzzago A., Levi S., Arosio P., Cesarini G., Thomas C.D., RA Shaw W.V., Harrison P.M.; RT "Solving the structure of human H ferritin by genetically engineering RT intermolecular crystal contacts."; RL Nature 349:541-544(1991). RN [28] {ECO:0007744|PDB:2FHA} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT. RX PubMed=9159481; DOI=10.1006/jmbi.1997.0970; RA Hempstead P.D., Yewdall S.J., Fernie A.R., Lawson D.M., Artymiuk P.J., RA Rice D.W., Ford G.C., Harrison P.M.; RT "Comparison of the three-dimensional structures of recombinant human H and RT horse L ferritins at high resolution."; RL J. Mol. Biol. 268:424-448(1997). CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form. CC Important for iron homeostasis. Has ferroxidase activity CC (PubMed:9003196). Iron is taken up in the ferrous form and deposited as CC ferric hydroxides after oxidation (PubMed:9003196). Also plays a role CC in delivery of iron to cells (By similarity). Mediates iron uptake in CC capsule cells of the developing kidney (By similarity). CC {ECO:0000250|UniProtKB:P09528, ECO:0000269|PubMed:9003196}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; CC Evidence={ECO:0000269|PubMed:9003196}; CC -!- SUBUNIT: Oligomer of 24 subunits (PubMed:9159481). There are two types CC of subunits: L (light) chain and H (heavy) chain (PubMed:9159481). The CC major chain can be light or heavy, depending on the species and tissue CC type. In the human liver, the heavy chain is predominant CC (PubMed:9159481). The functional molecule forms a roughly spherical CC shell with a diameter of 12 nm and contains a central cavity into which CC the insoluble mineral iron core is deposited (PubMed:9159481). CC {ECO:0000269|PubMed:9159481}. CC -!- INTERACTION: CC P02794; O95429: BAG4; NbExp=4; IntAct=EBI-713259, EBI-2949658; CC P02794; Q9UER7: DAXX; NbExp=5; IntAct=EBI-713259, EBI-77321; CC P02794; P02794: FTH1; NbExp=3; IntAct=EBI-713259, EBI-713259; CC P02794; P02792: FTL; NbExp=16; IntAct=EBI-713259, EBI-713279; CC P02794; P51116: FXR2; NbExp=3; IntAct=EBI-713259, EBI-740459; CC P02794; P04792: HSPB1; NbExp=2; IntAct=EBI-713259, EBI-352682; CC P02794; P61244: MAX; NbExp=2; IntAct=EBI-713259, EBI-751711; CC P02794; P02786: TFRC; NbExp=2; IntAct=EBI-713259, EBI-355727; CC P02794; Q92574: TSC1; NbExp=3; IntAct=EBI-713259, EBI-1047085; CC P02794; Q2Q067: HBZ; Xeno; NbExp=3; IntAct=EBI-713259, EBI-9675545; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P19130}. CC -!- TISSUE SPECIFICITY: Expressed in the liver. CC {ECO:0000269|PubMed:11389486}. CC -!- DISEASE: Hemochromatosis 5 (HFE5) [MIM:615517]: A disorder of iron CC metabolism characterized by iron overload. Excess iron is deposited in CC a variety of organs leading to their failure, and resulting in serious CC illnesses including cirrhosis, hepatomas, diabetes, cardiomyopathy, CC arthritis, and hypogonadotropic hypogonadism. Severe effects of the CC disease usually do not appear until after decades of progressive iron CC loading. {ECO:0000269|PubMed:11389486}. Note=The disease is caused by CC variants affecting the gene represented in this entry. In a Japanese CC family affected by HFE5, a single point mutation has been detected in CC the iron-responsive element (IRE) in the 5'-UTR of FTH1 mRNA. This CC mutation leads to an increased binding affinity for iron regulatory CC protein and thereby to the efficient suppression of mRNA translation. CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI05803.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ferritin entry; CC URL="https://en.wikipedia.org/wiki/Ferritin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X00318; CAA25086.1; -; mRNA. DR EMBL; M11146; AAA52437.1; -; mRNA. DR EMBL; M12937; AAA35830.1; -; mRNA. DR EMBL; X03487; CAA27205.1; -; Genomic_DNA. DR EMBL; X03488; CAA27205.1; JOINED; Genomic_DNA. DR EMBL; M14212; AAA52438.1; -; Genomic_DNA. DR EMBL; M14211; AAA52438.1; JOINED; Genomic_DNA. DR EMBL; M97164; AAA35832.1; -; mRNA. DR EMBL; L20941; AAA35833.1; -; mRNA. DR EMBL; AF088851; AAF89523.1; -; mRNA. DR EMBL; AY258285; AAP82230.1; -; mRNA. DR EMBL; AB062402; BAB93489.1; -; mRNA. DR EMBL; AK054816; BAG51427.1; -; mRNA. DR EMBL; DQ496108; ABF47097.1; -; Genomic_DNA. DR EMBL; CH471076; EAW73989.1; -; Genomic_DNA. DR EMBL; BC000857; AAH00857.1; -; mRNA. DR EMBL; BC001399; AAH01399.1; -; mRNA. DR EMBL; BC011359; AAH11359.1; -; mRNA. DR EMBL; BC013724; AAH13724.1; -; mRNA. DR EMBL; BC015156; AAH15156.1; -; mRNA. DR EMBL; BC016009; AAH16009.1; -; mRNA. DR EMBL; BC016857; AAH16857.1; -; mRNA. DR EMBL; BC063514; AAH63514.1; -; mRNA. DR EMBL; BC066961; AAH66961.1; -; mRNA. DR EMBL; BC073750; AAH73750.1; -; mRNA. DR EMBL; BC104643; AAI04644.1; -; mRNA. DR EMBL; BC105802; AAI05803.1; ALT_INIT; mRNA. DR EMBL; M15383; AAA52479.1; -; mRNA. DR CCDS; CCDS41655.1; -. DR PIR; A23517; FRHUH. DR RefSeq; NP_002023.2; NM_002032.2. DR PDB; 1FHA; X-ray; 2.40 A; A=1-183. DR PDB; 2CEI; X-ray; 1.80 A; A=2-183. DR PDB; 2CHI; X-ray; 1.60 A; A=2-183. DR PDB; 2CIH; X-ray; 1.50 A; A=2-183. DR PDB; 2CLU; X-ray; 2.10 A; A=2-183. DR PDB; 2CN6; X-ray; 2.20 A; A=2-183. DR PDB; 2CN7; X-ray; 1.75 A; A=2-183. DR PDB; 2FHA; X-ray; 1.90 A; A=1-183. DR PDB; 2IU2; X-ray; 1.80 A; A=2-183. DR PDB; 2Z6M; X-ray; 2.72 A; A/B/C/D/E/F/G/H/I/J/K/L=2-177. DR PDB; 3AJO; X-ray; 1.52 A; A=2-183. DR PDB; 3AJP; X-ray; 1.90 A; A=2-183. DR PDB; 3AJQ; X-ray; 1.58 A; A=2-183. DR PDB; 3ERZ; X-ray; 3.06 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183. DR PDB; 3ES3; X-ray; 2.79 A; A=1-183. DR PDB; 4DYX; X-ray; 1.85 A; A=6-177. DR PDB; 4DYY; X-ray; 1.90 A; A=6-177. DR PDB; 4DYZ; X-ray; 2.30 A; A=6-177. DR PDB; 4DZ0; X-ray; 2.50 A; A=6-177. DR PDB; 4OYN; X-ray; 1.43 A; A=1-183. DR PDB; 4Y08; X-ray; 1.34 A; A=1-183. DR PDB; 4YKH; X-ray; 1.52 A; A=1-183. DR PDB; 4ZJK; X-ray; 1.56 A; A=2-183. DR PDB; 5CMQ; X-ray; 1.94 A; A=2-183. DR PDB; 5CMR; X-ray; 3.79 A; A=2-183. DR PDB; 5GN8; X-ray; 2.81 A; A=2-183, B=2-153. DR PDB; 5GOU; X-ray; 2.91 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-183. DR PDB; 5JKK; X-ray; 1.60 A; A/B/C/D/E/F/G/H=1-183. DR PDB; 5JKL; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183. DR PDB; 5JKM; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183. DR PDB; 5N26; X-ray; 2.05 A; A=2-183. DR PDB; 5N27; X-ray; 1.74 A; A=2-183. DR PDB; 5UP7; X-ray; 1.79 A; A=2-183. DR PDB; 5UP8; X-ray; 2.63 A; A=2-183. DR PDB; 5UP9; X-ray; 2.45 A; A/B/C/D/E/F=2-183. DR PDB; 5VTD; X-ray; 1.95 A; A=2-183. DR PDB; 5XB1; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-160. DR PDB; 5YI5; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-177. DR PDB; 5ZND; X-ray; 3.00 A; A=1-134. DR PDB; 6B8F; X-ray; 1.06 A; A=2-183. DR PDB; 6B8G; X-ray; 1.13 A; A=2-183. DR PDB; 6FTV; X-ray; 1.58 A; A=2-183. DR PDB; 6GSR; EM; 5.50 A; Aa/Ac/Ad/Ae/Af/Ag/Ah/Ai/Aj/Ak/Al/Am/An/Ao/Ap/Ar/As/At/Au/Av/Aw/Ax/Ay/Az=2-183. DR PDB; 6H5I; EM; 3.90 A; Aa/Ac/Ad/Ae/Af/Ag/Ah/Ai/Aj/Ak/Al/Am/An/Ao/Ap/Ar/As/At/Au/Av/Aw/Ax/Ay/Az=6-177. DR PDB; 6H6T; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183. DR PDB; 6H6U; X-ray; 2.00 A; A/B/C/D/E/F=1-183. DR PDB; 6IPC; X-ray; 4.44 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-183. DR PDB; 6IPO; X-ray; 3.00 A; A/B=2-183. DR PDB; 6IPP; X-ray; 2.70 A; A/B=2-183. DR PDB; 6IPQ; X-ray; 3.10 A; A=2-183. DR PDB; 6J4A; X-ray; 3.99 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183. DR PDB; 6J7G; X-ray; 3.87 A; A/B/C/D/G/H/I/J/M/N/O/P/Q/R/S/T/W/X/Y/Z/a/b/e/f=2-183. DR PDB; 6JOB; Other; 2.93 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183. DR PDB; 6JPS; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-183. DR PDB; 6KE2; X-ray; 1.80 A; A=1-183. DR PDB; 6KE4; X-ray; 2.30 A; A=1-183. DR PDB; 6M52; EM; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-183. DR PDB; 6M54; EM; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-183. DR PDB; 6WYF; X-ray; 1.25 A; A=2-183. DR PDB; 6WYG; X-ray; 2.27 A; A/B/C/D=2-183. DR PDB; 6WYH; X-ray; 2.22 A; A/B/C/D=2-183. DR PDB; 6Z6U; EM; 1.25 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=1-183. DR PDB; 6Z9E; EM; 1.55 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=1-183. DR PDB; 6Z9F; EM; 1.56 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=1-183. DR PDB; 7A6A; EM; 1.15 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=1-183. DR PDB; 7A6B; EM; 1.33 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=1-183. DR PDB; 7CK8; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=5-177. DR PDB; 7CK9; X-ray; 1.60 A; A=6-177. DR PDB; 7JGK; X-ray; 2.68 A; A=2-183. DR PDB; 7JGL; X-ray; 2.34 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/a/b/c/d/e/f=2-183. DR PDB; 7JGM; X-ray; 2.31 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/a/b/c/d/e/f=2-183. DR PDB; 7JGN; X-ray; 2.07 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/a/b/c/d/e/f=2-183. DR PDB; 7JGO; X-ray; 3.08 A; A=2-183. DR PDB; 7JGP; X-ray; 6.42 A; A=2-183. DR PDB; 7JGQ; X-ray; 3.01 A; A=2-183. DR PDB; 7K26; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=2-183. DR PDB; 7K3V; EM; 1.34 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=6-177. DR PDB; 7K3W; EM; 1.36 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=6-177. DR PDB; 7KE3; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183. DR PDB; 7KE5; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-183. DR PDB; 7PF1; EM; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=4-177. DR PDB; 7R5O; EM; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=5-177. DR PDB; 7RRP; EM; 1.27 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=6-177. DR PDB; 7V66; EM; 1.89 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=6-177. DR PDB; 7VD8; EM; 1.96 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=6-177. DR PDB; 7ZG7; EM; 1.77 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=6-177. DR PDB; 8A2L; X-ray; 2.30 A; AAA=2-183. DR PDB; 8A2M; X-ray; 1.57 A; AAA=2-183. DR PDB; 8A5N; X-ray; 1.52 A; AAA=2-183. DR PDB; 8B7O; X-ray; 1.17 A; AAA=2-183. DR PDB; 8CPM; EM; 1.81 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=5-177. DR PDB; 8CPS; EM; 1.82 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=5-177. DR PDB; 8CPT; EM; 1.79 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=5-177. DR PDB; 8CPU; EM; 1.76 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=5-177. DR PDB; 8CPV; EM; 1.76 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=5-177. DR PDB; 8CPW; EM; 1.79 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=5-177. DR PDB; 8CPX; EM; 1.76 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=5-177. DR PDB; 8DHX; EM; 2.92 A; 1/2/4/6/A/B/E/F/G/H/I/K/M/O/P/Q/S/U/W/X/Y/a/e/r=1-183. DR PDB; 8DNP; EM; 2.69 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-183. DR PDB; 8F49; EM; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=6-177. DR PDB; 8HHS; EM; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=6-177. DR PDBsum; 1FHA; -. DR PDBsum; 2CEI; -. DR PDBsum; 2CHI; -. DR PDBsum; 2CIH; -. DR PDBsum; 2CLU; -. DR PDBsum; 2CN6; -. DR PDBsum; 2CN7; -. DR PDBsum; 2FHA; -. DR PDBsum; 2IU2; -. DR PDBsum; 2Z6M; -. DR PDBsum; 3AJO; -. DR PDBsum; 3AJP; -. DR PDBsum; 3AJQ; -. DR PDBsum; 3ERZ; -. DR PDBsum; 3ES3; -. DR PDBsum; 4DYX; -. DR PDBsum; 4DYY; -. DR PDBsum; 4DYZ; -. DR PDBsum; 4DZ0; -. DR PDBsum; 4OYN; -. DR PDBsum; 4Y08; -. DR PDBsum; 4YKH; -. DR PDBsum; 4ZJK; -. DR PDBsum; 5CMQ; -. DR PDBsum; 5CMR; -. DR PDBsum; 5GN8; -. DR PDBsum; 5GOU; -. DR PDBsum; 5JKK; -. DR PDBsum; 5JKL; -. DR PDBsum; 5JKM; -. DR PDBsum; 5N26; -. DR PDBsum; 5N27; -. DR PDBsum; 5UP7; -. DR PDBsum; 5UP8; -. DR PDBsum; 5UP9; -. DR PDBsum; 5VTD; -. DR PDBsum; 5XB1; -. DR PDBsum; 5YI5; -. DR PDBsum; 5ZND; -. DR PDBsum; 6B8F; -. DR PDBsum; 6B8G; -. DR PDBsum; 6FTV; -. DR PDBsum; 6GSR; -. DR PDBsum; 6H5I; -. DR PDBsum; 6H6T; -. DR PDBsum; 6H6U; -. DR PDBsum; 6IPC; -. DR PDBsum; 6IPO; -. DR PDBsum; 6IPP; -. DR PDBsum; 6IPQ; -. DR PDBsum; 6J4A; -. DR PDBsum; 6J7G; -. DR PDBsum; 6JOB; -. DR PDBsum; 6JPS; -. DR PDBsum; 6KE2; -. DR PDBsum; 6KE4; -. DR PDBsum; 6M52; -. DR PDBsum; 6M54; -. DR PDBsum; 6WYF; -. DR PDBsum; 6WYG; -. DR PDBsum; 6WYH; -. DR PDBsum; 6Z6U; -. DR PDBsum; 6Z9E; -. DR PDBsum; 6Z9F; -. DR PDBsum; 7A6A; -. DR PDBsum; 7A6B; -. DR PDBsum; 7CK8; -. DR PDBsum; 7CK9; -. DR PDBsum; 7JGK; -. DR PDBsum; 7JGL; -. DR PDBsum; 7JGM; -. DR PDBsum; 7JGN; -. DR PDBsum; 7JGO; -. DR PDBsum; 7JGP; -. DR PDBsum; 7JGQ; -. DR PDBsum; 7K26; -. DR PDBsum; 7K3V; -. DR PDBsum; 7K3W; -. DR PDBsum; 7KE3; -. DR PDBsum; 7KE5; -. DR PDBsum; 7PF1; -. DR PDBsum; 7R5O; -. DR PDBsum; 7RRP; -. DR PDBsum; 7V66; -. DR PDBsum; 7VD8; -. DR PDBsum; 7ZG7; -. DR PDBsum; 8A2L; -. DR PDBsum; 8A2M; -. DR PDBsum; 8A5N; -. DR PDBsum; 8B7O; -. DR PDBsum; 8CPM; -. DR PDBsum; 8CPS; -. DR PDBsum; 8CPT; -. DR PDBsum; 8CPU; -. DR PDBsum; 8CPV; -. DR PDBsum; 8CPW; -. DR PDBsum; 8CPX; -. DR PDBsum; 8DHX; -. DR PDBsum; 8DNP; -. DR PDBsum; 8F49; -. DR PDBsum; 8HHS; -. DR AlphaFoldDB; P02794; -. DR EMDB; EMD-0046; -. DR EMDB; EMD-0140; -. DR EMDB; EMD-11103; -. DR EMDB; EMD-11121; -. DR EMDB; EMD-11122; -. DR EMDB; EMD-11668; -. DR EMDB; EMD-11669; -. DR EMDB; EMD-13364; -. DR EMDB; EMD-14332; -. DR EMDB; EMD-14705; -. DR EMDB; EMD-16783; -. DR EMDB; EMD-16784; -. DR EMDB; EMD-16785; -. DR EMDB; EMD-16786; -. DR EMDB; EMD-16787; -. DR EMDB; EMD-16788; -. DR EMDB; EMD-16789; -. DR EMDB; EMD-22657; -. DR EMDB; EMD-22658; -. DR EMDB; EMD-24665; -. DR EMDB; EMD-27437; -. DR EMDB; EMD-27576; -. DR EMDB; EMD-30083; -. DR EMDB; EMD-30084; -. DR EMDB; EMD-31736; -. DR EMDB; EMD-31910; -. DR EMDB; EMD-3853; -. DR EMDB; EMD-3854; -. DR EMDB; EMD-6714; -. DR EMDB; EMD-6830; -. DR SMR; P02794; -. DR BioGRID; 108773; 175. DR CORUM; P02794; -. DR DIP; DIP-38301N; -. DR IntAct; P02794; 105. DR MINT; P02794; -. DR STRING; 9606.ENSP00000273550; -. DR DrugBank; DB13995; Ferric pyrophosphate citrate. DR DrugBank; DB14490; Ferrous ascorbate. DR DrugBank; DB14491; Ferrous fumarate. DR DrugBank; DB14488; Ferrous gluconate. DR DrugBank; DB14501; Ferrous glycine sulfate. DR DrugBank; DB14489; Ferrous succinate. DR DrugBank; DB06784; Gallium citrate Ga-67. DR DrugBank; DB01592; Iron. DR DrugBank; DB00893; Iron Dextran. DR GlyGen; P02794; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P02794; -. DR PhosphoSitePlus; P02794; -. DR SwissPalm; P02794; -. DR BioMuta; FTH1; -. DR DMDM; 120516; -. DR EPD; P02794; -. DR jPOST; P02794; -. DR MassIVE; P02794; -. DR MaxQB; P02794; -. DR PaxDb; 9606-ENSP00000273550; -. DR PeptideAtlas; P02794; -. DR ProteomicsDB; 51600; -. DR Pumba; P02794; -. DR TopDownProteomics; P02794; -. DR ABCD; P02794; 5 sequenced antibodies. DR Antibodypedia; 28385; 983 antibodies from 41 providers. DR DNASU; 2495; -. DR Ensembl; ENST00000273550.12; ENSP00000273550.7; ENSG00000167996.16. DR Ensembl; ENST00000620041.5; ENSP00000484477.1; ENSG00000167996.16. DR GeneID; 2495; -. DR KEGG; hsa:2495; -. DR MANE-Select; ENST00000273550.12; ENSP00000273550.7; NM_002032.3; NP_002023.2. DR UCSC; uc001nsu.3; human. DR AGR; HGNC:3976; -. DR CTD; 2495; -. DR DisGeNET; 2495; -. DR GeneCards; FTH1; -. DR HGNC; HGNC:3976; FTH1. DR HPA; ENSG00000167996; Low tissue specificity. DR MalaCards; FTH1; -. DR MIM; 134770; gene. DR MIM; 615517; phenotype. DR neXtProt; NX_P02794; -. DR OpenTargets; ENSG00000167996; -. DR Orphanet; 247790; FTH1-related iron overload. DR PharmGKB; PA28392; -. DR VEuPathDB; HostDB:ENSG00000167996; -. DR eggNOG; KOG2332; Eukaryota. DR GeneTree; ENSGT00950000182841; -. DR HOGENOM; CLU_065681_4_0_1; -. DR InParanoid; P02794; -. DR OMA; QKYSDEC; -. DR OrthoDB; 4611704at2759; -. DR PhylomeDB; P02794; -. DR TreeFam; TF313885; -. DR BRENDA; 1.16.3.1; 2681. DR PathwayCommons; P02794; -. DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-917937; Iron uptake and transport. DR SignaLink; P02794; -. DR SIGNOR; P02794; -. DR BioGRID-ORCS; 2495; 81 hits in 1125 CRISPR screens. DR ChiTaRS; FTH1; human. DR EvolutionaryTrace; P02794; -. DR GeneWiki; FTH1; -. DR GenomeRNAi; 2495; -. DR Pharos; P02794; Tbio. DR PRO; PR:P02794; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P02794; Protein. DR Bgee; ENSG00000167996; Expressed in stromal cell of endometrium and 198 other cell types or tissues. DR ExpressionAtlas; P02794; baseline and differential. DR GO; GO:0044754; C:autolysosome; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0008043; C:intracellular ferritin complex; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome. DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IMP:UniProtKB. DR GO; GO:0004322; F:ferroxidase activity; IMP:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005506; F:iron ion binding; TAS:ProtInc. DR GO; GO:0140315; F:iron ion sequestering activity; IDA:GO_Central. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0006879; P:intracellular iron ion homeostasis; TAS:ProtInc. DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central. DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central. DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB. DR CDD; cd01056; Euk_Ferritin; 1. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR012347; Ferritin-like. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR014034; Ferritin_CS. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; FERRITIN; 1. DR PANTHER; PTHR11431:SF37; FERRITIN HEAVY CHAIN; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00540; FERRITIN_1; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. DR UCD-2DPAGE; P02794; -. DR Genevisible; P02794; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Iron; Iron storage; Metal-binding; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1..183 FT /note="Ferritin heavy chain" FT /id="PRO_0000201048" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..183 FT /note="Ferritin heavy chain, N-terminally processed" FT /id="PRO_0000424472" FT DOMAIN 11..160 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 28 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:1992356, FT ECO:0007744|PDB:1FHA" FT BINDING 63 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:1992356, FT ECO:0007744|PDB:1FHA" FT BINDING 63 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 66 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:1992356, FT ECO:0007744|PDB:1FHA" FT BINDING 108 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 142 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 2 FT /note="N-acetylthreonine; in Ferritin heavy chain, N- FT terminally processed" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008" FT MUTAGEN 28 FT /note="E->A: Reduces iron binding and oxidation rate; when FT associated with Q-87." FT /evidence="ECO:0000269|PubMed:9003196" FT MUTAGEN 87 FT /note="K->Q: Reduces iron binding and oxidation rate; when FT associated with A-28. No effect on iron binding but the FT oxidation rate is severely reduced; when associated with FT A-108." FT /evidence="ECO:0000269|PubMed:9003196" FT MUTAGEN 108 FT /note="E->A: No effect on iron binding but the oxidation FT rate is severely reduced; when associated with Q-87." FT /evidence="ECO:0000269|PubMed:9003196" FT CONFLICT 176..183 FT /note="LGDSDNES -> WETVIMKAKPRANFP (in Ref. 1; CAA25086)" FT /evidence="ECO:0000305" FT HELIX 15..42 FT /evidence="ECO:0007829|PDB:6B8F" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:6B8F" FT HELIX 50..77 FT /evidence="ECO:0007829|PDB:6B8F" FT HELIX 97..124 FT /evidence="ECO:0007829|PDB:6B8F" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:6B8F" FT HELIX 139..159 FT /evidence="ECO:0007829|PDB:6B8F" FT TURN 160..163 FT /evidence="ECO:0007829|PDB:6B8F" FT HELIX 165..174 FT /evidence="ECO:0007829|PDB:6B8F" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:5UP8" SQ SEQUENCE 183 AA; 21226 MW; FEF75640A29CCF56 CRC64; MTTASTSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD CDDWESGLNA MECALHLEKN VNQSLLELHK LATDKNDPHL CDFIETHYLN EQVKAIKELG DHVTNLRKMG APESGLAEYL FDKHTLGDSD NES //