FRIH_HUMAN
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 03-AUG-2022, entry version 244.
DE RecName: Full=Ferritin heavy chain;
DE Short=Ferritin H subunit;
DE EC=1.16.3.1;
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 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 INVOLVEMENT IN HFE5, AND TISSUE SPECIFICITY.
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
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 [27]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
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. Iron is taken
CC up in the ferrous form and deposited as ferric hydroxides after
CC oxidation. Also plays a role in delivery of iron to cells. Mediates
CC iron uptake in capsule cells of the developing kidney (By similarity).
CC {ECO:0000250}.
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 -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L
CC (light) chain and H (heavy) chain. The major chain can be light or
CC heavy, depending on the species and tissue type. In the human liver,
CC the heavy chain is predominant. The functional molecule forms a roughly
CC spherical shell with a diameter of 12 nm and contains a central cavity
CC into which the insoluble mineral iron core is deposited.
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 -!- 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";
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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; 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; 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 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; 7RRP; -.
DR PDBsum; 7VD8; -.
DR AlphaFoldDB; P02794; -.
DR SMR; P02794; -.
DR BioGRID; 108773; 157.
DR CORUM; P02794; -.
DR DIP; DIP-38301N; -.
DR IntAct; P02794; 102.
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; 1 site.
DR iPTMnet; P02794; -.
DR PhosphoSitePlus; P02794; -.
DR SwissPalm; P02794; -.
DR BioMuta; FTH1; -.
DR DMDM; 120516; -.
DR UCD-2DPAGE; P02794; -.
DR EPD; P02794; -.
DR jPOST; P02794; -.
DR MassIVE; P02794; -.
DR MaxQB; P02794; -.
DR PaxDb; P02794; -.
DR PeptideAtlas; P02794; -.
DR PRIDE; P02794; -.
DR ProteomicsDB; 51600; -.
DR TopDownProteomics; P02794; -.
DR ABCD; P02794; 5 sequenced antibodies.
DR Antibodypedia; 28385; 887 antibodies from 41 providers.
DR DNASU; 2495; -.
DR Ensembl; ENST00000273550.12; ENSP00000273550.7; ENSG00000167996.16.
DR Ensembl; ENST00000620041.4; 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 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; YLSMGYF; -.
DR OrthoDB; 1249457at2759; -.
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 1044 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 196 other tissues.
DR ExpressionAtlas; P02794; baseline and differential.
DR Genevisible; P02794; HS.
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; IBA:GO_Central.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; TAS:ProtInc.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IDA:UniProtKB.
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 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; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00540; FERRITIN_1; 1.
DR PROSITE; PS00204; FERRITIN_2; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; 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 BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
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 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
