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Ferritin heavy chain (Ferritin H subunit) (EC 1.16.3.1) (Cell proliferation-inducing gene 15 protein) [Cleaved into: Ferritin heavy chain, N-terminally processed]

 FRIH_HUMAN              Reviewed;         183 AA.
P02794; B3KNR5; Q3KRA8; Q3SWW1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 211.
RecName: Full=Ferritin heavy chain;
Short=Ferritin H subunit;
EC=1.16.3.1;
AltName: Full=Cell proliferation-inducing gene 15 protein;
Contains:
RecName: Full=Ferritin heavy chain, N-terminally processed;
Name=FTH1; Synonyms=FTH, FTHL6; ORFNames=OK/SW-cl.84, PIG15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hepatocyte;
PubMed=6323167;
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. 3:23-27(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3840162;
Boyd D., Vecoli C., Belcher D.M., Jain S.K., Drysdale J.W.;
"Structural and functional relationships of human ferritin H and L
chains deduced from cDNA clones.";
J. Biol. Chem. 260:11755-11761(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3023856; DOI=10.1128/MCB.6.2.566;
Chou C.-C., Gatti R.A., Fuller M.L., Concannon P., Wong A., Chada S.,
Davis R.C., Salser W.A.;
"Structure and expression of ferritin genes in a human promyelocytic
cell line that differentiates in vitro.";
Mol. Cell. Biol. 6:566-573(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3003694; DOI=10.1093/nar/14.2.721;
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. 14:721-736(1986).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3020541; DOI=10.1073/pnas.83.19.7226;
Hentze M.W., Keim S., Papadopoulos P., O'Brien S., Modi W.,
Drysdale J.W., Leonard W.J., Harford J.B., Klausner R.D.;
"Cloning, characterization, expression, and chromosomal localization
of a human ferritin heavy-chain gene.";
Proc. Natl. Acad. Sci. U.S.A. 83:7226-7230(1986).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7916709; DOI=10.1016/0378-1119(93)90380-L;
Dhar M., Chauthaiwale V.M., Joshi J.G.;
"Sequence of a cDNA encoding the ferritin H-chain from an 11-week-old
human fetal brain.";
Gene 126:275-278(1993).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Chauthaiwale V.M., Dhar M., McLachlan D.R., Joshi J.G.;
"Cloning of a novel full length cDNA for ferritin heavy chain from
normal adult human and Alzheimer's brain.";
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA].
Franco A.V., Gray C.P., Myers K., Hersey P.;
"Detection of ferritin heavy chain by SEREX: a multifunctional
molecule in malignant tumour cells.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human cell proliferation gene 15.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Cervix, Colon, Lung, Ovary, Prostate, and
Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 128-183.
PubMed=6589621; DOI=10.1073/pnas.81.15.4751;
Boyd D., Jain S.K., Crampton J., Barrett K.J., Drysdale J.;
"Isolation and characterization of a cDNA clone for human ferritin
heavy chain.";
Proc. Natl. Acad. Sci. U.S.A. 81:4751-4755(1984).
[16]
INVOLVEMENT IN HFE5, AND TISSUE SPECIFICITY.
PubMed=11389486; DOI=10.1086/321261;
Kato J., Fujikawa K., Kanda M., Fukuda N., Sasaki K., Takayama T.,
Kobune M., Takada K., Takimoto R., Hamada H., Ikeda T., Niitsu Y.;
"A mutation, in the iron-responsive element of H ferritin mRNA,
causing autosomal dominant iron overload.";
Am. J. Hum. Genet. 69:191-197(2001).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-183, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
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 8:1346-1361(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=1992356; DOI=10.1038/349541a0;
Lawson D.M., Artymiuk P.J., Yewdall S.J., Smith J.M.A.,
Livingstone J.C., Treffry A., Luzzago A., Levi S., Arosio P.,
Cesarini G., Thomas C.D., Shaw W.V., Harrison P.M.;
"Solving the structure of human H ferritin by genetically engineering
intermolecular crystal contacts.";
Nature 349:541-544(1991).
[27]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=9159481; DOI=10.1006/jmbi.1997.0970;
Hempstead P.D., Yewdall S.J., Fernie A.R., Lawson D.M., Artymiuk P.J.,
Rice D.W., Ford G.C., Harrison P.M.;
"Comparison of the three-dimensional structures of recombinant human H
and horse L ferritins at high resolution.";
J. Mol. Biol. 268:424-448(1997).
-!- 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
-!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits:
L (light) chain and H (heavy) chain. The major chain can be light
or heavy, depending on the species and tissue type. In the human
liver, the heavy chain is predominant. The functional molecule
forms a roughly spherical shell with a diameter of 12 nm and
contains a central cavity into which the insoluble mineral iron
core is deposited.
-!- INTERACTION:
Q9UER7:DAXX; NbExp=5; IntAct=EBI-713259, EBI-77321;
P02792:FTL; NbExp=14; IntAct=EBI-713259, EBI-713279;
Q2Q067:HBZ (xeno); NbExp=3; IntAct=EBI-713259, EBI-9675545;
P04792:HSPB1; NbExp=2; IntAct=EBI-713259, EBI-352682;
P61244:MAX; NbExp=2; IntAct=EBI-713259, EBI-751711;
P02786:TFRC; NbExp=2; IntAct=EBI-713259, EBI-355727;
-!- TISSUE SPECIFICITY: Expressed in the liver.
{ECO:0000269|PubMed:11389486}.
-!- DISEASE: Hemochromatosis 5 (HFE5) [MIM:615517]: A disorder of iron
metabolism characterized by iron overload. Excess iron is
deposited in a variety of organs leading to their failure, and
resulting in serious illnesses including cirrhosis, hepatomas,
diabetes, cardiomyopathy, arthritis, and hypogonadotropic
hypogonadism. Severe effects of the disease usually do not appear
until after decades of progressive iron loading.
{ECO:0000269|PubMed:11389486}. Note=The disease is caused by
mutations affecting the gene represented in this entry. In a
Japanese family affected by HFE5, a single point mutation has been
detected in the iron-responsive element (IRE) in the 5'-UTR of
FTH1 mRNA. This mutation leads to an increased binding affinity
for iron regulatory protein and thereby to the efficient
suppression of mRNA translation.
-!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI05803.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Ferritin entry;
URL="https://en.wikipedia.org/wiki/Ferritin";
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EMBL; X00318; CAA25086.1; -; mRNA.
EMBL; M11146; AAA52437.1; -; mRNA.
EMBL; M12937; AAA35830.1; -; mRNA.
EMBL; X03487; CAA27205.1; -; Genomic_DNA.
EMBL; X03488; CAA27205.1; JOINED; Genomic_DNA.
EMBL; M14212; AAA52438.1; -; Genomic_DNA.
EMBL; M14211; AAA52438.1; JOINED; Genomic_DNA.
EMBL; M97164; AAA35832.1; -; mRNA.
EMBL; L20941; AAA35833.1; -; mRNA.
EMBL; AF088851; AAF89523.1; -; mRNA.
EMBL; AY258285; AAP82230.1; -; mRNA.
EMBL; AB062402; BAB93489.1; -; mRNA.
EMBL; AK054816; BAG51427.1; -; mRNA.
EMBL; DQ496108; ABF47097.1; -; Genomic_DNA.
EMBL; CH471076; EAW73989.1; -; Genomic_DNA.
EMBL; BC000857; AAH00857.1; -; mRNA.
EMBL; BC001399; AAH01399.1; -; mRNA.
EMBL; BC011359; AAH11359.1; -; mRNA.
EMBL; BC013724; AAH13724.1; -; mRNA.
EMBL; BC015156; AAH15156.1; -; mRNA.
EMBL; BC016009; AAH16009.1; -; mRNA.
EMBL; BC016857; AAH16857.1; -; mRNA.
EMBL; BC063514; AAH63514.1; -; mRNA.
EMBL; BC066961; AAH66961.1; -; mRNA.
EMBL; BC073750; AAH73750.1; -; mRNA.
EMBL; BC104643; AAI04644.1; -; mRNA.
EMBL; BC105802; AAI05803.1; ALT_INIT; mRNA.
EMBL; M15383; AAA52479.1; -; mRNA.
CCDS; CCDS41655.1; -.
PIR; A23517; FRHUH.
RefSeq; NP_002023.2; NM_002032.2.
UniGene; Hs.524910; -.
UniGene; Hs.645560; -.
PDB; 1FHA; X-ray; 2.40 A; A=1-183.
PDB; 2CEI; X-ray; 1.80 A; A=2-183.
PDB; 2CHI; X-ray; 1.60 A; A=2-183.
PDB; 2CIH; X-ray; 1.50 A; A=2-183.
PDB; 2CLU; X-ray; 2.10 A; A=2-183.
PDB; 2CN6; X-ray; 2.20 A; A=2-183.
PDB; 2CN7; X-ray; 1.75 A; A=2-183.
PDB; 2FHA; X-ray; 1.90 A; A=1-183.
PDB; 2IU2; X-ray; 1.80 A; A=2-183.
PDB; 2Z6M; X-ray; 2.72 A; A/B/C/D/E/F/G/H/I/J/K/L=2-177.
PDB; 3AJO; X-ray; 1.52 A; A=2-183.
PDB; 3AJP; X-ray; 1.90 A; A=2-183.
PDB; 3AJQ; X-ray; 1.58 A; A=2-183.
PDB; 3ERZ; X-ray; 3.06 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183.
PDB; 3ES3; X-ray; 2.79 A; A=1-183.
PDB; 4DYX; X-ray; 1.85 A; A=6-177.
PDB; 4DYY; X-ray; 1.90 A; A=6-177.
PDB; 4DYZ; X-ray; 2.30 A; A=6-177.
PDB; 4DZ0; X-ray; 2.50 A; A=6-177.
PDB; 4OYN; X-ray; 1.43 A; A=1-183.
PDB; 4Y08; X-ray; 1.34 A; A=1-183.
PDB; 4YKH; X-ray; 1.52 A; A=1-183.
PDB; 4ZJK; X-ray; 1.56 A; A=2-183.
PDB; 5CMQ; X-ray; 1.94 A; A=2-183.
PDB; 5CMR; X-ray; 3.79 A; A=2-183.
PDB; 5GN8; X-ray; 2.81 A; A=2-183, B=2-153.
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.
PDB; 5JKK; X-ray; 1.60 A; A/B/C/D/E/F/G/H=1-183.
PDB; 5JKL; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183.
PDB; 5JKM; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-183.
PDB; 5N26; X-ray; 2.05 A; A=2-183.
PDB; 5N27; X-ray; 1.74 A; A=2-183.
PDB; 5UP7; X-ray; 1.79 A; A=2-183.
PDB; 5UP8; X-ray; 2.63 A; A=2-183.
PDB; 5UP9; X-ray; 2.45 A; A/B/C/D/E/F=2-183.
PDB; 5VTD; X-ray; 1.95 A; A=2-183.
PDBsum; 1FHA; -.
PDBsum; 2CEI; -.
PDBsum; 2CHI; -.
PDBsum; 2CIH; -.
PDBsum; 2CLU; -.
PDBsum; 2CN6; -.
PDBsum; 2CN7; -.
PDBsum; 2FHA; -.
PDBsum; 2IU2; -.
PDBsum; 2Z6M; -.
PDBsum; 3AJO; -.
PDBsum; 3AJP; -.
PDBsum; 3AJQ; -.
PDBsum; 3ERZ; -.
PDBsum; 3ES3; -.
PDBsum; 4DYX; -.
PDBsum; 4DYY; -.
PDBsum; 4DYZ; -.
PDBsum; 4DZ0; -.
PDBsum; 4OYN; -.
PDBsum; 4Y08; -.
PDBsum; 4YKH; -.
PDBsum; 4ZJK; -.
PDBsum; 5CMQ; -.
PDBsum; 5CMR; -.
PDBsum; 5GN8; -.
PDBsum; 5GOU; -.
PDBsum; 5JKK; -.
PDBsum; 5JKL; -.
PDBsum; 5JKM; -.
PDBsum; 5N26; -.
PDBsum; 5N27; -.
PDBsum; 5UP7; -.
PDBsum; 5UP8; -.
PDBsum; 5UP9; -.
PDBsum; 5VTD; -.
ProteinModelPortal; P02794; -.
SMR; P02794; -.
BioGrid; 108773; 109.
CORUM; P02794; -.
DIP; DIP-38301N; -.
IntAct; P02794; 39.
MINT; MINT-4822446; -.
STRING; 9606.ENSP00000273550; -.
DrugBank; DB09147; Ferric pyrophosphate.
DrugBank; DB09412; Gallium citrate Ga-67.
DrugBank; DB00893; Iron Dextran.
iPTMnet; P02794; -.
PhosphoSitePlus; P02794; -.
SwissPalm; P02794; -.
BioMuta; FTH1; -.
DMDM; 120516; -.
UCD-2DPAGE; P02794; -.
EPD; P02794; -.
MaxQB; P02794; -.
PaxDb; P02794; -.
PeptideAtlas; P02794; -.
PRIDE; P02794; -.
TopDownProteomics; P02794; -.
DNASU; 2495; -.
Ensembl; ENST00000273550; ENSP00000273550; ENSG00000167996.
Ensembl; ENST00000620041; ENSP00000484477; ENSG00000167996.
GeneID; 2495; -.
KEGG; hsa:2495; -.
UCSC; uc001nsu.3; human.
CTD; 2495; -.
DisGeNET; 2495; -.
EuPathDB; HostDB:ENSG00000167996.15; -.
GeneCards; FTH1; -.
H-InvDB; HIX0128677; -.
H-InvDB; HIX0200367; -.
HGNC; HGNC:3976; FTH1.
HPA; CAB008623; -.
MalaCards; FTH1; -.
MIM; 134770; gene.
MIM; 615517; phenotype.
neXtProt; NX_P02794; -.
OpenTargets; ENSG00000167996; -.
Orphanet; 247790; FTH1-related iron overload.
PharmGKB; PA28392; -.
eggNOG; KOG2332; Eukaryota.
eggNOG; COG1528; LUCA.
GeneTree; ENSGT00760000119129; -.
HOVERGEN; HBG000410; -.
InParanoid; P02794; -.
KO; K00522; -.
OMA; QALHNFA; -.
OrthoDB; EOG091G0J20; -.
PhylomeDB; P02794; -.
TreeFam; TF313885; -.
BRENDA; 1.16.3.1; 2681.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-917937; Iron uptake and transport.
SIGNOR; P02794; -.
ChiTaRS; FTH1; human.
EvolutionaryTrace; P02794; -.
GeneWiki; FTH1; -.
GenomeRNAi; 2495; -.
PRO; PR:P02794; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000167996; -.
CleanEx; HS_FTH1; -.
ExpressionAtlas; P02794; baseline and differential.
Genevisible; P02794; HS.
GO; GO:0044754; C:autolysosome; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0008043; C:intracellular ferritin complex; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
GO; GO:0005506; F:iron ion binding; TAS:ProtInc.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0006955; P:immune response; ISS:UniProtKB.
GO; GO:0006880; P:intracellular sequestering of iron ion; IDA:UniProtKB.
GO; GO:0006826; P:iron ion transport; IEA:InterPro.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR001519; Ferritin.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009040; Ferritin-like_diiron.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR014034; Ferritin_CS.
InterPro; IPR008331; Ferritin_DPS_dom.
PANTHER; PTHR11431; PTHR11431; 1.
Pfam; PF00210; Ferritin; 1.
SUPFAM; SSF47240; SSF47240; 1.
PROSITE; PS00540; FERRITIN_1; 1.
PROSITE; PS00204; FERRITIN_2; 1.
PROSITE; PS50905; FERRITIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Iron; Iron storage;
Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome.
CHAIN 1 183 Ferritin heavy chain.
/FTId=PRO_0000201048.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:22814378}.
CHAIN 2 183 Ferritin heavy chain, N-terminally
processed.
/FTId=PRO_0000424472.
DOMAIN 11 160 Ferritin-like diiron.
{ECO:0000255|PROSITE-ProRule:PRU00085}.
METAL 28 28 Iron 1.
METAL 63 63 Iron 1.
METAL 63 63 Iron 2.
METAL 66 66 Iron 1.
METAL 108 108 Iron 2.
METAL 142 142 Iron 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 2 2 N-acetylthreonine; in Ferritin heavy
chain, N-terminally processed.
{ECO:0000244|PubMed:22814378}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:18318008}.
CONFLICT 176 183 LGDSDNES -> WETVIMKAKPRANFP (in Ref. 1;
CAA25086). {ECO:0000305}.
HELIX 15 42 {ECO:0000244|PDB:4Y08}.
TURN 45 47 {ECO:0000244|PDB:4Y08}.
HELIX 50 77 {ECO:0000244|PDB:4Y08}.
HELIX 97 124 {ECO:0000244|PDB:4Y08}.
HELIX 128 137 {ECO:0000244|PDB:4Y08}.
HELIX 139 159 {ECO:0000244|PDB:4Y08}.
TURN 160 163 {ECO:0000244|PDB:4Y08}.
HELIX 165 174 {ECO:0000244|PDB:4Y08}.
STRAND 176 178 {ECO:0000244|PDB:5UP8}.
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


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