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P02794 (FRIH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 175. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferritin heavy chain

Short name=Ferritin H subunit
EC=1.16.3.1
Alternative name(s):
Cell proliferation-inducing gene 15 protein

Cleaved into the following chain:

  1. Ferritin heavy chain, N-terminally processed
Gene names
Name:FTH1
Synonyms:FTH, FTHL6
ORF Names:OK/SW-cl.84, PIG15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Subunit structure

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.

Tissue specificity

Expressed in the liver. Ref.16

Involvement in 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.
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. Ref.16

Sequence similarities

Belongs to the ferritin family.

Contains 1 ferritin-like diiron domain.

Sequence caution

The sequence AAI05803.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processIron storage
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Traceable author statement. Source: Reactome

immune response

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular sequestering of iron ion

Inferred from direct assay PubMed 9924025. Source: UniProtKB

iron ion transport

Inferred from electronic annotation. Source: InterPro

membrane organization

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fibroblast proliferation

Inferred from direct assay PubMed 9924025. Source: UniProtKB

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

intracellular ferritin complex

Traceable author statement Ref.15. Source: ProtInc

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

ferroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

iron ion binding

Traceable author statement Ref.5. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 16169070PubMed 16189514PubMed 20195357PubMed 21516116PubMed 21573799PubMed 21988832. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 183183Ferritin heavy chain
PRO_0000201048
Initiator methionine11Removed; alternate Ref.23
Chain2 – 183182Ferritin heavy chain, N-terminally processed
PRO_0000424472

Regions

Domain11 – 160150Ferritin-like diiron

Sites

Metal binding281Iron 1
Metal binding631Iron 1
Metal binding631Iron 2
Metal binding661Iron 1
Metal binding1081Iron 2
Metal binding1421Iron 2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.23
Modified residue21N-acetylthreonine; in Ferritin heavy chain, N-terminally processed Ref.23
Modified residue1791Phosphoserine Ref.17 Ref.19 Ref.20 Ref.22
Modified residue1831Phosphoserine Ref.19

Experimental info

Sequence conflict176 – 1838LGDSDNES → WETVIMKAKPRANFP in CAA25086. Ref.1

Secondary structure

................ 183
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02794 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FEF75640A29CCF56

FASTA18321,226
        10         20         30         40         50         60 
MTTASTSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK NFAKYFLHQS 

        70         80         90        100        110        120 
HEEREHAEKL MKLQNQRGGR IFLQDIKKPD CDDWESGLNA MECALHLEKN VNQSLLELHK 

       130        140        150        160        170        180 
LATDKNDPHL CDFIETHYLN EQVKAIKELG DHVTNLRKMG APESGLAEYL FDKHTLGDSD 


NES 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family."
Costanzo F., Santoro C., Colantuoni V., Bensi G., Raugei G., Romano V., Cortese R.
EMBO J. 3:23-27(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatocyte.
[2]"Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones."
Boyd D., Vecoli C., Belcher D.M., Jain S.K., Drysdale J.W.
J. Biol. Chem. 260:11755-11761(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro."
Chou C.-C., Gatti R.A., Fuller M.L., Concannon P., Wong A., Chada S., Davis R.C., Salser W.A.
Mol. Cell. Biol. 6:566-573(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure of gene and pseudogenes of human apoferritin H."
Costanzo F., Colombo M., Staempfli S., Santoro C., Marone M., Frank R., Delius H., Cortese R.
Nucleic Acids Res. 14:721-736(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Cloning, characterization, expression, and chromosomal localization of a human ferritin heavy-chain gene."
Hentze M.W., Keim S., Papadopoulos P., O'Brien S., Modi W., Drysdale J.W., Leonard W.J., Harford J.B., Klausner R.D.
Proc. Natl. Acad. Sci. U.S.A. 83:7226-7230(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Sequence of a cDNA encoding the ferritin H-chain from an 11-week-old human fetal brain."
Dhar M., Chauthaiwale V.M., Joshi J.G.
Gene 126:275-278(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[7]"Cloning of a novel full length cDNA for ferritin heavy chain from normal adult human and Alzheimer's brain."
Chauthaiwale V.M., Dhar M., McLachlan D.R., Joshi J.G.
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[8]"Detection of ferritin heavy chain by SEREX: a multifunctional molecule in malignant tumour cells."
Franco A.V., Gray C.P., Myers K., Hersey P.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[9]"Identification of a human cell proliferation gene 15."
Kim J.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon adenocarcinoma.
[11]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[12]NHLBI resequencing and genotyping service (RS&G)
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[13]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Cervix, Colon, Lung, Ovary, Prostate and Salivary gland.
[15]"Isolation and characterization of a cDNA clone for human ferritin heavy chain."
Boyd D., Jain S.K., Crampton J., Barrett K.J., Drysdale J.
Proc. Natl. Acad. Sci. U.S.A. 81:4751-4755(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-183.
[16]"A mutation, in the iron-responsive element of H ferritin mRNA, causing autosomal dominant iron overload."
Kato J., Fujikawa K., Kanda M., Fukuda N., Sasaki K., Takayama T., Kobune M., Takada K., Takimoto R., Hamada H., Ikeda T., Niitsu Y.
Am. J. Hum. Genet. 69:191-197(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HFE5, TISSUE SPECIFICITY.
[17]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[24]"Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts."
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.
Nature 349:541-544(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[25]"Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution."
Hempstead P.D., Yewdall S.J., Fernie A.R., Lawson D.M., Artymiuk P.J., Rice D.W., Ford G.C., Harrison P.M.
J. Mol. Biol. 268:424-448(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Wikipedia

Ferritin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00318 mRNA. Translation: CAA25086.1.
M11146 mRNA. Translation: AAA52437.1.
M12937 mRNA. Translation: AAA35830.1.
X03487, X03488 Genomic DNA. Translation: CAA27205.1.
M14212, M14211 Genomic DNA. Translation: AAA52438.1.
M97164 mRNA. Translation: AAA35832.1.
L20941 mRNA. Translation: AAA35833.1.
AF088851 mRNA. Translation: AAF89523.1.
AY258285 mRNA. Translation: AAP82230.1.
AB062402 mRNA. Translation: BAB93489.1.
AK054816 mRNA. Translation: BAG51427.1.
DQ496108 Genomic DNA. Translation: ABF47097.1.
CH471076 Genomic DNA. Translation: EAW73989.1.
BC000857 mRNA. Translation: AAH00857.1.
BC001399 mRNA. Translation: AAH01399.1.
BC011359 mRNA. Translation: AAH11359.1.
BC013724 mRNA. Translation: AAH13724.1.
BC015156 mRNA. Translation: AAH15156.1.
BC016009 mRNA. Translation: AAH16009.1.
BC016857 mRNA. Translation: AAH16857.1.
BC063514 mRNA. Translation: AAH63514.1.
BC066961 mRNA. Translation: AAH66961.1.
BC073750 mRNA. Translation: AAH73750.1.
BC104643 mRNA. Translation: AAI04644.1.
BC105802 mRNA. Translation: AAI05803.1. Different initiation.
M15383 mRNA. Translation: AAA52479.1.
CCDSCCDS41655.1.
PIRFRHUH. A23517.
RefSeqNP_002023.2. NM_002032.2.
UniGeneHs.524910.
Hs.645560.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHAX-ray2.40A1-183[»]
2CEIX-ray1.80A2-183[»]
2CHIX-ray1.60A2-183[»]
2CIHX-ray1.50A2-183[»]
2CLUX-ray2.10A2-183[»]
2CN6X-ray2.20A2-183[»]
2CN7X-ray1.75A2-183[»]
2FHAX-ray1.90A1-183[»]
2IU2X-ray1.80A2-183[»]
2Z6MX-ray2.72A/B/C/D/E/F/G/H/I/J/K/L2-177[»]
3AJOX-ray1.52A2-183[»]
3AJPX-ray1.90A2-183[»]
3AJQX-ray1.58A2-183[»]
3ERZX-ray3.06A/B/C/D/E/F/G/H/I/J/K/L1-183[»]
3ES3X-ray2.79A1-183[»]
4DYXX-ray1.85A6-177[»]
4DYYX-ray1.90A6-177[»]
4DYZX-ray2.30A6-177[»]
4DZ0X-ray2.50A6-177[»]
ProteinModelPortalP02794.
SMRP02794. Positions 6-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108773. 41 interactions.
DIPDIP-38301N.
IntActP02794. 30 interactions.
MINTMINT-4822446.
STRING9606.ENSP00000273550.

Chemistry

DrugBankDB00893. Iron Dextran.

PTM databases

PhosphoSiteP02794.

Polymorphism databases

DMDM120516.

2D gel databases

UCD-2DPAGEP02794.

Proteomic databases

MaxQBP02794.
PaxDbP02794.
PRIDEP02794.

Protocols and materials databases

DNASU2495.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273550; ENSP00000273550; ENSG00000167996.
GeneID2495.
KEGGhsa:2495.
UCSCuc001nsu.3. human.

Organism-specific databases

CTD2495.
GeneCardsGC11M061731.
H-InvDBHIX0128677.
HIX0200367.
HGNCHGNC:3976. FTH1.
HPACAB008623.
HPA043650.
MIM134770. gene.
615517. phenotype.
neXtProtNX_P02794.
Orphanet247790. FTH1-related iron overload.
PharmGKBPA28392.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1528.
HOVERGENHBG000410.
InParanoidP02794.
KOK00522.
OMAESAHEER.
PhylomeDBP02794.
TreeFamTF313885.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_15518. Transmembrane transport of small molecules.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP02794.
BgeeP02794.
CleanExHS_FTH1.
GenevestigatorP02794.

Family and domain databases

Gene3D1.20.1260.10. 1 hit.
InterProIPR001519. Ferritin.
IPR009040. Ferritin-like_diiron.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR014034. Ferritin_CS.
IPR008331. Ferritin_DPS_dom.
[Graphical view]
PANTHERPTHR11431. PTHR11431. 1 hit.
PfamPF00210. Ferritin. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00540. FERRITIN_1. 1 hit.
PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFTH1. human.
EvolutionaryTraceP02794.
GeneWikiFTH1.
GenomeRNAi2495.
NextBio9857.
PROP02794.
SOURCESearch...

Entry information

Entry nameFRIH_HUMAN
AccessionPrimary (citable) accession number: P02794
Secondary accession number(s): B3KNR5, Q3KRA8, Q3SWW1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM