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P02794

- FRIH_HUMAN

UniProt

P02794 - FRIH_HUMAN

Protein

Ferritin heavy chain

Gene

FTH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi28 – 281Iron 1
    Metal bindingi63 – 631Iron 1
    Metal bindingi63 – 631Iron 2
    Metal bindingi66 – 661Iron 1
    Metal bindingi108 – 1081Iron 2
    Metal bindingi142 – 1421Iron 2

    GO - Molecular functioni

    1. ferric iron binding Source: InterPro
    2. ferroxidase activity Source: UniProtKB-EC
    3. iron ion binding Source: ProtInc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cellular iron ion homeostasis Source: Reactome
    2. immune response Source: UniProtKB
    3. intracellular sequestering of iron ion Source: UniProtKB
    4. iron ion transport Source: InterPro
    5. membrane organization Source: Reactome
    6. negative regulation of cell proliferation Source: UniProtKB
    7. negative regulation of fibroblast proliferation Source: UniProtKB
    8. post-Golgi vesicle-mediated transport Source: Reactome
    9. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Iron storage

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_163699. Scavenging by Class A Receptors.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_25060. Iron uptake and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferritin heavy chain (EC:1.16.3.1)
    Short name:
    Ferritin H subunit
    Alternative name(s):
    Cell proliferation-inducing gene 15 protein
    Cleaved into the following chain:
    Gene namesi
    Name:FTH1
    Synonyms:FTH, FTHL6
    ORF Names:OK/SW-cl.84, PIG15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3976. FTH1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular ferritin complex Source: ProtInc
    4. nucleus Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    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.

    Organism-specific databases

    MIMi615517. phenotype.
    Orphaneti247790. FTH1-related iron overload.
    PharmGKBiPA28392.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 183183Ferritin heavy chainPRO_0000201048Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 183182Ferritin heavy chain, N-terminally processedPRO_0000424472Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylthreonine; in Ferritin heavy chain, N-terminally processed1 Publication
    Modified residuei179 – 1791Phosphoserine4 Publications
    Modified residuei183 – 1831Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP02794.
    PaxDbiP02794.
    PRIDEiP02794.

    2D gel databases

    UCD-2DPAGEP02794.

    PTM databases

    PhosphoSiteiP02794.

    Expressioni

    Tissue specificityi

    Expressed in the liver.1 Publication

    Gene expression databases

    ArrayExpressiP02794.
    BgeeiP02794.
    CleanExiHS_FTH1.
    GenevestigatoriP02794.

    Organism-specific databases

    HPAiCAB008623.
    HPA043650.

    Interactioni

    Subunit structurei

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAXXQ9UER75EBI-713259,EBI-77321
    FTLP027923EBI-713259,EBI-713279
    MAXP612442EBI-713259,EBI-751711

    Protein-protein interaction databases

    BioGridi108773. 41 interactions.
    DIPiDIP-38301N.
    IntActiP02794. 30 interactions.
    MINTiMINT-4822446.
    STRINGi9606.ENSP00000273550.

    Structurei

    Secondary structure

    1
    183
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 4228
    Turni45 – 473
    Helixi50 – 7728
    Helixi97 – 12428
    Helixi128 – 13710
    Helixi139 – 15921
    Turni160 – 1634
    Helixi165 – 17410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP02794.
    SMRiP02794. Positions 6-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02794.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 160150Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ferritin family.Curated
    Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1528.
    HOVERGENiHBG000410.
    InParanoidiP02794.
    KOiK00522.
    OMAiESAHEER.
    PhylomeDBiP02794.
    TreeFamiTF313885.

    Family and domain databases

    Gene3Di1.20.1260.10. 1 hit.
    InterProiIPR001519. Ferritin.
    IPR009040. Ferritin-like_diiron.
    IPR009078. Ferritin-like_SF.
    IPR012347. Ferritin-rel.
    IPR014034. Ferritin_CS.
    IPR008331. Ferritin_DPS_dom.
    [Graphical view]
    PANTHERiPTHR11431. PTHR11431. 1 hit.
    PfamiPF00210. Ferritin. 1 hit.
    [Graphical view]
    SUPFAMiSSF47240. SSF47240. 1 hit.
    PROSITEiPS00540. FERRITIN_1. 1 hit.
    PS00204. FERRITIN_2. 1 hit.
    PS50905. FERRITIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02794-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTASTSQVR QNYHQDSEAA INRQINLELY ASYVYLSMSY YFDRDDVALK    50
    NFAKYFLHQS HEEREHAEKL MKLQNQRGGR IFLQDIKKPD CDDWESGLNA 100
    MECALHLEKN VNQSLLELHK LATDKNDPHL CDFIETHYLN EQVKAIKELG 150
    DHVTNLRKMG APESGLAEYL FDKHTLGDSD NES 183
    Length:183
    Mass (Da):21,226
    Last modified:January 23, 2007 - v2
    Checksum:iFEF75640A29CCF56
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1838LGDSDNES → WETVIMKAKPRANFP in CAA25086. (PubMed:6323167)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41655.1.
    PIRiA23517. FRHUH.
    RefSeqiNP_002023.2. NM_002032.2.
    UniGeneiHs.524910.
    Hs.645560.

    Genome annotation databases

    EnsembliENST00000273550; ENSP00000273550; ENSG00000167996.
    GeneIDi2495.
    KEGGihsa:2495.
    UCSCiuc001nsu.3. human.

    Polymorphism databases

    DMDMi120516.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Ferritin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS41655.1.
    PIRi A23517. FRHUH.
    RefSeqi NP_002023.2. NM_002032.2.
    UniGenei Hs.524910.
    Hs.645560.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FHA X-ray 2.40 A 1-183 [» ]
    2CEI X-ray 1.80 A 2-183 [» ]
    2CHI X-ray 1.60 A 2-183 [» ]
    2CIH X-ray 1.50 A 2-183 [» ]
    2CLU X-ray 2.10 A 2-183 [» ]
    2CN6 X-ray 2.20 A 2-183 [» ]
    2CN7 X-ray 1.75 A 2-183 [» ]
    2FHA X-ray 1.90 A 1-183 [» ]
    2IU2 X-ray 1.80 A 2-183 [» ]
    2Z6M X-ray 2.72 A/B/C/D/E/F/G/H/I/J/K/L 2-177 [» ]
    3AJO X-ray 1.52 A 2-183 [» ]
    3AJP X-ray 1.90 A 2-183 [» ]
    3AJQ X-ray 1.58 A 2-183 [» ]
    3ERZ X-ray 3.06 A/B/C/D/E/F/G/H/I/J/K/L 1-183 [» ]
    3ES3 X-ray 2.79 A 1-183 [» ]
    4DYX X-ray 1.85 A 6-177 [» ]
    4DYY X-ray 1.90 A 6-177 [» ]
    4DYZ X-ray 2.30 A 6-177 [» ]
    4DZ0 X-ray 2.50 A 6-177 [» ]
    ProteinModelPortali P02794.
    SMRi P02794. Positions 6-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108773. 41 interactions.
    DIPi DIP-38301N.
    IntActi P02794. 30 interactions.
    MINTi MINT-4822446.
    STRINGi 9606.ENSP00000273550.

    Chemistry

    DrugBanki DB00893. Iron Dextran.

    PTM databases

    PhosphoSitei P02794.

    Polymorphism databases

    DMDMi 120516.

    2D gel databases

    UCD-2DPAGE P02794.

    Proteomic databases

    MaxQBi P02794.
    PaxDbi P02794.
    PRIDEi P02794.

    Protocols and materials databases

    DNASUi 2495.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273550 ; ENSP00000273550 ; ENSG00000167996 .
    GeneIDi 2495.
    KEGGi hsa:2495.
    UCSCi uc001nsu.3. human.

    Organism-specific databases

    CTDi 2495.
    GeneCardsi GC11M061731.
    H-InvDB HIX0128677.
    HIX0200367.
    HGNCi HGNC:3976. FTH1.
    HPAi CAB008623.
    HPA043650.
    MIMi 134770. gene.
    615517. phenotype.
    neXtProti NX_P02794.
    Orphaneti 247790. FTH1-related iron overload.
    PharmGKBi PA28392.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1528.
    HOVERGENi HBG000410.
    InParanoidi P02794.
    KOi K00522.
    OMAi ESAHEER.
    PhylomeDBi P02794.
    TreeFami TF313885.

    Enzyme and pathway databases

    Reactomei REACT_163699. Scavenging by Class A Receptors.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_25060. Iron uptake and transport.

    Miscellaneous databases

    ChiTaRSi FTH1. human.
    EvolutionaryTracei P02794.
    GeneWikii FTH1.
    GenomeRNAii 2495.
    NextBioi 9857.
    PROi P02794.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02794.
    Bgeei P02794.
    CleanExi HS_FTH1.
    Genevestigatori P02794.

    Family and domain databases

    Gene3Di 1.20.1260.10. 1 hit.
    InterProi IPR001519. Ferritin.
    IPR009040. Ferritin-like_diiron.
    IPR009078. Ferritin-like_SF.
    IPR012347. Ferritin-rel.
    IPR014034. Ferritin_CS.
    IPR008331. Ferritin_DPS_dom.
    [Graphical view ]
    PANTHERi PTHR11431. PTHR11431. 1 hit.
    Pfami PF00210. Ferritin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47240. SSF47240. 1 hit.
    PROSITEi PS00540. FERRITIN_1. 1 hit.
    PS00204. FERRITIN_2. 1 hit.
    PS50905. FERRITIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. 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. 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).

    Entry informationi

    Entry nameiFRIH_HUMAN
    AccessioniPrimary (citable) accession number: P02794
    Secondary accession number(s): B3KNR5, Q3KRA8, Q3SWW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 177 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3