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P02792

- FRIL_HUMAN

UniProt

P02792 - FRIL_HUMAN

Protein

Ferritin light chain

Gene

FTL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi54 – 541Iron
    Metal bindingi57 – 571Iron
    Metal bindingi58 – 581Iron
    Metal bindingi61 – 611Iron
    Metal bindingi64 – 641Iron

    GO - Molecular functioni

    1. ferric iron binding Source: InterPro
    2. identical protein binding Source: IntAct
    3. iron ion binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular iron ion homeostasis Source: Reactome
    3. iron ion homeostasis Source: UniProtKB
    4. iron ion transport Source: InterPro
    5. membrane organization Source: Reactome
    6. post-Golgi vesicle-mediated transport Source: Reactome
    7. transmembrane transport Source: Reactome

    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 light chain
    Short name:
    Ferritin L subunit
    Gene namesi
    Name:FTL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3999. FTL.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Hereditary hyperferritinemia-cataract syndrome (HHCS) [MIM:600886]: An autosomal dominant disease characterized by elevated level of ferritin in serum and tissues, and early-onset bilateral cataract.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301T → I in HHCS. 1 Publication
    VAR_070948
    Neurodegeneration with brain iron accumulation 3 (NBIA3) [MIM:606159]: A neurodegenerative disorder associated with iron accumulation in the brain, primarily in the basal ganglia. It is characterized by a variety of neurological signs including parkinsonism, ataxia, corticospinal signs, mild non-progressive cognitive deficit and episodic psychosis. It is linked with decreased serum ferritin levels.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961A → T in NBIA3. 1 Publication
    VAR_026633
    L-ferritin deficiency (LFTD) [MIM:615604]: A condition characterized by low levels of ferritin in serum and tissues in the absence of other hematological symptoms. Seizures and mild neuropsychologic impairment may manifest in individuals with complete ferritin deficiency.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Cataract, Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi600886. phenotype.
    606159. phenotype.
    615604. phenotype.
    Orphaneti254704. Genetic hyperferritinemia without iron overload.
    163. Hereditary hyperferritinemia with congenital cataracts.
    157846. Neuroferritinopathy.
    PharmGKBiPA28412.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 175174Ferritin light chainPRO_0000201060Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP02792.
    PaxDbiP02792.
    PRIDEiP02792.

    PTM databases

    PhosphoSiteiP02792.

    Expressioni

    Gene expression databases

    ArrayExpressiP02792.
    BgeeiP02792.
    CleanExiHS_FTL.
    GenevestigatoriP02792.

    Organism-specific databases

    HPAiCAB020769.
    HPA041602.

    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. 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. Iron enters the spherical protein shell through pores that are formed between subunits. Mutations leading to truncation or the addition of extra residues at the C-terminus interfere with normal pore formation and with iron accumulation.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-713279,EBI-713279
    FTH1P027943EBI-713279,EBI-713259
    HTTP428582EBI-713279,EBI-466029
    NAMPTP434903EBI-713279,EBI-2829310
    PSENENQ9NZ424EBI-713279,EBI-998468

    Protein-protein interaction databases

    BioGridi108789. 28 interactions.
    DIPiDIP-31248N.
    IntActiP02792. 21 interactions.
    MINTiMINT-1187221.
    STRINGi9606.ENSP00000366525.

    Structurei

    Secondary structure

    1
    175
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni3 – 53
    Helixi11 – 3929
    Turni41 – 433
    Helixi46 – 7328
    Helixi93 – 12028
    Helixi124 – 13310
    Helixi135 – 15420
    Beta strandi155 – 1573
    Helixi160 – 17011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FFXX-ray1.90J2-174[»]
    2FG4X-ray2.10A2-175[»]
    2FG8X-ray2.50A/B/C/D/E/F/G/H2-175[»]
    3HX2X-ray2.85A/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/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x1-166[»]
    3HX5X-ray2.85A/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/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x1-166[»]
    3HX7X-ray2.85A/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/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x1-166[»]
    3KXUX-ray1.85A1-166[»]
    ProteinModelPortaliP02792.
    SMRiP02792. Positions 2-157.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02792.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 156150Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni54 – 618Catalytic site for iron oxidation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG321513.
    HOVERGENiHBG000410.
    InParanoidiP02792.
    KOiK13625.
    OMAiITIFRII.
    OrthoDBiEOG7DRJ49.
    PhylomeDBiP02792.
    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.

    P02792-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSQIRQNYS TDVEAAVNSL VNLYLQASYT YLSLGFYFDR DDVALEGVSH    50
    FFRELAEEKR EGYERLLKMQ NQRGGRALFQ DIKKPAEDEW GKTPDAMKAA 100
    MALEKKLNQA LLDLHALGSA RTDPHLCDFL ETHFLDEEVK LIKKMGDHLT 150
    NLHRLGGPEA GLGEYLFERL TLKHD 175
    Length:175
    Mass (Da):20,020
    Last modified:January 23, 2007 - v2
    Checksum:i0DB98081FF976BC2
    GO

    Sequence cautioni

    The sequence CAE11873.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541E → Q AA sequence (PubMed:6653779)Curated
    Sequence conflicti87 – 871E → Q AA sequence (PubMed:6653779)Curated
    Sequence conflicti89 – 891E → W AA sequence (PubMed:8706699)Curated
    Sequence conflicti102 – 1021A → T in AAA35831. (PubMed:3858810)Curated
    Sequence conflicti154 – 1541R → A AA sequence (PubMed:8706699)Curated
    Sequence conflicti175 – 1751D → N AA sequence (PubMed:6653779)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301T → I in HHCS. 1 Publication
    VAR_070948
    Natural varianti96 – 961A → T in NBIA3. 1 Publication
    VAR_026633

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11147 mRNA. Translation: AAA52439.1.
    M10119 mRNA. Translation: AAA35831.1.
    M12938 mRNA. Translation: AAA52440.1.
    AY207005 mRNA. Translation: AAO52739.1.
    CR456715 mRNA. Translation: CAG32996.1.
    AK311773 mRNA. Translation: BAG34716.1.
    BX571748 mRNA. Translation: CAE11873.1. Different initiation.
    AC026803 Genomic DNA. No translation available.
    BC002991 mRNA. Translation: AAH02991.2.
    BC004245 mRNA. Translation: AAH04245.1.
    BC008439 mRNA. Translation: AAH08439.1.
    BC013928 mRNA. Translation: AAH13928.1.
    BC016715 mRNA. Translation: AAH16715.1.
    BC016346 mRNA. Translation: AAH16346.1.
    BC016354 mRNA. Translation: AAH16354.1.
    BC018990 mRNA. Translation: AAH18990.1.
    BC021670 mRNA. Translation: AAH21670.1.
    BC058820 mRNA. Translation: AAH58820.1.
    BC062708 mRNA. Translation: AAH62708.1.
    X03742 Genomic DNA. Translation: CAA27382.1.
    X03743 Genomic DNA. Translation: CAA27383.1.
    X03743 Genomic DNA. Translation: CAA27384.1.
    CCDSiCCDS33070.1.
    PIRiB23920. FRHUL.
    RefSeqiNP_000137.2. NM_000146.3.
    UniGeneiHs.433670.
    Hs.728304.

    Genome annotation databases

    EnsembliENST00000331825; ENSP00000366525; ENSG00000087086.
    GeneIDi2512.
    KEGGihsa:2512.
    UCSCiuc002plo.3. human.

    Polymorphism databases

    DMDMi120523.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Ferritin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11147 mRNA. Translation: AAA52439.1 .
    M10119 mRNA. Translation: AAA35831.1 .
    M12938 mRNA. Translation: AAA52440.1 .
    AY207005 mRNA. Translation: AAO52739.1 .
    CR456715 mRNA. Translation: CAG32996.1 .
    AK311773 mRNA. Translation: BAG34716.1 .
    BX571748 mRNA. Translation: CAE11873.1 . Different initiation.
    AC026803 Genomic DNA. No translation available.
    BC002991 mRNA. Translation: AAH02991.2 .
    BC004245 mRNA. Translation: AAH04245.1 .
    BC008439 mRNA. Translation: AAH08439.1 .
    BC013928 mRNA. Translation: AAH13928.1 .
    BC016715 mRNA. Translation: AAH16715.1 .
    BC016346 mRNA. Translation: AAH16346.1 .
    BC016354 mRNA. Translation: AAH16354.1 .
    BC018990 mRNA. Translation: AAH18990.1 .
    BC021670 mRNA. Translation: AAH21670.1 .
    BC058820 mRNA. Translation: AAH58820.1 .
    BC062708 mRNA. Translation: AAH62708.1 .
    X03742 Genomic DNA. Translation: CAA27382.1 .
    X03743 Genomic DNA. Translation: CAA27383.1 .
    X03743 Genomic DNA. Translation: CAA27384.1 .
    CCDSi CCDS33070.1.
    PIRi B23920. FRHUL.
    RefSeqi NP_000137.2. NM_000146.3.
    UniGenei Hs.433670.
    Hs.728304.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FFX X-ray 1.90 J 2-174 [» ]
    2FG4 X-ray 2.10 A 2-175 [» ]
    2FG8 X-ray 2.50 A/B/C/D/E/F/G/H 2-175 [» ]
    3HX2 X-ray 2.85 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/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x 1-166 [» ]
    3HX5 X-ray 2.85 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/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x 1-166 [» ]
    3HX7 X-ray 2.85 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/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x 1-166 [» ]
    3KXU X-ray 1.85 A 1-166 [» ]
    ProteinModelPortali P02792.
    SMRi P02792. Positions 2-157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108789. 28 interactions.
    DIPi DIP-31248N.
    IntActi P02792. 21 interactions.
    MINTi MINT-1187221.
    STRINGi 9606.ENSP00000366525.

    Chemistry

    DrugBanki DB00893. Iron Dextran.

    PTM databases

    PhosphoSitei P02792.

    Polymorphism databases

    DMDMi 120523.

    Proteomic databases

    MaxQBi P02792.
    PaxDbi P02792.
    PRIDEi P02792.

    Protocols and materials databases

    DNASUi 2512.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331825 ; ENSP00000366525 ; ENSG00000087086 .
    GeneIDi 2512.
    KEGGi hsa:2512.
    UCSCi uc002plo.3. human.

    Organism-specific databases

    CTDi 2512.
    GeneCardsi GC19P049468.
    GeneReviewsi FTL.
    HGNCi HGNC:3999. FTL.
    HPAi CAB020769.
    HPA041602.
    MIMi 134790. gene.
    600886. phenotype.
    606159. phenotype.
    615604. phenotype.
    neXtProti NX_P02792.
    Orphaneti 254704. Genetic hyperferritinemia without iron overload.
    163. Hereditary hyperferritinemia with congenital cataracts.
    157846. Neuroferritinopathy.
    PharmGKBi PA28412.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG321513.
    HOVERGENi HBG000410.
    InParanoidi P02792.
    KOi K13625.
    OMAi ITIFRII.
    OrthoDBi EOG7DRJ49.
    PhylomeDBi P02792.
    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 FTL. human.
    EvolutionaryTracei P02792.
    GeneWikii Ferritin_light_chain.
    GenomeRNAii 2512.
    NextBioi 9899.
    PROi P02792.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02792.
    Bgeei P02792.
    CleanExi HS_FTL.
    Genevestigatori P02792.

    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. "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].
    2. "Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications."
      Dorner M.H., Salfeld J., Will H., Leibold E.A., Vass J.K., Munro H.N.
      Proc. Natl. Acad. Sci. U.S.A. 82:3139-3143(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Expression of a ferritin-like mRNA by abdominal aortic aneurysm (AAA) adventitial fibroblasts."
      Jordan T.P., Li X.G., Bhatti A.F., Obunike J.C., Tilson M.D.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "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: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon endothelium.
    8. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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, Skin, Testis and Urinary bladder.
    10. "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 [MRNA] OF 33-175.
    11. "The amino acid sequence of human liver apoferritin."
      Addison J.M., Fitton J.E., Lewis W.G., May K., Harrison P.M.
      FEBS Lett. 164:139-144(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-36 AND 41-175, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
      Tissue: Liver.
    12. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
      Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
      Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 84-90 AND 145-155.
      Tissue: Placenta.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Human L-ferritin deficiency is characterized by idiopathic generalized seizures and atypical restless leg syndrome."
      Cozzi A., Santambrogio P., Privitera D., Broccoli V., Rotundo L.I., Garavaglia B., Benz R., Altamura S., Goede J.S., Muckenthaler M.U., Levi S.
      J. Exp. Med. 210:1779-1791(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMNT IN LFTD.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-174, SUBUNIT.
    16. "Unraveling of the E-helices and disruption of 4-fold pores are associated with iron mishandling in a mutant ferritin causing neurodegeneration."
      Baraibar M.A., Muhoberac B.B., Garringer H.J., Hurley T.D., Vidal R.
      J. Biol. Chem. 285:1950-1956(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-191, FUNCTION, SUBUNIT, DOMAIN.
    17. "Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation."
      Luscieti S., Santambrogio P., Langlois d'Estaintot B., Granier T., Cozzi A., Poli M., Gallois B., Finazzi D., Cattaneo A., Levi S., Arosio P.
      J. Biol. Chem. 285:11948-11957(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-166, FUNCTION, SUBUNIT, DOMAIN, FUNCTION AS A FERROXIDASE, IDENTIFICATION BY MASS SPECTROMETRY, ROLE IN DISEASE.
    18. "Neuroferritinopathy: missense mutation in FTL causing early-onset bilateral pallidal involvement."
      Maciel P., Cruz V.T., Constante M., Iniesta I., Costa M.C., Gallati S., Sousa N., Sequeiros J., Coutinho P., Santos M.M.
      Neurology 65:603-605(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT NBIA3 THR-96.
    19. "A new missense mutation in the L ferritin coding sequence associated with elevated levels of glycosylated ferritin in serum and absence of iron overload."
      Kannengiesser C., Jouanolle A.M., Hetet G., Mosser A., Muzeau F., Henry D., Bardou-Jacquet E., Mornet M., Brissot P., Deugnier Y., Grandchamp B., Beaumont C.
      Haematologica 94:335-339(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HHCS ILE-30.

    Entry informationi

    Entry nameiFRIL_HUMAN
    AccessioniPrimary (citable) accession number: P02792
    Secondary accession number(s): B2R4B9
    , Q6IBT7, Q7Z2W1, Q86WI9, Q8WU07, Q96AU9, Q96CU0, Q9BTZ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 160 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3