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P02792

- FRIL_HUMAN

UniProt

P02792 - FRIL_HUMAN

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Protein
Ferritin light chain
Gene
FTL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.2 Publications

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 chain
PRO_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. 19 interactions.
MINTiMINT-1187221.
STRINGi9606.ENSP00000366525.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP02792.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 156150Ferritin-like diiron
Add
BLAST

Region

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

Sequence similaritiesi

Belongs to the ferritin family.

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541E → Q AA sequence 1 Publication
Sequence conflicti87 – 871E → Q AA sequence 1 Publication
Sequence conflicti89 – 891E → W AA sequence 1 Publication
Sequence conflicti102 – 1021A → T in AAA35831. 1 Publication
Sequence conflicti154 – 1541R → A AA sequence 1 Publication
Sequence conflicti175 – 1751D → N AA sequence 1 Publication

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. 19 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 159 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

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