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Q8N4E7

- FTMT_HUMAN

UniProt

Q8N4E7 - FTMT_HUMAN

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Protein

Ferritin, mitochondrial

Gene

FTMT

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. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Iron 1
Metal bindingi122 – 1221Iron 1
Metal bindingi122 – 1221Iron 2
Metal bindingi125 – 1251Iron 1
Metal bindingi167 – 1671Iron 2
Metal bindingi201 – 2011Iron 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. ferric iron binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular iron ion homeostasis Source: BHF-UCL
  2. iron ion transport Source: InterPro
  3. positive regulation of cell proliferation Source: BHF-UCL
  4. positive regulation of lyase activity Source: BHF-UCL
  5. positive regulation of oxidoreductase activity Source: BHF-UCL
  6. positive regulation of transferase activity Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin, mitochondrial (EC:1.16.3.1)
Gene namesi
Name:FTMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:17345. FTMT.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
  2. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi204 – 2041S → A: Increases ferroxidase activity and iron binding. 1 Publication

Organism-specific databases

PharmGKBiPA134941146.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4949MitochondrionSequence AnalysisAdd
BLAST
Chaini50 – 242193Ferritin, mitochondrialPRO_0000008850Add
BLAST

Proteomic databases

PaxDbiQ8N4E7.
PRIDEiQ8N4E7.

Expressioni

Tissue specificityi

Detected in testis and erythroleukemia. Expression is very low or not detectable in brain, colon, heart, kidney, liver, lung, muscle, placental, spleen and small intestine.1 Publication

Gene expression databases

BgeeiQ8N4E7.
CleanExiHS_FTMT.
GenevestigatoriQ8N4E7.

Interactioni

Subunit structurei

Homooligomer of 24 subunits. The functional molecule is roughly spherical and contains a central cavity into which the polymeric mineral iron core is deposited.

Protein-protein interaction databases

STRINGi9606.ENSP00000313691.

Structurei

Secondary structure

1
242
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi74 – 10027
Turni104 – 1063
Helixi109 – 13628
Helixi156 – 18328
Helixi187 – 19610
Helixi198 – 21821
Turni219 – 2224
Helixi226 – 2338

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R03X-ray1.70A61-242[»]
ProteinModelPortaliQ8N4E7.
SMRiQ8N4E7. Positions 66-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N4E7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 219150Ferritin-like diironPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1528.
GeneTreeiENSGT00760000119129.
HOGENOMiHOG000223383.
HOVERGENiHBG000410.
InParanoidiQ8N4E7.
KOiK18495.
OMAiFLETYYL.
OrthoDBiEOG7DRJ49.
PhylomeDBiQ8N4E7.
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.
PROSITEiPS00204. 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.

Q8N4E7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSCFRLLSR HISPSLASLR PVRCCFALPL RWAPGRPLDP RQIAPRRPLA
60 70 80 90 100
AAASSRDPTG PAAGPSRVRQ NFHPDSEAAI NRQINLELYA SYVYLSMAYY
110 120 130 140 150
FSRDDVALNN FSRYFLHQSR EETEHAEKLM RLQNQRGGRI RLQDIKKPEQ
160 170 180 190 200
DDWESGLHAM ECALLLEKNV NQSLLELHAL ASDKGDPHLC DFLETYYLNE
210 220 230 240
QVKSIKELGD HVHNLVKMGA PDAGLAEYLF DTHTLGNENK QN
Length:242
Mass (Da):27,538
Last modified:October 1, 2002 - v1
Checksum:i29E4B41616A74A3F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC034419 mRNA. Translation: AAH34419.1.
CCDSiCCDS4128.1.
RefSeqiNP_803431.1. NM_177478.1.
UniGeneiHs.105324.

Genome annotation databases

EnsembliENST00000321339; ENSP00000313691; ENSG00000181867.
GeneIDi94033.
KEGGihsa:94033.
UCSCiuc003kss.3. human.

Polymorphism databases

DMDMi62900307.

Cross-referencesi

Web resourcesi

Wikipedia

Ferritin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC034419 mRNA. Translation: AAH34419.1 .
CCDSi CCDS4128.1.
RefSeqi NP_803431.1. NM_177478.1.
UniGenei Hs.105324.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1R03 X-ray 1.70 A 61-242 [» ]
ProteinModelPortali Q8N4E7.
SMRi Q8N4E7. Positions 66-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000313691.

Polymorphism databases

DMDMi 62900307.

Proteomic databases

PaxDbi Q8N4E7.
PRIDEi Q8N4E7.

Protocols and materials databases

DNASUi 94033.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321339 ; ENSP00000313691 ; ENSG00000181867 .
GeneIDi 94033.
KEGGi hsa:94033.
UCSCi uc003kss.3. human.

Organism-specific databases

CTDi 94033.
GeneCardsi GC05P121187.
HGNCi HGNC:17345. FTMT.
MIMi 608847. gene.
neXtProti NX_Q8N4E7.
PharmGKBi PA134941146.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1528.
GeneTreei ENSGT00760000119129.
HOGENOMi HOG000223383.
HOVERGENi HBG000410.
InParanoidi Q8N4E7.
KOi K18495.
OMAi FLETYYL.
OrthoDBi EOG7DRJ49.
PhylomeDBi Q8N4E7.
TreeFami TF313885.

Miscellaneous databases

EvolutionaryTracei Q8N4E7.
GeneWikii Mitochondrial_ferritin.
GenomeRNAii 94033.
NextBioi 78343.
PROi Q8N4E7.
SOURCEi Search...

Gene expression databases

Bgeei Q8N4E7.
CleanExi HS_FTMT.
Genevestigatori Q8N4E7.

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 PS00204. FERRITIN_2. 1 hit.
PS50905. FERRITIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala."
    Langlois d'Estaintot B., Santambrogio P., Granier T., Gallois B., Chevalier J.M., Precigoux G., Levi S., Arosio P.
    J. Mol. Biol. 340:277-293(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 61-242, FUNCTION, MUTAGENESIS OF SER-204.

Entry informationi

Entry nameiFTMT_HUMAN
AccessioniPrimary (citable) accession number: Q8N4E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 102 of the entry and version 1 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 5
    Human chromosome 5: 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