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P02794

- FRIH_HUMAN

UniProt

P02794 - FRIH_HUMAN

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Protein

Ferritin heavy chain

Gene
FTH1, FTH, FTHL6, OK/SW-cl.84, PIG15
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. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney 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
Complete GO annotation...

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
Complete GO annotation...

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.
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.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiP02794.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 160150Ferritin-like diironAdd
BLAST

Sequence similaritiesi

Belongs to the ferritin family.

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1838LGDSDNES → WETVIMKAKPRANFP in CAA25086. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 176 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

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