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P22830

- HEMH_HUMAN

UniProt

P22830 - HEMH_HUMAN

Protein

Ferrochelatase, mitochondrial

Gene

FECH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 2 (10 May 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the ferrous insertion into protoporphyrin IX.

    Catalytic activityi

    Protoheme + 2 H+ = protoporphyrin + Fe2+.

    Cofactori

    Binds 1 2Fe-2S cluster.

    Enzyme regulationi

    Inhibited by nitric oxide (NO). The 2Fe-2S cluster could act as a NO sensor.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi196 – 1961Iron-sulfur (2Fe-2S)
    Active sitei230 – 2301
    Active sitei383 – 3831
    Metal bindingi403 – 4031Iron-sulfur (2Fe-2S)
    Metal bindingi406 – 4061Iron-sulfur (2Fe-2S)
    Metal bindingi411 – 4111Iron-sulfur (2Fe-2S)

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. ferrochelatase activity Source: BHF-UCL
    3. ferrous iron binding Source: ProtInc
    4. heme binding Source: Ensembl
    5. iron-responsive element binding Source: Ensembl
    6. protein binding Source: BHF-UCL

    GO - Biological processi

    1. cellular response to dexamethasone stimulus Source: Ensembl
    2. cholesterol metabolic process Source: Ensembl
    3. detection of UV Source: Ensembl
    4. erythrocyte differentiation Source: Ensembl
    5. generation of precursor metabolites and energy Source: ProtInc
    6. heme biosynthetic process Source: Reactome
    7. iron ion homeostasis Source: Ensembl
    8. porphyrin-containing compound metabolic process Source: Reactome
    9. protoporphyrinogen IX metabolic process Source: BHF-UCL
    10. regulation of eIF2 alpha phosphorylation by heme Source: Ensembl
    11. regulation of hemoglobin biosynthetic process Source: Ensembl
    12. response to arsenic-containing substance Source: Ensembl
    13. response to drug Source: Ensembl
    14. response to ethanol Source: Ensembl
    15. response to insecticide Source: Ensembl
    16. response to lead ion Source: Ensembl
    17. response to light stimulus Source: ProtInc
    18. response to methylmercury Source: Ensembl
    19. response to platinum ion Source: Ensembl
    20. small molecule metabolic process Source: Reactome
    21. very-low-density lipoprotein particle assembly Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    2Fe-2S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00891-MONOMER.
    BRENDAi4.99.1.1. 2681.
    ReactomeiREACT_9465. Heme biosynthesis.
    SABIO-RKP22830.
    UniPathwayiUPA00252; UER00325.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferrochelatase, mitochondrial (EC:4.99.1.1)
    Alternative name(s):
    Heme synthase
    Protoheme ferro-lyase
    Gene namesi
    Name:FECH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:3647. FECH.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB-SubCell
    2. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Erythropoietic protoporphyria (EPP) [MIM:177000]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Erythropoietic protoporphyria is marked by excessive protoporphyrin in erythrocytes, plasma, liver and feces, and by widely varying photosensitive skin changes ranging from a burning or pruritic sensation to erythema, edema and wheals.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551G → C in EPP. 1 Publication
    Corresponds to variant rs3848519 [ dbSNP | Ensembl ].
    VAR_002383
    Natural varianti62 – 621P → R in EPP. 1 Publication
    VAR_030553
    Natural varianti71 – 711I → K in EPP; enzyme totally inactive. 1 Publication
    VAR_030554
    Natural varianti139 – 1391Q → L in EPP; autosomal recessive EPP; enzyme retains 18% of activity. 1 Publication
    VAR_030555
    Natural varianti151 – 1511S → P in EPP; enzyme totally inactive. 1 Publication
    VAR_030556
    Natural varianti178 – 1781E → K in EPP. 1 Publication
    VAR_030557
    Natural varianti182 – 1821L → R in EPP; enzyme totally inactive. 1 Publication
    VAR_030558
    Natural varianti186 – 1861I → T in EPP. 1 Publication
    VAR_002384
    Natural varianti191 – 1911Y → H in EPP; enzyme retains 72% of activity. 1 Publication
    VAR_030559
    Natural varianti192 – 1921P → T in EPP; enzyme totally inactive. 1 Publication
    VAR_030560
    Natural varianti236 – 2361C → Y in EPP; enzyme retains 12% of activity. 1 Publication
    VAR_030561
    Natural varianti260 – 2601F → L in EPP; autosomal recessive EPP; enzyme retains 52% of activity. 1 Publication
    VAR_030562
    Natural varianti264 – 2641S → L in EPP. 1 Publication
    VAR_054629
    Natural varianti267 – 2671M → I in EPP; unchanged activity; but increased thermolability. 1 Publication
    Corresponds to variant rs118204037 [ dbSNP | Ensembl ].
    VAR_002385
    Natural varianti283 – 2831T → I in EPP; enzyme almost inactive. 1 Publication
    VAR_030563
    Natural varianti288 – 2881M → K in EPP; enzyme totally inactive. 1 Publication
    VAR_030564
    Natural varianti334 – 3341P → L in EPP; autosomal recessive EPP; enzyme retains 19% of activity. 2 Publications
    Corresponds to variant rs150146721 [ dbSNP | Ensembl ].
    VAR_030565
    Natural varianti362 – 3621V → G in EPP. 1 Publication
    VAR_030566
    Natural varianti379 – 3791K → N in EPP; autosomal recessive EPP; enzyme retains 37% of activity. 1 Publication
    VAR_030567
    Natural varianti386 – 3861H → P in EPP; loss of activity. 1 Publication
    VAR_002386
    Natural varianti406 – 4061C → S in EPP; enzyme almost inactive. 1 Publication
    VAR_030568
    Natural varianti406 – 4061C → Y in EPP; enzyme almost inactive. 1 Publication
    VAR_030569
    Natural varianti408 – 4114NPVC → KSVG in EPP; no detectable enzymatic activity.
    VAR_030570
    Natural varianti417 – 4171F → S in EPP; reduced activity. 1 Publication
    VAR_002387
    Natural varianti417 – 4171Missing in EPP; enzyme totally inactive. 1 Publication
    VAR_030571

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi196 – 1961C → S: Loss of activity. 1 Publication
    Mutagenesisi360 – 3601C → S: No loss of activity. 1 Publication
    Mutagenesisi395 – 3951C → S: No loss of activity. 1 Publication
    Mutagenesisi403 – 4031C → D or H: Loss of activity. 1 Publication
    Mutagenesisi406 – 4061C → D, H or S: Loss of activity. 1 Publication
    Mutagenesisi411 – 4111C → H or S: Loss of activity. 1 Publication
    Mutagenesisi417 – 4171F → L: Decreased activity. 1 Publication
    Mutagenesisi417 – 4171F → Y or W: Greatly reduced activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi177000. phenotype.
    Orphaneti79278. Erythropoietic protoporphyria.
    PharmGKBiPA28087.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5454MitochondrionSequence AnalysisAdd
    BLAST
    Chaini55 – 423369Ferrochelatase, mitochondrialPRO_0000008873Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571N6-acetyllysineBy similarity
    Modified residuei138 – 1381N6-succinyllysineBy similarity
    Modified residuei415 – 4151N6-acetyllysine; alternateBy similarity
    Modified residuei415 – 4151N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP22830.
    PaxDbiP22830.
    PRIDEiP22830.

    PTM databases

    PhosphoSiteiP22830.

    Expressioni

    Gene expression databases

    ArrayExpressiP22830.
    BgeeiP22830.
    CleanExiHS_FECH.
    GenevestigatoriP22830.

    Organism-specific databases

    HPAiCAB033205.
    HPA044100.
    HPA048177.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi108526. 16 interactions.
    DIPiDIP-39632N.
    IntActiP22830. 5 interactions.
    STRINGi9606.ENSP00000372326.

    Structurei

    Secondary structure

    1
    423
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi69 – 757
    Helixi82 – 843
    Helixi85 – 939
    Turni96 – 983
    Helixi104 – 12522
    Helixi132 – 15019
    Helixi152 – 1543
    Beta strandi156 – 16914
    Helixi170 – 17910
    Beta strandi183 – 1908
    Turni196 – 1983
    Helixi199 – 21214
    Beta strandi218 – 2247
    Helixi231 – 24515
    Turni250 – 2523
    Helixi253 – 2553
    Beta strandi257 – 2637
    Helixi267 – 2704
    Turni271 – 2733
    Helixi276 – 29015
    Turni291 – 2933
    Beta strandi297 – 3026
    Beta strandi306 – 3083
    Beta strandi310 – 3145
    Helixi315 – 32410
    Beta strandi329 – 3335
    Helixi345 – 3484
    Helixi350 – 35910
    Beta strandi364 – 3674
    Beta strandi371 – 3733
    Helixi375 – 39117
    Helixi397 – 4004
    Helixi410 – 41910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HRKX-ray2.00A/B65-423[»]
    2HRCX-ray1.70A/B65-423[»]
    2HREX-ray2.50A/B/C/D65-423[»]
    2PNJX-ray2.35A/B65-423[»]
    2PO5X-ray2.20A/B65-423[»]
    2PO7X-ray2.20A/B65-423[»]
    2QD1X-ray2.20A/B/C/D65-423[»]
    2QD2X-ray2.20A/B65-423[»]
    2QD3X-ray2.20A/B65-423[»]
    2QD4X-ray2.00A/B65-423[»]
    2QD5X-ray2.30A/B65-423[»]
    3AQIX-ray1.70A/B65-423[»]
    3HCNX-ray1.60A/B65-423[»]
    3HCOX-ray1.80A/B65-423[»]
    3HCPX-ray2.00A/B65-423[»]
    3HCRX-ray2.20A/B65-423[»]
    3W1WX-ray2.01A/B61-423[»]
    4F4DX-ray1.80A/B65-423[»]
    4KLAX-ray2.60A/B65-423[»]
    4KLCX-ray2.40A/B65-423[»]
    4KLRX-ray2.18A/B65-423[»]
    4KMMX-ray2.60A/B65-423[»]
    4MK4X-ray2.50A/B65-423[»]
    ProteinModelPortaliP22830.
    SMRiP22830. Positions 65-423.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22830.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ferrochelatase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0276.
    HOGENOMiHOG000060727.
    HOVERGENiHBG051898.
    KOiK01772.
    OMAiRCAESKK.
    OrthoDBiEOG70PBXZ.
    PhylomeDBiP22830.
    TreeFamiTF300859.

    Family and domain databases

    HAMAPiMF_00323. Ferrochelatase.
    InterProiIPR001015. Ferrochelatase.
    IPR019772. Ferrochelatase_AS.
    [Graphical view]
    PANTHERiPTHR11108. PTHR11108. 1 hit.
    PfamiPF00762. Ferrochelatase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00109. hemH. 1 hit.
    PROSITEiPS00534. FERROCHELATASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P22830-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRSLGANMAA ALRAAGVLLR DPLASSSWRV CQPWRWKSGA AAAAVTTETA    50
    QHAQGAKPQV QPQKRKPKTG ILMLNMGGPE TLGDVHDFLL RLFLDRDLMT 100
    LPIQNKLAPF IAKRRTPKIQ EQYRRIGGGS PIKIWTSKQG EGMVKLLDEL 150
    SPNTAPHKYY IGFRYVHPLT EEAIEEMERD GLERAIAFTQ YPQYSCSTTG 200
    SSLNAIYRYY NQVGRKPTMK WSTIDRWPTH HLLIQCFADH ILKELDHFPL 250
    EKRSEVVILF SAHSLPMSVV NRGDPYPQEV SATVQKVMER LEYCNPYRLV 300
    WQSKVGPMPW LGPQTDESIK GLCERGRKNI LLVPIAFTSD HIETLYELDI 350
    EYSQVLAKEC GVENIRRAES LNGNPLFSKA LADLVHSHIQ SNELCSKQLT 400
    LSCPLCVNPV CRETKSFFTS QQL 423
    Length:423
    Mass (Da):47,862
    Last modified:May 10, 2005 - v2
    Checksum:i3FD50965E8DEABCE
    GO
    Isoform 2 (identifier: P22830-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         64-64: K → KRYESNI

    Show »
    Length:429
    Mass (Da):48,625
    Checksum:iE1CBA7E0055A24F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti228 – 2281P → S in BAC03882. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551G → C in EPP. 1 Publication
    Corresponds to variant rs3848519 [ dbSNP | Ensembl ].
    VAR_002383
    Natural varianti62 – 621P → R in EPP. 1 Publication
    VAR_030553
    Natural varianti71 – 711I → K in EPP; enzyme totally inactive. 1 Publication
    VAR_030554
    Natural varianti96 – 961R → Q.2 Publications
    Corresponds to variant rs1041951 [ dbSNP | Ensembl ].
    VAR_012028
    Natural varianti139 – 1391Q → L in EPP; autosomal recessive EPP; enzyme retains 18% of activity. 1 Publication
    VAR_030555
    Natural varianti151 – 1511S → P in EPP; enzyme totally inactive. 1 Publication
    VAR_030556
    Natural varianti178 – 1781E → K in EPP. 1 Publication
    VAR_030557
    Natural varianti182 – 1821L → R in EPP; enzyme totally inactive. 1 Publication
    VAR_030558
    Natural varianti186 – 1861I → T in EPP. 1 Publication
    VAR_002384
    Natural varianti191 – 1911Y → H in EPP; enzyme retains 72% of activity. 1 Publication
    VAR_030559
    Natural varianti192 – 1921P → T in EPP; enzyme totally inactive. 1 Publication
    VAR_030560
    Natural varianti236 – 2361C → Y in EPP; enzyme retains 12% of activity. 1 Publication
    VAR_030561
    Natural varianti260 – 2601F → L in EPP; autosomal recessive EPP; enzyme retains 52% of activity. 1 Publication
    VAR_030562
    Natural varianti264 – 2641S → L in EPP. 1 Publication
    VAR_054629
    Natural varianti267 – 2671M → I in EPP; unchanged activity; but increased thermolability. 1 Publication
    Corresponds to variant rs118204037 [ dbSNP | Ensembl ].
    VAR_002385
    Natural varianti283 – 2831T → I in EPP; enzyme almost inactive. 1 Publication
    VAR_030563
    Natural varianti288 – 2881M → K in EPP; enzyme totally inactive. 1 Publication
    VAR_030564
    Natural varianti334 – 3341P → L in EPP; autosomal recessive EPP; enzyme retains 19% of activity. 2 Publications
    Corresponds to variant rs150146721 [ dbSNP | Ensembl ].
    VAR_030565
    Natural varianti362 – 3621V → G in EPP. 1 Publication
    VAR_030566
    Natural varianti379 – 3791K → N in EPP; autosomal recessive EPP; enzyme retains 37% of activity. 1 Publication
    VAR_030567
    Natural varianti386 – 3861H → P in EPP; loss of activity. 1 Publication
    VAR_002386
    Natural varianti406 – 4061C → S in EPP; enzyme almost inactive. 1 Publication
    VAR_030568
    Natural varianti406 – 4061C → Y in EPP; enzyme almost inactive. 1 Publication
    VAR_030569
    Natural varianti408 – 4114NPVC → KSVG in EPP; no detectable enzymatic activity.
    VAR_030570
    Natural varianti417 – 4171F → S in EPP; reduced activity. 1 Publication
    VAR_002387
    Natural varianti417 – 4171Missing in EPP; enzyme totally inactive. 1 Publication
    VAR_030571

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei64 – 641K → KRYESNI in isoform 2. 1 PublicationVSP_041208

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00726 mRNA. Translation: BAA00628.1.
    AJ250235 Genomic DNA. Translation: CAB65962.1.
    BT019958 mRNA. Translation: AAV38761.1.
    AK092416 mRNA. Translation: BAC03882.1.
    AK292937 mRNA. Translation: BAF85626.1.
    CH471096 Genomic DNA. Translation: EAW63046.1.
    BC039841 mRNA. Translation: AAH39841.2.
    L36178 Genomic DNA. Translation: AAA64787.1.
    AF495859 Genomic DNA. Translation: AAM18070.1.
    CCDSiCCDS11964.1. [P22830-1]
    CCDS32836.1. [P22830-2]
    PIRiA36403.
    RefSeqiNP_000131.2. NM_000140.3. [P22830-1]
    NP_001012533.1. NM_001012515.2. [P22830-2]
    UniGeneiHs.365365.

    Genome annotation databases

    EnsembliENST00000262093; ENSP00000262093; ENSG00000066926. [P22830-1]
    ENST00000382873; ENSP00000372326; ENSG00000066926. [P22830-2]
    GeneIDi2235.
    KEGGihsa:2235.
    UCSCiuc002lgp.4. human. [P22830-2]
    uc002lgq.4. human. [P22830-1]

    Polymorphism databases

    DMDMi85701348.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Ferrochelatase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00726 mRNA. Translation: BAA00628.1 .
    AJ250235 Genomic DNA. Translation: CAB65962.1 .
    BT019958 mRNA. Translation: AAV38761.1 .
    AK092416 mRNA. Translation: BAC03882.1 .
    AK292937 mRNA. Translation: BAF85626.1 .
    CH471096 Genomic DNA. Translation: EAW63046.1 .
    BC039841 mRNA. Translation: AAH39841.2 .
    L36178 Genomic DNA. Translation: AAA64787.1 .
    AF495859 Genomic DNA. Translation: AAM18070.1 .
    CCDSi CCDS11964.1. [P22830-1 ]
    CCDS32836.1. [P22830-2 ]
    PIRi A36403.
    RefSeqi NP_000131.2. NM_000140.3. [P22830-1 ]
    NP_001012533.1. NM_001012515.2. [P22830-2 ]
    UniGenei Hs.365365.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HRK X-ray 2.00 A/B 65-423 [» ]
    2HRC X-ray 1.70 A/B 65-423 [» ]
    2HRE X-ray 2.50 A/B/C/D 65-423 [» ]
    2PNJ X-ray 2.35 A/B 65-423 [» ]
    2PO5 X-ray 2.20 A/B 65-423 [» ]
    2PO7 X-ray 2.20 A/B 65-423 [» ]
    2QD1 X-ray 2.20 A/B/C/D 65-423 [» ]
    2QD2 X-ray 2.20 A/B 65-423 [» ]
    2QD3 X-ray 2.20 A/B 65-423 [» ]
    2QD4 X-ray 2.00 A/B 65-423 [» ]
    2QD5 X-ray 2.30 A/B 65-423 [» ]
    3AQI X-ray 1.70 A/B 65-423 [» ]
    3HCN X-ray 1.60 A/B 65-423 [» ]
    3HCO X-ray 1.80 A/B 65-423 [» ]
    3HCP X-ray 2.00 A/B 65-423 [» ]
    3HCR X-ray 2.20 A/B 65-423 [» ]
    3W1W X-ray 2.01 A/B 61-423 [» ]
    4F4D X-ray 1.80 A/B 65-423 [» ]
    4KLA X-ray 2.60 A/B 65-423 [» ]
    4KLC X-ray 2.40 A/B 65-423 [» ]
    4KLR X-ray 2.18 A/B 65-423 [» ]
    4KMM X-ray 2.60 A/B 65-423 [» ]
    4MK4 X-ray 2.50 A/B 65-423 [» ]
    ProteinModelPortali P22830.
    SMRi P22830. Positions 65-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108526. 16 interactions.
    DIPi DIP-39632N.
    IntActi P22830. 5 interactions.
    STRINGi 9606.ENSP00000372326.

    PTM databases

    PhosphoSitei P22830.

    Polymorphism databases

    DMDMi 85701348.

    Proteomic databases

    MaxQBi P22830.
    PaxDbi P22830.
    PRIDEi P22830.

    Protocols and materials databases

    DNASUi 2235.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262093 ; ENSP00000262093 ; ENSG00000066926 . [P22830-1 ]
    ENST00000382873 ; ENSP00000372326 ; ENSG00000066926 . [P22830-2 ]
    GeneIDi 2235.
    KEGGi hsa:2235.
    UCSCi uc002lgp.4. human. [P22830-2 ]
    uc002lgq.4. human. [P22830-1 ]

    Organism-specific databases

    CTDi 2235.
    GeneCardsi GC18M055191.
    GeneReviewsi FECH.
    HGNCi HGNC:3647. FECH.
    HPAi CAB033205.
    HPA044100.
    HPA048177.
    MIMi 177000. phenotype.
    612386. gene.
    neXtProti NX_P22830.
    Orphaneti 79278. Erythropoietic protoporphyria.
    PharmGKBi PA28087.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0276.
    HOGENOMi HOG000060727.
    HOVERGENi HBG051898.
    KOi K01772.
    OMAi RCAESKK.
    OrthoDBi EOG70PBXZ.
    PhylomeDBi P22830.
    TreeFami TF300859.

    Enzyme and pathway databases

    UniPathwayi UPA00252 ; UER00325 .
    BioCyci MetaCyc:HS00891-MONOMER.
    BRENDAi 4.99.1.1. 2681.
    Reactomei REACT_9465. Heme biosynthesis.
    SABIO-RK P22830.

    Miscellaneous databases

    ChiTaRSi FECH. human.
    EvolutionaryTracei P22830.
    GeneWikii Ferrochelatase.
    GenomeRNAii 2235.
    NextBioi 9047.
    PROi P22830.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22830.
    Bgeei P22830.
    CleanExi HS_FECH.
    Genevestigatori P22830.

    Family and domain databases

    HAMAPi MF_00323. Ferrochelatase.
    InterProi IPR001015. Ferrochelatase.
    IPR019772. Ferrochelatase_AS.
    [Graphical view ]
    PANTHERi PTHR11108. PTHR11108. 1 hit.
    Pfami PF00762. Ferrochelatase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00109. hemH. 1 hit.
    PROSITEi PS00534. FERROCHELATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase."
      Nakahashi Y., Taketani S., Okuda M., Inoue K., Tokunaga R.
      Biochem. Biophys. Res. Commun. 173:748-755(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-96.
    2. "Ferrochelatase: complete human gene sequence, amplifiable polymorphisms and molecular study of 12 families with erythropoietic protoporphyria."
      Gouya L.M., Martin C., Deybach J.-C., Puy H.V.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-96.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Placenta and Trachea.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Testis.
    7. "A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene."
      Tugores A., Magness S.T., Brenner D.A.
      J. Biol. Chem. 269:30789-30797(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    8. "Molecular analysis of ferrochelatase gene in erythropoietic protoporphyria."
      Di Pierro E., Martinez di Montemuros F., Moriondo V., Cappellini M.D.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    9. "Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases."
      Dailey H.A., Sellers V.M., Dailey T.A.
      J. Biol. Chem. 269:390-395(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS.
    10. "Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster."
      Crouse B.R., Sellers V.M., Finnegan M.G., Dailey H.A., Johnson M.K.
      Biochemistry 35:16222-16229(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF CYSTEINES COORDINATING THE 2FE-2S CLUSTER.
    11. "Evidence that the fourth ligand to the 2Fe-2S cluster in animal ferrochelatase is a cysteine. Characterization of the enzyme from Drosophila melanogaster."
      Sellers V.M., Wang K.-F., Johnson M.K., Dailey H.A.
      J. Biol. Chem. 273:22311-22316(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF CYSTEINES COORDINATING THE 2FE-2S CLUSTER.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis."
      Wu C.-K., Dailey H.A., Rose J.P., Burden A., Sellers V.M., Wang B.-C.
      Nat. Struct. Biol. 8:156-160(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 65-423 ALONE AND IN COMPLEX WITH PROTOPORPHYRIN IX, SUBUNIT, IRON-SULFUR CLUSTER.
    15. Cited for: REVIEW ON VARIANTS EPP.
    16. "Human erythropoietic protoporphyria: two point mutations in the ferrochelatase gene."
      Lamoril J., Boulechfar S., de Verneuil H., Grandchamp B., Nordmann Y., Deybach J.-C.
      Biochem. Biophys. Res. Commun. 181:594-599(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EPP CYS-55 AND ILE-267.
    17. "A molecular defect in human protoporphyria."
      Brenner D.A., Didier J.M., Frasier F., Christensen S.R., Evans G.A., Dailey H.A.
      Am. J. Hum. Genet. 50:1203-1210(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EPP SER-417.
    18. "Recessive inheritance of erythropoietic protoporphyria with liver failure."
      Sarkany R.P.E., Alexander G.J.M.A., Cox T.M.
      Lancet 343:1394-1396(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EPP GLY-362.
    19. "A novel mutation in the ferrochelatase gene associated with erythropoietic protoporphyria."
      Imoto S., Tanizawa Y., Sata Y., Kaku K., Oka Y.
      Br. J. Haematol. 94:191-197(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EPP THR-186.
    20. "Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria."
      Ruefenacht U.B., Gouya L., Schneider-Yin X., Puy H., Schaefer B.W., Aquaron R., Nordmann Y., Minder E.I., Deybach J.-C.
      Am. J. Hum. Genet. 62:1341-1352(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EPP LYS-71; PRO-151; HIS-191; THR-192; ILE-283; LYS-288; LEU-334 AND PHE-417 DEL, CHARACTERIZATION OF VARIANTS EPP LYS-71; PRO-151; HIS-191; THR-192; ILE-283; LYS-288; LEU-334 AND PHE-417 DEL.
    21. "Mutations in the ferrochelatase gene of four Spanish patients with erythropoietic protoporphyria."
      Gouya L., Schneider-Yin X., Rufenacht U., Herrero C., Lecha M., Mascaro J.M., Puy H., Deybach J.-C., Minder E.I.
      J. Invest. Dermatol. 111:406-409(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EPP PRO-386.
    22. "Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria."
      Schneider-Yin X., Gouya L., Dorsey M., Ruefenacht U., Deybach J.-C., Ferreira G.C.
      Blood 96:1545-1549(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EPP SER-406; TYR-406 AND 408-LYS-SER--GLY-411, CHARACTERIZATION OF VARIANTS EPP SER-406; TYR-406 AND 408-LYS-SER--GLY-411.
    23. "New missense mutation in the human ferrochelatase gene in a family with erythropoietic protoporphyria: functional studies and correlation of genotype and phenotype."
      Ruefenacht U.B., Gregor A., Gouya L., Tarczynska-Nosal S., Schneider-Yin X., Deybach J.-C.
      Clin. Chem. 47:1112-1113(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EPP ARG-182, CHARACTERIZATION OF VARIANT EPP ARG-182.
    24. "Erythropoietic protoporphyria: altered phenotype after bone marrow transplantation for myelogenous leukemia in a patient heteroallelic for ferrochelatase gene mutations."
      Poh-Fitzpatrick M.B., Wang X., Anderson K.E., Bloomer J.R., Bolwell B., Lichtin A.E.
      J. Am. Acad. Dermatol. 46:861-866(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EPP ARG-62.
    25. "Novel mutations and phenotypic effect of the splice site modulator IVS3-48C in nine Swedish families with erythropoietic protoporphyria."
      Wiman A., Floderus Y., Harper P.
      J. Hum. Genet. 48:70-76(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EPP LYS-178 AND LEU-334.
    26. "Autosomal recessive erythropoietic protoporphyria in the United Kingdom: prevalence and relationship to liver disease."
      Whatley S.D., Mason N.G., Khan M., Zamiri M., Badminton M.N., Missaoui W.N., Dailey T.A., Dailey H.A., Douglas W.S., Wainwright N.J., Elder G.H.
      J. Med. Genet. 41:E105-E105(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EPP LEU-139; TYR-236; LEU-260 AND ASN-379, CHARACTERIZATION OF VARIANTS EPP LEU-139; TYR-236; LEU-260 AND ASN-379.
    27. "Heterogeneity of mutations in the ferrochelatase gene in Italian patients with erythropoietic protoporphyria."
      Aurizi C., Schneider-Yin X., Sorge F., Macri A., Minder E.I., Biolcati G.
      Mol. Genet. Metab. 90:402-407(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EPP LEU-264.

    Entry informationi

    Entry nameiHEMH_HUMAN
    AccessioniPrimary (citable) accession number: P22830
    Secondary accession number(s): A8KA72, Q8IXN1, Q8NAN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 162 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 18
      Human chromosome 18: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3