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P22830

- HEMH_HUMAN

UniProt

P22830 - HEMH_HUMAN

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Protein
Ferrochelatase, mitochondrial
Gene
FECH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the ferrous insertion into protoporphyrin IX.UniRule annotation

Catalytic activityi

Protoheme + 2 H+ = protoporphyrin + Fe2+.UniRule annotation

Cofactori

Binds 1 2Fe-2S cluster.

Enzyme regulationi

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.12 Publications
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.
Mutagenesisi360 – 3601C → S: No loss of activity.
Mutagenesisi395 – 3951C → S: No loss of activity.
Mutagenesisi403 – 4031C → D or H: Loss of activity.
Mutagenesisi406 – 4061C → D, H or S: Loss of activity.
Mutagenesisi411 – 4111C → H or S: Loss of activity.
Mutagenesisi417 – 4171F → L: Decreased activity.
Mutagenesisi417 – 4171F → Y or W: Greatly reduced activity.

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 – 5454Mitochondrion Reviewed prediction
Add
BLAST
Chaini55 – 423369Ferrochelatase, mitochondrialUniRule annotation
PRO_0000008873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571N6-acetyllysine By similarity
Modified residuei138 – 1381N6-succinyllysine By similarity
Modified residuei415 – 4151N6-acetyllysine; alternate By similarity
Modified residuei415 – 4151N6-succinyllysine; alternate By 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.
IntActiP22830. 5 interactions.
STRINGi9606.ENSP00000372326.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP22830.

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.

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

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.
VSP_041208

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281P → S in BAC03882. 1 Publication

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.
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 161 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

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