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P22830 (HEMH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferrochelatase, mitochondrial

EC=4.99.1.1
Alternative name(s):
Heme synthase
Protoheme ferro-lyase
Gene names
Name:FECH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ferrous insertion into protoporphyrin IX. HAMAP-Rule MF_00323

Catalytic activity

Protoheme + 2 H+ = protoporphyrin + Fe2+. HAMAP-Rule MF_00323

Cofactor

Binds 1 2Fe-2S cluster.

Enzyme regulation

Inhibited by nitric oxide (NO). The 2Fe-2S cluster could act as a NO sensor. HAMAP-Rule MF_00323

Pathway

Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. HAMAP-Rule MF_00323

Subunit structure

Homodimer. Ref.14

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side HAMAP-Rule MF_00323.

Involvement in disease

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. Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Sequence similarities

Belongs to the ferrochelatase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   Ligand2Fe-2S
Iron
Iron-sulfur
Metal-binding
   Molecular functionLyase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: Ensembl

detection of UV

Inferred from electronic annotation. Source: Ensembl

erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

generation of precursor metabolites and energy

Traceable author statement PubMed 1729699. Source: ProtInc

heme biosynthetic process

Traceable author statement. Source: Reactome

iron ion homeostasis

Inferred from electronic annotation. Source: Ensembl

porphyrin-containing compound metabolic process

Traceable author statement. Source: Reactome

protoporphyrinogen IX metabolic process

Inferred from direct assay PubMed 15123683. Source: BHF-UCL

regulation of eIF2 alpha phosphorylation by heme

Inferred from electronic annotation. Source: Ensembl

regulation of hemoglobin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

response to arsenic-containing substance

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to insecticide

Inferred from electronic annotation. Source: Ensembl

response to lead ion

Inferred from electronic annotation. Source: Ensembl

response to light stimulus

Traceable author statement Ref.17. Source: ProtInc

response to methylmercury

Inferred from electronic annotation. Source: Ensembl

response to platinum ion

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

very-low-density lipoprotein particle assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Traceable author statement. Source: Reactome

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

ferrochelatase activity

Inferred from direct assay PubMed 15123683. Source: BHF-UCL

ferrous iron binding

Traceable author statement PubMed 1729699. Source: ProtInc

heme binding

Inferred from electronic annotation. Source: Ensembl

iron-responsive element binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P22830-1)

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.
Isoform 2 (identifier: P22830-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5454Mitochondrion Potential
Chain55 – 423369Ferrochelatase, mitochondrial HAMAP-Rule MF_00323
PRO_0000008873

Sites

Active site2301
Active site3831
Metal binding1961Iron-sulfur (2Fe-2S)
Metal binding4031Iron-sulfur (2Fe-2S)
Metal binding4061Iron-sulfur (2Fe-2S)
Metal binding4111Iron-sulfur (2Fe-2S)

Amino acid modifications

Modified residue571N6-acetyllysine By similarity
Modified residue1381N6-succinyllysine By similarity
Modified residue4151N6-acetyllysine; alternate By similarity
Modified residue4151N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence641K → KRYESNI in isoform 2.
VSP_041208
Natural variant551G → C in EPP. Ref.16
Corresponds to variant rs3848519 [ dbSNP | Ensembl ].
VAR_002383
Natural variant621P → R in EPP. Ref.24
VAR_030553
Natural variant711I → K in EPP; enzyme totally inactive. Ref.20
VAR_030554
Natural variant961R → Q. Ref.1 Ref.2
Corresponds to variant rs1041951 [ dbSNP | Ensembl ].
VAR_012028
Natural variant1391Q → L in EPP; autosomal recessive EPP; enzyme retains 18% of activity. Ref.26
VAR_030555
Natural variant1511S → P in EPP; enzyme totally inactive. Ref.20
VAR_030556
Natural variant1781E → K in EPP. Ref.25
VAR_030557
Natural variant1821L → R in EPP; enzyme totally inactive. Ref.23
VAR_030558
Natural variant1861I → T in EPP. Ref.19
VAR_002384
Natural variant1911Y → H in EPP; enzyme retains 72% of activity. Ref.20
VAR_030559
Natural variant1921P → T in EPP; enzyme totally inactive. Ref.20
VAR_030560
Natural variant2361C → Y in EPP; enzyme retains 12% of activity. Ref.26
VAR_030561
Natural variant2601F → L in EPP; autosomal recessive EPP; enzyme retains 52% of activity. Ref.26
VAR_030562
Natural variant2641S → L in EPP. Ref.27
VAR_054629
Natural variant2671M → I in EPP; unchanged activity; but increased thermolability. Ref.16
Corresponds to variant rs118204037 [ dbSNP | Ensembl ].
VAR_002385
Natural variant2831T → I in EPP; enzyme almost inactive. Ref.20
VAR_030563
Natural variant2881M → K in EPP; enzyme totally inactive. Ref.20
VAR_030564
Natural variant3341P → L in EPP; autosomal recessive EPP; enzyme retains 19% of activity. Ref.20 Ref.25
Corresponds to variant rs150146721 [ dbSNP | Ensembl ].
VAR_030565
Natural variant3621V → G in EPP. Ref.18
VAR_030566
Natural variant3791K → N in EPP; autosomal recessive EPP; enzyme retains 37% of activity. Ref.26
VAR_030567
Natural variant3861H → P in EPP; loss of activity. Ref.21
VAR_002386
Natural variant4061C → S in EPP; enzyme almost inactive. Ref.22
VAR_030568
Natural variant4061C → Y in EPP; enzyme almost inactive. Ref.22
VAR_030569
Natural variant408 – 4114NPVC → KSVG in EPP; no detectable enzymatic activity.
VAR_030570
Natural variant4171F → S in EPP; reduced activity. Ref.17
VAR_002387
Natural variant4171Missing in EPP; enzyme totally inactive. Ref.20
VAR_030571

Experimental info

Mutagenesis1961C → S: Loss of activity.
Mutagenesis3601C → S: No loss of activity.
Mutagenesis3951C → S: No loss of activity.
Mutagenesis4031C → D or H: Loss of activity.
Mutagenesis4061C → D, H or S: Loss of activity.
Mutagenesis4111C → H or S: Loss of activity.
Mutagenesis4171F → L: Decreased activity.
Mutagenesis4171F → Y or W: Greatly reduced activity.
Sequence conflict2281P → S in BAC03882. Ref.4

Secondary structure

............................................................ 423
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: 3FD50965E8DEABCE

FASTA42347,862
        10         20         30         40         50         60 
MRSLGANMAA ALRAAGVLLR DPLASSSWRV CQPWRWKSGA AAAAVTTETA QHAQGAKPQV 

        70         80         90        100        110        120 
QPQKRKPKTG ILMLNMGGPE TLGDVHDFLL RLFLDRDLMT LPIQNKLAPF IAKRRTPKIQ 

       130        140        150        160        170        180 
EQYRRIGGGS PIKIWTSKQG EGMVKLLDEL SPNTAPHKYY IGFRYVHPLT EEAIEEMERD 

       190        200        210        220        230        240 
GLERAIAFTQ YPQYSCSTTG SSLNAIYRYY NQVGRKPTMK WSTIDRWPTH HLLIQCFADH 

       250        260        270        280        290        300 
ILKELDHFPL EKRSEVVILF SAHSLPMSVV NRGDPYPQEV SATVQKVMER LEYCNPYRLV 

       310        320        330        340        350        360 
WQSKVGPMPW LGPQTDESIK GLCERGRKNI LLVPIAFTSD HIETLYELDI EYSQVLAKEC 

       370        380        390        400        410        420 
GVENIRRAES LNGNPLFSKA LADLVHSHIQ SNELCSKQLT LSCPLCVNPV CRETKSFFTS 


QQL 

« Hide

Isoform 2 [UniParc].

Checksum: E1CBA7E0055A24F5
Show »

FASTA42948,625

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Substrate interactions with human ferrochelatase."
Medlock A., Swartz L., Dailey T.A., Dailey H.A., Lanzilotta W.N.
Proc. Natl. Acad. Sci. U.S.A. 104:1789-1793(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 65-423 ALONE AND IN COMPLEX WITH PROTOPORPHYRIN IX, SUBUNIT, IRON-SULFUR CLUSTER.
[15]"Erythropoietic protoporphyria."
Cox T.M.
J. Inherit. Metab. Dis. 20:258-269(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Ferrochelatase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA36403.
RefSeqNP_000131.2. NM_000140.3.
NP_001012533.1. NM_001012515.2.
UniGeneHs.365365.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
4MK4X-ray2.50A/B65-423[»]
ProteinModelPortalP22830.
SMRP22830. Positions 65-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108526. 14 interactions.
IntActP22830. 5 interactions.
STRING9606.ENSP00000372326.

PTM databases

PhosphoSiteP22830.

Polymorphism databases

DMDM85701348.

Proteomic databases

PaxDbP22830.
PRIDEP22830.

Protocols and materials databases

DNASU2235.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262093; ENSP00000262093; ENSG00000066926. [P22830-1]
ENST00000382873; ENSP00000372326; ENSG00000066926. [P22830-2]
GeneID2235.
KEGGhsa:2235.
UCSCuc002lgp.4. human. [P22830-2]
uc002lgq.4. human. [P22830-1]

Organism-specific databases

CTD2235.
GeneCardsGC18M055191.
HGNCHGNC:3647. FECH.
HPACAB033205.
HPA044100.
HPA048177.
MIM177000. phenotype.
612386. gene.
neXtProtNX_P22830.
Orphanet79278. Erythropoietic protoporphyria.
PharmGKBPA28087.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0276.
HOGENOMHOG000060727.
HOVERGENHBG051898.
KOK01772.
OMALNMGGPN.
OrthoDBEOG70PBXZ.
PhylomeDBP22830.
TreeFamTF300859.

Enzyme and pathway databases

BioCycMetaCyc:HS00891-MONOMER.
BRENDA4.99.1.1. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP22830.
UniPathwayUPA00252; UER00325.

Gene expression databases

ArrayExpressP22830.
BgeeP22830.
CleanExHS_FECH.
GenevestigatorP22830.

Family and domain databases

HAMAPMF_00323. Ferrochelatase.
InterProIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
[Graphical view]
PANTHERPTHR11108. PTHR11108. 1 hit.
PfamPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00109. hemH. 1 hit.
PROSITEPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFECH. human.
EvolutionaryTraceP22830.
GeneWikiFerrochelatase.
GenomeRNAi2235.
NextBio9047.
PROP22830.
SOURCESearch...

Entry information

Entry nameHEMH_HUMAN
AccessionPrimary (citable) accession number: P22830
Secondary accession number(s): A8KA72, Q8IXN1, Q8NAN0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM