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Protein

Ferrochelatase, mitochondrial

Gene

FECH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ferrous insertion into protoporphyrin IX.

Catalytic activityi

Protoheme + 2 H+ = protoporphyrin + Fe2+.

Cofactori

[2Fe-2S] clusterNote: Binds 1 [2Fe-2S] cluster.

Enzyme regulationi

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

Pathwayi: protoheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes protoheme from protoporphyrin-IX.
Proteins known to be involved in this subpathway in this organism are:
  1. Ferrochelatase (DKFZp686P18130), Ferrochelatase, Ferrochelatase, Ferrochelatase, Ferrochelatase (FECH), Ferrochelatase, mitochondrial (FECH)
This subpathway is part of the pathway protoheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protoheme from protoporphyrin-IX, the pathway protoheme biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi196Iron-sulfur (2Fe-2S)1
Active sitei2301
Active sitei3831
Metal bindingi403Iron-sulfur (2Fe-2S)1
Metal bindingi406Iron-sulfur (2Fe-2S)1
Metal bindingi411Iron-sulfur (2Fe-2S)1

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  • ferrochelatase activity Source: BHF-UCL
  • ferrous iron binding Source: ProtInc

GO - Biological processi

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.
ZFISH:HS00891-MONOMER.
BRENDAi4.99.1.1. 2681.
ReactomeiR-HSA-189451. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:3647. FECH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Erythropoietic protoporphyria (EPP)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:177000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00238355G → C in EPP. 1 PublicationCorresponds to variant rs3848519dbSNPEnsembl.1
Natural variantiVAR_03055362P → R in EPP. 1 PublicationCorresponds to variant rs150830931dbSNPEnsembl.1
Natural variantiVAR_03055471I → K in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030555139Q → L in EPP; autosomal recessive EPP; enzyme retains 18% of activity. 1 Publication1
Natural variantiVAR_030556151S → P in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030557178E → K in EPP. 1 Publication1
Natural variantiVAR_030558182L → R in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_002384186I → T in EPP. 1 Publication1
Natural variantiVAR_030559191Y → H in EPP; enzyme retains 72% of activity. 1 Publication1
Natural variantiVAR_030560192P → T in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030561236C → Y in EPP; enzyme retains 12% of activity. 1 PublicationCorresponds to variant rs761962617dbSNPEnsembl.1
Natural variantiVAR_030562260F → L in EPP; autosomal recessive EPP; enzyme retains 52% of activity. 1 Publication1
Natural variantiVAR_054629264S → L in EPP. 1 Publication1
Natural variantiVAR_002385267M → I in EPP; unchanged activity; but increased thermolability. 1 PublicationCorresponds to variant rs118204037dbSNPEnsembl.1
Natural variantiVAR_030563283T → I in EPP; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030564288M → K in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030565334P → L in EPP; autosomal recessive EPP; enzyme retains 19% of activity. 2 PublicationsCorresponds to variant rs150146721dbSNPEnsembl.1
Natural variantiVAR_030566362V → G in EPP. 1 PublicationCorresponds to variant rs118204040dbSNPEnsembl.1
Natural variantiVAR_030567379K → N in EPP; autosomal recessive EPP; enzyme retains 37% of activity. 1 Publication1
Natural variantiVAR_002386386H → P in EPP; loss of activity. 1 Publication1
Natural variantiVAR_030568406C → S in EPP; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030569406C → Y in EPP; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030570408 – 411NPVC → KSVG in EPP; no detectable enzymatic activity. 4
Natural variantiVAR_002387417F → S in EPP; reduced activity. 1 PublicationCorresponds to variant rs118204039dbSNPEnsembl.1
Natural variantiVAR_030571417Missing in EPP; enzyme totally inactive. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi196C → S: Loss of activity. 1 Publication1
Mutagenesisi360C → S: No loss of activity. 1 Publication1
Mutagenesisi395C → S: No loss of activity. 1 Publication1
Mutagenesisi403C → D or H: Loss of activity. 1 Publication1
Mutagenesisi406C → D, H or S: Loss of activity. 1 Publication1
Mutagenesisi411C → H or S: Loss of activity. 1 Publication1
Mutagenesisi417F → L: Decreased activity. 1 Publication1
Mutagenesisi417F → Y or W: Greatly reduced activity. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2235.
MalaCardsiFECH.
MIMi177000. phenotype.
OpenTargetsiENSG00000066926.
Orphaneti79278. Erythropoietic protoporphyria.
PharmGKBiPA28087.

Chemistry databases

DrugBankiDB02659. Cholic Acid.

Polymorphism and mutation databases

BioMutaiFECH.
DMDMi85701348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 54MitochondrionSequence analysisAdd BLAST54
ChainiPRO_000000887355 – 423Ferrochelatase, mitochondrialAdd BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei57N6-acetyllysineBy similarity1
Modified residuei138N6-succinyllysineBy similarity1
Modified residuei415N6-acetyllysine; alternateBy similarity1
Modified residuei415N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP22830.
MaxQBiP22830.
PaxDbiP22830.
PeptideAtlasiP22830.
PRIDEiP22830.

PTM databases

iPTMnetiP22830.
PhosphoSitePlusiP22830.

Expressioni

Gene expression databases

BgeeiENSG00000066926.
CleanExiHS_FECH.
ExpressionAtlasiP22830. baseline and differential.
GenevisibleiP22830. HS.

Organism-specific databases

HPAiCAB033205.
HPA044100.
HPA048177.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PGRMC1O002643EBI-1390356,EBI-1045534

Protein-protein interaction databases

BioGridi108526. 43 interactors.
DIPiDIP-39632N.
IntActiP22830. 33 interactors.
STRINGi9606.ENSP00000372326.

Structurei

Secondary structure

1423
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi69 – 75Combined sources7
Helixi82 – 84Combined sources3
Helixi85 – 93Combined sources9
Turni96 – 98Combined sources3
Helixi104 – 125Combined sources22
Helixi132 – 150Combined sources19
Helixi152 – 154Combined sources3
Beta strandi156 – 169Combined sources14
Helixi170 – 179Combined sources10
Beta strandi183 – 190Combined sources8
Turni196 – 198Combined sources3
Helixi199 – 212Combined sources14
Beta strandi218 – 224Combined sources7
Helixi231 – 245Combined sources15
Turni250 – 252Combined sources3
Helixi253 – 255Combined sources3
Beta strandi257 – 263Combined sources7
Helixi267 – 270Combined sources4
Turni271 – 273Combined sources3
Helixi276 – 290Combined sources15
Turni291 – 293Combined sources3
Beta strandi297 – 302Combined sources6
Beta strandi306 – 308Combined sources3
Beta strandi310 – 314Combined sources5
Helixi315 – 324Combined sources10
Beta strandi329 – 333Combined sources5
Helixi345 – 348Combined sources4
Helixi350 – 359Combined sources10
Beta strandi364 – 367Combined sources4
Beta strandi371 – 373Combined sources3
Helixi375 – 391Combined sources17
Helixi397 – 400Combined sources4
Helixi410 – 419Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22830.

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1321. Eukaryota.
COG0276. LUCA.
GeneTreeiENSGT00390000016258.
HOGENOMiHOG000060727.
HOVERGENiHBG051898.
InParanoidiP22830.
KOiK01772.
OMAiLPIQNKL.
OrthoDBiEOG091G0850.
PhylomeDBiP22830.
TreeFamiTF300859.

Family and domain databases

CDDicd00419. Ferrochelatase_C. 1 hit.
cd03411. Ferrochelatase_N. 1 hit.
HAMAPiMF_00323. Ferrochelatase. 1 hit.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
IPR033644. Ferrochelatase_C.
IPR033659. Ferrochelatase_N.
[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. AlignAdd to basket

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

        10         20         30         40         50
MRSLGANMAA ALRAAGVLLR DPLASSSWRV CQPWRWKSGA AAAAVTTETA
60 70 80 90 100
QHAQGAKPQV QPQKRKPKTG ILMLNMGGPE TLGDVHDFLL RLFLDRDLMT
110 120 130 140 150
LPIQNKLAPF IAKRRTPKIQ EQYRRIGGGS PIKIWTSKQG EGMVKLLDEL
160 170 180 190 200
SPNTAPHKYY IGFRYVHPLT EEAIEEMERD GLERAIAFTQ YPQYSCSTTG
210 220 230 240 250
SSLNAIYRYY NQVGRKPTMK WSTIDRWPTH HLLIQCFADH ILKELDHFPL
260 270 280 290 300
EKRSEVVILF SAHSLPMSVV NRGDPYPQEV SATVQKVMER LEYCNPYRLV
310 320 330 340 350
WQSKVGPMPW LGPQTDESIK GLCERGRKNI LLVPIAFTSD HIETLYELDI
360 370 380 390 400
EYSQVLAKEC GVENIRRAES LNGNPLFSKA LADLVHSHIQ SNELCSKQLT
410 420
LSCPLCVNPV CRETKSFFTS QQL
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)DescriptionActionsGraphical viewLength
Sequence conflicti228P → S in BAC03882 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00238355G → C in EPP. 1 PublicationCorresponds to variant rs3848519dbSNPEnsembl.1
Natural variantiVAR_03055362P → R in EPP. 1 PublicationCorresponds to variant rs150830931dbSNPEnsembl.1
Natural variantiVAR_03055471I → K in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_01202896R → Q.2 PublicationsCorresponds to variant rs1041951dbSNPEnsembl.1
Natural variantiVAR_030555139Q → L in EPP; autosomal recessive EPP; enzyme retains 18% of activity. 1 Publication1
Natural variantiVAR_030556151S → P in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030557178E → K in EPP. 1 Publication1
Natural variantiVAR_030558182L → R in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_002384186I → T in EPP. 1 Publication1
Natural variantiVAR_030559191Y → H in EPP; enzyme retains 72% of activity. 1 Publication1
Natural variantiVAR_030560192P → T in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030561236C → Y in EPP; enzyme retains 12% of activity. 1 PublicationCorresponds to variant rs761962617dbSNPEnsembl.1
Natural variantiVAR_030562260F → L in EPP; autosomal recessive EPP; enzyme retains 52% of activity. 1 Publication1
Natural variantiVAR_054629264S → L in EPP. 1 Publication1
Natural variantiVAR_002385267M → I in EPP; unchanged activity; but increased thermolability. 1 PublicationCorresponds to variant rs118204037dbSNPEnsembl.1
Natural variantiVAR_030563283T → I in EPP; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030564288M → K in EPP; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030565334P → L in EPP; autosomal recessive EPP; enzyme retains 19% of activity. 2 PublicationsCorresponds to variant rs150146721dbSNPEnsembl.1
Natural variantiVAR_030566362V → G in EPP. 1 PublicationCorresponds to variant rs118204040dbSNPEnsembl.1
Natural variantiVAR_030567379K → N in EPP; autosomal recessive EPP; enzyme retains 37% of activity. 1 Publication1
Natural variantiVAR_002386386H → P in EPP; loss of activity. 1 Publication1
Natural variantiVAR_030568406C → S in EPP; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030569406C → Y in EPP; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030570408 – 411NPVC → KSVG in EPP; no detectable enzymatic activity. 4
Natural variantiVAR_002387417F → S in EPP; reduced activity. 1 PublicationCorresponds to variant rs118204039dbSNPEnsembl.1
Natural variantiVAR_030571417Missing in EPP; enzyme totally inactive. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04120864K → KRYESNI in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human. [P22830-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ferrochelatase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108526. 43 interactors.
DIPiDIP-39632N.
IntActiP22830. 33 interactors.
STRINGi9606.ENSP00000372326.

Chemistry databases

DrugBankiDB02659. Cholic Acid.

PTM databases

iPTMnetiP22830.
PhosphoSitePlusiP22830.

Polymorphism and mutation databases

BioMutaiFECH.
DMDMi85701348.

Proteomic databases

EPDiP22830.
MaxQBiP22830.
PaxDbiP22830.
PeptideAtlasiP22830.
PRIDEiP22830.

Protocols and materials databases

DNASUi2235.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262093; ENSP00000262093; ENSG00000066926. [P22830-1]
ENST00000382873; ENSP00000372326; ENSG00000066926. [P22830-2]
GeneIDi2235.
KEGGihsa:2235.
UCSCiuc002lgp.5. human. [P22830-1]

Organism-specific databases

CTDi2235.
DisGeNETi2235.
GeneCardsiFECH.
GeneReviewsiFECH.
HGNCiHGNC:3647. FECH.
HPAiCAB033205.
HPA044100.
HPA048177.
MalaCardsiFECH.
MIMi177000. phenotype.
612386. gene.
neXtProtiNX_P22830.
OpenTargetsiENSG00000066926.
Orphaneti79278. Erythropoietic protoporphyria.
PharmGKBiPA28087.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1321. Eukaryota.
COG0276. LUCA.
GeneTreeiENSGT00390000016258.
HOGENOMiHOG000060727.
HOVERGENiHBG051898.
InParanoidiP22830.
KOiK01772.
OMAiLPIQNKL.
OrthoDBiEOG091G0850.
PhylomeDBiP22830.
TreeFamiTF300859.

Enzyme and pathway databases

UniPathwayiUPA00252; UER00325.
BioCyciMetaCyc:HS00891-MONOMER.
ZFISH:HS00891-MONOMER.
BRENDAi4.99.1.1. 2681.
ReactomeiR-HSA-189451. Heme biosynthesis.
SABIO-RKP22830.

Miscellaneous databases

ChiTaRSiFECH. human.
EvolutionaryTraceiP22830.
GeneWikiiFerrochelatase.
GenomeRNAii2235.
PROiP22830.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000066926.
CleanExiHS_FECH.
ExpressionAtlasiP22830. baseline and differential.
GenevisibleiP22830. HS.

Family and domain databases

CDDicd00419. Ferrochelatase_C. 1 hit.
cd03411. Ferrochelatase_N. 1 hit.
HAMAPiMF_00323. Ferrochelatase. 1 hit.
InterProiIPR001015. Ferrochelatase.
IPR019772. Ferrochelatase_AS.
IPR033644. Ferrochelatase_C.
IPR033659. Ferrochelatase_N.
[Graphical view]
PANTHERiPTHR11108. PTHR11108. 1 hit.
PfamiPF00762. Ferrochelatase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00109. hemH. 1 hit.
PROSITEiPS00534. FERROCHELATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 183 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.