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Protein

Ferrochelatase, mitochondrial

Gene

FECH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

Activity 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, mitochondrial (FECH), Ferrochelatase, Ferrochelatase, Ferrochelatase (hemH), Ferrochelatase (FECH), Ferrochelatase, Ferrochelatase (DKFZp686P18130)
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

Keywordsi

Molecular functionLyase
Biological processHeme biosynthesis, Porphyrin biosynthesis
Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00891-MONOMER
BRENDAi4.99.1.1 2681
ReactomeiR-HSA-189451 Heme biosynthesis
SABIO-RKiP22830
UniPathwayi
UPA00252;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

EuPathDBiHostDB:ENSG00000066926.10
HGNCiHGNC:3647 FECH
MIMi612386 gene
neXtProtiNX_P22830

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Protoporphyria, erythropoietic, 1 (EPP1)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive form of porphyria with onset usually before age 10 years. 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 EPP1. 1 PublicationCorresponds to variant dbSNP:rs3848519EnsemblClinVar.1
Natural variantiVAR_03055362P → R in EPP1. 1 PublicationCorresponds to variant dbSNP:rs150830931Ensembl.1
Natural variantiVAR_03055471I → K in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030555139Q → L in EPP1; enzyme retains 18% of activity. 1 PublicationCorresponds to variant dbSNP:rs1356965294Ensembl.1
Natural variantiVAR_030556151S → P in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030557178E → K in EPP1. 1 Publication1
Natural variantiVAR_030558182L → R in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_002384186I → T in EPP1. 1 Publication1
Natural variantiVAR_030559191Y → H in EPP1; enzyme retains 72% of activity. 1 PublicationCorresponds to variant dbSNP:rs1055019947Ensembl.1
Natural variantiVAR_030560192P → T in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030561236C → Y in EPP1; enzyme retains 12% of activity. 1 PublicationCorresponds to variant dbSNP:rs761962617Ensembl.1
Natural variantiVAR_030562260F → L in EPP1; enzyme retains 52% of activity. 1 Publication1
Natural variantiVAR_054629264S → L in EPP1. 1 Publication1
Natural variantiVAR_002385267M → I in EPP1; unchanged activity; but increased thermolability. 1 PublicationCorresponds to variant dbSNP:rs118204037EnsemblClinVar.1
Natural variantiVAR_030563283T → I in EPP1; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030564288M → K in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030565334P → L in EPP1; enzyme retains 19% of activity. 2 PublicationsCorresponds to variant dbSNP:rs150146721EnsemblClinVar.1
Natural variantiVAR_030566362V → G in EPP1. 1 PublicationCorresponds to variant dbSNP:rs118204040Ensembl.1
Natural variantiVAR_030567379K → N in EPP1; enzyme retains 37% of activity. 1 Publication1
Natural variantiVAR_002386386H → P in EPP1; loss of activity. 1 Publication1
Natural variantiVAR_030568406C → S in EPP1; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030569406C → Y in EPP1; enzyme almost inactive. 1 PublicationCorresponds to variant dbSNP:rs1324421474Ensembl.1
Natural variantiVAR_030570408 – 411NPVC → KSVG in EPP1; no detectable enzymatic activity. 4
Natural variantiVAR_002387417F → S in EPP1; reduced activity. 1 PublicationCorresponds to variant dbSNP:rs118204039Ensembl.1
Natural variantiVAR_030571417Missing in EPP1; 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
GeneReviewsiFECH
MalaCardsiFECH
MIMi177000 phenotype
OpenTargetsiENSG00000066926
Orphaneti79278 Autosomal erythropoietic protoporphyria
PharmGKBiPA28087

Chemistry databases

ChEMBLiCHEMBL3879831
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
ProteomicsDBi54041
54042 [P22830-2]

PTM databases

iPTMnetiP22830
PhosphoSitePlusiP22830

Expressioni

Gene expression databases

BgeeiENSG00000066926 Expressed in 206 organ(s), highest expression level in trabecular bone tissue
CleanExiHS_FECH
ExpressionAtlasiP22830 baseline and differential
GenevisibleiP22830 HS

Organism-specific databases

HPAiHPA044100
HPA048177

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108526, 48 interactors
DIPiDIP-39632N
IntActiP22830, 38 interactors
MINTiP22830
STRINGi9606.ENSP00000372326

Structurei

Secondary structure

1423
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiLGDPYHC
OrthoDBiEOG091G0850
PhylomeDBiP22830
TreeFamiTF300859

Family and domain databases

CDDicd00419 Ferrochelatase_C, 1 hit
cd03411 Ferrochelatase_N, 1 hit
HAMAPiMF_00323 Ferrochelatase, 1 hit
InterProiView protein in InterPro
IPR001015 Ferrochelatase
IPR019772 Ferrochelatase_AS
IPR033644 Ferrochelatase_C
IPR033659 Ferrochelatase_N
PANTHERiPTHR11108 PTHR11108, 1 hit
PfamiView protein in Pfam
PF00762 Ferrochelatase, 1 hit
TIGRFAMsiTIGR00109 hemH, 1 hit
PROSITEiView protein in PROSITE
PS00534 FERROCHELATASE, 1 hit

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

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EJX5K7EJX5_HUMAN
Ferrochelatase
FECH
143Annotation score:
K7ELX4K7ELX4_HUMAN
Ferrochelatase, mitochondrial
FECH
326Annotation score:
K7EPN2K7EPN2_HUMAN
Ferrochelatase, mitochondrial
FECH
90Annotation score:
K7EJM8K7EJM8_HUMAN
Ferrochelatase, mitochondrial
FECH
111Annotation score:
K7EKP7K7EKP7_HUMAN
Ferrochelatase, mitochondrial
FECH
165Annotation score:

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 EPP1. 1 PublicationCorresponds to variant dbSNP:rs3848519EnsemblClinVar.1
Natural variantiVAR_03055362P → R in EPP1. 1 PublicationCorresponds to variant dbSNP:rs150830931Ensembl.1
Natural variantiVAR_03055471I → K in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_01202896R → Q2 PublicationsCorresponds to variant dbSNP:rs1041951EnsemblClinVar.1
Natural variantiVAR_030555139Q → L in EPP1; enzyme retains 18% of activity. 1 PublicationCorresponds to variant dbSNP:rs1356965294Ensembl.1
Natural variantiVAR_030556151S → P in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030557178E → K in EPP1. 1 Publication1
Natural variantiVAR_030558182L → R in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_002384186I → T in EPP1. 1 Publication1
Natural variantiVAR_030559191Y → H in EPP1; enzyme retains 72% of activity. 1 PublicationCorresponds to variant dbSNP:rs1055019947Ensembl.1
Natural variantiVAR_030560192P → T in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030561236C → Y in EPP1; enzyme retains 12% of activity. 1 PublicationCorresponds to variant dbSNP:rs761962617Ensembl.1
Natural variantiVAR_030562260F → L in EPP1; enzyme retains 52% of activity. 1 Publication1
Natural variantiVAR_054629264S → L in EPP1. 1 Publication1
Natural variantiVAR_002385267M → I in EPP1; unchanged activity; but increased thermolability. 1 PublicationCorresponds to variant dbSNP:rs118204037EnsemblClinVar.1
Natural variantiVAR_030563283T → I in EPP1; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030564288M → K in EPP1; enzyme totally inactive. 1 Publication1
Natural variantiVAR_030565334P → L in EPP1; enzyme retains 19% of activity. 2 PublicationsCorresponds to variant dbSNP:rs150146721EnsemblClinVar.1
Natural variantiVAR_030566362V → G in EPP1. 1 PublicationCorresponds to variant dbSNP:rs118204040Ensembl.1
Natural variantiVAR_030567379K → N in EPP1; enzyme retains 37% of activity. 1 Publication1
Natural variantiVAR_002386386H → P in EPP1; loss of activity. 1 Publication1
Natural variantiVAR_030568406C → S in EPP1; enzyme almost inactive. 1 Publication1
Natural variantiVAR_030569406C → Y in EPP1; enzyme almost inactive. 1 PublicationCorresponds to variant dbSNP:rs1324421474Ensembl.1
Natural variantiVAR_030570408 – 411NPVC → KSVG in EPP1; no detectable enzymatic activity. 4
Natural variantiVAR_002387417F → S in EPP1; reduced activity. 1 PublicationCorresponds to variant dbSNP:rs118204039Ensembl.1
Natural variantiVAR_030571417Missing in EPP1; 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

Similar proteinsi

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, 48 interactors
DIPiDIP-39632N
IntActiP22830, 38 interactors
MINTiP22830
STRINGi9606.ENSP00000372326

Chemistry databases

ChEMBLiCHEMBL3879831
DrugBankiDB02659 Cholic Acid

PTM databases

iPTMnetiP22830
PhosphoSitePlusiP22830

Polymorphism and mutation databases

BioMutaiFECH
DMDMi85701348

Proteomic databases

EPDiP22830
MaxQBiP22830
PaxDbiP22830
PeptideAtlasiP22830
PRIDEiP22830
ProteomicsDBi54041
54042 [P22830-2]

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
EuPathDBiHostDB:ENSG00000066926.10
GeneCardsiFECH
GeneReviewsiFECH
HGNCiHGNC:3647 FECH
HPAiHPA044100
HPA048177
MalaCardsiFECH
MIMi177000 phenotype
612386 gene
neXtProtiNX_P22830
OpenTargetsiENSG00000066926
Orphaneti79278 Autosomal erythropoietic protoporphyria
PharmGKBiPA28087
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi
UPA00252;UER00325

BioCyciMetaCyc:HS00891-MONOMER
BRENDAi4.99.1.1 2681
ReactomeiR-HSA-189451 Heme biosynthesis
SABIO-RKiP22830

Miscellaneous databases

ChiTaRSiFECH human
EvolutionaryTraceiP22830
GeneWikiiFerrochelatase
GenomeRNAii2235
PROiPR:P22830
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000066926 Expressed in 206 organ(s), highest expression level in trabecular bone tissue
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
InterProiView protein in InterPro
IPR001015 Ferrochelatase
IPR019772 Ferrochelatase_AS
IPR033644 Ferrochelatase_C
IPR033659 Ferrochelatase_N
PANTHERiPTHR11108 PTHR11108, 1 hit
PfamiView protein in Pfam
PF00762 Ferrochelatase, 1 hit
TIGRFAMsiTIGR00109 hemH, 1 hit
PROSITEiView protein in PROSITE
PS00534 FERROCHELATASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHEMH_HUMAN
AccessioniPrimary (citable) accession number: P22830
Secondary accession number(s): A8KA72, Q8IXN1, Q8NAN0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: May 10, 2005
Last modified: November 7, 2018
This is version 199 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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