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P36551

- HEM6_HUMAN

UniProt

P36551 - HEM6_HUMAN

Protein

Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Gene

CPOX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.

    Catalytic activityi

    Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei244 – 2441SubstrateCurated
    Active sitei258 – 2581Proton donor1 Publication
    Sitei327 – 3271Important for dimerization

    GO - Molecular functioni

    1. coproporphyrinogen oxidase activity Source: Reactome
    2. protein homodimerization activity Source: UniProtKB
    3. structural constituent of eye lens Source: Ensembl

    GO - Biological processi

    1. heme biosynthetic process Source: Reactome
    2. porphyrin-containing compound metabolic process Source: Reactome
    3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    4. response to arsenic-containing substance Source: Ensembl
    5. response to insecticide Source: Ensembl
    6. response to iron ion Source: Ensembl
    7. response to lead ion Source: Ensembl
    8. response to methylmercury Source: Ensembl
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01369-MONOMER.
    BRENDAi1.3.3.3. 2681.
    ReactomeiREACT_9465. Heme biosynthesis.
    UniPathwayiUPA00251; UER00322.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial (EC:1.3.3.3)
    Short name:
    COX
    Short name:
    Coprogen oxidase
    Short name:
    Coproporphyrinogenase
    Gene namesi
    Name:CPOX
    Synonyms:CPO, CPX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:2321. CPOX.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial intermembrane space Source: Reactome
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Hereditary coproporphyria (HCP) [MIM:121300]: 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. Hereditary coproporphyria is an acute hepatic porphyria characterized by skin photosensitivity, attacks of abdominal pain, neurological disturbances, and psychiatric symptoms. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors. Hereditary coproporphyria is biochemically characterized by overexcretion of coproporphyrin III in the urine and in the feces.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1351V → A in HCP. 1 Publication
    VAR_023444
    Natural varianti162 – 1687Missing in HCP.
    VAR_002151
    Natural varianti189 – 1891G → S in HCP; <5% of activity. 1 Publication
    VAR_002152
    Natural varianti197 – 1971G → W in HCP. 1 Publication
    VAR_002153
    Natural varianti201 – 2011E → K in HCP. 1 Publication
    VAR_002154
    Natural varianti208 – 2081S → F in HCP. 1 Publication
    Corresponds to variant rs28929486 [ dbSNP | Ensembl ].
    VAR_019067
    Natural varianti214 – 2141L → R in HCP. 1 Publication
    VAR_023445
    Natural varianti249 – 2491P → R in HCP. 1 Publication
    VAR_023446
    Natural varianti249 – 2491P → S in HCP. 1 Publication
    VAR_002155
    Natural varianti279 – 2791G → R in HCP; a patient carrying also the L-12 mutation in ALAD. 1 Publication
    VAR_058005
    Natural varianti280 – 2801G → R in HCP. 1 Publication
    VAR_002157
    Natural varianti295 – 2951H → D in HCP. 1 Publication
    VAR_002159
    Natural varianti328 – 3281R → C in HCP. 1 Publication
    Corresponds to variant rs28929487 [ dbSNP | Ensembl ].
    VAR_019068
    Natural varianti331 – 3311R → W in HCP. 2 Publications
    VAR_002160
    Natural varianti390 – 3901Missing in HCP. 1 Publication
    VAR_002161
    Natural varianti404 – 4041K → E in HCP; harderoporphyria form. 1 Publication
    VAR_002162
    Natural varianti427 – 4271W → R in HCP. 1 Publication
    VAR_002163
    Natural varianti447 – 4471R → C in HCP. 1 Publication
    Corresponds to variant rs28931603 [ dbSNP | Ensembl ].
    VAR_019069

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi392 – 41827Missing: Loss for dimerization. 1 PublicationAdd
    BLAST

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi121300. phenotype.
    Orphaneti79273. Hereditary coproporphyria.
    PharmGKBiPA134979958.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 110110MitochondrionBy similarityAdd
    BLAST
    Chaini111 – 454344Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrialPRO_0000006029Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei404 – 4041N6-acetyllysine; alternateBy similarity
    Modified residuei404 – 4041N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP36551.
    PaxDbiP36551.
    PeptideAtlasiP36551.
    PRIDEiP36551.

    PTM databases

    PhosphoSiteiP36551.

    Expressioni

    Gene expression databases

    ArrayExpressiP36551.
    BgeeiP36551.
    CleanExiHS_CPO.
    HS_CPOX.
    GenevestigatoriP36551.

    Organism-specific databases

    HPAiHPA015736.
    HPA054448.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi107763. 7 interactions.
    IntActiP36551. 1 interaction.
    STRINGi9606.ENSP00000264193.

    Structurei

    Secondary structure

    1
    454
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi122 – 1287
    Beta strandi130 – 1323
    Helixi138 – 1436
    Helixi148 – 17023
    Beta strandi177 – 1837
    Turni184 – 1863
    Beta strandi187 – 19610
    Beta strandi198 – 21316
    Helixi216 – 2249
    Beta strandi237 – 25115
    Beta strandi256 – 26712
    Beta strandi273 – 28412
    Helixi290 – 30516
    Helixi311 – 32212
    Helixi326 – 3283
    Beta strandi330 – 34213
    Helixi347 – 35913
    Helixi361 – 37212
    Helixi379 – 39921
    Helixi406 – 4083
    Beta strandi409 – 4113
    Helixi414 – 4207
    Helixi438 – 44710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AEXX-ray1.58A111-454[»]
    ProteinModelPortaliP36551.
    SMRiP36551. Positions 119-454.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36551.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni193 – 20210Important for dimerizationCurated
    Regioni260 – 2623Substrate binding
    Regioni392 – 42837Important for dimerizationAdd
    BLAST
    Regioni411 – 4133Substrate binding

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0408.
    HOGENOMiHOG000262768.
    HOVERGENiHBG051897.
    InParanoidiP36551.
    KOiK00228.
    OMAiRYFETAN.
    PhylomeDBiP36551.
    TreeFamiTF300703.

    Family and domain databases

    Gene3Di3.40.1500.10. 1 hit.
    InterProiIPR001260. Coprogen_oxidase_aer.
    IPR018375. Coprogen_oxidase_CS.
    [Graphical view]
    PANTHERiPTHR10755. PTHR10755. 1 hit.
    PfamiPF01218. Coprogen_oxidas. 1 hit.
    [Graphical view]
    PRINTSiPR00073. COPRGNOXDASE.
    SUPFAMiSSF102886. SSF102886. 1 hit.
    PROSITEiPS01021. COPROGEN_OXIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P36551-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALQLGRLSS GPCWLVARGG CGGPRAWSQC GGGGLRAWSQ RSAAGRVCRP    50
    PGPAGTEQSR GLGHGSTSRG GPWVGTGLAA ALAGLVGLAT AAFGHVQRAE 100
    MLPKTSGTRA TSLGRPEEEE DELAHRCSSF MAPPVTDLGE LRRRPGDMKT 150
    KMELLILETQ AQVCQALAQV DGGANFSVDR WERKEGGGGI SCVLQDGCVF 200
    EKAGVSISVV HGNLSEEAAK QMRSRGKVLK TKDGKLPFCA MGVSSVIHPK 250
    NPHAPTIHFN YRYFEVEEAD GNKQWWFGGG CDLTPTYLNQ EDAVHFHRTL 300
    KEACDQHGPD LYPKFKKWCD DYFFIAHRGE RRGIGGIFFD DLDSPSKEEV 350
    FRFVQSCARA VVPSYIPLVK KHCDDSFTPQ EKLWQQLRRG RYVEFNLLYD 400
    RGTKFGLFTP GSRIESILMS LPLTARWEYM HSPSENSKEA EILEVLRHPR 450
    DWVR 454
    Length:454
    Mass (Da):50,152
    Last modified:June 7, 2005 - v3
    Checksum:i6EC3D15FD8FD86B5
    GO

    Sequence cautioni

    The sequence BAA04033.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti247 – 2471I → T in CAA82250. (PubMed:8159699)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1351V → A in HCP. 1 Publication
    VAR_023444
    Natural varianti162 – 1687Missing in HCP.
    VAR_002151
    Natural varianti189 – 1891G → S in HCP; <5% of activity. 1 Publication
    VAR_002152
    Natural varianti197 – 1971G → W in HCP. 1 Publication
    VAR_002153
    Natural varianti201 – 2011E → K in HCP. 1 Publication
    VAR_002154
    Natural varianti208 – 2081S → F in HCP. 1 Publication
    Corresponds to variant rs28929486 [ dbSNP | Ensembl ].
    VAR_019067
    Natural varianti214 – 2141L → R in HCP. 1 Publication
    VAR_023445
    Natural varianti249 – 2491P → R in HCP. 1 Publication
    VAR_023446
    Natural varianti249 – 2491P → S in HCP. 1 Publication
    VAR_002155
    Natural varianti272 – 2721N → H.2 Publications
    Corresponds to variant rs1131857 [ dbSNP | Ensembl ].
    VAR_002156
    Natural varianti279 – 2791G → R in HCP; a patient carrying also the L-12 mutation in ALAD. 1 Publication
    VAR_058005
    Natural varianti280 – 2801G → R in HCP. 1 Publication
    VAR_002157
    Natural varianti294 – 2941V → I.3 Publications
    Corresponds to variant rs2228056 [ dbSNP | Ensembl ].
    VAR_002158
    Natural varianti295 – 2951H → D in HCP. 1 Publication
    VAR_002159
    Natural varianti328 – 3281R → C in HCP. 1 Publication
    Corresponds to variant rs28929487 [ dbSNP | Ensembl ].
    VAR_019068
    Natural varianti331 – 3311R → W in HCP. 2 Publications
    VAR_002160
    Natural varianti352 – 3521R → C.
    Corresponds to variant rs11921054 [ dbSNP | Ensembl ].
    VAR_048827
    Natural varianti390 – 3901Missing in HCP. 1 Publication
    VAR_002161
    Natural varianti404 – 4041K → E in HCP; harderoporphyria form. 1 Publication
    VAR_002162
    Natural varianti427 – 4271W → R in HCP. 1 Publication
    VAR_002163
    Natural varianti447 – 4471R → C in HCP. 1 Publication
    Corresponds to variant rs28931603 [ dbSNP | Ensembl ].
    VAR_019069

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z34531
    , Z34803, Z34804, Z34805, Z34806, Z34807, Z34808 Genomic DNA. Translation: CAA84292.1.
    AK290140 mRNA. Translation: BAF82829.1.
    AK223481 mRNA. Translation: BAD97201.1.
    CH471052 Genomic DNA. Translation: EAW79854.1.
    BC017210 mRNA. Translation: AAH17210.1.
    BC023551 mRNA. Translation: AAH23551.1.
    BC023554 mRNA. Translation: AAH23554.1.
    D16611 mRNA. Translation: BAA04033.1. Different initiation.
    Z28409 mRNA. Translation: CAA82250.1.
    CCDSiCCDS2932.1.
    PIRiI52444.
    RefSeqiNP_000088.3. NM_000097.5.
    UniGeneiHs.476982.

    Genome annotation databases

    EnsembliENST00000264193; ENSP00000264193; ENSG00000080819.
    GeneIDi1371.
    KEGGihsa:1371.
    UCSCiuc003dsx.3. human.

    Polymorphism databases

    DMDMi67476671.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z34531
    , Z34803 , Z34804 , Z34805 , Z34806 , Z34807 , Z34808 Genomic DNA. Translation: CAA84292.1 .
    AK290140 mRNA. Translation: BAF82829.1 .
    AK223481 mRNA. Translation: BAD97201.1 .
    CH471052 Genomic DNA. Translation: EAW79854.1 .
    BC017210 mRNA. Translation: AAH17210.1 .
    BC023551 mRNA. Translation: AAH23551.1 .
    BC023554 mRNA. Translation: AAH23554.1 .
    D16611 mRNA. Translation: BAA04033.1 . Different initiation.
    Z28409 mRNA. Translation: CAA82250.1 .
    CCDSi CCDS2932.1.
    PIRi I52444.
    RefSeqi NP_000088.3. NM_000097.5.
    UniGenei Hs.476982.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AEX X-ray 1.58 A 111-454 [» ]
    ProteinModelPortali P36551.
    SMRi P36551. Positions 119-454.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107763. 7 interactions.
    IntActi P36551. 1 interaction.
    STRINGi 9606.ENSP00000264193.

    Chemistry

    ChEMBLi CHEMBL1681618.

    PTM databases

    PhosphoSitei P36551.

    Polymorphism databases

    DMDMi 67476671.

    Proteomic databases

    MaxQBi P36551.
    PaxDbi P36551.
    PeptideAtlasi P36551.
    PRIDEi P36551.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264193 ; ENSP00000264193 ; ENSG00000080819 .
    GeneIDi 1371.
    KEGGi hsa:1371.
    UCSCi uc003dsx.3. human.

    Organism-specific databases

    CTDi 1371.
    GeneCardsi GC03M098239.
    GeneReviewsi CPOX.
    HGNCi HGNC:2321. CPOX.
    HPAi HPA015736.
    HPA054448.
    MIMi 121300. phenotype.
    612732. gene.
    neXtProti NX_P36551.
    Orphaneti 79273. Hereditary coproporphyria.
    PharmGKBi PA134979958.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0408.
    HOGENOMi HOG000262768.
    HOVERGENi HBG051897.
    InParanoidi P36551.
    KOi K00228.
    OMAi RYFETAN.
    PhylomeDBi P36551.
    TreeFami TF300703.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00322 .
    BioCyci MetaCyc:HS01369-MONOMER.
    BRENDAi 1.3.3.3. 2681.
    Reactomei REACT_9465. Heme biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei P36551.
    GeneWikii Coproporphyrinogen_III_oxidase.
    GenomeRNAii 1371.
    NextBioi 5561.
    PROi P36551.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36551.
    Bgeei P36551.
    CleanExi HS_CPO.
    HS_CPOX.
    Genevestigatori P36551.

    Family and domain databases

    Gene3Di 3.40.1500.10. 1 hit.
    InterProi IPR001260. Coprogen_oxidase_aer.
    IPR018375. Coprogen_oxidase_CS.
    [Graphical view ]
    PANTHERi PTHR10755. PTHR10755. 1 hit.
    Pfami PF01218. Coprogen_oxidas. 1 hit.
    [Graphical view ]
    PRINTSi PR00073. COPRGNOXDASE.
    SUPFAMi SSF102886. SSF102886. 1 hit.
    PROSITEi PS01021. COPROGEN_OXIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping."
      Delfau-Larue M.H., Martasek P., Grandchamp B.
      Hum. Mol. Genet. 3:1325-1330(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    2. "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].
      Tissue: Thalamus.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-294.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANT ILE-294.
      Tissue: Brain, Placenta and Uterus.
    6. "Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase."
      Taketani S., Kohno H., Furukawa T., Yoshinaga T., Tokunaga R.
      Biochim. Biophys. Acta 1183:547-549(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-454.
      Tissue: Placenta.
    7. "Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase."
      Martasek P., Camadro J.-M., Delfau-Larue M.H., Dumas J.B., Montagne J.J., de Verneuil H., Labbe P., Grandchamp B.
      Proc. Natl. Acad. Sci. U.S.A. 91:3024-3028(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-454, VARIANT HIS-272.
      Tissue: Foreskin.
    8. "The long, but not the short, presequence of human coproporphyrinogen oxidase is essential for its import and sorting to mitochondria."
      Susa S., Daimon M., Ono H., Li S., Yoshida T., Kato T.
      Tohoku J. Exp. Med. 200:39-45(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 111-453 IN COMPLEX WITH CITRATE, MUTAGENESIS OF 392-TYR--LEU-418, ACTIVE SITE, SUBUNIT.
    11. "Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms."
      Martasek P., Nordmann Y., Grandchamp B.
      Hum. Mol. Genet. 3:477-480(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HCP TRP-331.
    12. "Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria."
      Fujita H., Kondo M., Taketani S., Nomura N., Furuyama K., Akagi R., Nagai T., Terajima M., Galbraith R.A., Sassa S.
      Hum. Mol. Genet. 3:1807-1810(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HCP SER-189, VARIANTS HIS-272 AND ILE-294.
    13. "A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria."
      Lamoril J., Martasek P., Deybach J.-C., da Silva V., Grandchamp B., Nordmann Y.
      Hum. Mol. Genet. 4:275-278(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HCP GLU-404.
    14. "A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria."
      Daimon M., Gojyou E., Sugawara M., Yamatani K., Tominaga M., Sasaki H.
      Hum. Genet. 99:199-201(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HCP ARG-280.
    15. "Three novel mutations in the coproporphyrinogen oxidase gene."
      Lamoril J., Deybach J.-C., Puy H., Grandchamp B., Nordmann Y.
      Hum. Mutat. 9:78-80(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HCP 162-GLN--ALA-168 DEL AND ASP-295.
    16. "Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene."
      Schreiber W.E., Zhang X., Senz J., Jamani A.
      Hum. Mutat. 10:196-200(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HCP LYS-201 AND SER-249.
    17. "Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update."
      Rosipal R., Lamoril J., Puy H., da Silva V., Gouya L., de Rooij F.W.M., Te Velde K., Nordmann Y., Martasek P., Deybach J.-C.
      Hum. Mutat. 13:44-53(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HCP TRP-197; GLY-390 DEL AND ARG-427.
    18. "Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria."
      Wiman A., Floderus Y., Harper P.
      J. Hum. Genet. 47:407-412(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HCP PHE-208; CYS-328; TRP-331 AND CYS-447.
    19. "Biochemical and genetic characterization of four cases of hereditary coproporphyria in Spain."
      To-Figueras J., Badenas C., Enriquez M.T., Segura S., Alvarez C., Mila M., Lecha M., Herrero C.
      Mol. Genet. Metab. 85:160-163(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HCP ALA-135; ARG-214 AND ARG-249.
    20. "Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient."
      Akagi R., Inoue R., Muranaka S., Tahara T., Taketani S., Anderson K.E., Phillips J.D., Sassa S.
      Br. J. Haematol. 132:237-243(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HCP ARG-279.
    21. Erratum
      Akagi R., Inoue R., Muranaka S., Tahara T., Taketani S., Anderson K.E., Phillips J.D., Sassa S.
      Br. J. Haematol. 132:662-662(2006)

    Entry informationi

    Entry nameiHEM6_HUMAN
    AccessioniPrimary (citable) accession number: P36551
    Secondary accession number(s): A8K275
    , Q14060, Q53F08, Q8IZ45, Q96AF3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 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 3
      Human chromosome 3: 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