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P06132

- DCUP_HUMAN

UniProt

P06132 - DCUP_HUMAN

Protein

Uroporphyrinogen decarboxylase

Gene

UROD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 174 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.

    Catalytic activityi

    Uroporphyrinogen III = coproporphyrinogen + 4 CO2.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei55 – 551Substrate
    Binding sitei85 – 851Substrate
    Binding sitei86 – 861Substrate
    Sitei86 – 861Transition state stabilizer
    Binding sitei164 – 1641Substrate
    Binding sitei219 – 2191Substrate
    Binding sitei339 – 3391Substrate

    GO - Molecular functioni

    1. uroporphyrinogen decarboxylase activity Source: UniProtKB

    GO - Biological processi

    1. heme biosynthetic process Source: UniProtKB
    2. porphyrin-containing compound metabolic process Source: Reactome
    3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04993-MONOMER.
    BRENDAi4.1.1.37. 2681.
    ReactomeiREACT_9465. Heme biosynthesis.
    UniPathwayiUPA00251; UER00321.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Uroporphyrinogen decarboxylase (EC:4.1.1.37)
    Short name:
    UPD
    Short name:
    URO-D
    Gene namesi
    Name:UROD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12591. UROD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Familial porphyria cutanea tarda (FPCT) [MIM:176100]: 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. Familial porphyria cutanea tarda is an autosomal dominant disorder characterized by light-sensitive dermatitis, with onset in later life. It is associated with the excretion of large amounts of uroporphyrin in the urine. Iron overload is often present in association with varying degrees of liver damage.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251G → E in FPCT; insoluble protein. 1 Publication
    VAR_022567
    Natural varianti80 – 801A → S in FPCT; decrease of activity. 2 Publications
    VAR_022569
    Natural varianti134 – 1341V → Q in FPCT and HEP; requires 2 nucleotide substitutions; nearly normal activity. 4 Publications
    VAR_009104
    Natural varianti142 – 1421R → Q in FPCT. 1 Publication
    VAR_010985
    Natural varianti144 – 1441R → P in FPCT; decrease of activity. 1 Publication
    VAR_022570
    Natural varianti156 – 1561G → D in FPCT; decrease of activity. 1 Publication
    VAR_022571
    Natural varianti161 – 1611L → Q in FPCT. 1 Publication
    VAR_010986
    Natural varianti165 – 1651M → R in FPCT; activity < 2%. 2 Publications
    VAR_007911
    Natural varianti167 – 1671E → K in HEP and FPCT; nearly normal activity. 2 Publications
    VAR_007714
    Natural varianti193 – 1931R → P in FPCT; insoluble protein. 1 Publication
    VAR_022572
    Natural varianti195 – 1951L → F in FPCT. 1 Publication
    VAR_007912
    Natural varianti216 – 2161L → Q in FPCT. 1 Publication
    VAR_022573
    Natural varianti218 – 2181E → K in FPCT; significant decrease of activity. 1 Publication
    VAR_022574
    Natural varianti219 – 2191S → F in FPCT. 1 Publication
    VAR_010987
    Natural varianti229 – 2291F → L in FPCT. 1 Publication
    VAR_009106
    Natural varianti232 – 2321F → L in FPCT; decrease of activity. 1 Publication
    VAR_022575
    Natural varianti235 – 2351P → S in FPCT. 1 Publication
    VAR_010988
    Natural varianti253 – 2531L → Q in FPCT; decrease of activity. 2 Publications
    Corresponds to variant rs36033115 [ dbSNP | Ensembl ].
    VAR_007913
    Natural varianti260 – 2601I → T in FPCT; decrease of activity. 1 Publication
    VAR_022576
    Natural varianti281 – 2811G → V in FPCT. 2 Publications
    VAR_007716
    Natural varianti282 – 2821L → R in FPCT. 1 Publication
    VAR_022577
    Natural varianti303 – 3031G → S in FPCT. 1 Publication
    VAR_022578
    Natural varianti304 – 3041N → K in FPCT. 1 Publication
    VAR_007914
    Natural varianti318 – 3181G → R in FPCT. 2 Publications
    Corresponds to variant rs116233118 [ dbSNP | Ensembl ].
    VAR_007915
    Natural varianti324 – 3241M → T in FPCT. 1 Publication
    VAR_009108
    Natural varianti332 – 3321R → H in FPCT. 1 Publication
    VAR_007916
    Natural varianti334 – 3341I → T in FPCT. 1 Publication
    VAR_007917
    Hepatoerythropoietic porphyria (HEP) [MIM:176100]: 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. HEP is a cutaneous porphyria that presents in infancy. It is characterized biochemically by excessive excretion of acetate-substituted porphyrins and accumulation of protoporphyrin in erythrocytes. Uroporphyrinogen decarboxylase levels are very low in erythrocytes and cultured skin fibroblasts.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461F → L in HEP; mild phenotype; strong decrease of activity. 2 Publications
    VAR_022568
    Natural varianti62 – 621P → L in HEP. 1 Publication
    VAR_009103
    Natural varianti80 – 801A → G in HEP. 1 Publication
    VAR_007910
    Natural varianti134 – 1341V → Q in FPCT and HEP; requires 2 nucleotide substitutions; nearly normal activity. 4 Publications
    VAR_009104
    Natural varianti167 – 1671E → K in HEP and FPCT; nearly normal activity. 2 Publications
    VAR_007714
    Natural varianti168 – 1681G → R in HEP; relative activity of 65% of wild-type towards uroporphyrinogen III. 1 Publication
    VAR_065558
    Natural varianti170 – 1701G → D in HEP; relative activity of 17% and 60% of wild-type towards uroporphyrinogen I and III respectively. 1 Publication
    VAR_065559
    Natural varianti220 – 2201H → P in HEP; mild form. 1 Publication
    VAR_009105
    Natural varianti281 – 2811G → E in FPTC and HEP. 3 Publications
    VAR_007715
    Natural varianti292 – 2921R → G in HEP. 1 Publication
    VAR_007717
    Natural varianti311 – 3111Y → C in HEP. 1 Publication
    VAR_009107

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861D → E: 5-10% of wild-type activity. 1 Publication
    Mutagenesisi86 – 861D → G: Very low activity. Binds substrate with similar geometry as wild-type. 1 Publication
    Mutagenesisi86 – 861D → N: No activity. Unable to bind substrate. 1 Publication
    Mutagenesisi164 – 1641Y → F: 25-30% of wild-type activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi176100. phenotype.
    Orphaneti95159. Hepatoerythropoietic porphyria.
    101330. Porphyria cutanea tarda.
    PharmGKBiPA37221.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 367367Uroporphyrinogen decarboxylasePRO_0000187569Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP06132.
    PaxDbiP06132.
    PeptideAtlasiP06132.
    PRIDEiP06132.

    2D gel databases

    OGPiP06132.

    PTM databases

    PhosphoSiteiP06132.

    Expressioni

    Gene expression databases

    ArrayExpressiP06132.
    BgeeiP06132.
    CleanExiHS_UROD.
    GenevestigatoriP06132.

    Organism-specific databases

    HPAiHPA027468.
    HPA028668.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi113235. 11 interactions.
    IntActiP06132. 6 interactions.
    MINTiMINT-3005024.
    STRINGi9606.ENSP00000246337.

    Structurei

    Secondary structure

    1
    367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 247
    Beta strandi38 – 403
    Helixi44 – 518
    Helixi55 – 595
    Helixi62 – 7514
    Helixi89 – 935
    Beta strandi99 – 1013
    Turni102 – 1043
    Beta strandi105 – 1073
    Helixi115 – 1206
    Helixi124 – 1263
    Helixi127 – 1304
    Helixi132 – 14514
    Beta strandi151 – 1566
    Helixi158 – 16710
    Helixi175 – 1839
    Helixi185 – 20824
    Beta strandi212 – 2187
    Helixi221 – 2233
    Helixi226 – 2327
    Helixi234 – 25017
    Beta strandi258 – 2625
    Helixi266 – 2683
    Helixi269 – 2724
    Turni273 – 2764
    Beta strandi278 – 2814
    Helixi288 – 2958
    Beta strandi297 – 3059
    Helixi307 – 3115
    Helixi314 – 32815
    Beta strandi330 – 33910
    Helixi347 – 36519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JPHX-ray2.10A1-367[»]
    1JPIX-ray2.30A1-367[»]
    1JPKX-ray2.20A1-367[»]
    1R3QX-ray1.70A1-367[»]
    1R3RX-ray1.85A1-367[»]
    1R3SX-ray1.65A1-367[»]
    1R3TX-ray1.70A1-367[»]
    1R3VX-ray1.90A1-367[»]
    1R3WX-ray1.70A1-367[»]
    1R3YX-ray1.75A1-367[»]
    1UROX-ray1.80A1-367[»]
    2Q6ZX-ray2.00A11-366[»]
    2Q71X-ray1.90A11-366[»]
    3GVQX-ray2.10A1-367[»]
    3GVRX-ray2.20A1-367[»]
    3GVVX-ray2.80A1-367[»]
    3GVWX-ray2.80A1-367[»]
    3GW0X-ray2.00A1-367[»]
    3GW3X-ray1.70A1-367[»]
    DisProtiDP00308.
    ProteinModelPortaliP06132.
    SMRiP06132. Positions 10-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06132.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 415Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0407.
    HOVERGENiHBG000229.
    InParanoidiP06132.
    KOiK01599.
    OMAiLFAYMVE.
    PhylomeDBiP06132.
    TreeFamiTF300744.

    Family and domain databases

    HAMAPiMF_00218. URO_D.
    InterProiIPR006361. Uroporphyrinogen_deCO2ase_HemE.
    IPR000257. Uroporphyrinogen_deCOase.
    [Graphical view]
    PfamiPF01208. URO-D. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01464. hemE. 1 hit.
    PROSITEiPS00906. UROD_1. 1 hit.
    PS00907. UROD_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06132-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR    50
    AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM 100
    VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP 150
    LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV 200
    PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE 250
    AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT 300
    LQGNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV 350
    GAFVDAVHKH SRLLRQN 367
    Length:367
    Mass (Da):40,787
    Last modified:November 1, 1997 - v2
    Checksum:i840510B36CFC3856
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031G → S in AAA61258. (PubMed:3015909)Curated
    Sequence conflicti103 – 1031G → S in AAB59456. (PubMed:2243121)Curated
    Sequence conflicti120 – 1201R → A in AAA61258. (PubMed:3015909)Curated
    Sequence conflicti120 – 1201R → A in AAB59456. (PubMed:2243121)Curated
    Sequence conflicti212 – 2143Missing in AAB59456. (PubMed:2243121)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151K → E.
    Corresponds to variant rs11541959 [ dbSNP | Ensembl ].
    VAR_060683
    Natural varianti25 – 251G → E in FPCT; insoluble protein. 1 Publication
    VAR_022567
    Natural varianti46 – 461F → L in HEP; mild phenotype; strong decrease of activity. 2 Publications
    VAR_022568
    Natural varianti62 – 621P → L in HEP. 1 Publication
    VAR_009103
    Natural varianti77 – 771P → L.3 Publications
    Corresponds to variant rs1131147 [ dbSNP | Ensembl ].
    VAR_067457
    Natural varianti80 – 801A → G in HEP. 1 Publication
    VAR_007910
    Natural varianti80 – 801A → S in FPCT; decrease of activity. 2 Publications
    VAR_022569
    Natural varianti106 – 1061P → L.
    Corresponds to variant rs11541962 [ dbSNP | Ensembl ].
    VAR_060684
    Natural varianti113 – 1131R → T.
    Corresponds to variant rs11541963 [ dbSNP | Ensembl ].
    VAR_060685
    Natural varianti134 – 1341V → Q in FPCT and HEP; requires 2 nucleotide substitutions; nearly normal activity. 4 Publications
    VAR_009104
    Natural varianti142 – 1421R → Q in FPCT. 1 Publication
    VAR_010985
    Natural varianti144 – 1441R → P in FPCT; decrease of activity. 1 Publication
    VAR_022570
    Natural varianti156 – 1561G → D in FPCT; decrease of activity. 1 Publication
    VAR_022571
    Natural varianti161 – 1611L → Q in FPCT. 1 Publication
    VAR_010986
    Natural varianti165 – 1651M → R in FPCT; activity < 2%. 2 Publications
    VAR_007911
    Natural varianti167 – 1671E → K in HEP and FPCT; nearly normal activity. 2 Publications
    VAR_007714
    Natural varianti168 – 1681G → R in HEP; relative activity of 65% of wild-type towards uroporphyrinogen III. 1 Publication
    VAR_065558
    Natural varianti170 – 1701G → D in HEP; relative activity of 17% and 60% of wild-type towards uroporphyrinogen I and III respectively. 1 Publication
    VAR_065559
    Natural varianti193 – 1931R → P in FPCT; insoluble protein. 1 Publication
    VAR_022572
    Natural varianti195 – 1951L → F in FPCT. 1 Publication
    VAR_007912
    Natural varianti216 – 2161L → Q in FPCT. 1 Publication
    VAR_022573
    Natural varianti218 – 2181E → K in FPCT; significant decrease of activity. 1 Publication
    VAR_022574
    Natural varianti219 – 2191S → F in FPCT. 1 Publication
    VAR_010987
    Natural varianti220 – 2201H → P in HEP; mild form. 1 Publication
    VAR_009105
    Natural varianti229 – 2291F → L in FPCT. 1 Publication
    VAR_009106
    Natural varianti232 – 2321F → L in FPCT; decrease of activity. 1 Publication
    VAR_022575
    Natural varianti235 – 2351P → S in FPCT. 1 Publication
    VAR_010988
    Natural varianti253 – 2531L → Q in FPCT; decrease of activity. 2 Publications
    Corresponds to variant rs36033115 [ dbSNP | Ensembl ].
    VAR_007913
    Natural varianti260 – 2601I → T in FPCT; decrease of activity. 1 Publication
    VAR_022576
    Natural varianti281 – 2811G → E in FPTC and HEP. 3 Publications
    VAR_007715
    Natural varianti281 – 2811G → V in FPCT. 2 Publications
    VAR_007716
    Natural varianti282 – 2821L → R in FPCT. 1 Publication
    VAR_022577
    Natural varianti292 – 2921R → G in HEP. 1 Publication
    VAR_007717
    Natural varianti303 – 3031G → S in FPCT. 1 Publication
    VAR_022578
    Natural varianti303 – 3031G → V.2 Publications
    Corresponds to variant rs17849533 [ dbSNP | Ensembl ].
    VAR_060686
    Natural varianti304 – 3041N → K in FPCT. 1 Publication
    VAR_007914
    Natural varianti311 – 3111Y → C in HEP. 1 Publication
    VAR_009107
    Natural varianti318 – 3181G → R in FPCT. 2 Publications
    Corresponds to variant rs116233118 [ dbSNP | Ensembl ].
    VAR_007915
    Natural varianti324 – 3241M → T in FPCT. 1 Publication
    VAR_009108
    Natural varianti332 – 3321R → H in FPCT. 1 Publication
    VAR_007916
    Natural varianti334 – 3341I → T in FPCT. 1 Publication
    VAR_007917

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14016 mRNA. Translation: AAA61258.1.
    X89267 Genomic DNA. Translation: CAA61540.1.
    AF047383 Genomic DNA. Translation: AAC03563.1.
    AF104421 mRNA. Translation: AAD04571.1.
    AF104422 mRNA. Translation: AAD04572.1.
    AF104423 mRNA. Translation: AAD04573.1.
    AF104424 mRNA. Translation: AAD04574.1.
    AF104425 mRNA. Translation: AAD04575.1.
    AF104426 mRNA. Translation: AAD04576.1.
    AF104427 mRNA. Translation: AAD04577.1.
    AF104428 mRNA. Translation: AAD04578.1.
    AF104429 mRNA. Translation: AAD04579.1.
    AF104430 mRNA. Translation: AAD04580.1.
    AF104431 mRNA. Translation: AAD04581.1.
    AF104432 mRNA. Translation: AAD04582.1.
    AF104433 mRNA. Translation: AAD04583.1.
    AF104434 mRNA. Translation: AAD04584.1.
    AF104435 mRNA. Translation: AAD04585.1.
    AF104436 mRNA. Translation: AAD04586.1.
    AF104437 mRNA. Translation: AAD04587.1.
    AF104438 mRNA. Translation: AAD04588.1.
    AF104439 mRNA. Translation: AAD04589.1.
    AF104440 mRNA. Translation: AAD04590.1.
    AY292986 Genomic DNA. Translation: AAP44118.1.
    BT006737 mRNA. Translation: AAP35383.1.
    CR456976 mRNA. Translation: CAG33257.1.
    CR542057 mRNA. Translation: CAG46854.1.
    AK291877 mRNA. Translation: BAF84566.1.
    AL359473 Genomic DNA. Translation: CAI16440.1.
    CH471059 Genomic DNA. Translation: EAX07007.1.
    BC001778 mRNA. Translation: AAH01778.1.
    U30787 Genomic DNA. Translation: AAC50482.1.
    M60891 Genomic DNA. Translation: AAB59456.1.
    CCDSiCCDS518.1.
    PIRiA24411.
    G02786.
    RefSeqiNP_000365.3. NM_000374.4.
    UniGeneiHs.78601.

    Genome annotation databases

    EnsembliENST00000246337; ENSP00000246337; ENSG00000126088.
    GeneIDi7389.
    KEGGihsa:7389.
    UCSCiuc001cna.2. human.

    Polymorphism databases

    DMDMi2507533.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Uroporphyrinogen III decarboxylase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14016 mRNA. Translation: AAA61258.1 .
    X89267 Genomic DNA. Translation: CAA61540.1 .
    AF047383 Genomic DNA. Translation: AAC03563.1 .
    AF104421 mRNA. Translation: AAD04571.1 .
    AF104422 mRNA. Translation: AAD04572.1 .
    AF104423 mRNA. Translation: AAD04573.1 .
    AF104424 mRNA. Translation: AAD04574.1 .
    AF104425 mRNA. Translation: AAD04575.1 .
    AF104426 mRNA. Translation: AAD04576.1 .
    AF104427 mRNA. Translation: AAD04577.1 .
    AF104428 mRNA. Translation: AAD04578.1 .
    AF104429 mRNA. Translation: AAD04579.1 .
    AF104430 mRNA. Translation: AAD04580.1 .
    AF104431 mRNA. Translation: AAD04581.1 .
    AF104432 mRNA. Translation: AAD04582.1 .
    AF104433 mRNA. Translation: AAD04583.1 .
    AF104434 mRNA. Translation: AAD04584.1 .
    AF104435 mRNA. Translation: AAD04585.1 .
    AF104436 mRNA. Translation: AAD04586.1 .
    AF104437 mRNA. Translation: AAD04587.1 .
    AF104438 mRNA. Translation: AAD04588.1 .
    AF104439 mRNA. Translation: AAD04589.1 .
    AF104440 mRNA. Translation: AAD04590.1 .
    AY292986 Genomic DNA. Translation: AAP44118.1 .
    BT006737 mRNA. Translation: AAP35383.1 .
    CR456976 mRNA. Translation: CAG33257.1 .
    CR542057 mRNA. Translation: CAG46854.1 .
    AK291877 mRNA. Translation: BAF84566.1 .
    AL359473 Genomic DNA. Translation: CAI16440.1 .
    CH471059 Genomic DNA. Translation: EAX07007.1 .
    BC001778 mRNA. Translation: AAH01778.1 .
    U30787 Genomic DNA. Translation: AAC50482.1 .
    M60891 Genomic DNA. Translation: AAB59456.1 .
    CCDSi CCDS518.1.
    PIRi A24411.
    G02786.
    RefSeqi NP_000365.3. NM_000374.4.
    UniGenei Hs.78601.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JPH X-ray 2.10 A 1-367 [» ]
    1JPI X-ray 2.30 A 1-367 [» ]
    1JPK X-ray 2.20 A 1-367 [» ]
    1R3Q X-ray 1.70 A 1-367 [» ]
    1R3R X-ray 1.85 A 1-367 [» ]
    1R3S X-ray 1.65 A 1-367 [» ]
    1R3T X-ray 1.70 A 1-367 [» ]
    1R3V X-ray 1.90 A 1-367 [» ]
    1R3W X-ray 1.70 A 1-367 [» ]
    1R3Y X-ray 1.75 A 1-367 [» ]
    1URO X-ray 1.80 A 1-367 [» ]
    2Q6Z X-ray 2.00 A 11-366 [» ]
    2Q71 X-ray 1.90 A 11-366 [» ]
    3GVQ X-ray 2.10 A 1-367 [» ]
    3GVR X-ray 2.20 A 1-367 [» ]
    3GVV X-ray 2.80 A 1-367 [» ]
    3GVW X-ray 2.80 A 1-367 [» ]
    3GW0 X-ray 2.00 A 1-367 [» ]
    3GW3 X-ray 1.70 A 1-367 [» ]
    DisProti DP00308.
    ProteinModelPortali P06132.
    SMRi P06132. Positions 10-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113235. 11 interactions.
    IntActi P06132. 6 interactions.
    MINTi MINT-3005024.
    STRINGi 9606.ENSP00000246337.

    Chemistry

    ChEMBLi CHEMBL1681619.

    PTM databases

    PhosphoSitei P06132.

    Polymorphism databases

    DMDMi 2507533.

    2D gel databases

    OGPi P06132.

    Proteomic databases

    MaxQBi P06132.
    PaxDbi P06132.
    PeptideAtlasi P06132.
    PRIDEi P06132.

    Protocols and materials databases

    DNASUi 7389.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000246337 ; ENSP00000246337 ; ENSG00000126088 .
    GeneIDi 7389.
    KEGGi hsa:7389.
    UCSCi uc001cna.2. human.

    Organism-specific databases

    CTDi 7389.
    GeneCardsi GC01P045477.
    GeneReviewsi UROD.
    HGNCi HGNC:12591. UROD.
    HPAi HPA027468.
    HPA028668.
    MIMi 176100. phenotype.
    613521. gene.
    neXtProti NX_P06132.
    Orphaneti 95159. Hepatoerythropoietic porphyria.
    101330. Porphyria cutanea tarda.
    PharmGKBi PA37221.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0407.
    HOVERGENi HBG000229.
    InParanoidi P06132.
    KOi K01599.
    OMAi LFAYMVE.
    PhylomeDBi P06132.
    TreeFami TF300744.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00321 .
    BioCyci MetaCyc:HS04993-MONOMER.
    BRENDAi 4.1.1.37. 2681.
    Reactomei REACT_9465. Heme biosynthesis.

    Miscellaneous databases

    ChiTaRSi UROD. human.
    EvolutionaryTracei P06132.
    GeneWikii Uroporphyrinogen_III_decarboxylase.
    GenomeRNAii 7389.
    NextBioi 28930.
    PROi P06132.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06132.
    Bgeei P06132.
    CleanExi HS_UROD.
    Genevestigatori P06132.

    Family and domain databases

    HAMAPi MF_00218. URO_D.
    InterProi IPR006361. Uroporphyrinogen_deCO2ase_HemE.
    IPR000257. Uroporphyrinogen_deCOase.
    [Graphical view ]
    Pfami PF01208. URO-D. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01464. hemE. 1 hit.
    PROSITEi PS00906. UROD_1. 1 hit.
    PS00907. UROD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of a complete human uroporphyrinogen decarboxylase cDNA."
      Romeo P.-H., Raich N., Dubart A., Beaupain D., Pryor M., Kushner J.P., Cohen-Solal M., Goossens M.
      J. Biol. Chem. 261:9825-9831(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21; 37-65; 101-123; 175-251; 259-322; 325-344 AND 346-367.
    2. "Uroporphyrinogen decarboxylase: complete human gene sequence and molecular study of three families with hepatoerythropoietic porphyria."
      Moran-Jimenez M.J., Ged C., Romana M., de Salamanca R.E., Taieb A., Topi G., D'Alessandro L., de Verneuil H.
      Am. J. Hum. Genet. 58:712-721(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HEP LEU-62; LEU-77; GLU-281 AND CYS-311.
    3. Mendez M.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Uroporphyrinogen decarboxylase (UROD) cDNA sequence from Italian population."
      Martinez di Montemuros F., Fiorelli G., Cappellini M.D.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-77.
    5. "Molecular characterization of UROD gene in Italian patients with familial porphyria cutanea tarda (f-PCT)."
      Martinez di Montemuros F., Cappellini M.D.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-77.
    6. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-303.
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. "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: Skeletal muscle.
    10. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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 VAL-303.
      Tissue: Lymph.
    13. "Structure of the gene for human uroporphyrinogen decarboxylase."
      Romana M., Dubart A., Beaupain D., Chabret C., Goossens M., Romeo P.-H.
      Nucleic Acids Res. 15:7343-7356(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
    14. "Uroporphyrinogen decarboxylase: a splice site mutation causes the deletion of exon 6 in multiple families with porphyria cutanea tarda."
      Garey J.R., Harrison L.M., Franklin K.F., Metcalf K.M., Radisky E.S., Kushner J.P.
      J. Clin. Invest. 86:1416-1422(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-258, INVOLVEMENT IN FPCT.
    15. "Characterization and crystallization of human uroporphyrinogen decarboxylase."
      Phillips J.D., Whitby F.G., Kushner J.P., Hill C.P.
      Protein Sci. 6:1343-1346(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Crystal structure of human uroporphyrinogen decarboxylase."
      Whitby F.G., Phillips J.D., Kushner J.P., Hill C.P.
      EMBO J. 17:2463-2471(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT.
    21. "Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase."
      Phillips J.D., Parker T.L., Schubert H.L., Whitby F.G., Hill C.P., Kushner J.P.
      Blood 98:3179-3185(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANTS FPCT ASP-156; LEU-232 AND THR-260, VARIANTS FPCT GLU-25; SER-80; GLN-134; ASP-156; ARG-165; LYS-167; PRO-193; LEU-232; GLN-253 AND THR-260, CHARACTERIZATION OF VARIANTS FPCT GLU-25; SER-80; GLN-134; ASP-156; ARG-165; LYS-167; PRO-193; LEU-232; GLN-253 AND THR-260.
    22. "Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase."
      Phillips J.D., Whitby F.G., Kushner J.P., Hill C.P.
      EMBO J. 22:6225-6233(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF WILD-TYPE AND MUTANTS ASN-86; GLU-86; GLY-86 AND PHE-164 IN COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF ASP-86 AND TYR-164, REACTION MECHANISM.
    23. "Uroporphyrinogen decarboxylase structural mutant (Gly-281-->Glu) in a case of porphyria."
      de Verneuil H., Grandchamp B., Beaumont C., Picat C., Nordmann Y.
      Science 234:732-734(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEP GLU-281.
    24. "A point mutation in the coding region of uroporphyrinogen decarboxylase associated with familial porphyria cutanea tarda."
      Garey J.R., Hansen J.L., Harrison L.M., Kennedy J.B., Kushner J.P.
      Blood 73:892-895(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FPCT VAL-281.
    25. "Identification of a new mutation responsible for hepatoerythropoietic porphyria."
      Romana M., Grandchamp B., Dubart A., Amselem S., Chabret C., Nordmann Y., Goossens M., Romeo P.-H.
      Eur. J. Clin. Invest. 21:225-229(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEP LYS-167.
    26. "Characterization of a new mutation (R292G) and a deletion at the human uroporphyrinogen decarboxylase locus in two patients with hepatoerythropoietic porphyria."
      de Verneuil H., Bourgeois F., de Rooij F.W.M., Siersema P.D., Wilson J.H.P., Grandchamp B., Nordmann Y.
      Hum. Genet. 89:548-552(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEP GLY-292.
    27. "Molecular defects of uroporphyrinogen decarboxylase in a patient with mild hepatoerythropoietic porphyria."
      Meguro K., Fujita H., Ishida N., Akagi R., Kurihara T., Galbraith R.A., Kappas A., Zabriskie J.B., Toback A.C., Harber L.C., Sassa S.
      J. Invest. Dermatol. 102:681-685(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HEP GLN-134 AND PRO-220.
    28. "A mutation 'G281E' of the human uroporphyrinogen decarboxylase gene causes both hepatoerythropoietic porphyria and overt familial porphyria cutanea tarda: biochemical and genetic studies on Spanish patients."
      Roberts A.G., Elder G.H., de Salamanca R.E., Herrero C., Lecha M., Mascaro J.M.
      J. Invest. Dermatol. 104:500-502(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FPCT/HEP GLU-281.
    29. "Five new mutations in the uroporphyrinogen decarboxylase gene identified in families with cutaneous porphyria."
      McManus J.F., Begley C.G., Sassa S., Ratnaike S.
      Blood 88:3589-3600(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEP GLY-80, VARIANTS FPCT GLN-253; ARG-318 AND THR-334.
    30. "Familial porphyria cutanea tarda: characterization of seven novel uroporphyrinogen decarboxylase mutations and frequency of common hemochromatosis alleles."
      Mendez M., Sorkin L., Rossetti M.V., Astrin K.H., Batlle A.M.C., Parera V.E., Aizencang G.I., Desnick R.J.
      Am. J. Hum. Genet. 63:1363-1375(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FPCT ARG-165; PHE-195; LYS-304 AND HIS-332.
    31. "Three new mutations in the uroporphyrinogen decarboxylase gene in familial porphyria cutanea tarda."
      McManus J.F., Begley C.G., Sassa S., Ratnaike S.
      Hum. Mutat. 13:412-412(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FPCT GLN-134.
    32. "Screening for mutations in the uroporphyrinogen decarboxylase gene using denaturing gradient gel electrophoresis. Identification and characterization of six novel mutations associated with familial PCT."
      Christiansen L., Ged C., Hombrados I., Broens-Poulsen J., Fontanellas A., de Verneuil H., Hoerder M., Petersen N.E.
      Hum. Mutat. 14:222-232(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FPCT LEU-229 AND THR-324.
    33. "Co-inheritance of mutations in the uroporphyrinogen decarboxylase and hemochromatosis genes accelerates the onset of porphyria cutanea tarda."
      Brady J.J., Jackson H.A., Roberts A.G., Morgan R.R., Whatley S.D., Rowlands G.L., Darby C., Shudell E., Watson R., Paiker J., Worwood M.W., Elder G.H.
      J. Invest. Dermatol. 115:868-874(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FPCT SER-80; GLN-134; PRO-144; GLN-216; LYS-218; VAL-281; ARG-282; SER-303 AND ARG-318, CHARACTERIZATION OF VARIANTS FPCT PRO-144 AND LYS-218.
    34. "Seven novel point mutations in the uroporphyrinogen decarboxylase (UROD) gene in patients with familial porphyria cutanea tarda (f-PCT)."
      Cappellini M.D., Martinez Di Montemuros F., Tavazzi D., Fargion S., Pizzuti A., Comino A., Cainelli T., Fiorelli G.
      Hum. Mutat. 17:350-350(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FPCT GLN-142; GLN-161; PHE-219 AND SER-235.
    35. "Description of a new mutation in hepatoerythropoietic porphyria and prenatal exclusion of a homozygous fetus."
      Ged C., Ozalla D., Herrero C., Lecha M., Mendez M., de Verneuil H., Mascaro J.M.
      Arch. Dermatol. 138:957-960(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEP LEU-46, CHARACTERIZATION OF VARIANT HEP LEU-46.
    36. "Hepatoerythropoietic porphyria: a missense mutation in the UROD gene is associated with mild disease and an unusual porphyrin excretion pattern."
      Armstrong D.K.B., Sharpe P.C., Chambers C.R., Whatley S.D., Roberts A.G., Elder G.H.
      Br. J. Dermatol. 151:920-923(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEP LEU-46.
    37. "Two novel uroporphyrinogen decarboxylase (URO-D) mutations causing hepatoerythropoietic porphyria (HEP)."
      Phillips J.D., Whitby F.G., Stadtmueller B.M., Edwards C.Q., Hill C.P., Kushner J.P.
      Transl. Res. 149:85-91(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEP ARG-168, CHARACTERIZATION OF VARIANT HEP ARG-168.
    38. "Hepatoerythropoietic porphyria due to a novel mutation in the uroporphyrinogen decarboxylase gene."
      To-Figueras J., Phillips J., Gonzalez-Lopez J.M., Badenas C., Madrigal I., Gonzalez-Romaris E.M., Ramos C., Aguirre J.M., Herrero C.
      Br. J. Dermatol. 165:499-505(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEP ASP-170, CHARACTERIZATION OF VARIANT HEP ASP-170.

    Entry informationi

    Entry nameiDCUP_HUMAN
    AccessioniPrimary (citable) accession number: P06132
    Secondary accession number(s): A8K762
    , Q16863, Q16883, Q53YB8, Q53ZP6, Q6IB28, Q9BUZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 174 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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