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P06132 (DCUP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 172. Feed History...

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

Names and origin

Protein namesRecommended name:
Uroporphyrinogen decarboxylase

Short name=UPD
Short name=URO-D
EC=4.1.1.37
Gene names
Name:UROD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. HAMAP-Rule MF_00218

Catalytic activity

Uroporphyrinogen III = coproporphyrinogen + 4 CO2. HAMAP-Rule MF_00218

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. HAMAP-Rule MF_00218

Subunit structure

Homodimer. Ref.15 Ref.20

Subcellular location

Cytoplasm HAMAP-Rule MF_00218.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.21 Ref.24 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.23 Ref.25 Ref.26 Ref.27 Ref.29 Ref.35 Ref.36 Ref.37 Ref.38

Sequence similarities

Belongs to the uroporphyrinogen decarboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Uroporphyrinogen decarboxylase HAMAP-Rule MF_00218
PRO_0000187569

Regions

Region37 – 415Substrate binding HAMAP-Rule MF_00218

Sites

Binding site551Substrate
Binding site851Substrate
Binding site861Substrate
Binding site1641Substrate
Binding site2191Substrate
Binding site3391Substrate
Site861Transition state stabilizer

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16 Ref.18 Ref.19

Natural variations

Natural variant151K → E.
Corresponds to variant rs11541959 [ dbSNP | Ensembl ].
VAR_060683
Natural variant251G → E in FPCT; insoluble protein. Ref.21
VAR_022567
Natural variant461F → L in HEP; mild phenotype; strong decrease of activity. Ref.35 Ref.36
VAR_022568
Natural variant621P → L in HEP. Ref.2
VAR_009103
Natural variant771P → L. Ref.2 Ref.4 Ref.5
Corresponds to variant rs1131147 [ dbSNP | Ensembl ].
VAR_067457
Natural variant801A → G in HEP. Ref.29
VAR_007910
Natural variant801A → S in FPCT; decrease of activity. Ref.21 Ref.33
VAR_022569
Natural variant1061P → L.
Corresponds to variant rs11541962 [ dbSNP | Ensembl ].
VAR_060684
Natural variant1131R → T.
Corresponds to variant rs11541963 [ dbSNP | Ensembl ].
VAR_060685
Natural variant1341V → Q in FPCT and HEP; requires 2 nucleotide substitutions; nearly normal activity. Ref.21 Ref.27 Ref.31 Ref.33
VAR_009104
Natural variant1421R → Q in FPCT. Ref.34
VAR_010985
Natural variant1441R → P in FPCT; decrease of activity. Ref.33
VAR_022570
Natural variant1561G → D in FPCT; decrease of activity. Ref.21
VAR_022571
Natural variant1611L → Q in FPCT. Ref.34
VAR_010986
Natural variant1651M → R in FPCT; activity < 2%. Ref.21 Ref.30
VAR_007911
Natural variant1671E → K in HEP and FPCT; nearly normal activity. Ref.21 Ref.25
VAR_007714
Natural variant1681G → R in HEP; relative activity of 65% of wild-type towards uroporphyrinogen III. Ref.37
VAR_065558
Natural variant1701G → D in HEP; relative activity of 17% and 60% of wild-type towards uroporphyrinogen I and III respectively. Ref.38
VAR_065559
Natural variant1931R → P in FPCT; insoluble protein. Ref.21
VAR_022572
Natural variant1951L → F in FPCT. Ref.30
VAR_007912
Natural variant2161L → Q in FPCT. Ref.33
VAR_022573
Natural variant2181E → K in FPCT; significant decrease of activity. Ref.33
VAR_022574
Natural variant2191S → F in FPCT. Ref.34
VAR_010987
Natural variant2201H → P in HEP; mild form. Ref.27
VAR_009105
Natural variant2291F → L in FPCT. Ref.32
VAR_009106
Natural variant2321F → L in FPCT; decrease of activity. Ref.21
VAR_022575
Natural variant2351P → S in FPCT. Ref.34
VAR_010988
Natural variant2531L → Q in FPCT; decrease of activity. Ref.21 Ref.29
Corresponds to variant rs36033115 [ dbSNP | Ensembl ].
VAR_007913
Natural variant2601I → T in FPCT; decrease of activity. Ref.21
VAR_022576
Natural variant2811G → E in FPTC and HEP. Ref.2 Ref.23 Ref.28
VAR_007715
Natural variant2811G → V in FPCT. Ref.24 Ref.33
VAR_007716
Natural variant2821L → R in FPCT. Ref.33
VAR_022577
Natural variant2921R → G in HEP. Ref.26
VAR_007717
Natural variant3031G → S in FPCT. Ref.33
VAR_022578
Natural variant3031G → V. Ref.6 Ref.12
Corresponds to variant rs17849533 [ dbSNP | Ensembl ].
VAR_060686
Natural variant3041N → K in FPCT. Ref.30
VAR_007914
Natural variant3111Y → C in HEP. Ref.2
VAR_009107
Natural variant3181G → R in FPCT. Ref.29 Ref.33
Corresponds to variant rs116233118 [ dbSNP | Ensembl ].
VAR_007915
Natural variant3241M → T in FPCT. Ref.32
VAR_009108
Natural variant3321R → H in FPCT. Ref.30
VAR_007916
Natural variant3341I → T in FPCT. Ref.29
VAR_007917

Experimental info

Mutagenesis861D → E: 5-10% of wild-type activity. Ref.22
Mutagenesis861D → G: Very low activity. Binds substrate with similar geometry as wild-type. Ref.22
Mutagenesis861D → N: No activity. Unable to bind substrate. Ref.22
Mutagenesis1641Y → F: 25-30% of wild-type activity. Ref.22
Sequence conflict1031G → S in AAA61258. Ref.1
Sequence conflict1031G → S in AAB59456. Ref.14
Sequence conflict1201R → A in AAA61258. Ref.1
Sequence conflict1201R → A in AAB59456. Ref.14
Sequence conflict212 – 2143Missing in AAB59456. Ref.14

Secondary structure

............................................................ 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06132 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 840510B36CFC3856

FASTA36740,787
        10         20         30         40         50         60 
MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR 

        70         80         90        100        110        120 
SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER 

       130        140        150        160        170        180 
LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW 

       190        200        210        220        230        240 
LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV 

       250        260        270        280        290        300 
AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT 

       310        320        330        340        350        360 
LQGNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH 


SRLLRQN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Uroporphyrinogen III decarboxylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS518.1.
PIRA24411.
G02786.
RefSeqNP_000365.3. NM_000374.4.
UniGeneHs.78601.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00308.
ProteinModelPortalP06132.
SMRP06132. Positions 10-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113235. 11 interactions.
IntActP06132. 6 interactions.
MINTMINT-3005024.
STRING9606.ENSP00000246337.

Chemistry

ChEMBLCHEMBL1681619.

PTM databases

PhosphoSiteP06132.

Polymorphism databases

DMDM2507533.

2D gel databases

OGPP06132.

Proteomic databases

MaxQBP06132.
PaxDbP06132.
PeptideAtlasP06132.
PRIDEP06132.

Protocols and materials databases

DNASU7389.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246337; ENSP00000246337; ENSG00000126088.
GeneID7389.
KEGGhsa:7389.
UCSCuc001cna.2. human.

Organism-specific databases

CTD7389.
GeneCardsGC01P045477.
GeneReviewsUROD.
HGNCHGNC:12591. UROD.
HPAHPA027468.
HPA028668.
MIM176100. phenotype.
613521. gene.
neXtProtNX_P06132.
Orphanet95159. Hepatoerythropoietic porphyria.
101330. Porphyria cutanea tarda.
PharmGKBPA37221.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0407.
HOVERGENHBG000229.
InParanoidP06132.
KOK01599.
OMALFAYMVE.
PhylomeDBP06132.
TreeFamTF300744.

Enzyme and pathway databases

BioCycMetaCyc:HS04993-MONOMER.
BRENDA4.1.1.37. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00251; UER00321.

Gene expression databases

ArrayExpressP06132.
BgeeP06132.
CleanExHS_UROD.
GenevestigatorP06132.

Family and domain databases

HAMAPMF_00218. URO_D.
InterProIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
PfamPF01208. URO-D. 1 hit.
[Graphical view]
TIGRFAMsTIGR01464. hemE. 1 hit.
PROSITEPS00906. UROD_1. 1 hit.
PS00907. UROD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUROD. human.
EvolutionaryTraceP06132.
GeneWikiUroporphyrinogen_III_decarboxylase.
GenomeRNAi7389.
NextBio28930.
PROP06132.
SOURCESearch...

Entry information

Entry nameDCUP_HUMAN
AccessionPrimary (citable) accession number: P06132
Secondary accession number(s): A8K762 expand/collapse secondary AC list , Q16863, Q16883, Q53YB8, Q53ZP6, Q6IB28, Q9BUZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM