P06132 (DCUP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uroporphyrinogen decarboxylase
Short name=UPD
Short name=URO-D
EC=4.1.1.37

Gene names

Name:

UROD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic activity	Uroporphyrinogen III = coproporphyrinogen + 4 CO2.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Subunit structure	Homodimer. Ref.15 Ref.17
Subcellular location	Cytoplasm.
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.18 Ref.21 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 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.20 Ref.22 Ref.23 Ref.24 Ref.26 Ref.32 Ref.33 Ref.34 Ref.35
Sequence similarities	Belongs to the uroporphyrinogen decarboxylase family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Disease	Disease mutation
Molecular function	Decarboxylase Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	heme biosynthetic process Inferred by curator PubMed 18004775. Source: UniProtKB protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	uroporphyrinogen decarboxylase activity Inferred from direct assay PubMed 18004775. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

Uroporphyrinogen decarboxylase

PRO_0000187569

Regions

Region

37 – 41

5

Substrate binding

Sites

Binding site

55

1

Substrate

Binding site

85

1

Substrate

Binding site

86

1

Substrate

Binding site

164

1

Substrate

Binding site

219

1

Substrate

Binding site

339

1

Substrate

Site

86

1

Transition state stabilizer

Amino acid modifications

Modified residue

61

1

Phosphoserine By similarity

Natural variations

Natural variant

15

1

K → E.
Corresponds to variant rs11541959 [ dbSNP | Ensembl ].

VAR_060683

Natural variant

25

1

G → E in FPCT; insoluble protein. Ref.18

VAR_022567

Natural variant

46

1

F → L in HEP; mild phenotype; strong decrease of activity. Ref.32 Ref.33

VAR_022568

Natural variant

62

1

P → L in HEP. Ref.2

VAR_009103

Natural variant

77

1

P → L. Ref.2 Ref.4 Ref.5
Corresponds to variant rs1131147 [ dbSNP | Ensembl ].

VAR_067457

Natural variant

80

1

A → G in HEP. Ref.26

VAR_007910

Natural variant

80

1

A → S in FPCT; decrease of activity. Ref.18 Ref.30

VAR_022569

Natural variant

106

1

P → L.
Corresponds to variant rs11541962 [ dbSNP | Ensembl ].

VAR_060684

Natural variant

113

1

R → T.
Corresponds to variant rs11541963 [ dbSNP | Ensembl ].

VAR_060685

Natural variant

134

1

V → Q in FPCT and HEP; requires 2 nucleotide substitutions; nearly normal activity. Ref.18 Ref.24 Ref.28 Ref.30

VAR_009104

Natural variant

142

1

R → Q in FPCT. Ref.31

VAR_010985

Natural variant

144

1

R → P in FPCT; decrease of activity. Ref.30

VAR_022570

Natural variant

156

1

G → D in FPCT; decrease of activity. Ref.18

VAR_022571

Natural variant

161

1

L → Q in FPCT. Ref.31

VAR_010986

Natural variant

165

1

M → R in FPCT; activity < 2%. Ref.18 Ref.27

VAR_007911

Natural variant

167

1

E → K in HEP and FPCT; nearly normal activity. Ref.18 Ref.22

VAR_007714

Natural variant

168

1

G → R in HEP; relative activity of 65% of wild-type towards uroporphyrinogen III. Ref.34

VAR_065558

Natural variant

170

1

G → D in HEP; relative activity of 17% and 60% of wild-type towards uroporphyrinogen I and III respectively. Ref.35

VAR_065559

Natural variant

193

1

R → P in FPCT; insoluble protein. Ref.18

VAR_022572

Natural variant

195

1

L → F in FPCT. Ref.27

VAR_007912

Natural variant

216

1

L → Q in FPCT. Ref.30

VAR_022573

Natural variant

218

1

E → K in FPCT; significant decrease of activity. Ref.30

VAR_022574

Natural variant

219

1

S → F in FPCT. Ref.31

VAR_010987

Natural variant

220

1

H → P in HEP; mild form. Ref.24

VAR_009105

Natural variant

229

1

F → L in FPCT. Ref.29

VAR_009106

Natural variant

232

1

F → L in FPCT; decrease of activity. Ref.18

VAR_022575

Natural variant

235

1

P → S in FPCT. Ref.31

VAR_010988

Natural variant

253

1

L → Q in FPCT; decrease of activity. Ref.18 Ref.26
Corresponds to variant rs36033115 [ dbSNP | Ensembl ].

VAR_007913

Natural variant

260

1

I → T in FPCT; decrease of activity. Ref.18

VAR_022576

Natural variant

281

1

G → E in FPTC and HEP. Ref.2 Ref.20 Ref.25

VAR_007715

Natural variant

281

1

G → V in FPCT. Ref.21 Ref.30

VAR_007716

Natural variant

282

1

L → R in FPCT. Ref.30

VAR_022577

Natural variant

292

1

R → G in HEP. Ref.23

VAR_007717

Natural variant

303

1

G → S in FPCT. Ref.30

VAR_022578

Natural variant

303

1

G → V. Ref.6 Ref.12
Corresponds to variant rs17849533 [ dbSNP | Ensembl ].

VAR_060686

Natural variant

304

1

N → K in FPCT. Ref.27

VAR_007914

Natural variant

311

1

Y → C in HEP. Ref.2

VAR_009107

Natural variant

318

1

G → R in FPCT. Ref.26 Ref.30

VAR_007915

Natural variant

324

1

M → T in FPCT. Ref.29

VAR_009108

Natural variant

332

1

R → H in FPCT. Ref.27

VAR_007916

Natural variant

334

1

I → T in FPCT. Ref.26

VAR_007917

Experimental info

Mutagenesis

86

1

D → E: 5-10% of wild-type activity. Ref.19

Mutagenesis

86

1

D → G: Very low activity. Binds substrate with similar geometry as wild-type. Ref.19

Mutagenesis

86

1

D → N: No activity. Unable to bind substrate. Ref.19

Mutagenesis

164

1

Y → F: 25-30% of wild-type activity. Ref.19

Sequence conflict

103

1

G → S in AAA61258. Ref.1

Sequence conflict

103

1

G → S in AAB59456. Ref.14

Sequence conflict

120

1

R → A in AAA61258. Ref.1

Sequence conflict

120

1

R → A in AAB59456. Ref.14

Sequence conflict

212 – 214

3

Missing in AAB59456. Ref.14

Secondary structure

1

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367

Helix Strand Turn

Details...

Helix

18 – 24

7

Beta strand

38 – 40

3

Helix

44 – 51

8

Helix

55 – 59

5

Helix

62 – 75

14

Helix

89 – 93

5

Beta strand

99 – 101

3

Turn

102 – 104

3

Beta strand

105 – 107

3

Helix

115 – 120

6

Helix

124 – 126

3

Helix

127 – 130

4

Helix

132 – 145

14

Beta strand

151 – 156

6

Helix

158 – 167

10

Helix

175 – 183

9

Helix

185 – 208

24

Beta strand

212 – 218

7

Helix

221 – 223

3

Helix

226 – 232

7

Helix

234 – 250

17

Beta strand

258 – 262

5

Helix

266 – 268

3

Helix

269 – 272

4

Turn

273 – 276

4

Beta strand

278 – 281

4

Helix

288 – 295

8

Beta strand

297 – 305

9

Helix

307 – 311

5

Helix

314 – 328

15

Beta strand

330 – 339

10

Helix

347 – 365

19

Sequences

	Sequence		Length	Mass (Da)
	P06132 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 840510B36CFC3856	FASTA	367	40,787
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY, SUBUNIT.
[16]	"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].
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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

GeneReviews

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.

IPI

IPI00301489.

PIR

A24411.
G02786.

RefSeq

NP_000365.3. NM_000374.4.

UniGene

Hs.78601.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00308.

ProteinModelPortal

P06132.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06132. 2 interactions.

STRING

9606.ENSP00000246337.

PTM databases

PhosphoSite

P06132.

Polymorphism databases

DMDM

2507533.

2D gel databases

OGP

P06132.

Proteomic databases

PaxDb

P06132.

PeptideAtlas

P06132.

PRIDE

P06132.

Protocols and materials databases

DNASU

7389.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000246337; ENSP00000246337; ENSG00000126088.

GeneID

7389.

KEGG

hsa:7389.

UCSC

uc001cna.2. human.

Organism-specific databases

CTD

7389.

GeneCards

GC01P045477.

HGNC

HGNC:12591. UROD.

HPA

HPA027468.
HPA028668.

MIM

176100. phenotype.
613521. gene.

neXtProt

NX_P06132.

Orphanet

95159. Hepatoerythropoietic porphyria.
101330. Porphyria cutanea tarda.

PharmGKB

PA37221.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0407.

HOVERGEN

HBG000229.

InParanoid

P06132.

KO

K01599.

OMA

TLATYMI.

OrthoDB

EOG46DM33.

PhylomeDB

P06132.

Enzyme and pathway databases

BRENDA

4.1.1.37. 2681.

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00251; UER00321.

Gene expression databases

ArrayExpress

P06132.

Bgee

P06132.

CleanEx

HS_UROD.

Genevestigator

P06132.

GermOnline

ENSG00000126088. Homo sapiens.

Family and domain databases

InterPro

IPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]

PANTHER

PTHR21091:SF2. PTHR21091:SF2. 1 hit.

Pfam

PF01208. URO-D. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01464. hemE. 1 hit.

PROSITE

PS00906. UROD_1. 1 hit.
PS00907. UROD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1681619.

ChiTaRS

UROD. human.

EvolutionaryTrace

P06132.

GenomeRNAi

7389.

NextBio

28930.

SOURCE

Search...

Entry information

Entry name

DCUP_HUMAN

Accession

Primary (citable) accession number: P06132
Secondary accession number(s): A8K762 , Q16863, Q16883, Q53YB8, Q53ZP6, Q6IB28, Q9BUZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 159 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.