P10746 (HEM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uroporphyrinogen-III synthase
Short name=UROIIIS
Short name=UROS
EC=4.2.1.75

Alternative name(s):
Hydroxymethylbilane hydrolyase [cyclizing]
Uroporphyrinogen-III cosynthase

Gene names

Name:

UROS

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	265 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme).
Catalytic activity	Hydroxymethylbilane = uroporphyrinogen III + H2O. Ref.8
Pathway	Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Subunit structure	Monomer. Ref.8
Tissue specificity	Ubiquitous. Ref.2
Involvement in disease	Congenital erythropoietic porphyria (CEP) [MIM:263700]: 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. The manifestations of CEP are heterogeneous, ranging from nonimmune hydrops fetalis due to severe hemolytic anemia in utero to milder, later onset forms, which have only skin lesions due to cutaneous photosensitivity in adult life. The deficiency in UROS activity results in the non-enzymatic conversion of hydroxymethylbilane (HMB) into the uroporphyrinogen-I isomer. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Severe congenital erythropoietic porphyria is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders.
Sequence similarities	Belongs to the uroporphyrinogen-III synthase family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to amine stimulus Inferred from electronic annotation. Source: Compara cellular response to arsenic-containing substance Inferred from electronic annotation. Source: Compara heme biosynthetic process Inferred from direct assay PubMed 3805019. Source: UniProtKB protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway response to antibiotic Inferred from electronic annotation. Source: Compara uroporphyrinogen III biosynthetic process Inferred from direct assay PubMed 18004775Ref.1PubMed 3805019. Source: UniProtKB
Cellular_component	cytosol Non-traceable author statement PubMed 3805019. Source: UniProtKB mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	cofactor binding Inferred from electronic annotation. Source: Compara uroporphyrinogen-III synthase activity Inferred from direct assay PubMed 18004775Ref.1PubMed 3805019. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 265

265

Uroporphyrinogen-III synthase

PRO_0000135251

Natural variations

Natural variant

3

1

V → F in CEP; no residual activity. Ref.14

VAR_021615

Natural variant

4

1

L → F in CEP. Ref.10

VAR_003674

Natural variant

19

1

Y → C in CEP. Ref.12

VAR_003675

Natural variant

47

1

S → P in CEP; less than 3% wild-type activity; severe cutaneous lesions. Ref.19

VAR_021616

Natural variant

53

1

P → L in CEP; no detectable activity; severe phenotype. Ref.9

VAR_003676

Natural variant

62

1

T → A in CEP; no detectable activity according to PubMed:1737856, while it does not affect enzymatic activity according to PubMed:11689424. Ref.8 Ref.11
Corresponds to variant rs28941775 [ dbSNP | Ensembl ].

VAR_003677

Natural variant

66

1

A → V in CEP; residual activity; mild phenotype. Ref.11
Corresponds to variant rs28941774 [ dbSNP | Ensembl ].

VAR_003678

Natural variant

69

1

A → T in CEP; less than 2% wild-type activity; moderately-severe phenotype. Ref.18

VAR_021617

Natural variant

73

1

C → R in CEP; frequent mutation in Western countries; no detectable activity; severe phenotype. Ref.9 Ref.10 Ref.11 Ref.16 Ref.18

VAR_003679

Natural variant

82

1

V → F in CEP; high residual activity; mild phenotype. Ref.12

VAR_003680

Natural variant

99

1

V → A in CEP. Ref.12

VAR_003681

Natural variant

104

1

A → V in CEP; residual activity. Ref.12

VAR_003682

Natural variant

124

1

K → R.
Corresponds to variant rs17153561 [ dbSNP | Ensembl ].

VAR_049345

Natural variant

129

1

I → T in CEP; no residual activity. Ref.17

VAR_021618

Natural variant

171

1

V → G.
Corresponds to variant rs17173752 [ dbSNP | Ensembl ].

VAR_049346

Natural variant

188

1

G → R in CEP; less than 5% wild-type activity. Ref.15

VAR_013558

Natural variant

188

1

G → W in CEP; less than 2% wild-type activity; mild phenotype. Ref.18

VAR_021619

Natural variant

210 – 211

2

EL → HIQSQAQSQAQDN in CEP.

VAR_021620

Natural variant

212

1

S → P in CEP; no residual activity. Ref.13

VAR_003683

Natural variant

219

1

I → S in CEP; less than 2% wild-type activity; moderately-severe phenotype. Ref.18

VAR_021621

Natural variant

225

1

G → S in CEP. Ref.12

VAR_003684

Natural variant

228

1

T → M in CEP; no detectable activity. Ref.10 Ref.11 Ref.18

VAR_003685

Natural variant

237

1

L → P in CEP. Ref.21

VAR_067318

Natural variant

248

1

P → Q in CEP. Ref.20

VAR_066247

Experimental info

Mutagenesis

63

1

S → A: Does not affect enzymatic activity. Ref.8

Mutagenesis

65

1

R → A: Slightly affects enzymatic activity. Ref.8

Mutagenesis

103

1

T → A: Slightly affects enzymatic activity. Ref.8

Mutagenesis

127

1

E → A: Does not affect enzymatic activity. Ref.8

Mutagenesis

168

1

Y → F: Impairs enzymatic activity. Ref.8

Mutagenesis

197

1

S → A: Does not affect enzymatic activity. Ref.8

Mutagenesis

220

1

K → A: Does not affect enzymatic activity. Ref.8

Mutagenesis

227

1

T → A: Does not affect enzymatic activity. Ref.8

Mutagenesis

228

1

T → A: Impairs enzymatic activity. Ref.8

Secondary structure

1

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265

Helix Strand Turn

Details...

Beta strand

2 – 9

8

Helix

18 – 24

7

Turn

25 – 27

3

Beta strand

29 – 34

6

Beta strand

36 – 40

5

Helix

43 – 50

8

Helix

53 – 55

3

Beta strand

57 – 61

5

Helix

64 – 76

13

Helix

80 – 86

7

Helix

88 – 93

6

Beta strand

94 – 98

5

Helix

101 – 109

9

Helix

122 – 130

9

Beta strand

139 – 144

6

Helix

146 – 148

3

Helix

151 – 156

6

Turn

157 – 159

3

Beta strand

162 – 166

5

Beta strand

168 – 172

5

Helix

176 – 187

12

Beta strand

191 – 197

7

Helix

198 – 212

15

Helix

213 – 218

6

Beta strand

219 – 225

7

Helix

226 – 234

9

Beta strand

240 – 242

3

Beta strand

244 – 247

4

Helix

248 – 258

11

Sequences

	Sequence		Length	Mass (Da)
	P10746 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: CEF171401361F61E	FASTA	265	28,628
	10 20 30 40 50 60 MKVLLLKDAK EDDCGQDPYI RELGLYGLEA TLIPVLSFEF LSLPSFSEKL SHPEDYGGLI 70 80 90 100 110 120 FTSPRAVEAA ELCLEQNNKT EVWERSLKEK WNAKSVYVVG NATASLVSKI GLDTEGETCG 130 140 150 160 170 180 NAEKLAEYIC SRESSALPLL FPCGNLKREI LPKALKDKGI AMESITVYQT VAHPGIQGNL 190 200 210 220 230 240 NSYYSQQGVP ASITFFSPSG LTYSLKHIQE LSGDNIDQIK FAAIGPTTAR ALAAQGLPVS 250 260 CTAESPTPQA LATGIRKALQ PHGCC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human uroporphyrinogen III synthase: molecular cloning, nucleotide sequence, and expression of a full-length cDNA." Tsai S.-F., Bishop D.F., Desnick R.J. Proc. Natl. Acad. Sci. U.S.A. 85:7049-7053(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Human uroporphyrinogen-III synthase: genomic organization, alternative promoters, and erythroid-specific expression." Aizencang G., Solis C., Bishop D.F., Warner C., Desnick R.J. Genomics 70:223-231(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY. Tissue: Liver.
[3]	"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: Cerebellum.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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]. Tissue: Brain.
[7]	"Molecular basis of congenital erythropoietic porphyria: mutations in the human uroporphyrinogen III synthase gene." Xu W., Astrin K.H., Desnick R.J. Hum. Mutat. 7:187-192(1996) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[8]	"Crystal structure of human uroporphyrinogen III synthase." Mathews M.A., Schubert H.L., Whitby F.G., Alexander K.J., Schadick K., Bergonia H.A., Phillips J.D., Hill C.P. EMBO J. 20:5832-5839(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS), CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF SER-63; ARG-65; THR-103; GLU-127; TYR-168; SER-197; LYS-220; THR-227 AND THR-228, CHARACTERIZATION OF VARIANT ALA-62.
[9]	"Point mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria (Gunther's disease)." Deybach J.-C., de Verneuil H., Boulechfar S., Grandchamp B., Nordmann Y. Blood 75:1763-1765(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CEP LEU-53 AND ARG-73.
[10]	"Heterogeneity of mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria." Boulechfar S., da Silva V., Deybach J.-C., Nordmann Y., Grandchamp B., de Verneuil H. Hum. Genet. 88:320-324(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CEP PHE-4; ARG-73 AND MET-228.
[11]	"Congenital erythropoietic porphyria: identification and expression of exonic mutations in the uroporphyrinogen III synthase gene." Warner C.A., Yoo H.-W., Roberts A.G., Desnick R.J. J. Clin. Invest. 89:693-700(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CEP ALA-62; VAL-66; ARG-73 AND MET-228.
[12]	"Congenital erythropoietic porphyria: identification and expression of 10 mutations in the uroporphyrinogen III synthase gene." Xu W., Warner C.A., Desnick R.J. J. Clin. Invest. 95:905-912(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CEP CYS-19; PHE-82; ALA-99; VAL-104 AND SER-225.
[13]	"A novel point mutation in congenital erythropoietic porphyria in two members of Japanese family." Tanigawa K., Bensidhoum M., Takamura N., Namba H., Yamashita S., de Verneuil H., Ged C. Hum. Genet. 97:557-560(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CEP PRO-212.
[14]	"Novel point mutation in the uroporphyrinogen III synthase gene causes congenital erythropoietic porphyria of a Japanese family." Takamura N., Hombrados I., Tanigawa K., Namba H., Nagayama Y., de Verneuil H., Yamashita S. Am. J. Med. Genet. 70:299-302(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CEP PHE-3, CHARACTERIZATION OF VARIANT CEP PHE-3.
[15]	"Congenital erythropoietic porphyria successfully treated by allogeneic bone marrow transplantation." Tezcan I., Xu W., Gurgey A., Tuncer M., Cetin M., Oener C., Yetgin S., Ersoy F., Aizencang G., Astrin K.H., Desnick R.J. Blood 92:4053-4058(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CEP ARG-188.
[16]	"C73R is a hotspot mutation in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria." Frank J., Wang X., Lam H.M., Aita V.M., Jugert F.K., Goerz G., Merk H.F., Poh-Fitzpatrick M.B., Christiano A.M. Ann. Hum. Genet. 62:225-230(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CEP ARG-73.
[17]	"Congenital erythropoietic porphyria: a novel homozygous mutation in a Japanese patient." Rogounovitch T., Takamura N., Hombrados I., Morel C., Tanaka T., Kameyoshi Y., Shimizu-Yoshida Y., de Verneuil H., Yamashita S. J. Invest. Dermatol. 115:1156-1156(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CEP THR-129, CHARACTERIZATION OF VARIANT CEP THR-129.
[18]	"Congenital erythropoietic porphyria: identification and expression of eight novel mutations in the uroporphyrinogen III synthase gene." Shady A.A., Colby B.R., Cunha L.F., Astrin K.H., Bishop D.F., Desnick R.J. Br. J. Haematol. 117:980-987(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CEP THR-69; ARG-73; TRP-188; 210-GLU-LEU-211 DELINS HIS-ILE-GLN-SER-GLN-ALA-GLN-SER-GLN-ALA-GLN-ASP-ASN; SER-219 AND MET-228, CHARACTERIZATION OF VARIANTS CEP THR-69; TRP-188 AND SER-219.
[19]	"Congenital erythropoietic porphyria: report of a novel mutation with absence of clinical manifestations in a homozygous mutant sibling." Ged C., Megarbane H., Chouery E., Lalanne M., Megarbane A., de Verneuil H. J. Invest. Dermatol. 123:589-591(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CEP PRO-47, CHARACTERIZATION OF VARIANT CEP PRO-47.
[20]	"ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria." To-Figueras J., Ducamp S., Clayton J., Badenas C., Delaby C., Ged C., Lyoumi S., Gouya L., de Verneuil H., Beaumont C., Ferreira G.C., Deybach J.C., Herrero C., Puy H. Blood 118:1443-1451(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CEP GLN-248.
[21]	"Mutational analysis of uroporphyrinogen III cosynthase gene in Iranian families with congenital erythropoietic porphyria." Moghbeli M., Maleknejad M., Arabi A., Abbaszadegan M.R. Mol. Biol. Rep. 39:6731-6735(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CEP PRO-237.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03824 mRNA. Translation: AAA60273.1.
AF230665 mRNA. Translation: AAG36795.1.
AH010036 Genomic DNA. Translation: AAG36794.1.
AK314896 mRNA. Translation: BAG37410.1.
AL360176 Genomic DNA. Translation: CAI12087.1.
CH471066 Genomic DNA. Translation: EAW49221.1.
CH471066 Genomic DNA. Translation: EAW49222.1.
BC002573 mRNA. Translation: AAH02573.1.

IPI

IPI00745889.

PIR

A40483.

RefSeq

NP_000366.1. NM_000375.2.

UniGene

Hs.501376.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JR2	X-ray	1.84	A/B	1-265	[»]

ProteinModelPortal

P10746.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10746. 2 interactions.

MINT

MINT-2863993.

STRING

9606.ENSP00000357775.

PTM databases

PhosphoSite

P10746.

Polymorphism databases

DMDM

122849.

Proteomic databases

PaxDb

P10746.

PRIDE

P10746.

Protocols and materials databases

DNASU

7390.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368786; ENSP00000357775; ENSG00000188690.
ENST00000368797; ENSP00000357787; ENSG00000188690.

GeneID

7390.

KEGG

hsa:7390.

UCSC

uc001liw.4. human.

Organism-specific databases

CTD

7390.

GeneCards

GC10M127467.

HGNC

HGNC:12592. UROS.

HPA

HPA044038.

MIM

263700. phenotype.
606938. gene.

neXtProt

NX_P10746.

Orphanet

79277. Congenital erythropoietic porphyria.

PharmGKB

PA37222.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1587.

HOGENOM

HOG000007209.

HOVERGEN

HBG000492.

InParanoid

P10746.

KO

K01719.

OMA

DDCGQDP.

OrthoDB

EOG45B1GF.

PhylomeDB

P10746.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00251; UER00320.

Gene expression databases

ArrayExpress

P10746.

Bgee

P10746.

CleanEx

HS_UROS.

Genevestigator

P10746.

GermOnline

ENSG00000188690. Homo sapiens.

Family and domain databases

InterPro

IPR003754. 4pyrrol_synth_uPrphyn_synth.
[Graphical view]

Pfam

PF02602. HEM4. 1 hit.
[Graphical view]

SUPFAM

SSF69618. HEM4_synth. 1 hit.

ProtoNet

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Other

ChEMBL

CHEMBL4433.

EvolutionaryTrace

P10746.

GenomeRNAi

7390.

NextBio

28934.

SOURCE

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Entry information

Entry name

HEM4_HUMAN

Accession

Primary (citable) accession number: P10746
Secondary accession number(s): B2RC13, D3DRF7, Q9H2T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 29, 2013
This is version 130 of the entry and version 1 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.