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P06132

- DCUP_HUMAN

UniProt

P06132 - DCUP_HUMAN

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Protein

Uroporphyrinogen decarboxylase

Gene
UROD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Uroporphyrinogen III = coproporphyrinogen + 4 CO2.UniRule annotation

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
Complete GO annotation...

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.10 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.10 Publications
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 decarboxylaseUniRule annotationPRO_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.2 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.

Miscellaneous databases

EvolutionaryTraceiP06132.

Family & Domainsi

Region

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

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031G → S in AAA61258. 1 Publication
Sequence conflicti103 – 1031G → S in AAB59456. 1 Publication
Sequence conflicti120 – 1201R → A in AAA61258. 1 Publication
Sequence conflicti120 – 1201R → A in AAB59456. 1 Publication
Sequence conflicti212 – 2143Missing in AAB59456. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 173 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

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