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P13716

- HEM2_HUMAN

UniProt

P13716 - HEM2_HUMAN

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Protein

Delta-aminolevulinic acid dehydratase

Gene

ALAD

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

Functioni

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.2 Publications

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.3 Publications

Cofactori

Zn2+1 PublicationNote: Binds 8 zinc ions per octamer. Requires four zinc ions per octamer for full catalytic activity. Can bind up to 2 zinc ions per subunit.1 Publication

Enzyme regulationi

Can alternate between a fully active homooctamer and a low-activity homohexamer. A bound magnesium ion may promote the assembly of the fully active homooctamer. The magnesium-binding site is absent in the low-activity homohexamer. Inhibited by compounds that favor the hexameric state. Inhibited by divalent lead ions. The lead ions partially displace the zinc cofactor.3 Publications

Kineticsi

  1. KM=0.09 mM for 5-aminolevulinate at pH 71 Publication

Vmax=43 µmol/h/mg enzyme at pH 71 Publication

pH dependencei

Optimum pH is 6.8-7.3.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi122 – 1221Zinc 1; catalytic
Metal bindingi124 – 1241Zinc 1; catalytic
Metal bindingi131 – 1311Zinc 2
Metal bindingi132 – 1321Zinc 1; catalytic
Active sitei199 – 1991Schiff-base intermediate with substrate1 Publication
Binding sitei209 – 2091Substrate 1
Binding sitei221 – 2211Substrate 1
Metal bindingi223 – 2231Zinc 2
Active sitei252 – 2521Schiff-base intermediate with substrate1 Publication
Binding sitei279 – 2791Substrate 2
Binding sitei318 – 3181Substrate 2

GO - Molecular functioni

  1. catalytic activity Source: ProtInc
  2. identical protein binding Source: UniProtKB
  3. lead ion binding Source: UniProtKB
  4. porphobilinogen synthase activity Source: UniProtKB
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to interleukin-4 Source: Ensembl
  2. heme biosynthetic process Source: UniProtKB
  3. porphyrin-containing compound metabolic process Source: Reactome
  4. protein homooligomerization Source: UniProtKB
  5. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS07501-MONOMER.
ReactomeiREACT_9465. Heme biosynthesis.
UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:ALAD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:395. ALAD.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleus Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Acute hepatic porphyria (AHEPP) [MIM:612740]: 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. AHP is characterized by attacks of gastrointestinal disturbances, abdominal colic, paralyses and peripheral neuropathy. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti133 – 1331G → R in AHEPP; mixture of about 50% hexamer and 50% octamer; about 10% residual activity. 1 Publication
VAR_003634
Natural varianti153 – 1531V → M in AHEPP; about 95% octamer; about 40% residual activity. 1 Publication
VAR_020974
Natural varianti240 – 2401R → W in AHEPP; mixture of about 80% hexamer and 20% octamer; about 4% residual activity. 2 Publications
VAR_003635
Natural varianti274 – 2741A → T in AHEPP; mixture of about 14% hexamer and 86% octamer; about 20% enzyme residual activity. 2 Publications
VAR_003636
Natural varianti275 – 2751V → M in AHEPP; mainly octamer; reduced activity. 1 Publication
VAR_003637

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi122 – 1221C → A: Reduces enzyme activity about 1000000-fold; when associated with A-124 and A-132. 1 Publication
Mutagenesisi124 – 1241C → A: Reduces enzyme activity about 1000000-fold; when associated with A-122 and A-132. 1 Publication
Mutagenesisi131 – 1311H → A: No effect on catalytic activity; when associated with A-223. 1 Publication
Mutagenesisi132 – 1321C → A: Reduces enzyme activity about 1000000-fold; when associated with A-122 and A-124. 1 Publication
Mutagenesisi223 – 2231C → A: No effect on catalytic activity; when associated with A-131. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi612740. phenotype.
Orphaneti100924. Porphyria due to ALA dehydratase deficiency.
PharmGKBiPA24687.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Delta-aminolevulinic acid dehydratasePRO_0000140526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991N6-succinyllysineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei252 – 2521N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP13716.
PaxDbiP13716.
PRIDEiP13716.

2D gel databases

OGPiP13716.
REPRODUCTION-2DPAGEP13716.
SWISS-2DPAGEP13716.

PTM databases

PhosphoSiteiP13716.

Expressioni

Gene expression databases

BgeeiP13716.
CleanExiHS_ALAD.
ExpressionAtlasiP13716. baseline and differential.
GenevestigatoriP13716.

Organism-specific databases

HPAiHPA021023.
HPA022124.

Interactioni

Subunit structurei

Homooctamer; active form. Homohexamer; low activity form.3 Publications

Protein-protein interaction databases

BioGridi106712. 19 interactions.
STRINGi9606.ENSP00000386284.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Helixi14 – 207Combined sources
Turni21 – 244Combined sources
Helixi28 – 303Combined sources
Beta strandi31 – 377Combined sources
Beta strandi44 – 463Combined sources
Beta strandi48 – 503Combined sources
Beta strandi54 – 563Combined sources
Helixi58 – 7114Combined sources
Beta strandi75 – 806Combined sources
Beta strandi83 – 853Combined sources
Beta strandi94 – 985Combined sources
Helixi100 – 11112Combined sources
Beta strandi115 – 1217Combined sources
Beta strandi123 – 1264Combined sources
Helixi141 – 16020Combined sources
Beta strandi163 – 1675Combined sources
Helixi174 – 18411Combined sources
Turni188 – 1903Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi198 – 2003Combined sources
Helixi203 – 2053Combined sources
Helixi206 – 2105Combined sources
Helixi221 – 2233Combined sources
Helixi231 – 24313Combined sources
Beta strandi247 – 2537Combined sources
Helixi255 – 2573Combined sources
Helixi258 – 26710Combined sources
Beta strandi273 – 2775Combined sources
Helixi279 – 29012Combined sources
Helixi296 – 31015Combined sources
Beta strandi313 – 3175Combined sources
Helixi320 – 3267Combined sources
Turni327 – 3293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E51X-ray2.83A/B1-330[»]
1PV8X-ray2.20A/B1-330[»]
ProteinModelPortaliP13716.
SMRiP13716. Positions 1-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13716.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
GeneTreeiENSGT00390000006998.
HOGENOMiHOG000020323.
HOVERGENiHBG001222.
InParanoidiP13716.
KOiK01698.
OMAiDHPTACY.
OrthoDBiEOG751NFP.
PhylomeDBiP13716.
TreeFamiTF300665.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P13716-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQPQSVLHSG YFHPLLRAWQ TATTTLNASN LIYPIFVTDV PDDIQPITSL
60 70 80 90 100
PGVARYGVKR LEEMLRPLVE EGLRCVLIFG VPSRVPKDER GSAADSEESP
110 120 130 140 150
AIEAIHLLRK TFPNLLVACD VCLCPYTSHG HCGLLSENGA FRAEESRQRL
160 170 180 190 200
AEVALAYAKA GCQVVAPSDM MDGRVEAIKE ALMAHGLGNR VSVMSYSAKF
210 220 230 240 250
ASCFYGPFRD AAKSSPAFGD RRCYQLPPGA RGLALRAVDR DVREGADMLM
260 270 280 290 300
VKPGMPYLDI VREVKDKHPD LPLAVYHVSG EFAMLWHGAQ AGAFDLKAAV
310 320 330
LEAMTAFRRA GADIIITYYT PQLLQWLKEE
Length:330
Mass (Da):36,295
Last modified:January 1, 1990 - v1
Checksum:iE005F3055F6D9403
GO
Isoform 2 (identifier: P13716-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MQPQSVLHSG...SNLIYPIFVT → MPPTSSTPSL...QSISHPRSCR

Show »
Length:359
Mass (Da):39,034
Checksum:i4AD5F3B2570ACD81
GO

Sequence cautioni

The sequence AAH00977.3 differs from that shown. Reason: Erroneous initiation. Curated

Polymorphismi

There are two common alleles of ALAD. Individuals heterozygous or homozygous for ALAD*2 Asn-59 have significantly higher blood lead levels than do ALAD*1 Lys-59 homozygotes when exposed to environmental lead.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121F → L in an asymptomatic patient with ALAD deficiency; hexamer with almost no residual activity; also found in a hereditary coproporphyria patient carrying the R-279 mutation in CPOX. 2 Publications
VAR_020973
Natural varianti59 – 591K → N in allele ALAD*2; 10% of population; fully active octamer. 2 Publications
Corresponds to variant rs1800435 [ dbSNP | Ensembl ].
VAR_003633
Natural varianti133 – 1331G → R in AHEPP; mixture of about 50% hexamer and 50% octamer; about 10% residual activity. 1 Publication
VAR_003634
Natural varianti153 – 1531V → M in AHEPP; about 95% octamer; about 40% residual activity. 1 Publication
VAR_020974
Natural varianti240 – 2401R → W in AHEPP; mixture of about 80% hexamer and 20% octamer; about 4% residual activity. 2 Publications
VAR_003635
Natural varianti274 – 2741A → T in AHEPP; mixture of about 14% hexamer and 86% octamer; about 20% enzyme residual activity. 2 Publications
VAR_003636
Natural varianti275 – 2751V → M in AHEPP; mainly octamer; reduced activity. 1 Publication
VAR_003637

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838MQPQS…PIFVT → MPPTSSTPSLSRPGLGQAGK PDTGSHPPPTISTSIFLSCF PTIPLSRPRTTGPSHSYQSI SHPRSCR in isoform 2. 1 PublicationVSP_037866Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13928 mRNA. Translation: AAA51687.1.
X64467 Genomic DNA. Translation: CAA45796.1.
S99468 mRNA. Translation: AAC60581.1.
S99471 mRNA. Translation: AAC60582.1.
AK290490 mRNA. Translation: BAF83179.1.
AK312552 mRNA. Translation: BAG35449.1.
AY319481 Genomic DNA. Translation: AAP72012.1.
AL137066 Genomic DNA. Translation: CAH70099.3.
BC000977 mRNA. Translation: AAH00977.3. Different initiation.
CCDSiCCDS6794.2. [P13716-1]
PIRiA26478.
RefSeqiNP_000022.3. NM_000031.5. [P13716-1]
XP_005251856.1. XM_005251799.1. [P13716-2]
UniGeneiHs.1227.

Genome annotation databases

EnsembliENST00000409155; ENSP00000386284; ENSG00000148218. [P13716-1]
GeneIDi210.
KEGGihsa:210.
UCSCiuc004bhl.4. human. [P13716-2]
uc011lxf.2. human. [P13716-1]

Polymorphism databases

DMDMi122833.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13928 mRNA. Translation: AAA51687.1 .
X64467 Genomic DNA. Translation: CAA45796.1 .
S99468 mRNA. Translation: AAC60581.1 .
S99471 mRNA. Translation: AAC60582.1 .
AK290490 mRNA. Translation: BAF83179.1 .
AK312552 mRNA. Translation: BAG35449.1 .
AY319481 Genomic DNA. Translation: AAP72012.1 .
AL137066 Genomic DNA. Translation: CAH70099.3 .
BC000977 mRNA. Translation: AAH00977.3 . Different initiation.
CCDSi CCDS6794.2. [P13716-1 ]
PIRi A26478.
RefSeqi NP_000022.3. NM_000031.5. [P13716-1 ]
XP_005251856.1. XM_005251799.1. [P13716-2 ]
UniGenei Hs.1227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E51 X-ray 2.83 A/B 1-330 [» ]
1PV8 X-ray 2.20 A/B 1-330 [» ]
ProteinModelPortali P13716.
SMRi P13716. Positions 1-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106712. 19 interactions.
STRINGi 9606.ENSP00000386284.

Chemistry

BindingDBi P13716.
ChEMBLi CHEMBL3126.
DrugBanki DB00855. Aminolevulinic acid.

PTM databases

PhosphoSitei P13716.

Polymorphism databases

DMDMi 122833.

2D gel databases

OGPi P13716.
REPRODUCTION-2DPAGE P13716.
SWISS-2DPAGE P13716.

Proteomic databases

MaxQBi P13716.
PaxDbi P13716.
PRIDEi P13716.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000409155 ; ENSP00000386284 ; ENSG00000148218 . [P13716-1 ]
GeneIDi 210.
KEGGi hsa:210.
UCSCi uc004bhl.4. human. [P13716-2 ]
uc011lxf.2. human. [P13716-1 ]

Organism-specific databases

CTDi 210.
GeneCardsi GC09M116148.
HGNCi HGNC:395. ALAD.
HPAi HPA021023.
HPA022124.
MIMi 125270. gene.
612740. phenotype.
neXtProti NX_P13716.
Orphaneti 100924. Porphyria due to ALA dehydratase deficiency.
PharmGKBi PA24687.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0113.
GeneTreei ENSGT00390000006998.
HOGENOMi HOG000020323.
HOVERGENi HBG001222.
InParanoidi P13716.
KOi K01698.
OMAi DHPTACY.
OrthoDBi EOG751NFP.
PhylomeDBi P13716.
TreeFami TF300665.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .
BioCyci MetaCyc:HS07501-MONOMER.
Reactomei REACT_9465. Heme biosynthesis.

Miscellaneous databases

ChiTaRSi ALAD. human.
EvolutionaryTracei P13716.
GeneWikii ALAD.
GenomeRNAii 210.
NextBioi 840.
PROi P13716.
SOURCEi Search...

Gene expression databases

Bgeei P13716.
CleanExi HS_ALAD.
ExpressionAtlasi P13716. baseline and differential.
Genevestigatori P13716.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view ]
PANTHERi PTHR11458. PTHR11458. 1 hit.
Pfami PF00490. ALAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human delta-aminolevulinate dehydratase: nucleotide sequence of a full-length cDNA clone."
    Wetmur J.G., Bishop D.F., Cantelmo C., Desnick R.J.
    Proc. Natl. Acad. Sci. U.S.A. 83:7703-7707(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "RsaI polymorphism in the human delta-aminolevulinate dehydratase gene at 9q34."
    Wetmur J.G.
    Nucleic Acids Res. 19:4307-4307(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  3. "Cloning and expression of the defective genes from a patient with delta-aminolevulinate dehydratase porphyria."
    Ishida N., Fujita H., Fukuda Y., Noguchi T., Doss M., Kappas A., Sassa S.
    J. Clin. Invest. 89:1431-1437(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS AHEPP TRP-240 AND THR-274.
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Tongue.
  5. NIEHS SNPs program
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-59.
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Placenta.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-17.
    Tissue: Platelet.
  9. "Identification of lysine at the active site of human 5-aminolevulinate dehydratase."
    Gibbs P.N.B., Jordan P.M.
    Biochem. J. 236:447-451(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  10. "The molecular mechanism of lead inhibition of human porphobilinogen synthase."
    Jaffe E.K., Martins J., Li J., Kervinen J., Dunbrack R.L. Jr.
    J. Biol. Chem. 276:1531-1537(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-122; CYS-124; HIS-131; CYS-132 AND CYS-223.
  11. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The crystal structure of human Ala-dehydratase."
    Mills-Davies N.L., Thompson D., Cooper J.B., Shoolingin-Jordan P.M.
    Submitted (OCT-1998) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) IN COMPLEX WITH PORPHOBILINOGEN AND ZINC IONS.
  14. "Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase."
    Breinig S., Kervinen J., Stith L., Wasson A.S., Fairman R., Wlodawer A., Zdanov A., Jaffe E.K.
    Nat. Struct. Biol. 10:757-763(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LEU-12 IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, ENZYME REGULATION.
  15. "Molecular characterization of the human delta-aminolevulinate dehydratase 2 (ALAD2) allele: implications for molecular screening of individuals for genetic susceptibility to lead poisoning."
    Wetmur J.G., Kaya A.H., Plewinska M., Desnick R.J.
    Am. J. Hum. Genet. 49:757-763(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-59.
  16. "Delta-aminolevulinate dehydratase deficient porphyria: identification of the molecular lesions in a severely affected homozygote."
    Plewinska M., Thunell S., Holmberg L., Wetmur J.G., Desnick R.J.
    Am. J. Hum. Genet. 49:167-174(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AHEPP ARG-133 AND MET-275.
  17. "Cloning and expression of the defective genes in delta-aminolevulinate dehydratase porphyria: compound heterozygosity in this hereditary liver disease."
    Sassa S., Ishida N., Fujita H., Fukuda Y., Noguchi T., Doss M., Kappas A.
    Trans. Assoc. Am. Physicians 105:250-259(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AHEPP TRP-240 AND THR-274, CHARACTERIZATION OF VARIANTS AHEPP TRP-240 AND THR-274.
  18. "A novel mutation of delta-aminolaevulinate dehydratase in a healthy child with 12% erythrocyte enzyme activity."
    Akagi R., Yasui Y., Harper P., Sassa S.
    Br. J. Haematol. 106:931-937(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-12, CHARACTERIZATION OF VARIANT LEU-12.
  19. "Novel molecular defects of the delta-aminolevulinate dehydratase gene in a patient with inherited acute hepatic porphyria."
    Akagi R., Shimizu R., Furuyama K., Doss M.O., Sassa S.
    Hepatology 31:704-708(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AHEPP MET-153, CHARACTERIZATION OF VARIANT AHEPP MET-153.
  20. "Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient."
    Akagi R., Inoue R., Muranaka S., Tahara T., Taketani S., Anderson K.E., Phillips J.D., Sassa S.
    Br. J. Haematol. 132:237-243(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-12.
  21. "ALAD porphyria is a conformational disease."
    Jaffe E.K., Stith L.
    Am. J. Hum. Genet. 80:329-337(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS AHEPP ARG-133; MET-153; TRP-240; THR-274 AND MET-275, CHARACTERIZATION OF VARIANTS LEU-12 AND ASN-59.

Entry informationi

Entry nameiHEM2_HUMAN
AccessioniPrimary (citable) accession number: P13716
Secondary accession number(s): A8K375
, B2R6F2, Q16870, Q16871, Q9BVQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 26, 2014
This is version 168 of the entry and version 1 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

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