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P13716 (HEM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 160. Feed History...

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

Names and origin

Protein namesRecommended name:
Delta-aminolevulinic acid dehydratase

Short name=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:ALAD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O. Ref.10 Ref.11 Ref.14

Cofactor

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. Ref.10

Enzyme regulation

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. Ref.10 Ref.11 Ref.14

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.

Subunit structure

Homooctamer; active form. Homohexamer; low activity form. Ref.11 Ref.14

Polymorphism

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.16 Ref.17 Ref.19 Ref.21

Sequence similarities

Belongs to the ALADH family.

Biophysicochemical properties

Kinetic parameters:

KM=0.09 mM for 5-aminolevulinate at pH 7 Ref.10

Vmax=43 µmol/h/mg enzyme at pH 7

pH dependence:

Optimum pH is 6.8-7.3.

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P13716-1)

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.
Isoform 2 (identifier: P13716-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Delta-aminolevulinic acid dehydratase
PRO_0000140526

Sites

Active site1991Schiff-base intermediate with substrate Ref.9
Active site2521Schiff-base intermediate with substrate Ref.9
Metal binding1221Zinc 1; catalytic
Metal binding1241Zinc 1; catalytic
Metal binding1311Zinc 2
Metal binding1321Zinc 1; catalytic
Metal binding2231Zinc 2
Binding site2091Substrate 1
Binding site2211Substrate 1
Binding site2791Substrate 2
Binding site3181Substrate 2

Amino acid modifications

Modified residue1991N6-succinyllysine By similarity
Modified residue2151Phosphoserine By similarity
Modified residue2521N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 3838MQPQS…PIFVT → MPPTSSTPSLSRPGLGQAGK PDTGSHPPPTISTSIFLSCF PTIPLSRPRTTGPSHSYQSI SHPRSCR in isoform 2.
VSP_037866
Natural variant121F → 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. Ref.14 Ref.18 Ref.20 Ref.21
VAR_020973
Natural variant591K → N in allele ALAD*2; 10% of population; fully active octamer. Ref.5 Ref.15 Ref.21
Corresponds to variant rs1800435 [ dbSNP | Ensembl ].
VAR_003633
Natural variant1331G → R in AHEPP; mixture of about 50% hexamer and 50% octamer; about 10% residual activity. Ref.16 Ref.21
VAR_003634
Natural variant1531V → M in AHEPP; about 95% octamer; about 40% residual activity. Ref.19 Ref.21
VAR_020974
Natural variant2401R → W in AHEPP; mixture of about 80% hexamer and 20% octamer; about 4% residual activity. Ref.3 Ref.17 Ref.21
VAR_003635
Natural variant2741A → T in AHEPP; mixture of about 14% hexamer and 86% octamer; about 20% enzyme residual activity. Ref.3 Ref.17 Ref.21
VAR_003636
Natural variant2751V → M in AHEPP; mainly octamer; reduced activity. Ref.16 Ref.21
VAR_003637

Experimental info

Mutagenesis1221C → A: Reduces enzyme activity about 1000000-fold; when associated with A-124 and A-132. Ref.10
Mutagenesis1241C → A: Reduces enzyme activity about 1000000-fold; when associated with A-122 and A-132. Ref.10
Mutagenesis1311H → A: No effect on catalytic activity; when associated with A-223. Ref.10
Mutagenesis1321C → A: Reduces enzyme activity about 1000000-fold; when associated with A-122 and A-124. Ref.10
Mutagenesis2231C → A: No effect on catalytic activity; when associated with A-131. Ref.10

Secondary structure

................................................................ 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: E005F3055F6D9403

FASTA33036,295
        10         20         30         40         50         60 
MQPQSVLHSG YFHPLLRAWQ TATTTLNASN LIYPIFVTDV PDDIQPITSL PGVARYGVKR 

        70         80         90        100        110        120 
LEEMLRPLVE EGLRCVLIFG VPSRVPKDER GSAADSEESP AIEAIHLLRK TFPNLLVACD 

       130        140        150        160        170        180 
VCLCPYTSHG HCGLLSENGA FRAEESRQRL AEVALAYAKA GCQVVAPSDM MDGRVEAIKE 

       190        200        210        220        230        240 
ALMAHGLGNR VSVMSYSAKF ASCFYGPFRD AAKSSPAFGD RRCYQLPPGA RGLALRAVDR 

       250        260        270        280        290        300 
DVREGADMLM VKPGMPYLDI VREVKDKHPD LPLAVYHVSG EFAMLWHGAQ AGAFDLKAAV 

       310        320        330 
LEAMTAFRRA GADIIITYYT PQLLQWLKEE 

« Hide

Isoform 2 [UniParc].

Checksum: 4AD5F3B2570ACD81
Show »

FASTA35939,034

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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. expand/collapse author list , 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, MASS SPECTROMETRY, MUTAGENESIS OF CYS-122; CYS-124; HIS-131; CYS-132 AND CYS-223.
[11]"Allosteric inhibition of human porphobilinogen synthase."
Lawrence S.H., Ramirez U.D., Selwood T., Stith L., Jaffe E.K.
J. Biol. Chem. 284:35807-35817(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION.
[12]"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].
[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, 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA26478.
RefSeqNP_000022.3. NM_000031.5.
XP_005251856.1. XM_005251799.1.
UniGeneHs.1227.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E51X-ray2.83A/B1-330[»]
1PV8X-ray2.20A/B1-330[»]
ProteinModelPortalP13716.
SMRP13716. Positions 1-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106712. 18 interactions.
STRING9606.ENSP00000386284.

Chemistry

ChEMBLCHEMBL3126.
DrugBankDB00855. Aminolevulinic acid.

PTM databases

PhosphoSiteP13716.

Polymorphism databases

DMDM122833.

2D gel databases

OGPP13716.
REPRODUCTION-2DPAGEP13716.
SWISS-2DPAGEP13716.

Proteomic databases

PaxDbP13716.
PRIDEP13716.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000409155; ENSP00000386284; ENSG00000148218. [P13716-1]
GeneID210.
KEGGhsa:210.
UCSCuc004bhl.4. human. [P13716-2]
uc011lxf.2. human. [P13716-1]

Organism-specific databases

CTD210.
GeneCardsGC09M116148.
HGNCHGNC:395. ALAD.
HPAHPA021023.
HPA022124.
MIM125270. gene.
612740. phenotype.
neXtProtNX_P13716.
Orphanet100924. Porphyria due to ALA dehydratase deficiency.
PharmGKBPA24687.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
HOVERGENHBG001222.
KOK01698.
OMAIITYFTP.
OrthoDBEOG751NFP.
TreeFamTF300665.

Enzyme and pathway databases

BioCycMetaCyc:HS07501-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00251; UER00318.

Gene expression databases

ArrayExpressP13716.
BgeeP13716.
CleanExHS_ALAD.
GenevestigatorP13716.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALAD. human.
EvolutionaryTraceP13716.
GeneWikiALAD.
GenomeRNAi210.
NextBio840.
PROP13716.
SOURCESearch...

Entry information

Entry nameHEM2_HUMAN
AccessionPrimary (citable) accession number: P13716
Secondary accession number(s): A8K375 expand/collapse secondary AC list , B2R6F2, Q16870, Q16871, Q9BVQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: March 19, 2014
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM