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P30566 (PUR8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. 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:
Adenylosuccinate lyase

Short name=ASL
EC=4.3.2.2
Alternative name(s):
Adenylosuccinase
Short name=ASase
Gene names
Name:ADSL
Synonyms:AMPS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.

Catalytic activity

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. Ref.9 Ref.14

(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. Ref.9 Ref.14

Enzyme regulation

The enzyme reaction kinetics indicate cooperativity between subunits. Ref.14 Ref.21

Pathway

Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.

Subunit structure

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site. Ref.9 Ref.14

Tissue specificity

Ubiquitously expressed. Both isoforms are produced by all tissues. Isoform 2 is 10-fold less abundant than isoform 1.

Involvement in disease

Adenylosuccinase deficiency (ADSL deficiency) [MIM:103050]: An autosomal recessive disorder characterized by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Most children display marked psychomotor delay, often accompanied by epilepsy or autistic features, or both, although some patients may be less profoundly retarded. Occasionally, growth retardation and muscular wasting are also present.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Sequence caution

The sequence AAC60603.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA46697.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Epilepsy
   Molecular functionLyase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' AMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

AMP biosynthetic process

Inferred from direct assay PubMed 11428554. Source: UniProtKB

aerobic respiration

Inferred from electronic annotation. Source: Ensembl

metabolic process

Inferred from direct assay Ref.2. Source: GOC

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

protein tetramerization

Inferred from direct assay Ref.9. Source: UniProtKB

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine nucleotide biosynthetic process

Inferred by curator Ref.2. Source: UniProtKB

purine ribonucleoside monophosphate biosynthetic process

Traceable author statement. Source: Reactome

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to muscle activity

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_function(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity

Inferred from electronic annotation. Source: UniProtKB-EC

N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity

Inferred from direct assay Ref.9Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30566-1)

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: P30566-2)

Also known as: Delta-ADSL;

The sequence of this isoform differs from the canonical sequence as follows:
     398-456: Missing.
Note: Lacks enzymatic activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 484483Adenylosuccinate lyase
PRO_0000137892

Regions

Region20 – 212Substrate binding; shared with neighboring subunit
Region85 – 873Substrate binding
Region111 – 1122Substrate binding

Sites

Active site1591Proton donor/acceptor Ref.14
Active site2891Proton donor/acceptor Ref.14
Binding site2411Substrate
Binding site3031Substrate; shared with neighboring subunit
Binding site3291Substrate
Binding site3341Substrate
Binding site3381Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.10
Modified residue1471N6-acetyllysine Ref.11
Modified residue2951N6-acetyllysine Ref.11

Natural variations

Alternative sequence398 – 45659Missing in isoform 2.
VSP_000318
Natural variant21A → V in ADSL deficiency; severe. Ref.18
Corresponds to variant rs143083947 [ dbSNP | Ensembl ].
VAR_016930
Natural variant31A → V in ADSL deficiency; severe. Ref.2
VAR_017078
Natural variant261M → L in ADSL deficiency; severe. Ref.18
VAR_016931
Natural variant311S → N.
Corresponds to variant rs5757921 [ dbSNP | Ensembl ].
VAR_037883
Natural variant721I → V in ADSL deficiency; severe. Ref.17
VAR_007972
Natural variant1001P → A in ADSL deficiency; moderate. Ref.16
VAR_017079
Natural variant1141Y → H in ADSL deficiency; severe. Total loss of activity. Ref.2
VAR_017080
Natural variant1411R → W in ADSL deficiency; severe. Ref.17 Ref.18
VAR_007973
Natural variant1471K → M.
Corresponds to variant rs11089991 [ dbSNP | Ensembl ].
VAR_037884
Natural variant1901R → Q in ADSL deficiency; moderate. Ref.2 Ref.17
Corresponds to variant rs28941471 [ dbSNP | Ensembl ].
VAR_007974
Natural variant1941R → C in ADSL deficiency; severe. Reduces protein stability. Ref.2 Ref.21
VAR_017081
Natural variant2461K → E in ADSL deficiency; moderate. Strongly reduced catalytic activity. Ref.17 Ref.21
VAR_007975
Natural variant2681D → N in ADSL deficiency; severe. Total loss of activity. Ref.2
VAR_017082
Natural variant3031R → C in ADSL deficiency; mild. Strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR. Abolishes cooperativity. Ref.14 Ref.17 Ref.18
VAR_007976
Natural variant3111L → V in ADSL deficiency; severe. Slightly reduced enzyme activity. Ref.19 Ref.21
VAR_017083
Natural variant3181P → L in ADSL deficiency; severe.
VAR_017084
Natural variant3641V → M in ADSL deficiency; severe. Ref.19
VAR_017085
Natural variant3741R → W in ADSL deficiency; severe.
VAR_017086
Natural variant3951S → R in ADSL deficiency; severe. Ref.17 Ref.18
VAR_007977
Natural variant3961R → C in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity. Ref.21
VAR_017087
Natural variant3961R → H in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity. Ref.19 Ref.21
VAR_017088
Natural variant4221D → Y in ADSL deficiency; moderate. Ref.16
VAR_017089
Natural variant4231L → V in ADSL deficiency; moderate.
VAR_017090
Natural variant4261R → H in ADSL deficiency; severe. Most frequent mutation. Ref.2 Ref.15 Ref.17 Ref.18 Ref.20
VAR_007978
Natural variant4301D → N in ADSL deficiency; mild. Ref.2
VAR_017091
Natural variant4381S → P in ADSL deficiency; severe. Ref.7
VAR_000680
Natural variant4471S → P in ADSL deficiency; severe.
VAR_017092
Natural variant4501T → S in ADSL deficiency; moderate. Ref.18
VAR_016932
Natural variant4521R → P in ADSL deficiency; severe. Ref.19
VAR_017093

Secondary structure

................................................................... 484
Helix Strand Turn

Details...

Sequences

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

Last modified May 30, 2000. Version 2.
Checksum: 7AA3A0A2C681FD94

FASTA48454,889
        10         20         30         40         50         60 
MAAGGDHGSP DSYRSPLASR YASPEMCFVF SDRYKFRTWR QLWLWLAEAE QTLGLPITDE 

        70         80         90        100        110        120 
QIQEMKSNLE NIDFKMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTD 

       130        140        150        160        170        180 
LIILRNALDL LLPKLARVIS RLADFAKERA SLPTLGFTHF QPAQLTTVGK RCCLWIQDLC 

       190        200        210        220        230        240 
MDLQNLKRVR DDLRFRGVKG TTGTQASFLQ LFEGDDHKVE QLDKMVTEKA GFKRAFIITG 

       250        260        270        280        290        300 
QTYTRKVDIE VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR 

       310        320        330        340        350        360 
SERCCSLARH LMTLVMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT ILNTLQNISE 

       370        380        390        400        410        420 
GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH EKIRVLSQQA ASVVKQEGGD 

       430        440        450        460        470        480 
NDLIERIQVD AYFSPIHSQL DHLLDPSSFT GRASQQVQRF LEEEVYPLLK PYESVMKVKA 


ELCL 

« Hide

Isoform 2 (Delta-ADSL) [UniParc].

Checksum: 66356963E46FDA3D
Show »

FASTA42548,328

References

« Hide 'large scale' references
[1]"Mapping of the human adenylosuccinate lyase (ADSL) gene to chromosome 22q13.1-->q13.2."
Fon E.A., Demczuk S., Delattre O., Thomas G., Rouleau G.A.
Cytogenet. Cell Genet. 64:201-203(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients."
Kmoch S., Hartmannova H., Stiburkova B., Krijt J., Zikanova M., Sebesta I.
Hum. Mol. Genet. 9:1501-1513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS ADSL DEFICIENCY VAL-3; HIS-114; GLN-190; CYS-194; ASN-268; HIS-426 AND ASN-430.
Tissue: Skeletal muscle.
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [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. expand/collapse author list , 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 (JUL-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] (ISOFORM 1).
Tissue: Eye.
[7]"A mutation in adenylosuccinate lyase associated with mental retardation and autistic features."
Stone R.L., Aimi J., Barshop B.A., Jaeken J., van den Berghe G., Zalkin H., Dixon J.E.
Nat. Genet. 1:59-63(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-484 (ISOFORM 1), VARIANT ADSL DEFICIENCY PRO-438.
[8]Bienvenut W.V., Ramsay A., Leung H.Y.
Submitted (JUN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-20 AND 235-245, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[9]"Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase."
Lee P., Colman R.F.
Protein Expr. Purif. 51:227-234(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBUNIT.
[10]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"Human adenylosuccinate lyase in complex with its substrate N6-(1,2-dicarboxyethyl)-AMP, and its products AMP and fumarate."
Structural genomics consortium (SGC)
Submitted (SEP-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; FUMARATE AND AMP.
[14]"Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation."
Ray S.P., Deaton M.K., Capodagli G.C., Calkins L.A., Sawle L., Ghosh K., Patterson D., Pegan S.D.
Biochemistry 51:6701-6713(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF WILD-TYPE AND VARIANT ADSL DEFICIENCY CYS-303, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT ADSL DEFICIENCY CYS-303, ACTIVE SITE, ENZYME REGULATION, SUBUNIT.
[15]"Adenylosuccinase deficiency presenting with epilepsy in early infancy."
Maaswinkel-Mooij P.D., Laan L.A.E.M., Onkenhout W., Brouwer O.F., Jaeken J., Poorthuis B.J.H.M.
J. Inherit. Metab. Dis. 20:606-607(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ADSL DEFICIENCY HIS-426.
[16]"Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells."
Verginelli D., Luckow B., Crifo C., Salerno C., Gross M.
Biochim. Biophys. Acta 1406:81-84(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADSL DEFICIENCY ALA-100 AND TYR-422.
[17]"Mutation analysis in adenylosuccinate lyase deficiency: eight novel mutations in the re-evaluated full ADSL coding sequence."
Marie S., Cuppens H., Heuterspreute M., Jaspers M., Tola E.Z., Gu X.X., Legius E., Vincent M.-F., Jaeken J., Cassiman J.-J., van den Berghe G.
Hum. Mutat. 13:197-202(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADSL DEFICIENCY VAL-72; TRP-141; GLN-190; GLU-246; CYS-303; ARG-395 AND HIS-426.
[18]"Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency."
Race V., Marie S., Vincent M.-F., Van den Berghe G.
Hum. Mol. Genet. 9:2159-2165(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ADSL DEFICIENCY VAL-2; LEU-26; TRP-141; CYS-303; ARG-395; HIS-426 AND SER-450.
[19]"Screening for adenylosuccinate lyase deficiency: clinical, biochemical and molecular findings in four patients."
Castro M., Perez-Cerda C., Merinero B., Garcia M.J., Bernar J., Gil Nagel A., Torres J., Bermudez M., Garavito P., Marie S., Vincent F., Van den Berghe G., Ugarte M.
Neuropediatrics 33:186-189(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADSL DEFICIENCY VAL-311; MET-364; HIS-396 AND PRO-452.
[20]"Intrafamilial variability in the phenotypic expression of adenylosuccinate lyase deficiency: a report on three patients."
Edery P., Chabrier S., Ceballos-Picot I., Marie S., Vincent M.-F., Tardieu M.
Am. J. Med. Genet. A 120:185-190(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ADSL DEFICIENCY HIS-426.
[21]"Biochemical and biophysical analysis of five disease-associated human adenylosuccinate lyase mutants."
Ariyananda Lde Z., Lee P., Antonopoulos C., Colman R.F.
Biochemistry 48:5291-5302(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ADSL DEFICIENCY CYS-194; GLU-246; VAL-311; CYS-396 AND HIS-396, ENZYME REGULATION.
+Additional computationally mapped references.

Web resources

ADSLdb

Adenylosuccinate lyase mutations database

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65867 mRNA. Translation: CAA46696.1.
X65867 mRNA. Translation: CAA46697.1. Different initiation.
AF067853 mRNA. Translation: AAC21560.1.
AF067854 mRNA. Translation: AAC21561.1.
CR456368 mRNA. Translation: CAG30254.1.
AL022238 Genomic DNA. Translation: CAI18983.1.
AL022238 Genomic DNA. Translation: CAQ08930.1.
CH471095 Genomic DNA. Translation: EAW60375.1.
BC000253 mRNA. Translation: AAH00253.1.
S60710 mRNA. Translation: AAC60603.1. Different initiation.
RefSeqNP_000017.1. NM_000026.2.
NP_001116850.1. NM_001123378.1.
UniGeneHs.75527.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J91X-ray1.80A/B/C/D1-481[»]
2VD6X-ray2.00A/B/C/D1-481[»]
4FFXX-ray2.70A/B/C/D1-484[»]
4FLCX-ray2.60A/B/C/D1-484[»]
ProteinModelPortalP30566.
SMRP30566. Positions 5-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106667. 28 interactions.
IntActP30566. 4 interactions.
STRING9606.ENSP00000216194.

PTM databases

PhosphoSiteP30566.

Polymorphism databases

DMDM6686318.

Proteomic databases

PaxDbP30566.
PeptideAtlasP30566.
PRIDEP30566.

Protocols and materials databases

DNASU158.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216194; ENSP00000216194; ENSG00000239900. [P30566-1]
ENST00000342312; ENSP00000341429; ENSG00000239900. [P30566-2]
GeneID158.
KEGGhsa:158.
UCSCuc003ayp.4. human. [P30566-1]
uc003ays.4. human. [P30566-2]

Organism-specific databases

CTD158.
GeneCardsGC22P040742.
HGNCHGNC:291. ADSL.
HPACAB019285.
HPA000525.
MIM103050. phenotype.
608222. gene.
neXtProtNX_P30566.
Orphanet46. Adenylosuccinate lyase deficiency.
PharmGKBPA24600.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0015.
HOGENOMHOG000033915.
HOVERGENHBG000214.
InParanoidP30566.
KOK01756.
OrthoDBEOG7GQXVD.
PhylomeDBP30566.
TreeFamTF106385.

Enzyme and pathway databases

BioCycMetaCyc:HS02059-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00074; UER00132.
UPA00075; UER00336.

Gene expression databases

ArrayExpressP30566.
BgeeP30566.
CleanExHS_ADSL.
GenevestigatorP30566.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
InterProIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF2. PTHR11444:SF2. 1 hit.
PfamPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SMARTSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00928. purB. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30566.
GeneWikiAdenylosuccinate_lyase.
GenomeRNAi158.
NextBio629.
PROP30566.
SOURCESearch...

Entry information

Entry namePUR8_HUMAN
AccessionPrimary (citable) accession number: P30566
Secondary accession number(s): B0QY76, O75495, Q5TI34
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 156 of the entry and version 2 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 22

Human chromosome 22: entries, gene names and cross-references to MIM