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P30566

- PUR8_HUMAN

UniProt

P30566 - PUR8_HUMAN

Protein

Adenylosuccinate lyase

Gene

ADSL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    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 activityi

    N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
    (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

    Enzyme regulationi

    The enzyme reaction kinetics indicate cooperativity between subunits.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei159 – 1591Proton donor/acceptor1 Publication
    Binding sitei241 – 2411Substrate
    Active sitei289 – 2891Proton donor/acceptor1 Publication
    Binding sitei303 – 3031Substrate; shared with neighboring subunit
    Binding sitei329 – 3291Substrate
    Binding sitei334 – 3341Substrate
    Binding sitei338 – 3381Substrate

    GO - Molecular functioni

    1. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Source: UniProtKB-EC
    2. N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Source: UniProtKB

    GO - Biological processi

    1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
    2. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    3. aerobic respiration Source: Ensembl
    4. AMP biosynthetic process Source: UniProtKB
    5. metabolic process Source: GOC
    6. nucleobase-containing small molecule metabolic process Source: Reactome
    7. protein tetramerization Source: UniProtKB
    8. purine nucleobase metabolic process Source: Reactome
    9. purine nucleotide biosynthetic process Source: UniProtKB
    10. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    11. response to hypoxia Source: Ensembl
    12. response to muscle activity Source: Ensembl
    13. response to nutrient Source: Ensembl
    14. response to starvation Source: Ensembl
    15. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02059-MONOMER.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00074; UER00132.
    UPA00075; UER00336.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylosuccinate lyase (EC:4.3.2.2)
    Short name:
    ASL
    Alternative name(s):
    Adenylosuccinase
    Short name:
    ASase
    Gene namesi
    Name:ADSL
    Synonyms:AMPS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:291. ADSL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Involvement in diseasei

    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.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21A → V in ADSL deficiency; severe.
    Corresponds to variant rs143083947 [ dbSNP | Ensembl ].
    VAR_016930
    Natural varianti3 – 31A → V in ADSL deficiency; severe. 1 Publication
    VAR_017078
    Natural varianti26 – 261M → L in ADSL deficiency; severe.
    VAR_016931
    Natural varianti72 – 721I → V in ADSL deficiency; severe. 1 Publication
    VAR_007972
    Natural varianti100 – 1001P → A in ADSL deficiency; moderate. 1 Publication
    VAR_017079
    Natural varianti114 – 1141Y → H in ADSL deficiency; severe. Total loss of activity. 1 Publication
    VAR_017080
    Natural varianti141 – 1411R → W in ADSL deficiency; severe. 1 Publication
    VAR_007973
    Natural varianti190 – 1901R → Q in ADSL deficiency; moderate. 2 Publications
    Corresponds to variant rs28941471 [ dbSNP | Ensembl ].
    VAR_007974
    Natural varianti194 – 1941R → C in ADSL deficiency; severe. Reduces protein stability. 1 Publication
    VAR_017081
    Natural varianti246 – 2461K → E in ADSL deficiency; moderate. Strongly reduced catalytic activity. 1 Publication
    VAR_007975
    Natural varianti268 – 2681D → N in ADSL deficiency; severe. Total loss of activity. 1 Publication
    VAR_017082
    Natural varianti303 – 3031R → C in ADSL deficiency; mild. Strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR. Abolishes cooperativity. 1 Publication
    VAR_007976
    Natural varianti311 – 3111L → V in ADSL deficiency; severe. Slightly reduced enzyme activity. 1 Publication
    VAR_017083
    Natural varianti318 – 3181P → L in ADSL deficiency; severe.
    VAR_017084
    Natural varianti364 – 3641V → M in ADSL deficiency; severe. 1 Publication
    VAR_017085
    Natural varianti374 – 3741R → W in ADSL deficiency; severe.
    VAR_017086
    Natural varianti395 – 3951S → R in ADSL deficiency; severe. 1 Publication
    VAR_007977
    Natural varianti396 – 3961R → C in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity.
    VAR_017087
    Natural varianti396 – 3961R → H in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity. 1 Publication
    VAR_017088
    Natural varianti422 – 4221D → Y in ADSL deficiency; moderate. 1 Publication
    VAR_017089
    Natural varianti423 – 4231L → V in ADSL deficiency; moderate.
    VAR_017090
    Natural varianti426 – 4261R → H in ADSL deficiency; severe. Most frequent mutation. 4 Publications
    VAR_007978
    Natural varianti430 – 4301D → N in ADSL deficiency; mild. 1 Publication
    VAR_017091
    Natural varianti438 – 4381S → P in ADSL deficiency; severe. 1 Publication
    VAR_000680
    Natural varianti447 – 4471S → P in ADSL deficiency; severe.
    VAR_017092
    Natural varianti450 – 4501T → S in ADSL deficiency; moderate.
    VAR_016932
    Natural varianti452 – 4521R → P in ADSL deficiency; severe. 1 Publication
    VAR_017093

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi103050. phenotype.
    Orphaneti46. Adenylosuccinate lyase deficiency.
    PharmGKBiPA24600.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 484483Adenylosuccinate lyasePRO_0000137892Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei147 – 1471N6-acetyllysine1 Publication
    Modified residuei295 – 2951N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30566.
    PaxDbiP30566.
    PeptideAtlasiP30566.
    PRIDEiP30566.

    PTM databases

    PhosphoSiteiP30566.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP30566.
    BgeeiP30566.
    CleanExiHS_ADSL.
    GenevestigatoriP30566.

    Organism-specific databases

    HPAiCAB019285.
    HPA000525.

    Interactioni

    Subunit structurei

    Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.2 Publications

    Protein-protein interaction databases

    BioGridi106667. 28 interactions.
    IntActiP30566. 4 interactions.
    STRINGi9606.ENSP00000216194.

    Structurei

    Secondary structure

    1
    484
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 194
    Helixi24 – 296
    Helixi32 – 5322
    Helixi59 – 668
    Beta strandi68 – 703
    Helixi74 – 8411
    Helixi87 – 9812
    Turni100 – 1023
    Helixi103 – 1053
    Turni106 – 1094
    Helixi113 – 14836
    Turni149 – 1513
    Beta strandi153 – 1586
    Beta strandi161 – 1677
    Helixi168 – 19225
    Beta strandi201 – 2044
    Helixi206 – 2116
    Turni212 – 2143
    Helixi216 – 22914
    Beta strandi240 – 2423
    Helixi246 – 27429
    Beta strandi277 – 2793
    Helixi299 – 31315
    Helixi316 – 3238
    Helixi331 – 3333
    Helixi334 – 36027
    Helixi366 – 38015
    Helixi382 – 3898
    Helixi396 – 41621
    Helixi423 – 4297
    Helixi431 – 4333
    Helixi434 – 4374
    Helixi440 – 4434
    Helixi446 – 4494
    Helixi453 – 46311
    Helixi465 – 4695
    Helixi470 – 4723

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP30566.
    SMRiP30566. Positions 5-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30566.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 212Substrate binding; shared with neighboring subunit
    Regioni85 – 873Substrate binding
    Regioni111 – 1122Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0015.
    HOGENOMiHOG000033915.
    HOVERGENiHBG000214.
    InParanoidiP30566.
    KOiK01756.
    OrthoDBiEOG7GQXVD.
    PhylomeDBiP30566.
    TreeFamiTF106385.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    InterProiIPR019468. 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]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF10397. ADSL_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SMARTiSM00998. ADSL_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00928. purB. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30566-1) [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

    MAAGGDHGSP DSYRSPLASR YASPEMCFVF SDRYKFRTWR QLWLWLAEAE    50
    QTLGLPITDE QIQEMKSNLE NIDFKMAAEE EKRLRHDVMA HVHTFGHCCP 100
    KAAGIIHLGA TSCYVGDNTD LIILRNALDL LLPKLARVIS RLADFAKERA 150
    SLPTLGFTHF QPAQLTTVGK RCCLWIQDLC MDLQNLKRVR DDLRFRGVKG 200
    TTGTQASFLQ LFEGDDHKVE QLDKMVTEKA GFKRAFIITG QTYTRKVDIE 250
    VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR 300
    SERCCSLARH LMTLVMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT 350
    ILNTLQNISE GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH 400
    EKIRVLSQQA ASVVKQEGGD NDLIERIQVD AYFSPIHSQL DHLLDPSSFT 450
    GRASQQVQRF LEEEVYPLLK PYESVMKVKA ELCL 484
    Length:484
    Mass (Da):54,889
    Last modified:May 30, 2000 - v2
    Checksum:i7AA3A0A2C681FD94
    GO
    Isoform 2 (identifier: P30566-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta-ADSL

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

    Note: Lacks enzymatic activity.

    Show »
    Length:425
    Mass (Da):48,328
    Checksum:i66356963E46FDA3D
    GO

    Sequence cautioni

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21A → V in ADSL deficiency; severe.
    Corresponds to variant rs143083947 [ dbSNP | Ensembl ].
    VAR_016930
    Natural varianti3 – 31A → V in ADSL deficiency; severe. 1 Publication
    VAR_017078
    Natural varianti26 – 261M → L in ADSL deficiency; severe.
    VAR_016931
    Natural varianti31 – 311S → N.
    Corresponds to variant rs5757921 [ dbSNP | Ensembl ].
    VAR_037883
    Natural varianti72 – 721I → V in ADSL deficiency; severe. 1 Publication
    VAR_007972
    Natural varianti100 – 1001P → A in ADSL deficiency; moderate. 1 Publication
    VAR_017079
    Natural varianti114 – 1141Y → H in ADSL deficiency; severe. Total loss of activity. 1 Publication
    VAR_017080
    Natural varianti141 – 1411R → W in ADSL deficiency; severe. 1 Publication
    VAR_007973
    Natural varianti147 – 1471K → M.
    Corresponds to variant rs11089991 [ dbSNP | Ensembl ].
    VAR_037884
    Natural varianti190 – 1901R → Q in ADSL deficiency; moderate. 2 Publications
    Corresponds to variant rs28941471 [ dbSNP | Ensembl ].
    VAR_007974
    Natural varianti194 – 1941R → C in ADSL deficiency; severe. Reduces protein stability. 1 Publication
    VAR_017081
    Natural varianti246 – 2461K → E in ADSL deficiency; moderate. Strongly reduced catalytic activity. 1 Publication
    VAR_007975
    Natural varianti268 – 2681D → N in ADSL deficiency; severe. Total loss of activity. 1 Publication
    VAR_017082
    Natural varianti303 – 3031R → C in ADSL deficiency; mild. Strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR. Abolishes cooperativity. 1 Publication
    VAR_007976
    Natural varianti311 – 3111L → V in ADSL deficiency; severe. Slightly reduced enzyme activity. 1 Publication
    VAR_017083
    Natural varianti318 – 3181P → L in ADSL deficiency; severe.
    VAR_017084
    Natural varianti364 – 3641V → M in ADSL deficiency; severe. 1 Publication
    VAR_017085
    Natural varianti374 – 3741R → W in ADSL deficiency; severe.
    VAR_017086
    Natural varianti395 – 3951S → R in ADSL deficiency; severe. 1 Publication
    VAR_007977
    Natural varianti396 – 3961R → C in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity.
    VAR_017087
    Natural varianti396 – 3961R → H in ADSL deficiency; severe. Abolishes cooperativity and reduces enzyme activity. 1 Publication
    VAR_017088
    Natural varianti422 – 4221D → Y in ADSL deficiency; moderate. 1 Publication
    VAR_017089
    Natural varianti423 – 4231L → V in ADSL deficiency; moderate.
    VAR_017090
    Natural varianti426 – 4261R → H in ADSL deficiency; severe. Most frequent mutation. 4 Publications
    VAR_007978
    Natural varianti430 – 4301D → N in ADSL deficiency; mild. 1 Publication
    VAR_017091
    Natural varianti438 – 4381S → P in ADSL deficiency; severe. 1 Publication
    VAR_000680
    Natural varianti447 – 4471S → P in ADSL deficiency; severe.
    VAR_017092
    Natural varianti450 – 4501T → S in ADSL deficiency; moderate.
    VAR_016932
    Natural varianti452 – 4521R → P in ADSL deficiency; severe. 1 Publication
    VAR_017093

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei398 – 45659Missing in isoform 2. 2 PublicationsVSP_000318Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14001.1. [P30566-1]
    CCDS46714.1. [P30566-2]
    RefSeqiNP_000017.1. NM_000026.2. [P30566-1]
    NP_001116850.1. NM_001123378.1. [P30566-2]
    UniGeneiHs.75527.

    Genome annotation databases

    EnsembliENST00000216194; ENSP00000216194; ENSG00000239900. [P30566-1]
    ENST00000342312; ENSP00000341429; ENSG00000239900. [P30566-2]
    GeneIDi158.
    KEGGihsa:158.
    UCSCiuc003ayp.4. human. [P30566-1]
    uc003ays.4. human. [P30566-2]

    Polymorphism databases

    DMDMi6686318.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    ADSLdb

    Adenylosuccinate lyase mutations database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS14001.1. [P30566-1 ]
    CCDS46714.1. [P30566-2 ]
    RefSeqi NP_000017.1. NM_000026.2. [P30566-1 ]
    NP_001116850.1. NM_001123378.1. [P30566-2 ]
    UniGenei Hs.75527.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2J91 X-ray 1.80 A/B/C/D 1-481 [» ]
    2VD6 X-ray 2.00 A/B/C/D 1-481 [» ]
    4FFX X-ray 2.70 A/B/C/D 1-484 [» ]
    4FLC X-ray 2.60 A/B/C/D 1-484 [» ]
    ProteinModelPortali P30566.
    SMRi P30566. Positions 5-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106667. 28 interactions.
    IntActi P30566. 4 interactions.
    STRINGi 9606.ENSP00000216194.

    PTM databases

    PhosphoSitei P30566.

    Polymorphism databases

    DMDMi 6686318.

    Proteomic databases

    MaxQBi P30566.
    PaxDbi P30566.
    PeptideAtlasi P30566.
    PRIDEi P30566.

    Protocols and materials databases

    DNASUi 158.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216194 ; ENSP00000216194 ; ENSG00000239900 . [P30566-1 ]
    ENST00000342312 ; ENSP00000341429 ; ENSG00000239900 . [P30566-2 ]
    GeneIDi 158.
    KEGGi hsa:158.
    UCSCi uc003ayp.4. human. [P30566-1 ]
    uc003ays.4. human. [P30566-2 ]

    Organism-specific databases

    CTDi 158.
    GeneCardsi GC22P040742.
    HGNCi HGNC:291. ADSL.
    HPAi CAB019285.
    HPA000525.
    MIMi 103050. phenotype.
    608222. gene.
    neXtProti NX_P30566.
    Orphaneti 46. Adenylosuccinate lyase deficiency.
    PharmGKBi PA24600.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0015.
    HOGENOMi HOG000033915.
    HOVERGENi HBG000214.
    InParanoidi P30566.
    KOi K01756.
    OrthoDBi EOG7GQXVD.
    PhylomeDBi P30566.
    TreeFami TF106385.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00132 .
    UPA00075 ; UER00336 .
    BioCyci MetaCyc:HS02059-MONOMER.
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei P30566.
    GeneWikii Adenylosuccinate_lyase.
    GenomeRNAii 158.
    NextBioi 629.
    PROi P30566.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30566.
    Bgeei P30566.
    CleanExi HS_ADSL.
    Genevestigatori P30566.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    InterProi IPR019468. 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 ]
    PANTHERi PTHR11444. PTHR11444. 1 hit.
    Pfami PF10397. ADSL_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00149. FUMRATELYASE.
    SMARTi SM00998. ADSL_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR00928. purB. 1 hit.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiPUR8_HUMAN
    AccessioniPrimary (citable) accession number: P30566
    Secondary accession number(s): B0QY76, O75495, Q5TI34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 161 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 22
      Human chromosome 22: 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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