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P54822

- PUR8_MOUSE

UniProt

P54822 - PUR8_MOUSE

Protein

Adenylosuccinate lyase

Gene

Adsl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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.By similarity

    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.

    Pathwayi

    Sites

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

    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: MGI

    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: MGI
    5. protein tetramerization Source: Ensembl
    6. response to hypoxia Source: Ensembl
    7. response to muscle activity Source: Ensembl
    8. response to nutrient Source: Ensembl
    9. response to starvation Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    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:Adl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:103202. Adsl.

    Subcellular locationi

    GO - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 484483Adenylosuccinate lyasePRO_0000137894Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei147 – 1471N6-acetyllysineBy similarity
    Modified residuei295 – 2951N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP54822.
    PaxDbiP54822.
    PRIDEiP54822.

    PTM databases

    PhosphoSiteiP54822.

    Expressioni

    Gene expression databases

    ArrayExpressiP54822.
    BgeeiP54822.
    CleanExiMM_ADSL.
    GenevestigatoriP54822.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi198009. 1 interaction.
    IntActiP54822. 3 interactions.
    MINTiMINT-4109237.
    STRINGi10090.ENSMUSP00000023043.

    Structurei

    3D structure databases

    ProteinModelPortaliP54822.
    SMRiP54822. Positions 5-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0015.
    GeneTreeiENSGT00390000013486.
    HOGENOMiHOG000033915.
    HOVERGENiHBG000214.
    InParanoidiQ8VCD4.
    KOiK01756.
    OMAiMAHVHAY.
    OrthoDBiEOG7GQXVD.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P54822-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE    50
    QTLGLPITDE QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP 100
    KAAGIIHLGA TSCYVGDNTD LIILRNAFDL LLPKLARVIS RLADFAKDRA 150
    DLPTLGFTHF QPAQLTTVGK RCCLWIQDLC MDLQNLKRVR DELRFRGVKG 200
    TTGTQASFLQ LFEGDHQKVE QLDKMVTEKA GFKRAFIITG QTYTRKVDIE 250
    VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR 300
    SERCCSLARH LMALTMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT 350
    ILNTLQNISE GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH 400
    EKIRVLSQQA AAVVKQEGGD NDLIERIRAD AYFSPIHSQL EHLLDPSSFT 450
    GRAPQQVHRF LEEEVRPLLK PYGNEMAVKA ELCL 484
    Length:484
    Mass (Da):54,866
    Last modified:July 27, 2011 - v2
    Checksum:i9F11689AD41D1453
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti179 – 1802LC → SV in AAB60684. (PubMed:8530047)Curated
    Sequence conflicti192 – 1932EL → DV in AAB60684. (PubMed:8530047)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20225 mRNA. Translation: AAB60684.1.
    AK049372 mRNA. Translation: BAC33717.1.
    AK051111 mRNA. Translation: BAC34529.1.
    AK152092 mRNA. Translation: BAE30940.1.
    AK168906 mRNA. Translation: BAE40720.1.
    AK171725 mRNA. Translation: BAE42633.1.
    CH466550 Genomic DNA. Translation: EDL04592.1.
    BC020187 mRNA. Translation: AAH20187.1.
    CCDSiCCDS27664.1.
    RefSeqiNP_033764.2. NM_009634.6.
    UniGeneiMm.38151.

    Genome annotation databases

    EnsembliENSMUST00000023043; ENSMUSP00000023043; ENSMUSG00000022407.
    GeneIDi11564.
    KEGGimmu:11564.
    UCSCiuc007wvz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20225 mRNA. Translation: AAB60684.1 .
    AK049372 mRNA. Translation: BAC33717.1 .
    AK051111 mRNA. Translation: BAC34529.1 .
    AK152092 mRNA. Translation: BAE30940.1 .
    AK168906 mRNA. Translation: BAE40720.1 .
    AK171725 mRNA. Translation: BAE42633.1 .
    CH466550 Genomic DNA. Translation: EDL04592.1 .
    BC020187 mRNA. Translation: AAH20187.1 .
    CCDSi CCDS27664.1.
    RefSeqi NP_033764.2. NM_009634.6.
    UniGenei Mm.38151.

    3D structure databases

    ProteinModelPortali P54822.
    SMRi P54822. Positions 5-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198009. 1 interaction.
    IntActi P54822. 3 interactions.
    MINTi MINT-4109237.
    STRINGi 10090.ENSMUSP00000023043.

    PTM databases

    PhosphoSitei P54822.

    Proteomic databases

    MaxQBi P54822.
    PaxDbi P54822.
    PRIDEi P54822.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023043 ; ENSMUSP00000023043 ; ENSMUSG00000022407 .
    GeneIDi 11564.
    KEGGi mmu:11564.
    UCSCi uc007wvz.1. mouse.

    Organism-specific databases

    CTDi 158.
    MGIi MGI:103202. Adsl.

    Phylogenomic databases

    eggNOGi COG0015.
    GeneTreei ENSGT00390000013486.
    HOGENOMi HOG000033915.
    HOVERGENi HBG000214.
    InParanoidi Q8VCD4.
    KOi K01756.
    OMAi MAHVHAY.
    OrthoDBi EOG7GQXVD.
    TreeFami TF106385.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00132 .
    UPA00075 ; UER00336 .

    Miscellaneous databases

    NextBioi 279062.
    PROi P54822.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54822.
    Bgeei P54822.
    CleanExi MM_ADSL.
    Genevestigatori P54822.

    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. "Characterization of the cDNA and the gene encoding murine adenylosuccinate lyase."
      Wong L.J., O'Brien W.E.
      Genomics 28:341-343(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129.
      Tissue: Kidney.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Kidney and Spleen.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Strain: FVB/N.
      Tissue: Salivary gland.

    Entry informationi

    Entry nameiPUR8_MOUSE
    AccessioniPrimary (citable) accession number: P54822
    Secondary accession number(s): Q8VCD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3