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P30520

- PURA2_HUMAN

UniProt

P30520 - PURA2_HUMAN

Protein

Adenylosuccinate synthetase isozyme 2

Gene

ADSS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (27 May 2002)
      Previous versions | rss
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    Functioni

    Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.

    Catalytic activityi

    GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.UniRule annotation

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei40 – 401Proton acceptorUniRule annotation
    Metal bindingi40 – 401MagnesiumUniRule annotation
    Binding sitei40 – 401SubstrateUniRule annotation
    Metal bindingi67 – 671Magnesium; via carbonyl oxygenUniRule annotation
    Active sitei68 – 681Proton donorUniRule annotation
    Binding sitei162 – 1621IMPUniRule annotation
    Binding sitei176 – 1761IMP; shared with dimeric partnerUniRule annotation
    Binding sitei255 – 2551IMPUniRule annotation
    Binding sitei270 – 2701IMPUniRule annotation
    Binding sitei334 – 3341IMPUniRule annotation
    Binding sitei336 – 3361GTPUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi39 – 457GTP
    Nucleotide bindingi67 – 693GTP
    Nucleotide bindingi362 – 3643GTP
    Nucleotide bindingi444 – 4474GTP

    GO - Molecular functioni

    1. adenylosuccinate synthase activity Source: UniProtKB
    2. GTP binding Source: UniProtKB
    3. magnesium ion binding Source: UniProtKB-HAMAP
    4. phosphate ion binding Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. 'de novo' AMP biosynthetic process Source: UniProtKB-UniPathway
    2. AMP biosynthetic process Source: UniProtKB
    3. aspartate metabolic process Source: Ensembl
    4. cellular response to electrical stimulus Source: Ensembl
    5. GTP catabolic process Source: Ensembl
    6. immune system process Source: UniProtKB
    7. IMP metabolic process Source: Ensembl
    8. nucleobase-containing small molecule metabolic process Source: Reactome
    9. purine nucleobase metabolic process Source: Reactome
    10. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    11. response to ammonium ion Source: Ensembl
    12. response to purine-containing compound Source: Ensembl
    13. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00075; UER00335.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylosuccinate synthetase isozyme 2UniRule annotation (EC:6.3.4.4UniRule annotation)
    Short name:
    AMPSase 2UniRule annotation
    Short name:
    AdSS 2UniRule annotation
    Alternative name(s):
    Adenylosuccinate synthetase, acidic isozymeUniRule annotation
    Adenylosuccinate synthetase, liver isozymeUniRule annotation
    Short name:
    L-type adenylosuccinate synthetaseUniRule annotation
    IMP--aspartate ligase 2UniRule annotation
    Gene namesi
    Name:ADSSUniRule annotation
    Synonyms:ADSS2UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:292. ADSS.

    Subcellular locationi

    Cytoplasm
    Note: Partially associated with particulate fractions.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 456456Adenylosuccinate synthetase isozyme 2PRO_0000095130Add
    BLAST

    Proteomic databases

    MaxQBiP30520.
    PaxDbiP30520.
    PeptideAtlasiP30520.
    PRIDEiP30520.

    PTM databases

    PhosphoSiteiP30520.

    Expressioni

    Gene expression databases

    BgeeiP30520.
    CleanExiHS_ADSS.
    GenevestigatoriP30520.

    Organism-specific databases

    HPAiHPA024400.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SMYD1Q8NB122EBI-1042898,EBI-8463848

    Protein-protein interaction databases

    BioGridi106668. 24 interactions.
    IntActiP30520. 5 interactions.
    MINTiMINT-5004177.
    STRINGi9606.ENSP00000355493.

    Structurei

    Secondary structure

    1
    456
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 3910
    Helixi43 – 519
    Beta strandi55 – 595
    Beta strandi68 – 725
    Beta strandi75 – 828
    Helixi84 – 874
    Beta strandi92 – 954
    Beta strandi99 – 1024
    Helixi103 – 11614
    Helixi118 – 1203
    Helixi123 – 1253
    Beta strandi126 – 1305
    Beta strandi134 – 1363
    Helixi138 – 14912
    Helixi166 – 1749
    Helixi181 – 1844
    Helixi188 – 20518
    Helixi213 – 22715
    Helixi228 – 2303
    Helixi234 – 24310
    Beta strandi249 – 2524
    Helixi257 – 2593
    Turni261 – 2633
    Helixi277 – 2837
    Helixi287 – 2893
    Beta strandi290 – 30718
    Helixi316 – 3249
    Turni330 – 3323
    Beta strandi337 – 3393
    Helixi343 – 35311
    Beta strandi356 – 3616
    Helixi363 – 3686
    Beta strandi370 – 38011
    Beta strandi383 – 3875
    Helixi392 – 3954
    Beta strandi399 – 4068
    Helixi418 – 4203
    Helixi423 – 43614
    Beta strandi440 – 4445
    Beta strandi446 – 4483
    Beta strandi451 – 4544

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V40X-ray1.90A21-456[»]
    ProteinModelPortaliP30520.
    SMRiP30520. Positions 26-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30520.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 434IMP bindingUniRule annotation
    Regioni65 – 684IMP bindingUniRule annotation
    Regioni330 – 3367Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the adenylosuccinate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0104.
    HOGENOMiHOG000260959.
    HOVERGENiHBG053768.
    InParanoidiP30520.
    KOiK01939.
    OMAiNARAFKE.
    OrthoDBiEOG7M6D76.
    PhylomeDBiP30520.
    TreeFamiTF300486.

    Family and domain databases

    HAMAPiMF_00011. Adenylosucc_synth.
    MF_03127. Adenylosucc_synth_vert_acid.
    InterProiIPR018220. Adenylosuccinate_synthase_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027529. AdSS_2_vert.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11846. PTHR11846. 1 hit.
    PfamiPF00709. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SMARTiSM00788. Adenylsucc_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00184. purA. 1 hit.
    PROSITEiPS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
    PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P30520-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL    50
    AQDADIVCRC QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV 100
    IHLPGLFEEA EKNVQKGKGL EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ 150
    RQEQAGKNLG TTKKGIGPVY SSKAARSGLR MCDLVSDFDG FSERFKVLAN 200
    QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE ALHGPPKKIL 250
    VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY 300
    TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH 350
    MINGFTALAL TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV 400
    QYKTLPGWNT DISNARAFKE LPVNAQNYVR FIEDELQIPV KWIGVGKSRE 450
    SMIQLF 456
    Length:456
    Mass (Da):50,097
    Last modified:May 27, 2002 - v3
    Checksum:i23B7AAC58A238783
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 252RP → A in CAA47123. (PubMed:1592113)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791L → F.
    Corresponds to variant rs12134870 [ dbSNP | Ensembl ].
    VAR_051881

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66503 Genomic DNA. Translation: CAA47123.1.
    AL591594, AL645465 Genomic DNA. Translation: CAI14037.1.
    AL645465, AL591594 Genomic DNA. Translation: CAI15031.1.
    CH471148 Genomic DNA. Translation: EAW77102.1.
    BC012356 mRNA. Translation: AAH12356.1.
    CCDSiCCDS1624.1.
    PIRiS21166.
    RefSeqiNP_001117.2. NM_001126.3.
    UniGeneiHs.498313.

    Genome annotation databases

    EnsembliENST00000366535; ENSP00000355493; ENSG00000035687.
    GeneIDi159.
    KEGGihsa:159.
    UCSCiuc001iaj.3. human.

    Polymorphism databases

    DMDMi21264498.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66503 Genomic DNA. Translation: CAA47123.1 .
    AL591594 , AL645465 Genomic DNA. Translation: CAI14037.1 .
    AL645465 , AL591594 Genomic DNA. Translation: CAI15031.1 .
    CH471148 Genomic DNA. Translation: EAW77102.1 .
    BC012356 mRNA. Translation: AAH12356.1 .
    CCDSi CCDS1624.1.
    PIRi S21166.
    RefSeqi NP_001117.2. NM_001126.3.
    UniGenei Hs.498313.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V40 X-ray 1.90 A 21-456 [» ]
    ProteinModelPortali P30520.
    SMRi P30520. Positions 26-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106668. 24 interactions.
    IntActi P30520. 5 interactions.
    MINTi MINT-5004177.
    STRINGi 9606.ENSP00000355493.

    Chemistry

    BindingDBi P30520.
    ChEMBLi CHEMBL4875.
    DrugBanki DB00128. L-Aspartic Acid.

    PTM databases

    PhosphoSitei P30520.

    Polymorphism databases

    DMDMi 21264498.

    Proteomic databases

    MaxQBi P30520.
    PaxDbi P30520.
    PeptideAtlasi P30520.
    PRIDEi P30520.

    Protocols and materials databases

    DNASUi 159.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366535 ; ENSP00000355493 ; ENSG00000035687 .
    GeneIDi 159.
    KEGGi hsa:159.
    UCSCi uc001iaj.3. human.

    Organism-specific databases

    CTDi 159.
    GeneCardsi GC01M244571.
    HGNCi HGNC:292. ADSS.
    HPAi HPA024400.
    MIMi 103060. gene.
    neXtProti NX_P30520.
    PharmGKBi PA24601.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0104.
    HOGENOMi HOG000260959.
    HOVERGENi HBG053768.
    InParanoidi P30520.
    KOi K01939.
    OMAi NARAFKE.
    OrthoDBi EOG7M6D76.
    PhylomeDBi P30520.
    TreeFami TF300486.

    Enzyme and pathway databases

    UniPathwayi UPA00075 ; UER00335 .
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei P30520.
    GenomeRNAii 159.
    NextBioi 633.
    PROi P30520.
    SOURCEi Search...

    Gene expression databases

    Bgeei P30520.
    CleanExi HS_ADSS.
    Genevestigatori P30520.

    Family and domain databases

    HAMAPi MF_00011. Adenylosucc_synth.
    MF_03127. Adenylosucc_synth_vert_acid.
    InterProi IPR018220. Adenylosuccinate_synthase_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027529. AdSS_2_vert.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR11846. PTHR11846. 1 hit.
    Pfami PF00709. Adenylsucc_synt. 1 hit.
    [Graphical view ]
    SMARTi SM00788. Adenylsucc_synt. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00184. purA. 1 hit.
    PROSITEi PS01266. ADENYLOSUCCIN_SYN_1. 1 hit.
    PS00513. ADENYLOSUCCIN_SYN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase."
      Powell S.M., Zalkin H., Dixon J.E.
      FEBS Lett. 303:4-10(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    2. Stone R.L.
      Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Eye.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Human adenylosuccinate synthetase isozyme 2 in complex with GDP."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-456 IN COMPLEX WITH GDP.

    Entry informationi

    Entry nameiPURA2_HUMAN
    AccessioniPrimary (citable) accession number: P30520
    Secondary accession number(s): B1AQM5, Q96EG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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

    Dasty 3