Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8N142

- PURA1_HUMAN

UniProt

Q8N142 - PURA1_HUMAN

Protein

Adenylosuccinate synthetase isozyme 1

Gene

ADSSL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP By similarity.By similarity

    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 sitei43 – 431Proton acceptorUniRule annotation
    Metal bindingi43 – 431MagnesiumUniRule annotation
    Binding sitei43 – 431SubstrateUniRule annotation
    Metal bindingi70 – 701Magnesium; via carbonyl oxygenUniRule annotation
    Active sitei71 – 711Proton donorUniRule annotation
    Binding sitei163 – 1631IMPUniRule annotation
    Binding sitei177 – 1771IMP; shared with dimeric partnerUniRule annotation
    Binding sitei256 – 2561IMPUniRule annotation
    Binding sitei271 – 2711IMPUniRule annotation
    Binding sitei335 – 3351IMPUniRule annotation
    Binding sitei337 – 3371GTPUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi42 – 487GTPUniRule annotation
    Nucleotide bindingi70 – 723GTPUniRule annotation
    Nucleotide bindingi363 – 3653GTPUniRule annotation
    Nucleotide bindingi445 – 4484GTPUniRule annotation

    GO - Molecular functioni

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

    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 drug Source: Ensembl
    5. cellular response to electrical stimulus Source: Ensembl
    6. glutamine metabolic process Source: Ensembl
    7. immune system process Source: UniProtKB
    8. IMP metabolic process Source: Ensembl
    9. nucleobase-containing small molecule metabolic process Source: Reactome
    10. purine nucleobase metabolic process Source: Reactome
    11. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    12. response to muscle activity Source: Ensembl
    13. response to starvation Source: Ensembl
    14. 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

    BRENDAi6.3.4.4. 2681.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00075; UER00335.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylosuccinate synthetase isozyme 1UniRule annotation (EC:6.3.4.4UniRule annotation)
    Short name:
    AMPSase 1UniRule annotation
    Short name:
    AdSS 1UniRule annotation
    Alternative name(s):
    Adenylosuccinate synthetase, basic isozymeUniRule annotation
    Adenylosuccinate synthetase, muscle isozymeUniRule annotation
    Short name:
    M-type adenylosuccinate synthetaseUniRule annotation
    IMP--aspartate ligase 1UniRule annotation
    Gene namesi
    Name:ADSSL1UniRule annotation
    Synonyms:ADSS1UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:20093. ADSSL1.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134974111.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 457457Adenylosuccinate synthetase isozyme 1PRO_0000095132Add
    BLAST

    Proteomic databases

    MaxQBiQ8N142.
    PaxDbiQ8N142.
    PRIDEiQ8N142.

    PTM databases

    PhosphoSiteiQ8N142.

    Expressioni

    Tissue specificityi

    Predominantly expressed in skeletal muscle and heart, as well as in several hematopoietic cell lines and solid tumors.1 Publication

    Gene expression databases

    ArrayExpressiQ8N142.
    BgeeiQ8N142.
    CleanExiHS_ADSSL1.
    GenevestigatoriQ8N142.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    BioGridi125783. 2 interactions.
    IntActiQ8N142. 3 interactions.
    MINTiMINT-3319213.
    STRINGi9606.ENSP00000333019.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GJOmodel-A27-457[»]
    ProteinModelPortaliQ8N142.
    SMRiQ8N142. Positions 27-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 464IMP bindingUniRule annotation
    Regioni68 – 714IMP bindingUniRule annotation
    Regioni331 – 3377Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the adenylosuccinate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0104.
    HOGENOMiHOG000260959.
    HOVERGENiHBG053768.
    KOiK01939.
    OMAiNGAVIHV.
    OrthoDBiEOG7M6D76.
    PhylomeDBiQ8N142.
    TreeFamiTF300486.

    Family and domain databases

    HAMAPiMF_00011. Adenylosucc_synth.
    MF_03126. Adenylosucc_synth_vert_basic.
    InterProiIPR018220. Adenylosuccinate_synthase_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027509. AdSS_1_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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N142-1) [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

    MSGTRASNDR PPGAGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV    50
    DLLATDADII SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN 100
    GVVIHLPGLF EEAEKNEKKG LKDWEKRLII SDRAHLVFDF HQAVDGLQEV 150
    QRQAQEGKNI GTTKKGIGPT YSSKAARTGL RICDLLSDFD EFSSRFKNLA 200
    HQHQSMFPTL EIDIEGQLKR LKGFAERIRP MVRDGVYFMY EALHGPPKKI 250
    LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA 300
    YTTRVGIGAF PTEQINEIGG LLQTRGHEWG VTTGRKRRCG WLDLMILRYA 350
    HMVNGFTALA LTKLDILDVL GEVKVGVSYK LNGKRIPYFP ANQEMLQKVE 400
    VEYETLPGWK ADTTGARRWE DLPPQAQNYI RFVENHVGVA VKWVGVGKSR 450
    ESMIQLF 457
    Length:457
    Mass (Da):50,208
    Last modified:October 1, 2002 - v1
    Checksum:i387341D49721B2EF
    GO
    Isoform 2 (identifier: Q8N142-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-64: MSGTRASNDR...TDADIISRCQ → MVGRSCGVAT...AGSLTPGGER

    Note: No experimental confirmation available.

    Show »
    Length:500
    Mass (Da):54,562
    Checksum:i9C561192088BDAAF
    GO

    Sequence cautioni

    The sequence AAH32039.1 differs from that shown. Reason: Frameshift at position 1.
    The sequence CAD62614.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6464MSGTR…ISRCQ → MVGRSCGVATQRQGGGQRPT NLALTLSSSPAHSTALPWLP PRSLQLLSGHSVPAQPTPHL PSACGGPTRVTLGEERAWRS HGSNAGGHTCLPRRTAGAGS LTPGGER in isoform 2. 1 PublicationVSP_008421Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY037159 mRNA. Translation: AAK67646.1.
    AK095921 mRNA. Translation: BAC04649.1.
    BX248286 mRNA. Translation: CAD62614.1. Different initiation.
    BC032039 mRNA. Translation: AAH32039.1. Frameshift.
    BC047904 mRNA. Translation: AAH47904.1.
    CCDSiCCDS9990.1. [Q8N142-1]
    CCDS9991.1. [Q8N142-2]
    RefSeqiNP_689541.1. NM_152328.3. [Q8N142-1]
    NP_954634.1. NM_199165.1. [Q8N142-2]
    UniGeneiHs.592327.

    Genome annotation databases

    EnsembliENST00000330877; ENSP00000331260; ENSG00000185100. [Q8N142-1]
    ENST00000332972; ENSP00000333019; ENSG00000185100. [Q8N142-2]
    GeneIDi122622.
    KEGGihsa:122622.
    UCSCiuc001ypd.3. human. [Q8N142-1]
    uc001ype.3. human. [Q8N142-2]

    Polymorphism databases

    DMDMi37537958.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY037159 mRNA. Translation: AAK67646.1 .
    AK095921 mRNA. Translation: BAC04649.1 .
    BX248286 mRNA. Translation: CAD62614.1 . Different initiation.
    BC032039 mRNA. Translation: AAH32039.1 . Frameshift.
    BC047904 mRNA. Translation: AAH47904.1 .
    CCDSi CCDS9990.1. [Q8N142-1 ]
    CCDS9991.1. [Q8N142-2 ]
    RefSeqi NP_689541.1. NM_152328.3. [Q8N142-1 ]
    NP_954634.1. NM_199165.1. [Q8N142-2 ]
    UniGenei Hs.592327.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GJO model - A 27-457 [» ]
    ProteinModelPortali Q8N142.
    SMRi Q8N142. Positions 27-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125783. 2 interactions.
    IntActi Q8N142. 3 interactions.
    MINTi MINT-3319213.
    STRINGi 9606.ENSP00000333019.

    Chemistry

    DrugBanki DB00128. L-Aspartic Acid.

    PTM databases

    PhosphoSitei Q8N142.

    Polymorphism databases

    DMDMi 37537958.

    Proteomic databases

    MaxQBi Q8N142.
    PaxDbi Q8N142.
    PRIDEi Q8N142.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330877 ; ENSP00000331260 ; ENSG00000185100 . [Q8N142-1 ]
    ENST00000332972 ; ENSP00000333019 ; ENSG00000185100 . [Q8N142-2 ]
    GeneIDi 122622.
    KEGGi hsa:122622.
    UCSCi uc001ypd.3. human. [Q8N142-1 ]
    uc001ype.3. human. [Q8N142-2 ]

    Organism-specific databases

    CTDi 122622.
    GeneCardsi GC14P105190.
    HGNCi HGNC:20093. ADSSL1.
    MIMi 612498. gene.
    neXtProti NX_Q8N142.
    PharmGKBi PA134974111.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0104.
    HOGENOMi HOG000260959.
    HOVERGENi HBG053768.
    KOi K01939.
    OMAi NGAVIHV.
    OrthoDBi EOG7M6D76.
    PhylomeDBi Q8N142.
    TreeFami TF300486.

    Enzyme and pathway databases

    UniPathwayi UPA00075 ; UER00335 .
    BRENDAi 6.3.4.4. 2681.
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    GenomeRNAii 122622.
    NextBioi 80937.
    PROi Q8N142.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N142.
    Bgeei Q8N142.
    CleanExi HS_ADSSL1.
    Genevestigatori Q8N142.

    Family and domain databases

    HAMAPi MF_00011. Adenylosucc_synth.
    MF_03126. Adenylosucc_synth_vert_basic.
    InterProi IPR018220. Adenylosuccinate_synthase_AS.
    IPR001114. Adenylosuccinate_synthetase.
    IPR027509. AdSS_1_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. "Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells."
      Sun H., Li N., Wang X., Chen T., Shi L., Zhang L., Wang J., Wan T., Cao X.
      Mol. Cell. Biochem. 269:85-94(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Bone marrow stroma.
    2. "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.
      , 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] (ISOFORM 1).
      Tissue: Heart.
    3. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    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] (ISOFORMS 1 AND 2).
      Tissue: Testis.

    Entry informationi

    Entry nameiPURA1_HUMAN
    AccessioniPrimary (citable) accession number: Q8N142
    Secondary accession number(s): Q86TT6, Q8N714
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3