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P08243

- ASNS_HUMAN

UniProt

P08243 - ASNS_HUMAN

Protein

Asparagine synthetase [glutamine-hydrolyzing]

Gene

ASNS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21For GATase activity2 Publications
    Binding sitei97 – 971GlutamineBy similarity
    Binding sitei256 – 2561ATP; via carbonyl oxygenBy similarity
    Binding sitei288 – 2881ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Sitei365 – 3651Important for beta-aspartyl-AMP intermediate formationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi363 – 3642ATPBy similarity

    GO - Molecular functioni

    1. asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. cofactor binding Source: Ensembl

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. asparagine biosynthetic process Source: UniProtKB
    3. cellular amino acid biosynthetic process Source: Reactome
    4. cellular nitrogen compound metabolic process Source: Reactome
    5. cellular protein metabolic process Source: Reactome
    6. cellular response to glucose starvation Source: UniProtKB
    7. cellular response to hormone stimulus Source: Ensembl
    8. endoplasmic reticulum unfolded protein response Source: Reactome
    9. glutamine metabolic process Source: UniProtKB-KW
    10. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
    11. liver development Source: Ensembl
    12. negative regulation of apoptotic process Source: UniProtKB
    13. positive regulation of mitotic cell cycle Source: UniProtKB
    14. response to amino acid Source: Ensembl
    15. response to follicle-stimulating hormone Source: Ensembl
    16. response to light stimulus Source: Ensembl
    17. response to mechanical stimulus Source: Ensembl
    18. response to methotrexate Source: Ensembl
    19. response to toxic substance Source: Ensembl
    20. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Amino-acid biosynthesis, Asparagine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.3.5.4. 2681.
    ReactomeiREACT_18355. ATF4 activates genes.
    REACT_238. Amino acid synthesis and interconversion (transamination).
    UniPathwayiUPA00134; UER00195.

    Protein family/group databases

    MEROPSiC44.974.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] (EC:6.3.5.4)
    Alternative name(s):
    Cell cycle control protein TS11
    Glutamine-dependent asparagine synthetase
    Gene namesi
    Name:ASNS
    Synonyms:TS11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:753. ASNS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Involvement in diseasei

    Asparagine synthetase deficiency (ASNSD) [MIM:615574]: An inborn error of asparagine biosynthesis that results in a severe neurologic disorder characterized by microcephaly, severely delayed psychomotor development, progressive encephalopathy, cortical atrophy, and seizure or hyperekplexic activity.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61A → E in ASNSD; dramatic reduction in protein abundance. 1 Publication
    VAR_070896
    Natural varianti362 – 3621F → V in ASNSD; dramatic reduction in protein abundance. 1 Publication
    VAR_070897
    Natural varianti550 – 5501R → C in ASNSD; increases level of protein abundance. 1 Publication
    VAR_070898

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21C → A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi615574. phenotype.
    Orphaneti391376. Congenital microcephaly-severe encephalopathy-progressive cerebral atrophy syndrome.
    PharmGKBiPA25052.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 561560Asparagine synthetase [glutamine-hydrolyzing]PRO_0000056910Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei385 – 3851N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP08243.
    PaxDbiP08243.
    PeptideAtlasiP08243.
    PRIDEiP08243.

    PTM databases

    PhosphoSiteiP08243.

    Expressioni

    Gene expression databases

    ArrayExpressiP08243.
    BgeeiP08243.
    CleanExiHS_ASNS.
    GenevestigatoriP08243.

    Organism-specific databases

    HPAiHPA004924.
    HPA029318.

    Interactioni

    Protein-protein interaction databases

    BioGridi106932. 43 interactions.
    IntActiP08243. 5 interactions.
    MINTiMINT-1371662.
    STRINGi9606.ENSP00000175506.

    Structurei

    3D structure databases

    ProteinModelPortaliP08243.
    SMRiP08243. Positions 253-481.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 191190Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
    BLAST
    Domaini213 – 536324Asparagine synthetaseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 535Glutamine bindingBy similarity
    Regioni75 – 773Glutamine bindingBy similarity

    Sequence similaritiesi

    Contains 1 asparagine synthetase domain.Curated
    Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0367.
    HOVERGENiHBG003103.
    InParanoidiP08243.
    KOiK01953.
    OMAiWMPRWIE.
    OrthoDBiEOG75MVVS.
    PhylomeDBiP08243.
    TreeFamiTF300603.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProiIPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00733. Asn_synthase. 1 hit.
    PF13537. GATase_7. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
    SUPFAMiSSF56235. SSF56235. 1 hit.
    TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
    PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P08243-1) [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

    MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL    50
    AVVDPLFGMQ PIRVKKYPYL WLCYNGEIYN HKKMQQHFEF EYQTKVDGEI 100
    ILHLYDKGGI EQTICMLDGV FAFVLLDTAN KKVFLGRDTY GVRPLFKAMT 150
    EDGFLAVCSE AKGLVTLKHS ATPFLKVEPF LPGHYEVLDL KPNGKVASVE 200
    MVKYHHCRDV PLHALYDNVE KLFPGFEIET VKNNLRILFN NAVKKRLMTD 250
    RRIGCLLSGG LDSSLVAATL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR 300
    KVADHIGSEH YEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK 350
    YIRKNTDSVV IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLRELYLF 400
    DVLRADRTTA AHGLELRVPF LDHRFSSYYL SLPPEMRIPK NGIEKHLLRE 450
    TFEDSNLIPK EILWRPKEAF SDGITSVKNS WFKILQEYVE HQVDDAMMAN 500
    AAQKFPFNTP KTKEGYYYRQ VFERHYPGRA DWLSHYWMPK WINATDPSAR 550
    TLTHYKSAVK A 561
    Length:561
    Mass (Da):64,370
    Last modified:January 23, 2007 - v4
    Checksum:i3E9B75E21D799FBE
    GO
    Isoform 2 (identifier: P08243-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:540
    Mass (Da):62,168
    Checksum:i7531F53E232D5AB0
    GO
    Isoform 3 (identifier: P08243-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-83: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:478
    Mass (Da):54,818
    Checksum:iF8AE4D4375F38522
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti333 – 34311TYDITTVRASV → LMTLQQFVLRI in AAA36781. (PubMed:3470743)CuratedAdd
    BLAST
    Sequence conflicti353 – 3608RKNTDSVV → GRTQIAWL in AAA36781. (PubMed:3470743)Curated
    Sequence conflicti426 – 4261S → F(PubMed:2886907)Curated
    Sequence conflicti426 – 4261S → F(PubMed:2565875)Curated
    Sequence conflicti462 – 4621I → V in BAG63553. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61A → E in ASNSD; dramatic reduction in protein abundance. 1 Publication
    VAR_070896
    Natural varianti210 – 2101V → E.5 Publications
    Corresponds to variant rs1049674 [ dbSNP | Ensembl ].
    VAR_023443
    Natural varianti362 – 3621F → V in ASNSD; dramatic reduction in protein abundance. 1 Publication
    VAR_070897
    Natural varianti550 – 5501R → C in ASNSD; increases level of protein abundance. 1 Publication
    VAR_070898

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8383Missing in isoform 3. 1 PublicationVSP_045817Add
    BLAST
    Alternative sequencei1 – 2121Missing in isoform 2. 1 PublicationVSP_045818Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27396 mRNA. Translation: AAA51789.1.
    L35946
    , L35936, L35937, L35938, L35939, L35940, L35941, L35942, L35943, L35944, L35945 Genomic DNA. Translation: AAA52756.1.
    BT007113 mRNA. Translation: AAP35777.1.
    AK302189 mRNA. Translation: BAG63553.1.
    AK316224 mRNA. Translation: BAH14595.1.
    AC005326 Genomic DNA. No translation available.
    AC079781 Genomic DNA. Translation: AAQ96856.1.
    CH236949 Genomic DNA. Translation: EAL24115.1.
    CH471091 Genomic DNA. Translation: EAW76730.1.
    CH471091 Genomic DNA. Translation: EAW76723.1.
    CH471091 Genomic DNA. Translation: EAW76731.1.
    CH471091 Genomic DNA. Translation: EAW76732.1.
    CH471091 Genomic DNA. Translation: EAW76733.1.
    BC008723 mRNA. Translation: AAH08723.1.
    BC014621 mRNA. Translation: AAH14621.1.
    M15798 mRNA. Translation: AAA36781.1.
    M27054 Genomic DNA. Translation: AAA63266.1.
    CCDSiCCDS55131.1. [P08243-3]
    CCDS55132.1. [P08243-2]
    CCDS5652.1. [P08243-1]
    PIRiA27062. AJHUN1.
    RefSeqiNP_001171546.1. NM_001178075.1. [P08243-2]
    NP_001171547.1. NM_001178076.1. [P08243-3]
    NP_001171548.1. NM_001178077.1. [P08243-3]
    NP_001664.3. NM_001673.4. [P08243-1]
    NP_597680.2. NM_133436.3. [P08243-1]
    NP_899199.2. NM_183356.3. [P08243-1]
    UniGeneiHs.489207.

    Genome annotation databases

    EnsembliENST00000175506; ENSP00000175506; ENSG00000070669. [P08243-1]
    ENST00000394308; ENSP00000377845; ENSG00000070669. [P08243-1]
    ENST00000394309; ENSP00000377846; ENSG00000070669. [P08243-1]
    ENST00000422745; ENSP00000414901; ENSG00000070669. [P08243-2]
    ENST00000437628; ENSP00000414379; ENSG00000070669. [P08243-3]
    ENST00000444334; ENSP00000406994; ENSG00000070669. [P08243-2]
    ENST00000455086; ENSP00000408472; ENSG00000070669. [P08243-3]
    GeneIDi440.
    KEGGihsa:440.
    UCSCiuc003uot.4. human. [P08243-1]

    Polymorphism databases

    DMDMi13432102.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27396 mRNA. Translation: AAA51789.1 .
    L35946
    , L35936 , L35937 , L35938 , L35939 , L35940 , L35941 , L35942 , L35943 , L35944 , L35945 Genomic DNA. Translation: AAA52756.1 .
    BT007113 mRNA. Translation: AAP35777.1 .
    AK302189 mRNA. Translation: BAG63553.1 .
    AK316224 mRNA. Translation: BAH14595.1 .
    AC005326 Genomic DNA. No translation available.
    AC079781 Genomic DNA. Translation: AAQ96856.1 .
    CH236949 Genomic DNA. Translation: EAL24115.1 .
    CH471091 Genomic DNA. Translation: EAW76730.1 .
    CH471091 Genomic DNA. Translation: EAW76723.1 .
    CH471091 Genomic DNA. Translation: EAW76731.1 .
    CH471091 Genomic DNA. Translation: EAW76732.1 .
    CH471091 Genomic DNA. Translation: EAW76733.1 .
    BC008723 mRNA. Translation: AAH08723.1 .
    BC014621 mRNA. Translation: AAH14621.1 .
    M15798 mRNA. Translation: AAA36781.1 .
    M27054 Genomic DNA. Translation: AAA63266.1 .
    CCDSi CCDS55131.1. [P08243-3 ]
    CCDS55132.1. [P08243-2 ]
    CCDS5652.1. [P08243-1 ]
    PIRi A27062. AJHUN1.
    RefSeqi NP_001171546.1. NM_001178075.1. [P08243-2 ]
    NP_001171547.1. NM_001178076.1. [P08243-3 ]
    NP_001171548.1. NM_001178077.1. [P08243-3 ]
    NP_001664.3. NM_001673.4. [P08243-1 ]
    NP_597680.2. NM_133436.3. [P08243-1 ]
    NP_899199.2. NM_183356.3. [P08243-1 ]
    UniGenei Hs.489207.

    3D structure databases

    ProteinModelPortali P08243.
    SMRi P08243. Positions 253-481.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106932. 43 interactions.
    IntActi P08243. 5 interactions.
    MINTi MINT-1371662.
    STRINGi 9606.ENSP00000175506.

    Chemistry

    BindingDBi P08243.
    ChEMBLi CHEMBL3120.
    DrugBanki DB00171. Adenosine triphosphate.
    DB00174. L-Asparagine.
    DB00128. L-Aspartic Acid.
    DB00142. L-Glutamic Acid.
    DB00130. L-Glutamine.

    Protein family/group databases

    MEROPSi C44.974.

    PTM databases

    PhosphoSitei P08243.

    Polymorphism databases

    DMDMi 13432102.

    Proteomic databases

    MaxQBi P08243.
    PaxDbi P08243.
    PeptideAtlasi P08243.
    PRIDEi P08243.

    Protocols and materials databases

    DNASUi 440.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000175506 ; ENSP00000175506 ; ENSG00000070669 . [P08243-1 ]
    ENST00000394308 ; ENSP00000377845 ; ENSG00000070669 . [P08243-1 ]
    ENST00000394309 ; ENSP00000377846 ; ENSG00000070669 . [P08243-1 ]
    ENST00000422745 ; ENSP00000414901 ; ENSG00000070669 . [P08243-2 ]
    ENST00000437628 ; ENSP00000414379 ; ENSG00000070669 . [P08243-3 ]
    ENST00000444334 ; ENSP00000406994 ; ENSG00000070669 . [P08243-2 ]
    ENST00000455086 ; ENSP00000408472 ; ENSG00000070669 . [P08243-3 ]
    GeneIDi 440.
    KEGGi hsa:440.
    UCSCi uc003uot.4. human. [P08243-1 ]

    Organism-specific databases

    CTDi 440.
    GeneCardsi GC07M097481.
    HGNCi HGNC:753. ASNS.
    HPAi HPA004924.
    HPA029318.
    MIMi 108370. gene.
    615574. phenotype.
    neXtProti NX_P08243.
    Orphaneti 391376. Congenital microcephaly-severe encephalopathy-progressive cerebral atrophy syndrome.
    PharmGKBi PA25052.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0367.
    HOVERGENi HBG003103.
    InParanoidi P08243.
    KOi K01953.
    OMAi WMPRWIE.
    OrthoDBi EOG75MVVS.
    PhylomeDBi P08243.
    TreeFami TF300603.

    Enzyme and pathway databases

    UniPathwayi UPA00134 ; UER00195 .
    BRENDAi 6.3.5.4. 2681.
    Reactomei REACT_18355. ATF4 activates genes.
    REACT_238. Amino acid synthesis and interconversion (transamination).

    Miscellaneous databases

    GenomeRNAii 440.
    NextBioi 1843.
    PROi P08243.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08243.
    Bgeei P08243.
    CleanExi HS_ASNS.
    Genevestigatori P08243.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    3.60.20.10. 1 hit.
    InterProi IPR006426. Asn_synth_AEB.
    IPR001962. Asn_synthase.
    IPR017932. GATase_2_dom.
    IPR000583. GATase_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00733. Asn_synthase. 1 hit.
    PF13537. GATase_7. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001589. Asn_synthetase_glu-h. 1 hit.
    SUPFAMi SSF56235. SSF56235. 1 hit.
    TIGRFAMsi TIGR01536. asn_synth_AEB. 1 hit.
    PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of human cDNAs for asparagine synthetase and expression in Jensen rat sarcoma cells."
      Andrulis I.L., Chen J., Ray P.N.
      Mol. Cell. Biol. 7:2435-2443(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular structure of the human asparagine synthetase gene."
      Zhang Y.P., Lambert M.A., Cairney A.E., Wills D., Ray P.N., Andrulis I.L.
      Genomics 4:259-265(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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] (ISOFORMS 2 AND 3), VARIANT GLU-210.
      Tissue: Testis.
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-210.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-210.
    7. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-210.
    8. "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), VARIANT GLU-210.
      Tissue: Muscle.
    9. "Molecular cloning of a gene that is necessary for G1 progression in mammalian cells."
      Greco A., Ittmann M., Basilico C.
      Proc. Natl. Acad. Sci. U.S.A. 84:1565-1569(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-561 (ISOFORM 1).
    10. "Organization and expression of the cell cycle gene, ts11, that encodes asparagine synthetase."
      Greco A., Gong S.S., Ittmann M., Basilico C.
      Mol. Cell. Biol. 9:2350-2359(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83.
    11. "Expression of human asparagine synthetase in Escherichia coli."
      van Heeke G., Schuster S.M.
      J. Biol. Chem. 264:5503-5509(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    12. "The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity."
      van Heeke G., Schuster S.M.
      J. Biol. Chem. 264:19475-19477(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-2, CATALYTIC ACTIVITY, ACTIVE SITE.
    13. "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-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: VARIANTS ASNSD GLU-6; VAL-362 AND CYS-550, CHARACTERIZATION OF VARIANTS ASNSD GLU-6; VAL-362 AND CYS-550.

    Entry informationi

    Entry nameiASNS_HUMAN
    AccessioniPrimary (citable) accession number: P08243
    Secondary accession number(s): A4D1I8
    , B4DXZ1, B7ZAA9, D6W5R3, E9PCI3, E9PCX6, P08184, Q15666, Q549T9, Q96HD0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 165 of the entry and version 4 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3