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Q9NR45

- SIAS_HUMAN

UniProt

Q9NR45 - SIAS_HUMAN

Protein

Sialic acid synthase

Gene

NANS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (15 May 2002)
      Previous versions | rss
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    Functioni

    Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.

    Catalytic activityi

    Phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O = phosphate + N-acetylneuraminate.
    Phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H2O = N-acylneuraminate 9-phosphate + phosphate.

    GO - Molecular functioni

    1. N-acetylneuraminate synthase activity Source: UniProtKB-EC
    2. N-acylneuraminate-9-phosphate synthase activity Source: UniProtKB-EC
    3. N-acylneuraminate cytidylyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. lipopolysaccharide biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01818-MONOMER.
    BRENDAi2.5.1.57. 2681.
    ReactomeiREACT_200874. Sialic acid metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialic acid synthase
    Alternative name(s):
    N-acetylneuraminate synthase (EC:2.5.1.56)
    N-acetylneuraminate-9-phosphate synthase (EC:2.5.1.57)
    N-acetylneuraminic acid phosphate synthase
    N-acetylneuraminic acid synthase
    Gene namesi
    Name:NANS
    Synonyms:SAS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:19237. NANS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134978885.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 359358Sialic acid synthasePRO_0000097750Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NR45.
    PaxDbiQ9NR45.
    PeptideAtlasiQ9NR45.
    PRIDEiQ9NR45.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00147874.

    PTM databases

    PhosphoSiteiQ9NR45.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9NR45.
    BgeeiQ9NR45.
    CleanExiHS_NANS.
    GenevestigatoriQ9NR45.

    Organism-specific databases

    HPAiHPA019223.

    Interactioni

    Protein-protein interaction databases

    BioGridi119921. 23 interactions.
    IntActiQ9NR45. 1 interaction.
    MINTiMINT-5002014.
    STRINGi9606.ENSP00000210444.

    Structurei

    Secondary structure

    1
    359
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi294 – 2996
    Helixi309 – 3113
    Beta strandi312 – 3154
    Beta strandi324 – 3263
    Helixi327 – 3304
    Beta strandi334 – 3374
    Helixi347 – 3493
    Beta strandi356 – 3583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WVONMR-A294-359[»]
    ProteinModelPortaliQ9NR45.
    SMRiQ9NR45. Positions 11-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NR45.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini294 – 35360AFP-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AFP-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2089.
    HOGENOMiHOG000284783.
    HOVERGENiHBG000665.
    InParanoidiQ9NR45.
    KOiK05304.
    OMAiSGDANNF.
    OrthoDBiEOG7PP57F.
    PhylomeDBiQ9NR45.
    TreeFamiTF324826.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    3.90.1210.10. 1 hit.
    InterProiIPR006190. AFP_Neu5c_C.
    IPR013785. Aldolase_TIM.
    IPR006013. Antifreeze_III.
    IPR013132. Neu5Ac_N.
    IPR013974. SAF.
    [Graphical view]
    PfamiPF03102. NeuB. 1 hit.
    PF08666. SAF. 1 hit.
    [Graphical view]
    PRINTSiPR00357. ANTIFREEZIII.
    SMARTiSM00858. SAF. 1 hit.
    [Graphical view]
    SUPFAMiSSF51269. SSF51269. 1 hit.
    PROSITEiPS50844. AFP_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9NR45-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC    50
    AKFQKSELEF KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR 100
    YAEEVGIFFT ASGMDEMAVE FLHELNVPFF KVGSGDTNNF PYLEKTAKKG 150
    RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC FLQCTSAYPL QPEDVNLRVI 200
    SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT LDKTWKGSDH 250
    SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK 300
    IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV 350
    DNHGKKIKS 359
    Length:359
    Mass (Da):40,308
    Last modified:May 15, 2002 - v2
    Checksum:i2E02D47F4F98592F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti232 – 2321A → T in BAA91818. (PubMed:14702039)Curated
    Sequence conflicti321 – 3211G → A in AAF75261. (PubMed:10749855)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681E → D.1 Publication
    Corresponds to variant rs1058446 [ dbSNP | Ensembl ].
    VAR_013308

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF257466 mRNA. Translation: AAF75261.1.
    AK001659 mRNA. Translation: BAA91818.1.
    AK316608 mRNA. Translation: BAG38195.1.
    AL137073 Genomic DNA. Translation: CAI13886.1.
    CH471105 Genomic DNA. Translation: EAW58867.1.
    BC000008 mRNA. Translation: AAH00008.1.
    BC019315 mRNA. Translation: AAH19315.1.
    CCDSiCCDS6733.1.
    RefSeqiNP_061819.2. NM_018946.3.
    UniGeneiHs.522310.
    Hs.665191.

    Genome annotation databases

    EnsembliENST00000210444; ENSP00000210444; ENSG00000095380.
    GeneIDi54187.
    KEGGihsa:54187.
    UCSCiuc004ayc.3. human.

    Polymorphism databases

    DMDMi20978759.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF257466 mRNA. Translation: AAF75261.1 .
    AK001659 mRNA. Translation: BAA91818.1 .
    AK316608 mRNA. Translation: BAG38195.1 .
    AL137073 Genomic DNA. Translation: CAI13886.1 .
    CH471105 Genomic DNA. Translation: EAW58867.1 .
    BC000008 mRNA. Translation: AAH00008.1 .
    BC019315 mRNA. Translation: AAH19315.1 .
    CCDSi CCDS6733.1.
    RefSeqi NP_061819.2. NM_018946.3.
    UniGenei Hs.522310.
    Hs.665191.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WVO NMR - A 294-359 [» ]
    ProteinModelPortali Q9NR45.
    SMRi Q9NR45. Positions 11-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119921. 23 interactions.
    IntActi Q9NR45. 1 interaction.
    MINTi MINT-5002014.
    STRINGi 9606.ENSP00000210444.

    PTM databases

    PhosphoSitei Q9NR45.

    Polymorphism databases

    DMDMi 20978759.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00147874.

    Proteomic databases

    MaxQBi Q9NR45.
    PaxDbi Q9NR45.
    PeptideAtlasi Q9NR45.
    PRIDEi Q9NR45.

    Protocols and materials databases

    DNASUi 54187.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000210444 ; ENSP00000210444 ; ENSG00000095380 .
    GeneIDi 54187.
    KEGGi hsa:54187.
    UCSCi uc004ayc.3. human.

    Organism-specific databases

    CTDi 54187.
    GeneCardsi GC09P100818.
    HGNCi HGNC:19237. NANS.
    HPAi HPA019223.
    MIMi 605202. gene.
    neXtProti NX_Q9NR45.
    PharmGKBi PA134978885.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2089.
    HOGENOMi HOG000284783.
    HOVERGENi HBG000665.
    InParanoidi Q9NR45.
    KOi K05304.
    OMAi SGDANNF.
    OrthoDBi EOG7PP57F.
    PhylomeDBi Q9NR45.
    TreeFami TF324826.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01818-MONOMER.
    BRENDAi 2.5.1.57. 2681.
    Reactomei REACT_200874. Sialic acid metabolism.

    Miscellaneous databases

    ChiTaRSi NANS. human.
    EvolutionaryTracei Q9NR45.
    GeneWikii NANS.
    GenomeRNAii 54187.
    NextBioi 56522.
    PROi Q9NR45.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NR45.
    Bgeei Q9NR45.
    CleanExi HS_NANS.
    Genevestigatori Q9NR45.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    3.90.1210.10. 1 hit.
    InterProi IPR006190. AFP_Neu5c_C.
    IPR013785. Aldolase_TIM.
    IPR006013. Antifreeze_III.
    IPR013132. Neu5Ac_N.
    IPR013974. SAF.
    [Graphical view ]
    Pfami PF03102. NeuB. 1 hit.
    PF08666. SAF. 1 hit.
    [Graphical view ]
    PRINTSi PR00357. ANTIFREEZIII.
    SMARTi SM00858. SAF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51269. SSF51269. 1 hit.
    PROSITEi PS50844. AFP_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid biosynthetic ability."
      Lawrence S.M., Huddleston K.A., Pitts L.R., Nguyen N., Lee Y.C., Vann W.F., Coleman T.A., Betenbaugh M.J.
      J. Biol. Chem. 275:17869-17877(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Tissue: Liver.
    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].
      Tissue: Placenta.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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], VARIANT ASP-68.
      Tissue: Lung and Placenta.
    6. Bienvenut W.V.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 132-145; 150-166; 247-264 AND 299-315, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "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-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: STRUCTURE BY NMR OF 294-359.

    Entry informationi

    Entry nameiSIAS_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR45
    Secondary accession number(s): B2RE98
    , Q8WUV9, Q9BWS6, Q9NVD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2002
    Last sequence update: May 15, 2002
    Last modified: October 1, 2014
    This is version 130 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 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3