Full text data of NANS
NANS
(SAS)
[Confidence: low (only semi-automatic identification from reviews)]
Sialic acid synthase (N-acetylneuraminate synthase; 2.5.1.56; N-acetylneuraminate-9-phosphate synthase; 2.5.1.57; N-acetylneuraminic acid phosphate synthase; N-acetylneuraminic acid synthase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Sialic acid synthase (N-acetylneuraminate synthase; 2.5.1.56; N-acetylneuraminate-9-phosphate synthase; 2.5.1.57; N-acetylneuraminic acid phosphate synthase; N-acetylneuraminic acid synthase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NR45
ID SIAS_HUMAN Reviewed; 359 AA.
AC Q9NR45; B2RE98; Q8WUV9; Q9BWS6; Q9NVD4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Sialic acid synthase;
DE AltName: Full=N-acetylneuraminate synthase;
DE EC=2.5.1.56;
DE AltName: Full=N-acetylneuraminate-9-phosphate synthase;
DE EC=2.5.1.57;
DE AltName: Full=N-acetylneuraminic acid phosphate synthase;
DE AltName: Full=N-acetylneuraminic acid synthase;
GN Name=NANS; Synonyms=SAS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=10749855; DOI=10.1074/jbc.M000217200;
RA Lawrence S.M., Huddleston K.A., Pitts L.R., Nguyen N., Lee Y.C.,
RA Vann W.F., Coleman T.A., Betenbaugh M.J.;
RT "Cloning and expression of the human N-acetylneuraminic acid phosphate
RT synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
RT biosynthetic ability.";
RL J. Biol. Chem. 275:17869-17877(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-68.
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-11; 132-145; 150-166; 247-264 AND 299-315,
RP CLEAVAGE OF INITIATOR METHIONINE, LACK OF N-TERMINAL ACETYLATION, AND
RP MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP STRUCTURE BY NMR OF 294-359.
RX PubMed=16597820; DOI=10.1110/ps.051700406;
RA Hamada T., Ito Y., Abe T., Hayashi F., Guentert P., Inoue M.,
RA Kigawa T., Terada T., Shirouzu M., Yoshida M., Tanaka A., Sugano S.,
RA Yokoyama S., Hirota H.;
RT "Solution structure of the antifreeze-like domain of human sialic acid
RT synthase.";
RL Protein Sci. 15:1010-1016(2006).
CC -!- FUNCTION: Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-
CC deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-
CC acetylmannosamine 6-phosphate and mannose 6-phosphate as
CC substrates to generate phosphorylated forms of Neu5Ac and KDN,
CC respectively.
CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + N-acetyl-D-mannosamine +
CC H(2)O = phosphate + N-acetylneuraminate.
CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + N-acyl-D-mannosamine 6-
CC phosphate + H(2)O = N-acylneuraminate 9-phosphate + phosphate.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 AFP-like domain.
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DR EMBL; AF257466; AAF75261.1; -; mRNA.
DR EMBL; AK001659; BAA91818.1; -; mRNA.
DR EMBL; AK316608; BAG38195.1; -; mRNA.
DR EMBL; AL137073; CAI13886.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW58867.1; -; Genomic_DNA.
DR EMBL; BC000008; AAH00008.1; -; mRNA.
DR EMBL; BC019315; AAH19315.1; -; mRNA.
DR RefSeq; NP_061819.2; NM_018946.3.
DR UniGene; Hs.522310; -.
DR UniGene; Hs.665191; -.
DR PDB; 1WVO; NMR; -; A=294-359.
DR PDBsum; 1WVO; -.
DR ProteinModelPortal; Q9NR45; -.
DR SMR; Q9NR45; 11-359.
DR IntAct; Q9NR45; 1.
DR MINT; MINT-5002014; -.
DR STRING; 9606.ENSP00000210444; -.
DR PhosphoSite; Q9NR45; -.
DR DMDM; 20978759; -.
DR REPRODUCTION-2DPAGE; IPI00147874; -.
DR PaxDb; Q9NR45; -.
DR PeptideAtlas; Q9NR45; -.
DR PRIDE; Q9NR45; -.
DR DNASU; 54187; -.
DR Ensembl; ENST00000210444; ENSP00000210444; ENSG00000095380.
DR GeneID; 54187; -.
DR KEGG; hsa:54187; -.
DR UCSC; uc004ayc.3; human.
DR CTD; 54187; -.
DR GeneCards; GC09P100818; -.
DR HGNC; HGNC:19237; NANS.
DR HPA; HPA019223; -.
DR MIM; 605202; gene.
DR neXtProt; NX_Q9NR45; -.
DR PharmGKB; PA134978885; -.
DR eggNOG; COG2089; -.
DR HOGENOM; HOG000284783; -.
DR HOVERGEN; HBG000665; -.
DR InParanoid; Q9NR45; -.
DR KO; K05304; -.
DR OMA; VPFIKIG; -.
DR OrthoDB; EOG7PP57F; -.
DR BioCyc; MetaCyc:HS01818-MONOMER; -.
DR BRENDA; 2.5.1.57; 2681.
DR ChiTaRS; NANS; human.
DR EvolutionaryTrace; Q9NR45; -.
DR GeneWiki; NANS; -.
DR GenomeRNAi; 54187; -.
DR NextBio; 56522; -.
DR PRO; PR:Q9NR45; -.
DR ArrayExpress; Q9NR45; -.
DR Bgee; Q9NR45; -.
DR CleanEx; HS_NANS; -.
DR Genevestigator; Q9NR45; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0050462; F:N-acetylneuraminate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; NAS:UniProtKB.
DR GO; GO:0047444; F:N-acylneuraminate-9-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; NAS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.90.1210.10; -; 1.
DR InterPro; IPR006190; AFP_Neu5c_C.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006013; Antifreeze_III.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR Pfam; PF03102; NeuB; 1.
DR Pfam; PF08666; SAF; 1.
DR PRINTS; PR00357; ANTIFREEZIII.
DR SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; SSF51269; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Polymorphism; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 359 Sialic acid synthase.
FT /FTId=PRO_0000097750.
FT DOMAIN 294 353 AFP-like.
FT SITE 2 2 Not acetylated.
FT MOD_RES 79 79 N6-acetyllysine.
FT VARIANT 68 68 E -> D (in dbSNP:rs1058446).
FT /FTId=VAR_013308.
FT CONFLICT 232 232 A -> T (in Ref. 2; BAA91818).
FT CONFLICT 321 321 G -> A (in Ref. 1; AAF75261).
FT STRAND 294 299
FT HELIX 309 311
FT STRAND 312 315
FT STRAND 324 326
FT HELIX 327 330
FT STRAND 334 337
FT HELIX 347 349
FT STRAND 356 358
SQ SEQUENCE 359 AA; 40308 MW; 2E02D47F4F98592F CRC64;
MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC AKFQKSELEF
KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR YAEEVGIFFT ASGMDEMAVE
FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC
FLQCTSAYPL QPEDVNLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT
LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK
IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV DNHGKKIKS
//
ID SIAS_HUMAN Reviewed; 359 AA.
AC Q9NR45; B2RE98; Q8WUV9; Q9BWS6; Q9NVD4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Sialic acid synthase;
DE AltName: Full=N-acetylneuraminate synthase;
DE EC=2.5.1.56;
DE AltName: Full=N-acetylneuraminate-9-phosphate synthase;
DE EC=2.5.1.57;
DE AltName: Full=N-acetylneuraminic acid phosphate synthase;
DE AltName: Full=N-acetylneuraminic acid synthase;
GN Name=NANS; Synonyms=SAS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=10749855; DOI=10.1074/jbc.M000217200;
RA Lawrence S.M., Huddleston K.A., Pitts L.R., Nguyen N., Lee Y.C.,
RA Vann W.F., Coleman T.A., Betenbaugh M.J.;
RT "Cloning and expression of the human N-acetylneuraminic acid phosphate
RT synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid
RT biosynthetic ability.";
RL J. Biol. Chem. 275:17869-17877(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-68.
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-11; 132-145; 150-166; 247-264 AND 299-315,
RP CLEAVAGE OF INITIATOR METHIONINE, LACK OF N-TERMINAL ACETYLATION, AND
RP MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP STRUCTURE BY NMR OF 294-359.
RX PubMed=16597820; DOI=10.1110/ps.051700406;
RA Hamada T., Ito Y., Abe T., Hayashi F., Guentert P., Inoue M.,
RA Kigawa T., Terada T., Shirouzu M., Yoshida M., Tanaka A., Sugano S.,
RA Yokoyama S., Hirota H.;
RT "Solution structure of the antifreeze-like domain of human sialic acid
RT synthase.";
RL Protein Sci. 15:1010-1016(2006).
CC -!- FUNCTION: Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-
CC deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N-
CC acetylmannosamine 6-phosphate and mannose 6-phosphate as
CC substrates to generate phosphorylated forms of Neu5Ac and KDN,
CC respectively.
CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + N-acetyl-D-mannosamine +
CC H(2)O = phosphate + N-acetylneuraminate.
CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + N-acyl-D-mannosamine 6-
CC phosphate + H(2)O = N-acylneuraminate 9-phosphate + phosphate.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 AFP-like domain.
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DR EMBL; AF257466; AAF75261.1; -; mRNA.
DR EMBL; AK001659; BAA91818.1; -; mRNA.
DR EMBL; AK316608; BAG38195.1; -; mRNA.
DR EMBL; AL137073; CAI13886.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW58867.1; -; Genomic_DNA.
DR EMBL; BC000008; AAH00008.1; -; mRNA.
DR EMBL; BC019315; AAH19315.1; -; mRNA.
DR RefSeq; NP_061819.2; NM_018946.3.
DR UniGene; Hs.522310; -.
DR UniGene; Hs.665191; -.
DR PDB; 1WVO; NMR; -; A=294-359.
DR PDBsum; 1WVO; -.
DR ProteinModelPortal; Q9NR45; -.
DR SMR; Q9NR45; 11-359.
DR IntAct; Q9NR45; 1.
DR MINT; MINT-5002014; -.
DR STRING; 9606.ENSP00000210444; -.
DR PhosphoSite; Q9NR45; -.
DR DMDM; 20978759; -.
DR REPRODUCTION-2DPAGE; IPI00147874; -.
DR PaxDb; Q9NR45; -.
DR PeptideAtlas; Q9NR45; -.
DR PRIDE; Q9NR45; -.
DR DNASU; 54187; -.
DR Ensembl; ENST00000210444; ENSP00000210444; ENSG00000095380.
DR GeneID; 54187; -.
DR KEGG; hsa:54187; -.
DR UCSC; uc004ayc.3; human.
DR CTD; 54187; -.
DR GeneCards; GC09P100818; -.
DR HGNC; HGNC:19237; NANS.
DR HPA; HPA019223; -.
DR MIM; 605202; gene.
DR neXtProt; NX_Q9NR45; -.
DR PharmGKB; PA134978885; -.
DR eggNOG; COG2089; -.
DR HOGENOM; HOG000284783; -.
DR HOVERGEN; HBG000665; -.
DR InParanoid; Q9NR45; -.
DR KO; K05304; -.
DR OMA; VPFIKIG; -.
DR OrthoDB; EOG7PP57F; -.
DR BioCyc; MetaCyc:HS01818-MONOMER; -.
DR BRENDA; 2.5.1.57; 2681.
DR ChiTaRS; NANS; human.
DR EvolutionaryTrace; Q9NR45; -.
DR GeneWiki; NANS; -.
DR GenomeRNAi; 54187; -.
DR NextBio; 56522; -.
DR PRO; PR:Q9NR45; -.
DR ArrayExpress; Q9NR45; -.
DR Bgee; Q9NR45; -.
DR CleanEx; HS_NANS; -.
DR Genevestigator; Q9NR45; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0050462; F:N-acetylneuraminate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; NAS:UniProtKB.
DR GO; GO:0047444; F:N-acylneuraminate-9-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; NAS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.90.1210.10; -; 1.
DR InterPro; IPR006190; AFP_Neu5c_C.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006013; Antifreeze_III.
DR InterPro; IPR013132; Neu5Ac_N.
DR InterPro; IPR013974; SAF.
DR Pfam; PF03102; NeuB; 1.
DR Pfam; PF08666; SAF; 1.
DR PRINTS; PR00357; ANTIFREEZIII.
DR SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; SSF51269; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Polymorphism; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 359 Sialic acid synthase.
FT /FTId=PRO_0000097750.
FT DOMAIN 294 353 AFP-like.
FT SITE 2 2 Not acetylated.
FT MOD_RES 79 79 N6-acetyllysine.
FT VARIANT 68 68 E -> D (in dbSNP:rs1058446).
FT /FTId=VAR_013308.
FT CONFLICT 232 232 A -> T (in Ref. 2; BAA91818).
FT CONFLICT 321 321 G -> A (in Ref. 1; AAF75261).
FT STRAND 294 299
FT HELIX 309 311
FT STRAND 312 315
FT STRAND 324 326
FT HELIX 327 330
FT STRAND 334 337
FT HELIX 347 349
FT STRAND 356 358
SQ SEQUENCE 359 AA; 40308 MW; 2E02D47F4F98592F CRC64;
MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC AKFQKSELEF
KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR YAEEVGIFFT ASGMDEMAVE
FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC
FLQCTSAYPL QPEDVNLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT
LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK
IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV DNHGKKIKS
//
MIM
605202
*RECORD*
*FIELD* NO
605202
*FIELD* TI
*605202 N-ACETYLNEURAMINIC ACID PHOSPHATE SYNTHASE; NANS
;;SIALIC ACID SYNTHASE; SAS
read more*FIELD* TX
DESCRIPTION
The sialic acids are a family of 9-carbon 2-keto-3-deoxy sugars. They
are frequently the terminal sugars on secreted and cell surface
glycoproteins and glycolipids. Sialic acids participate in many
important biologic recognition events.
CLONING
By searching a human EST database for sequences that are homologous to
the E. coli sialic acid synthase gene neuB, Lawrence et al. (2000)
identified SAS. They isolated a full-length human SAS coding sequence.
The deduced 359-amino acid SAS protein shares approximately 36% amino
acid sequence identity with the E. coli neuB protein. Expression of the
SAS gene in an E. coli neuB-negative mutant resulted in partial
restoration of sialic acid synthase activity. In insect cells,
expression of SAS caused N-acetylneuraminic acid (Neu5Ac) and
2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) production. In
vitro, SAS used N-acetylmannosamine 6-phosphate and mannose-6-phosphate
as substrates to generate phosphorylated forms of Neu5Ac and KDN,
respectively; however, it exhibited much higher activity toward the
Neu5Ac phosphate product. Northern blot analysis detected an
approximately 1.3-kb SAS transcript in all human tissues examined.
*FIELD* RF
1. Lawrence, S. M.; Huddleston, K. A.; Pitts, L. R.; Nguyen, N.; Lee,
Y. C.; Vann, W. F.; Coleman, T. A.; Betenbaugh, M. J.: 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. J. Biol. Chem. 275: 17869-17877, 2000.
*FIELD* CD
Patti M. Sherman: 8/7/2000
*FIELD* ED
carol: 12/23/2002
mcapotos: 8/30/2000
psherman: 8/8/2000
*RECORD*
*FIELD* NO
605202
*FIELD* TI
*605202 N-ACETYLNEURAMINIC ACID PHOSPHATE SYNTHASE; NANS
;;SIALIC ACID SYNTHASE; SAS
read more*FIELD* TX
DESCRIPTION
The sialic acids are a family of 9-carbon 2-keto-3-deoxy sugars. They
are frequently the terminal sugars on secreted and cell surface
glycoproteins and glycolipids. Sialic acids participate in many
important biologic recognition events.
CLONING
By searching a human EST database for sequences that are homologous to
the E. coli sialic acid synthase gene neuB, Lawrence et al. (2000)
identified SAS. They isolated a full-length human SAS coding sequence.
The deduced 359-amino acid SAS protein shares approximately 36% amino
acid sequence identity with the E. coli neuB protein. Expression of the
SAS gene in an E. coli neuB-negative mutant resulted in partial
restoration of sialic acid synthase activity. In insect cells,
expression of SAS caused N-acetylneuraminic acid (Neu5Ac) and
2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN) production. In
vitro, SAS used N-acetylmannosamine 6-phosphate and mannose-6-phosphate
as substrates to generate phosphorylated forms of Neu5Ac and KDN,
respectively; however, it exhibited much higher activity toward the
Neu5Ac phosphate product. Northern blot analysis detected an
approximately 1.3-kb SAS transcript in all human tissues examined.
*FIELD* RF
1. Lawrence, S. M.; Huddleston, K. A.; Pitts, L. R.; Nguyen, N.; Lee,
Y. C.; Vann, W. F.; Coleman, T. A.; Betenbaugh, M. J.: 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. J. Biol. Chem. 275: 17869-17877, 2000.
*FIELD* CD
Patti M. Sherman: 8/7/2000
*FIELD* ED
carol: 12/23/2002
mcapotos: 8/30/2000
psherman: 8/8/2000