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Protein

Sialic acid synthase

Gene

NANS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS01818-MONOMER.
BRENDAi2.5.1.57. 2681.
ReactomeiREACT_264366. 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 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:19237. NANS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134978885.

Polymorphism and mutation databases

BioMutaiNANS.
DMDMi20978759.

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

BgeeiQ9NR45.
CleanExiHS_NANS.
ExpressionAtlasiQ9NR45. baseline and differential.
GenevisibleiQ9NR45. HS.

Organism-specific databases

HPAiHPA019223.

Interactioni

Protein-protein interaction databases

BioGridi119921. 26 interactions.
IntActiQ9NR45. 19 interactions.
MINTiMINT-5002014.
STRINGi9606.ENSP00000210444.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000011081.
HOGENOMiHOG000284783.
HOVERGENiHBG000665.
InParanoidiQ9NR45.
KOiK05304.
OMAiAYPSKIE.
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

        10         20         30         40         50
MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC
60 70 80 90 100
AKFQKSELEF KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR
110 120 130 140 150
YAEEVGIFFT ASGMDEMAVE FLHELNVPFF KVGSGDTNNF PYLEKTAKKG
160 170 180 190 200
RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC FLQCTSAYPL QPEDVNLRVI
210 220 230 240 250
SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT LDKTWKGSDH
260 270 280 290 300
SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK
310 320 330 340 350
IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV

DNHGKKIKS
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi119921. 26 interactions.
IntActiQ9NR45. 19 interactions.
MINTiMINT-5002014.
STRINGi9606.ENSP00000210444.

PTM databases

PhosphoSiteiQ9NR45.

Polymorphism and mutation databases

BioMutaiNANS.
DMDMi20978759.

2D gel databases

REPRODUCTION-2DPAGEIPI00147874.

Proteomic databases

MaxQBiQ9NR45.
PaxDbiQ9NR45.
PeptideAtlasiQ9NR45.
PRIDEiQ9NR45.

Protocols and materials databases

DNASUi54187.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi54187.
GeneCardsiGC09P100818.
HGNCiHGNC:19237. NANS.
HPAiHPA019223.
MIMi605202. gene.
neXtProtiNX_Q9NR45.
PharmGKBiPA134978885.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2089.
GeneTreeiENSGT00390000011081.
HOGENOMiHOG000284783.
HOVERGENiHBG000665.
InParanoidiQ9NR45.
KOiK05304.
OMAiAYPSKIE.
OrthoDBiEOG7PP57F.
PhylomeDBiQ9NR45.
TreeFamiTF324826.

Enzyme and pathway databases

BioCyciMetaCyc:HS01818-MONOMER.
BRENDAi2.5.1.57. 2681.
ReactomeiREACT_264366. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSiNANS. human.
EvolutionaryTraceiQ9NR45.
GeneWikiiNANS.
GenomeRNAii54187.
NextBioi56522.
PROiQ9NR45.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NR45.
CleanExiHS_NANS.
ExpressionAtlasiQ9NR45. baseline and differential.
GenevisibleiQ9NR45. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. 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: June 24, 2015
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.