Q9NR45 (SIAS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NANS
Synonyms:	SAS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O = phosphate + N-acetylneuraminate. Phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H2O = N-acylneuraminate 9-phosphate + phosphate.
Tissue specificity	Ubiquitous.
Sequence similarities	Contains 1 AFP-like domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Molecular function	Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipopolysaccharide biosynthetic process Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	cytoplasm Non-traceable author statement Ref.1. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara
Molecular_function	N-acetylneuraminate synthase activity Inferred from electronic annotation. Source: EC N-acylneuraminate cytidylyltransferase activity Non-traceable author statement Ref.1. Source: UniProtKB N-acylneuraminate-9-phosphate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 359

358

Sialic acid synthase

PRO_0000097750

Regions

Domain

294 – 353

60

AFP-like

Sites

Site

2

1

Not acetylated

Amino acid modifications

Modified residue

79

1

N6-acetyllysine Ref.7

Natural variations

Natural variant

68

1

E → D. Ref.5
Corresponds to variant rs1058446 [ dbSNP | Ensembl ].

VAR_013308

Experimental info

Sequence conflict

232

1

A → T in BAA91818. Ref.2

Sequence conflict

321

1

G → A in AAF75261. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

359

Helix Strand Turn

Details...

Beta strand

294 – 299

6

Helix

309 – 311

3

Beta strand

312 – 315

4

Beta strand

324 – 326

3

Helix

327 – 330

4

Beta strand

334 – 337

4

Helix

347 – 349

3

Beta strand

356 – 358

3

Sequences

	Sequence		Length	Mass (Da)
	Q9NR45 [UniParc]. Last modified May 15, 2002. Version 2. Checksum: 2E02D47F4F98592F	FASTA	359	40,308
	10 20 30 40 50 60 MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC AKFQKSELEF 70 80 90 100 110 120 KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR YAEEVGIFFT ASGMDEMAVE 130 140 150 160 170 180 FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC 190 200 210 220 230 240 FLQCTSAYPL QPEDVNLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT 250 260 270 280 290 300 LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK 310 320 330 340 350 IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV DNHGKKIKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, LACK OF N-TERMINAL ACETYLATION, 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, MASS SPECTROMETRY.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Solution structure of the antifreeze-like domain of human sialic acid synthase." Hamada T., Ito Y., Abe T., Hayashi F., Guentert P., Inoue M., Kigawa T., Terada T., Shirouzu M., Yoshida M., Tanaka A., Sugano S., Yokoyama S., Hirota H. Protein Sci. 15:1010-1016(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 294-359.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00147874.

RefSeq

NP_061819.2. NM_018946.3.

UniGene

Hs.522310.
Hs.665191.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WVO	NMR	-	A	294-359	[»]

ProteinModelPortal

Q9NR45.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NR45. 2 interactions.

MINT

MINT-5002014.

STRING

9606.ENSP00000210444.

PTM databases

PhosphoSite

Q9NR45.

Polymorphism databases

DMDM

20978759.

2D gel databases

REPRODUCTION-2DPAGE

IPI00147874.

Proteomic databases

PaxDb

Q9NR45.

PeptideAtlas

Q9NR45.

PRIDE

Q9NR45.

Protocols and materials databases

DNASU

54187.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000210444; ENSP00000210444; ENSG00000095380.

GeneID

54187.

KEGG

hsa:54187.

UCSC

uc004ayc.3. human.

Organism-specific databases

CTD

54187.

GeneCards

GC09P100818.

HGNC

HGNC:19237. NANS.

HPA

HPA019223.

MIM

605202. gene.

neXtProt

NX_Q9NR45.

PharmGKB

PA134978885.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2089.

HOGENOM

HOG000284783.

HOVERGEN

HBG000665.

InParanoid

Q9NR45.

KO

K05304.

OMA

VPFIKIG.

OrthoDB

EOG4H9XKV.

Enzyme and pathway databases

BioCyc

MetaCyc:HS01818-MONOMER.

BRENDA

2.5.1.57. 2681.

Gene expression databases

ArrayExpress

Q9NR45.

Bgee

Q9NR45.

CleanEx

HS_NANS.

Genevestigator

Q9NR45.

GermOnline

ENSG00000095380. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.
3.90.1210.10. 1 hit.

InterPro

IPR006190. AFP_Neu5c_C.
IPR013785. Aldolase_TIM.
IPR006013. Antifreeze_III.
IPR013132. Neu5Ac_N.
IPR013974. SAF.
[Graphical view]

Pfam

PF03102. NeuB. 1 hit.
PF08666. SAF. 1 hit.
[Graphical view]

PRINTS

PR00357. ANTIFREEZIII.

SMART

SM00858. SAF. 1 hit.
[Graphical view]

SUPFAM

SSF51269. AFP_Neu5c_C. 1 hit.

PROSITE

PS50844. AFP_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NANS. human.

EvolutionaryTrace

Q9NR45.

GenomeRNAi

54187.

NextBio

56522.

SOURCE

Search...

Entry information

Entry name

SIAS_HUMAN

Accession

Primary (citable) accession number: Q9NR45
Secondary accession number(s): B2RE98 , Q8WUV9, Q9BWS6, Q9NVD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2002
Last sequence update:	May 15, 2002
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.