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Protein

N-acylneuraminate-9-phosphatase

Gene

NANP

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

Functioni

Catalytic activityi

N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by vanadate and calcium.1 Publication

Kineticsi

  1. KM=0.09 mM for N-acetylneuraminate 9-P1 Publication
  2. KM=19.2 mM for fructose 1,6-P21 Publication
  3. KM=2.7 mM for 6-P-gluconate1 Publication
  4. KM=5.9 mM for N-acetylglucosamine 6-P1 Publication
  1. Vmax=112 µmol/min/mg enzyme with N-acetylneuraminate 9-P as substrate1 Publication
  2. Vmax=6.10 µmol/min/mg enzyme with fructose 1,6-P2 as substrate1 Publication
  3. Vmax=2.79 µmol/min/mg enzyme with 6-P-gluconate as substrate1 Publication
  4. Vmax=2.46 µmol/min/mg enzyme with N-acetylglucosamine 6-P as substrate1 Publication
  5. Vmax=0.149 µmol/min/mg enzyme with sorbitol 6-P as substrate1 Publication
  6. Vmax=0.140 µmol/min/mg enzyme with 3-P glycerate as substrate1 Publication
  7. Vmax=0.095 µmol/min/mg enzyme with P-serine as substrate1 Publication
  8. Vmax=0.094 µmol/min/mg enzyme with glycerol 3-P as substrate1 Publication
  9. Vmax=0.090 µmol/min/mg enzyme with ribulose 5-P as substrate1 Publication
  10. Vmax=0.072 µmol/min/mg enzyme with N-acetylmannosamine 6-P as substrate1 Publication
  11. Vmax=0.063 µmol/min/mg enzyme with arabinose 6-P as substrate1 Publication
  12. Vmax=0.042 µmol/min/mg enzyme with ribose 6-P as substrate1 Publication
  13. Vmax=0.023 µmol/min/mg enzyme with glucosamine 6-P as substrate1 Publication
  14. Vmax=0.019 µmol/min/mg enzyme with phosphoglycolate as substrate1 Publication
  15. Vmax=0.019 µmol/min/mg enzyme with fructose 6-P as substrate1 Publication
  16. Vmax=0.017 µmol/min/mg enzyme with glycerol 2-P as substrate1 Publication
  17. Vmax=0.016 µmol/min/mg enzyme with glucose 6-P as substrate1 Publication
  18. Vmax=0.015 µmol/min/mg enzyme with mannose 6-P as substrate1 Publication
  19. Vmax=0.004 µmol/min/mg enzyme with glucose 1-P as substrate1 Publication
  20. Vmax=0.002 µmol/min/mg enzyme with P-enolpyruvate as substrate1 Publication
  21. Vmax=0.001 µmol/min/mg enzyme with ATP as substrate1 Publication

Pathwayi: N-acetylneuraminate biosynthesis

This protein is involved in the pathway N-acetylneuraminate biosynthesis, which is part of Amino-sugar metabolism.
View all proteins of this organism that are known to be involved in the pathway N-acetylneuraminate biosynthesis and in Amino-sugar metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei164 – 1641Substrate

GO - Molecular functioni

  • N-acylneuraminate-9-phosphatase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciMetaCyc:HS10082-MONOMER.
ReactomeiR-HSA-4085001. Sialic acid metabolism.
SABIO-RKQ8TBE9.
UniPathwayiUPA00630.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acylneuraminate-9-phosphatase (EC:3.1.3.29)
Alternative name(s):
Haloacid dehalogenase-like hydrolase domain-containing protein 4
Neu5Ac-9-Pase
Gene namesi
Name:NANP
Synonyms:C20orf147, HDHD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16140. NANP.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25689.

Chemistry

ChEMBLiCHEMBL2401602.

Polymorphism and mutation databases

BioMutaiNANP.
DMDMi30315932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248N-acylneuraminate-9-phosphatasePRO_0000083938Add
BLAST

Proteomic databases

EPDiQ8TBE9.
MaxQBiQ8TBE9.
PaxDbiQ8TBE9.
PeptideAtlasiQ8TBE9.
PRIDEiQ8TBE9.

PTM databases

DEPODiQ8TBE9.
iPTMnetiQ8TBE9.
PhosphoSiteiQ8TBE9.

Expressioni

Gene expression databases

BgeeiQ8TBE9.
CleanExiHS_NANP.
GenevisibleiQ8TBE9. HS.

Organism-specific databases

HPAiHPA050342.

Interactioni

Protein-protein interaction databases

BioGridi126729. 10 interactions.
IntActiQ8TBE9. 6 interactions.
STRINGi9606.ENSP00000302441.

Chemistry

BindingDBiQ8TBE9.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Turni15 – 173Combined sources
Helixi20 – 3819Combined sources
Helixi44 – 5815Combined sources
Turni63 – 653Combined sources
Helixi68 – 8417Combined sources
Helixi90 – 10718Combined sources
Helixi112 – 12211Combined sources
Beta strandi125 – 1317Combined sources
Helixi135 – 14410Combined sources
Helixi148 – 1503Combined sources
Beta strandi152 – 1565Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 1623Combined sources
Helixi167 – 17610Combined sources
Helixi181 – 1833Combined sources
Beta strandi184 – 1896Combined sources
Turni191 – 1933Combined sources
Helixi194 – 2007Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi224 – 2285Combined sources
Helixi230 – 2323Combined sources
Helixi233 – 2375Combined sources
Turni238 – 2414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W4MX-ray2.60A1-248[»]
4KNVX-ray1.99A/B7-242[»]
4KNWX-ray2.70A/B/C2-248[»]
ProteinModelPortaliQ8TBE9.
SMRiQ8TBE9. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TBE9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 143Substrate binding
Regioni131 – 1322Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00390000003094.
HOGENOMiHOG000248345.
HOVERGENiHBG051895.
InParanoidiQ8TBE9.
KOiK01097.
OMAiYHPALRD.
OrthoDBiEOG7JDQZJ.
PhylomeDBiQ8TBE9.
TreeFamiTF324589.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011950. HAD-SF_hydro_IA_CTE7.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02253. CTE7. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8TBE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLSRVRAVF FDLDNTLIDT AGASRRGMLE VIKLLQSKYH YKEEAEIICD
60 70 80 90 100
KVQVKLSKEC FHPYNTCITD LRTSHWEEAI QETKGGAANR KLAEECYFLW
110 120 130 140 150
KSTRLQHMTL AEDVKAMLTE LRKEVRLLLL TNGDRQTQRE KIEACACQSY
160 170 180 190 200
FDAVVVGGEQ REEKPAPSIF YYCCNLLGVQ PGDCVMVGDT LETDIQGGLN
210 220 230 240
AGLKATVWIN KNGIVPLKSS PVPHYMVSSV LELPALLQSI DCKVSMST
Length:248
Mass (Da):27,813
Last modified:June 1, 2002 - v1
Checksum:i360E6D7AB965294B
GO

Sequence cautioni

The sequence BAB85055.1 differs from that shown.It seems to be derived from genomic DNA and not from cDNA.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 5524IKLLQ…KVQVK → TSPPMALLWAGSVRPAPSCT LTSP in BAB85055 (PubMed:14702039).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055472 mRNA. Translation: BAG51524.1.
AK074335 mRNA. Translation: BAB85055.1. Sequence problems.
AL031673 Genomic DNA. Translation: CAI22444.1.
CH471133 Genomic DNA. Translation: EAX10081.1.
BC022552 mRNA. Translation: AAH22552.1.
CCDSiCCDS13173.1.
RefSeqiNP_689880.1. NM_152667.2.
UniGeneiHs.143137.
Hs.606268.

Genome annotation databases

EnsembliENST00000304788; ENSP00000302441; ENSG00000170191.
GeneIDi140838.
KEGGihsa:140838.
UCSCiuc002wuy.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055472 mRNA. Translation: BAG51524.1.
AK074335 mRNA. Translation: BAB85055.1. Sequence problems.
AL031673 Genomic DNA. Translation: CAI22444.1.
CH471133 Genomic DNA. Translation: EAX10081.1.
BC022552 mRNA. Translation: AAH22552.1.
CCDSiCCDS13173.1.
RefSeqiNP_689880.1. NM_152667.2.
UniGeneiHs.143137.
Hs.606268.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W4MX-ray2.60A1-248[»]
4KNVX-ray1.99A/B7-242[»]
4KNWX-ray2.70A/B/C2-248[»]
ProteinModelPortaliQ8TBE9.
SMRiQ8TBE9. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126729. 10 interactions.
IntActiQ8TBE9. 6 interactions.
STRINGi9606.ENSP00000302441.

Chemistry

BindingDBiQ8TBE9.
ChEMBLiCHEMBL2401602.

PTM databases

DEPODiQ8TBE9.
iPTMnetiQ8TBE9.
PhosphoSiteiQ8TBE9.

Polymorphism and mutation databases

BioMutaiNANP.
DMDMi30315932.

Proteomic databases

EPDiQ8TBE9.
MaxQBiQ8TBE9.
PaxDbiQ8TBE9.
PeptideAtlasiQ8TBE9.
PRIDEiQ8TBE9.

Protocols and materials databases

DNASUi140838.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304788; ENSP00000302441; ENSG00000170191.
GeneIDi140838.
KEGGihsa:140838.
UCSCiuc002wuy.5. human.

Organism-specific databases

CTDi140838.
GeneCardsiNANP.
HGNCiHGNC:16140. NANP.
HPAiHPA050342.
MIMi610763. gene.
neXtProtiNX_Q8TBE9.
PharmGKBiPA25689.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00390000003094.
HOGENOMiHOG000248345.
HOVERGENiHBG051895.
InParanoidiQ8TBE9.
KOiK01097.
OMAiYHPALRD.
OrthoDBiEOG7JDQZJ.
PhylomeDBiQ8TBE9.
TreeFamiTF324589.

Enzyme and pathway databases

UniPathwayiUPA00630.
BioCyciMetaCyc:HS10082-MONOMER.
ReactomeiR-HSA-4085001. Sialic acid metabolism.
SABIO-RKQ8TBE9.

Miscellaneous databases

EvolutionaryTraceiQ8TBE9.
GenomeRNAii140838.
PROiQ8TBE9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TBE9.
CleanExiHS_NANP.
GenevisibleiQ8TBE9. HS.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011950. HAD-SF_hydro_IA_CTE7.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02253. CTE7. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Brain.
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain.
  5. "Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase."
    Maliekal P., Vertommen D., Delpierre G., Van Schaftingen E.
    Glycobiology 16:165-172(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "The crystal structure of human N-acetylneuraminic acid phosphatase, NANP."
    Structural genomics consortium (SGC)
    Submitted (DEC-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE IONS.

Entry informationi

Entry nameiNANP_HUMAN
AccessioniPrimary (citable) accession number: Q8TBE9
Secondary accession number(s): B3KP12
, Q5JYN8, Q8TE97, Q9Y3N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 125 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.