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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)DescriptionActionsGraphical viewLength
Binding sitei164Substrate1

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.
ZFISH: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

DisGeNETi140838.
OpenTargetsiENSG00000170191.
PharmGKBiPA25689.

Chemistry databases

ChEMBLiCHEMBL2401602.

Polymorphism and mutation databases

BioMutaiNANP.
DMDMi30315932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000839381 – 248N-acylneuraminate-9-phosphataseAdd BLAST248

Proteomic databases

EPDiQ8TBE9.
MaxQBiQ8TBE9.
PaxDbiQ8TBE9.
PeptideAtlasiQ8TBE9.
PRIDEiQ8TBE9.

PTM databases

DEPODiQ8TBE9.
iPTMnetiQ8TBE9.
PhosphoSitePlusiQ8TBE9.

Expressioni

Gene expression databases

BgeeiENSG00000170191.
CleanExiHS_NANP.
GenevisibleiQ8TBE9. HS.

Organism-specific databases

HPAiHPA050342.

Interactioni

Protein-protein interaction databases

BioGridi126729. 10 interactors.
IntActiQ8TBE9. 6 interactors.
STRINGi9606.ENSP00000302441.

Chemistry databases

BindingDBiQ8TBE9.

Structurei

Secondary structure

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Turni15 – 17Combined sources3
Helixi20 – 38Combined sources19
Helixi44 – 58Combined sources15
Turni63 – 65Combined sources3
Helixi68 – 84Combined sources17
Helixi90 – 107Combined sources18
Helixi112 – 122Combined sources11
Beta strandi125 – 131Combined sources7
Helixi135 – 144Combined sources10
Helixi148 – 150Combined sources3
Beta strandi152 – 156Combined sources5
Helixi157 – 159Combined sources3
Beta strandi160 – 162Combined sources3
Helixi167 – 176Combined sources10
Helixi181 – 183Combined sources3
Beta strandi184 – 189Combined sources6
Turni191 – 193Combined sources3
Helixi194 – 200Combined sources7
Beta strandi204 – 209Combined sources6
Beta strandi224 – 228Combined sources5
Helixi230 – 232Combined sources3
Helixi233 – 237Combined sources5
Turni238 – 241Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8TBE9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni12 – 14Substrate binding3
Regioni131 – 132Substrate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00390000003094.
HOGENOMiHOG000248345.
HOVERGENiHBG051895.
InParanoidiQ8TBE9.
KOiK01097.
OMAiYHPALRD.
OrthoDBiEOG091G0G6E.
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 differs from that shown. It seems to be derived from genomic DNA and not from cDNA.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32 – 55IKLLQ…KVQVK → TSPPMALLWAGSVRPAPSCT LTSP in BAB85055 (PubMed:14702039).CuratedAdd BLAST24

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W4MX-ray2.60A1-248[»]
4KNVX-ray1.99A/B7-242[»]
4KNWX-ray2.70A/B/C2-248[»]
ProteinModelPortaliQ8TBE9.
SMRiQ8TBE9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126729. 10 interactors.
IntActiQ8TBE9. 6 interactors.
STRINGi9606.ENSP00000302441.

Chemistry databases

BindingDBiQ8TBE9.
ChEMBLiCHEMBL2401602.

PTM databases

DEPODiQ8TBE9.
iPTMnetiQ8TBE9.
PhosphoSitePlusiQ8TBE9.

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.
DisGeNETi140838.
GeneCardsiNANP.
HGNCiHGNC:16140. NANP.
HPAiHPA050342.
MIMi610763. gene.
neXtProtiNX_Q8TBE9.
OpenTargetsiENSG00000170191.
PharmGKBiPA25689.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00390000003094.
HOGENOMiHOG000248345.
HOVERGENiHBG051895.
InParanoidiQ8TBE9.
KOiK01097.
OMAiYHPALRD.
OrthoDBiEOG091G0G6E.
PhylomeDBiQ8TBE9.
TreeFamiTF324589.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ8TBE9.
GenomeRNAii140838.
PROiQ8TBE9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170191.
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...

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: November 2, 2016
This is version 128 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.