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Protein

N-acylneuraminate-9-phosphatase

Gene

Nanp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by vanadate and calcium.By similarity

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

ReactomeiR-MMU-4085001. Sialic acid metabolism.
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:Hdhd4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 17, Chromosome 2

Organism-specific databases

MGIiMGI:1914561. Nanp.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248N-acylneuraminate-9-phosphatasePRO_0000083939Add
BLAST

Proteomic databases

EPDiQ9CPT3.
MaxQBiQ9CPT3.
PaxDbiQ9CPT3.
PRIDEiQ9CPT3.

PTM databases

PhosphoSiteiQ9CPT3.

Expressioni

Gene expression databases

BgeeiQ9CPT3.
GenevisibleiQ9CPT3. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000094869.

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 – 3718Combined sources
Helixi44 – 5714Combined sources
Helixi68 – 8417Combined sources
Helixi90 – 10617Combined sources
Helixi112 – 12211Combined sources
Beta strandi125 – 1317Combined sources
Helixi135 – 14511Combined sources
Helixi148 – 1503Combined sources
Beta strandi152 – 1565Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 1623Combined sources
Helixi167 – 17711Combined sources
Helixi181 – 1833Combined sources
Beta strandi184 – 1896Combined sources
Turni191 – 1933Combined sources
Helixi194 – 2007Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi224 – 2296Combined sources
Helixi230 – 2323Combined sources
Helixi233 – 2408Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GFHX-ray1.90A1-248[»]
ProteinModelPortaliQ9CPT3.
SMRiQ9CPT3. Positions 1-247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CPT3.

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.
InParanoidiQ9CPT3.
KOiK01097.
OMAiVRATVWI.
OrthoDBiEOG7JDQZJ.
PhylomeDBiQ9CPT3.
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.

Q9CPT3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLSRVRAVF FDLDNTLIDT AGASRRGMLE VIKLLQSKYH YKEEAEIICD
60 70 80 90 100
KVQVKLSKEC FHPYSTCITD VRTSHWEEAI QETKGGADNR KLAEECYFLW
110 120 130 140 150
KSTRLQHMIL ADDVKAMLTE LRKEVRLLLL TNGDRQTQRE KIEACACQSY
160 170 180 190 200
FDAIVIGGEQ KEEKPAPSIF YHCCDLLGVQ PGDCVMVGDT LETDIQGGLN
210 220 230 240
AGLKATVWIN KSGRVPLTSS PMPHYMVSSV LELPALLQSI DCKVSMSV
Length:248
Mass (Da):27,808
Last modified:June 1, 2001 - v1
Checksum:iFA1703873D7CC069
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005566 mRNA. Translation: BAB24126.1.
AK021344 mRNA. Translation: BAB32381.1.
BC018527 mRNA. Translation: AAH18527.1.
BC083086 mRNA. Translation: AAH83086.1.
CCDSiCCDS16864.1.
RefSeqiNP_080362.1. NM_026086.2.
UniGeneiMm.480682.

Genome annotation databases

EnsembliENSMUST00000057074; ENSMUSP00000094869; ENSMUSG00000043346.
ENSMUST00000066640; ENSMUSP00000063895; ENSMUSG00000053916.
GeneIDi67311.
KEGGimmu:67311.
UCSCiuc008muv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005566 mRNA. Translation: BAB24126.1.
AK021344 mRNA. Translation: BAB32381.1.
BC018527 mRNA. Translation: AAH18527.1.
BC083086 mRNA. Translation: AAH83086.1.
CCDSiCCDS16864.1.
RefSeqiNP_080362.1. NM_026086.2.
UniGeneiMm.480682.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GFHX-ray1.90A1-248[»]
ProteinModelPortaliQ9CPT3.
SMRiQ9CPT3. Positions 1-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000094869.

PTM databases

PhosphoSiteiQ9CPT3.

Proteomic databases

EPDiQ9CPT3.
MaxQBiQ9CPT3.
PaxDbiQ9CPT3.
PRIDEiQ9CPT3.

Protocols and materials databases

DNASUi67311.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057074; ENSMUSP00000094869; ENSMUSG00000043346.
ENSMUST00000066640; ENSMUSP00000063895; ENSMUSG00000053916.
GeneIDi67311.
KEGGimmu:67311.
UCSCiuc008muv.2. mouse.

Organism-specific databases

CTDi140838.
MGIiMGI:1914561. Nanp.

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00390000003094.
HOGENOMiHOG000248345.
HOVERGENiHBG051895.
InParanoidiQ9CPT3.
KOiK01097.
OMAiVRATVWI.
OrthoDBiEOG7JDQZJ.
PhylomeDBiQ9CPT3.
TreeFamiTF324589.

Enzyme and pathway databases

UniPathwayiUPA00630.
ReactomeiR-MMU-4085001. Sialic acid metabolism.

Miscellaneous databases

EvolutionaryTraceiQ9CPT3.
NextBioi324202.
PROiQ9CPT3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CPT3.
GenevisibleiQ9CPT3. MM.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland and Placenta.
  2. "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].
    Strain: FVB/N.
    Tissue: Limb and Mammary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney and Spleen.
  4. "Crystal structure of protein C20orf147 homolog (17391249) from Mus musculus at 1.90 A resolution."
    Joint center for structural genomics (JCSG)
    Submitted (MAR-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PHOSPHATE IONS.

Entry informationi

Entry nameiNANP_MOUSE
AccessioniPrimary (citable) accession number: Q9CPT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.