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P49902 (5NTC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Cytosolic purine 5'-nucleotidase

EC=3.1.3.5
Alternative name(s):
Cytosolic 5'-nucleotidase II
Gene names
Name:NT5C2
Synonyms:NT5B, NT5CP, PNT5
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.

Catalytic activity

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactor

Binds 1 magnesium ion per subunit.

Enzyme regulation

Allosterically activated by various compounds, including ATP.

Subunit structure

Homotetramer. Ref.6

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the 5'(3')-deoxyribonucleotidase family.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological processnucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function5'-nucleotidase activity

Traceable author statement. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 561561Cytosolic purine 5'-nucleotidase
PRO_0000064389

Regions

Region202 – 2109Substrate binding Potential
Compositional bias549 – 56113Asp/Glu-rich (acidic)

Sites

Active site521Nucleophile
Active site541Proton donor
Metal binding521Magnesium
Metal binding541Magnesium; via carbonyl oxygen
Metal binding3511Magnesium
Binding site1271Allosteric activator 1
Binding site1541Allosteric activator 2
Binding site3541Allosteric activator 2
Binding site4361Allosteric activator 1; via carbonyl oxygen
Binding site4531Allosteric activator 2

Amino acid modifications

Modified residue5021Phosphoserine Ref.4
Modified residue5271Phosphoserine By similarity

Natural variations

Natural variant31T → A. [dbSNP:rs10883841]
VAR_024244
Natural variant1361Q → R. [dbSNP:rs12262171]
VAR_030242

Secondary structure

............................................................................................ 561
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49902-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4C27D762575E0EA2

FASTA56164,970
        10         20         30         40         50         60 
MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY 

        70         80         90        100        110        120 
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV 

       130        140        150        160        170        180 
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS 

       190        200        210        220        230        240 
CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK 

       250        260        270        280        290        300 
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT 

       310        320        330        340        350        360 
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS 

       370        380        390        400        410        420 
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ 

       430        440        450        460        470        480 
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA 

       490        500        510        520        530        540 
HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA 

       550        560 
PQEITHCHDE DDDEEEEEEE E 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of human cytosolic purine 5'-nucleotidase."
Oka J., Matsumoto A., Hosokawa Y., Inoue S.
Biochem. Biophys. Res. Commun. 205:917-922(1994) [PubMed: 7999131] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed: 15164054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymph.
[4]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition."
Wallden K., Stenmark P., Nyman T., Flodin S., Graeslund S., Loppnau P., Bianchi V., Nordlund P.
J. Biol. Chem. 282:17828-17836(2007) [PubMed: 17405878] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-536 IN COMPLEX WITH ALLOSTERIC EFFECTOR AND MAGNESIUM IONS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38524 mRNA. Translation: BAA07529.1.
AL139817, AL360001 Genomic DNA. Translation: CAI40080.1.
AL360001, AL139817 Genomic DNA. Translation: CAI13473.1.
BC001595 mRNA. Translation: AAH01595.1.
IPIIPI00029054.
PIRJC2436.
RefSeqNP_001127845.1.
NP_036361.1.
UniGeneHs.97439.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J2CX-ray2.20A1-536[»]
2JC9X-ray1.50A1-536[»]
2JCMX-ray2.15A1-536[»]
ProteinModelPortalP49902.
ModBaseSearch...

Protein-protein interaction databases

IntActP49902. 12 interactions.
MINTMINT-1436872.
STRINGP49902.

PTM databases

PhosphoSiteP49902.

Proteomic databases

PeptideAtlasP49902.
PRIDEP49902.

Genome annotation databases

EnsemblENST00000343289; ENSP00000339479; ENSG00000076685; Homo sapiens. [Genome view]
ENST00000404739; ENSP00000383960; ENSG00000076685; Homo sapiens. [Genome view]
GeneID22978.
KEGGhsa:22978.
UCSCuc001kwo.1. human.

Organism-specific databases

CTD22978.
GeneCardsGC10M104837.
H-InvDBHIX0009172.
HGNCHGNC:8022. NT5C2.
HPAHPA003751.
MIM600417. gene.
PharmGKBPA31801.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16561.
HOGENOMHBG506335.
HOVERGENHBG000025.
InParanoidP49902.
OMACDRYTSC.
OrthoDBEOG9HTCBT.
PhylomeDBP49902.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15169.
BRENDA3.1.3.5. 247.
ReactomeREACT_1698. Metabolism of nucleotides.
REACT_1791. Xanthine formation.

Gene expression databases

ArrayExpressP49902.
BgeeP49902.
CleanExHS_NT5C2.
GenevestigatorP49902.
GermOnlineENSG00000076685. Homo sapiens.

Family and domain databases

InterProIPR008380. HAD-SF_hydro_IG_5-nucl.
IPR016695. Pur_nucleotidase.
[Graphical view]
PANTHERPTHR12103. HAD-SF_hydro_IG_5-nucl. 1 hit.
PfamPF05761. 5_nucleotid. 1 hit.
[Graphical view]
PIRSFPIRSF017434. Purine_5'-nucleotidase. 1 hit.
TIGRFAMsTIGR02244. HAD-IG-Ncltidse. 1 hit.
ProtoNetSearch...

Other Resources

DrugBankDB00171. Adenosine triphosphate.
DB00811. Ribavirin.
NextBio43793.
SOURCESearch...

Entry information

Entry name5NTC_HUMAN
AccessionPrimary (citable) accession number: P49902
Secondary accession number(s): Q5JUV5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: August 10, 2010
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families