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

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Nucleotide metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5'-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

With	Entry	#Exp.	IntAct	Notes
FXR2	P51116	2	EBI-742084,EBI-740459
MOBKL2B	Q86TA1	2	EBI-742084,EBI-751703
NUDT18	Q6ZVK8	2	EBI-742084,EBI-740486

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 561

561

Cytosolic purine 5'-nucleotidase

PRO_0000064389

Regions

Region

202 – 210

9

Substrate binding Potential

Compositional bias

549 – 561

13

Asp/Glu-rich (acidic)

Sites

Active site

52

1

Nucleophile

Active site

54

1

Proton donor

Metal binding

52

1

Magnesium

Metal binding

54

1

Magnesium; via carbonyl oxygen

Metal binding

351

1

Magnesium

Binding site

127

1

Allosteric activator 1

Binding site

154

1

Allosteric activator 2

Binding site

354

1

Allosteric activator 2

Binding site

436

1

Allosteric activator 1; via carbonyl oxygen

Binding site

453

1

Allosteric activator 2

Amino acid modifications

Modified residue

502

1

Phosphoserine Ref.4

Modified residue

527

1

Phosphoserine By similarity

Natural variations

Natural variant

3

1

T → A. [dbSNP:rs10883841]

VAR_024244

Natural variant

136

1

Q → R. [dbSNP:rs12262171]

VAR_030242

Secondary structure

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561

Helix Strand Turn

Details...

Helix

5 – 13

9

Helix

21 – 29

9

Helix

31 – 33

3

Beta strand

36 – 39

4

Helix

43 – 45

3

Beta strand

48 – 51

4

Turn

55 – 57

3

Helix

64 – 79

16

Helix

84 – 88

5

Beta strand

101 – 103

3

Turn

104 – 107

4

Beta strand

108 – 112

5

Beta strand

117 – 123

7

Helix

130 – 133

4

Turn

134 – 136

3

Turn

147 – 149

3

Beta strand

150 – 152

3

Helix

156 – 158

3

Helix

159 – 174

16

Beta strand

178 – 180

3

Beta strand

182 – 187

6

Beta strand

190 – 193

4

Helix

194 – 210

17

Helix

214 – 219

6

Helix

222 – 225

4

Helix

231 – 242

12

Beta strand

243 – 248

6

Helix

253 – 263

11

Beta strand

266 – 271

6

Helix

279 – 282

4

Beta strand

284 – 289

6

Helix

294 – 296

3

Beta strand

302 – 305

4

Turn

307 – 309

3

Beta strand

314 – 317

4

Beta strand

327 – 329

3

Helix

332 – 339

8

Helix

343 – 345

3

Beta strand

346 – 351

6

Helix

353 – 357

5

Helix

358 – 364

7

Beta strand

367 – 371

5

Helix

375 – 384

10

Helix

386 – 399

14

Helix

418 – 432

15

Beta strand

440 – 443

4

Helix

449 – 457

9

Beta strand

459 – 463

5

Helix

465 – 470

6

Helix

485 – 487

3

Sequences

	Sequence		Length	Mass (Da)
	P49902-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4C27D762575E0EA2	FASTA	561	64,970
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00029054.

PIR

JC2436.

RefSeq

NP_001127845.1.
NP_036361.1.

UniGene

Hs.97439.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J2C	X-ray	2.20	A	1-536	[»]
2JC9	X-ray	1.50	A	1-536	[»]
2JCM	X-ray	2.15	A	1-536	[»]

ProteinModelPortal

P49902.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49902. 12 interactions.

MINT

MINT-1436872.

STRING

P49902.

PTM databases

PhosphoSite

P49902.

Proteomic databases

PeptideAtlas

P49902.

PRIDE

P49902.

Genome annotation databases

Ensembl

ENST00000343289; ENSP00000339479; ENSG00000076685; Homo sapiens. [Genome view]
ENST00000404739; ENSP00000383960; ENSG00000076685; Homo sapiens. [Genome view]

GeneID

22978.

KEGG

hsa:22978.

UCSC

uc001kwo.1. human.

Organism-specific databases

CTD

22978.

GeneCards

GC10M104837.

H-InvDB

HIX0009172.

HGNC

HGNC:8022. NT5C2.

HPA

HPA003751.

MIM

600417. gene.

PharmGKB

PA31801.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16561.

HOGENOM

HBG506335.

HOVERGEN

HBG000025.

InParanoid

P49902.

OMA

CDRYTSC.

OrthoDB

EOG9HTCBT.

PhylomeDB

P49902.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-15169.

BRENDA

3.1.3.5. 247.

Reactome

REACT_1698. Metabolism of nucleotides.
REACT_1791. Xanthine formation.

Gene expression databases

ArrayExpress

P49902.

Bgee

P49902.

CleanEx

HS_NT5C2.

Genevestigator

P49902.

GermOnline

ENSG00000076685. Homo sapiens.

Family and domain databases

InterPro

IPR008380. HAD-SF_hydro_IG_5-nucl.
IPR016695. Pur_nucleotidase.
[Graphical view]

PANTHER

PTHR12103. HAD-SF_hydro_IG_5-nucl. 1 hit.

Pfam

PF05761. 5_nucleotid. 1 hit.
[Graphical view]

PIRSF

PIRSF017434. Purine_5'-nucleotidase. 1 hit.

TIGRFAMs

TIGR02244. HAD-IG-Ncltidse. 1 hit.

ProtoNet

Search...

Other Resources

DrugBank

DB00171. Adenosine triphosphate.
DB00811. Ribavirin.

NextBio

43793.

SOURCE

Search...

Entry information

Entry name

5NTC_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.