Full text data of NT5C2
NT5C2
(NT5B, NT5CP, PNT5)
[Confidence: low (only semi-automatic identification from reviews)]
Cytosolic purine 5'-nucleotidase; 3.1.3.5 (Cytosolic 5'-nucleotidase II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cytosolic purine 5'-nucleotidase; 3.1.3.5 (Cytosolic 5'-nucleotidase II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P49902
ID 5NTC_HUMAN Reviewed; 561 AA.
AC P49902; D3DR91; Q5JUV5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Cytosolic purine 5'-nucleotidase;
DE EC=3.1.3.5;
DE AltName: Full=Cytosolic 5'-nucleotidase II;
GN Name=NT5C2; Synonyms=NT5B, NT5CP, PNT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=7999131; DOI=10.1006/bbrc.1994.2752;
RA Oka J., Matsumoto A., Hosokawa Y., Inoue S.;
RT "Molecular cloning of human cytosolic purine 5'-nucleotidase.";
RL Biochem. Biophys. Res. Commun. 205:917-922(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-3.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-536 IN COMPLEX WITH
RP ALLOSTERIC EFFECTOR AND MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=17405878; DOI=10.1074/jbc.M700917200;
RA Wallden K., Stenmark P., Nyman T., Flodin S., Graeslund S.,
RA Loppnau P., Bianchi V., Nordlund P.;
RT "Crystal structure of human cytosolic 5'-nucleotidase II: insights
RT into allosteric regulation and substrate recognition.";
RL J. Biol. Chem. 282:17828-17836(2007).
CC -!- FUNCTION: May have a critical role in the maintenance of a
CC constant composition of intracellular purine/pyrimidine
CC nucleotides in cooperation with other nucleotidases.
CC Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other
CC purine nucleotides.
CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
CC + phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit.
CC -!- ENZYME REGULATION: Allosterically activated by various compounds,
CC including ATP.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P51116:FXR2; NbExp=3; IntAct=EBI-742084, EBI-740459;
CC Q86TA1:MOB3B; NbExp=3; IntAct=EBI-742084, EBI-751703;
CC Q6ZVK8:NUDT18; NbExp=3; IntAct=EBI-742084, EBI-740486;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
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DR EMBL; D38524; BAA07529.1; -; mRNA.
DR EMBL; AL139817; CAI40080.1; -; Genomic_DNA.
DR EMBL; AL360001; CAI40080.1; JOINED; Genomic_DNA.
DR EMBL; AL360001; CAI13473.1; -; Genomic_DNA.
DR EMBL; AL139817; CAI13473.1; JOINED; Genomic_DNA.
DR EMBL; CH471066; EAW49656.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49657.1; -; Genomic_DNA.
DR EMBL; BC001595; AAH01595.1; -; mRNA.
DR PIR; JC2436; JC2436.
DR RefSeq; NP_001127845.1; NM_001134373.2.
DR RefSeq; NP_036361.1; NM_012229.4.
DR RefSeq; XP_005269693.1; XM_005269636.1.
DR UniGene; Hs.97439; -.
DR PDB; 2J2C; X-ray; 2.20 A; A=1-536.
DR PDB; 2JC9; X-ray; 1.50 A; A=1-536.
DR PDB; 2JCM; X-ray; 2.15 A; A=1-536.
DR PDB; 2XCV; X-ray; 2.30 A; A=1-536.
DR PDB; 2XCW; X-ray; 1.90 A; A=1-536.
DR PDB; 2XCX; X-ray; 2.30 A; A=1-536.
DR PDB; 2XJB; X-ray; 2.30 A; A=1-536.
DR PDB; 2XJC; X-ray; 2.00 A; A=1-536.
DR PDB; 2XJD; X-ray; 2.00 A; A=1-536.
DR PDB; 2XJE; X-ray; 2.30 A; A=1-536.
DR PDB; 2XJF; X-ray; 2.10 A; A=1-536.
DR PDB; 4H4B; X-ray; 2.90 A; A=1-536.
DR PDBsum; 2J2C; -.
DR PDBsum; 2JC9; -.
DR PDBsum; 2JCM; -.
DR PDBsum; 2XCV; -.
DR PDBsum; 2XCW; -.
DR PDBsum; 2XCX; -.
DR PDBsum; 2XJB; -.
DR PDBsum; 2XJC; -.
DR PDBsum; 2XJD; -.
DR PDBsum; 2XJE; -.
DR PDBsum; 2XJF; -.
DR PDBsum; 4H4B; -.
DR ProteinModelPortal; P49902; -.
DR SMR; P49902; 3-488.
DR IntAct; P49902; 7.
DR MINT; MINT-1436872; -.
DR STRING; 9606.ENSP00000339479; -.
DR DrugBank; DB00171; Adenosine triphosphate.
DR DrugBank; DB00811; Ribavirin.
DR PhosphoSite; P49902; -.
DR DMDM; 1703012; -.
DR PaxDb; P49902; -.
DR PeptideAtlas; P49902; -.
DR PRIDE; P49902; -.
DR DNASU; 22978; -.
DR Ensembl; ENST00000343289; ENSP00000339479; ENSG00000076685.
DR Ensembl; ENST00000404739; ENSP00000383960; ENSG00000076685.
DR GeneID; 22978; -.
DR KEGG; hsa:22978; -.
DR UCSC; uc001kwo.3; human.
DR CTD; 22978; -.
DR GeneCards; GC10M104837; -.
DR HGNC; HGNC:8022; NT5C2.
DR HPA; HPA003751; -.
DR MIM; 600417; gene.
DR neXtProt; NX_P49902; -.
DR PharmGKB; PA31801; -.
DR eggNOG; NOG75103; -.
DR HOGENOM; HOG000246075; -.
DR HOVERGEN; HBG000025; -.
DR InParanoid; P49902; -.
DR KO; K01081; -.
DR OMA; HLENIKF; -.
DR OrthoDB; EOG7QK0BX; -.
DR PhylomeDB; P49902; -.
DR BioCyc; MetaCyc:HS01216-MONOMER; -.
DR BRENDA; 3.1.3.5; 2681.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P49902; -.
DR EvolutionaryTrace; P49902; -.
DR GenomeRNAi; 22978; -.
DR NextBio; 43793; -.
DR PRO; PR:P49902; -.
DR ArrayExpress; P49902; -.
DR Bgee; P49902; -.
DR CleanEx; HS_NT5C2; -.
DR Genevestigator; P49902; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008253; F:5'-nucleotidase activity; EXP:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050146; F:nucleoside phosphotransferase activity; TAS:Reactome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017144; P:drug metabolic process; TAS:Reactome.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.1000; -; 3.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR016695; Pur_nucleotidase.
DR PANTHER; PTHR12103; PTHR12103; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Complete proteome; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 561 Cytosolic purine 5'-nucleotidase.
FT /FTId=PRO_0000064389.
FT REGION 202 210 Substrate binding (Potential).
FT COMPBIAS 549 561 Asp/Glu-rich (acidic).
FT ACT_SITE 52 52 Nucleophile.
FT ACT_SITE 54 54 Proton donor.
FT METAL 52 52 Magnesium.
FT METAL 54 54 Magnesium; via carbonyl oxygen.
FT METAL 351 351 Magnesium.
FT BINDING 127 127 Allosteric activator 1.
FT BINDING 154 154 Allosteric activator 2.
FT BINDING 354 354 Allosteric activator 2.
FT BINDING 436 436 Allosteric activator 1; via carbonyl
FT oxygen.
FT BINDING 453 453 Allosteric activator 2.
FT MOD_RES 502 502 Phosphoserine.
FT VARIANT 3 3 T -> A (in dbSNP:rs10883841).
FT /FTId=VAR_024244.
FT VARIANT 136 136 Q -> R (in dbSNP:rs12262171).
FT /FTId=VAR_030242.
FT HELIX 5 13
FT HELIX 21 28
FT HELIX 31 33
FT STRAND 36 39
FT HELIX 43 45
FT STRAND 48 51
FT TURN 55 57
FT STRAND 58 60
FT HELIX 64 79
FT HELIX 84 88
FT STRAND 101 103
FT TURN 104 107
FT STRAND 108 112
FT STRAND 117 123
FT STRAND 126 128
FT HELIX 130 136
FT TURN 147 149
FT STRAND 150 152
FT HELIX 156 158
FT HELIX 159 174
FT STRAND 178 181
FT STRAND 184 187
FT STRAND 190 193
FT HELIX 194 210
FT HELIX 214 220
FT HELIX 222 225
FT HELIX 231 242
FT STRAND 243 248
FT HELIX 253 263
FT STRAND 266 271
FT HELIX 279 282
FT STRAND 284 289
FT HELIX 294 296
FT STRAND 302 306
FT TURN 307 310
FT STRAND 327 329
FT HELIX 332 339
FT HELIX 343 345
FT STRAND 346 351
FT HELIX 353 357
FT HELIX 358 364
FT STRAND 367 371
FT HELIX 375 384
FT HELIX 386 398
FT HELIX 421 432
FT STRAND 440 443
FT HELIX 449 457
FT STRAND 459 463
FT HELIX 465 470
FT HELIX 485 487
SQ SEQUENCE 561 AA; 64970 MW; 4C27D762575E0EA2 CRC64;
MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS
CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA
HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA
PQEITHCHDE DDDEEEEEEE E
//
ID 5NTC_HUMAN Reviewed; 561 AA.
AC P49902; D3DR91; Q5JUV5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Cytosolic purine 5'-nucleotidase;
DE EC=3.1.3.5;
DE AltName: Full=Cytosolic 5'-nucleotidase II;
GN Name=NT5C2; Synonyms=NT5B, NT5CP, PNT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=7999131; DOI=10.1006/bbrc.1994.2752;
RA Oka J., Matsumoto A., Hosokawa Y., Inoue S.;
RT "Molecular cloning of human cytosolic purine 5'-nucleotidase.";
RL Biochem. Biophys. Res. Commun. 205:917-922(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-3.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-536 IN COMPLEX WITH
RP ALLOSTERIC EFFECTOR AND MAGNESIUM IONS, AND SUBUNIT.
RX PubMed=17405878; DOI=10.1074/jbc.M700917200;
RA Wallden K., Stenmark P., Nyman T., Flodin S., Graeslund S.,
RA Loppnau P., Bianchi V., Nordlund P.;
RT "Crystal structure of human cytosolic 5'-nucleotidase II: insights
RT into allosteric regulation and substrate recognition.";
RL J. Biol. Chem. 282:17828-17836(2007).
CC -!- FUNCTION: May have a critical role in the maintenance of a
CC constant composition of intracellular purine/pyrimidine
CC nucleotides in cooperation with other nucleotidases.
CC Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other
CC purine nucleotides.
CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
CC + phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit.
CC -!- ENZYME REGULATION: Allosterically activated by various compounds,
CC including ATP.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P51116:FXR2; NbExp=3; IntAct=EBI-742084, EBI-740459;
CC Q86TA1:MOB3B; NbExp=3; IntAct=EBI-742084, EBI-751703;
CC Q6ZVK8:NUDT18; NbExp=3; IntAct=EBI-742084, EBI-740486;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D38524; BAA07529.1; -; mRNA.
DR EMBL; AL139817; CAI40080.1; -; Genomic_DNA.
DR EMBL; AL360001; CAI40080.1; JOINED; Genomic_DNA.
DR EMBL; AL360001; CAI13473.1; -; Genomic_DNA.
DR EMBL; AL139817; CAI13473.1; JOINED; Genomic_DNA.
DR EMBL; CH471066; EAW49656.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49657.1; -; Genomic_DNA.
DR EMBL; BC001595; AAH01595.1; -; mRNA.
DR PIR; JC2436; JC2436.
DR RefSeq; NP_001127845.1; NM_001134373.2.
DR RefSeq; NP_036361.1; NM_012229.4.
DR RefSeq; XP_005269693.1; XM_005269636.1.
DR UniGene; Hs.97439; -.
DR PDB; 2J2C; X-ray; 2.20 A; A=1-536.
DR PDB; 2JC9; X-ray; 1.50 A; A=1-536.
DR PDB; 2JCM; X-ray; 2.15 A; A=1-536.
DR PDB; 2XCV; X-ray; 2.30 A; A=1-536.
DR PDB; 2XCW; X-ray; 1.90 A; A=1-536.
DR PDB; 2XCX; X-ray; 2.30 A; A=1-536.
DR PDB; 2XJB; X-ray; 2.30 A; A=1-536.
DR PDB; 2XJC; X-ray; 2.00 A; A=1-536.
DR PDB; 2XJD; X-ray; 2.00 A; A=1-536.
DR PDB; 2XJE; X-ray; 2.30 A; A=1-536.
DR PDB; 2XJF; X-ray; 2.10 A; A=1-536.
DR PDB; 4H4B; X-ray; 2.90 A; A=1-536.
DR PDBsum; 2J2C; -.
DR PDBsum; 2JC9; -.
DR PDBsum; 2JCM; -.
DR PDBsum; 2XCV; -.
DR PDBsum; 2XCW; -.
DR PDBsum; 2XCX; -.
DR PDBsum; 2XJB; -.
DR PDBsum; 2XJC; -.
DR PDBsum; 2XJD; -.
DR PDBsum; 2XJE; -.
DR PDBsum; 2XJF; -.
DR PDBsum; 4H4B; -.
DR ProteinModelPortal; P49902; -.
DR SMR; P49902; 3-488.
DR IntAct; P49902; 7.
DR MINT; MINT-1436872; -.
DR STRING; 9606.ENSP00000339479; -.
DR DrugBank; DB00171; Adenosine triphosphate.
DR DrugBank; DB00811; Ribavirin.
DR PhosphoSite; P49902; -.
DR DMDM; 1703012; -.
DR PaxDb; P49902; -.
DR PeptideAtlas; P49902; -.
DR PRIDE; P49902; -.
DR DNASU; 22978; -.
DR Ensembl; ENST00000343289; ENSP00000339479; ENSG00000076685.
DR Ensembl; ENST00000404739; ENSP00000383960; ENSG00000076685.
DR GeneID; 22978; -.
DR KEGG; hsa:22978; -.
DR UCSC; uc001kwo.3; human.
DR CTD; 22978; -.
DR GeneCards; GC10M104837; -.
DR HGNC; HGNC:8022; NT5C2.
DR HPA; HPA003751; -.
DR MIM; 600417; gene.
DR neXtProt; NX_P49902; -.
DR PharmGKB; PA31801; -.
DR eggNOG; NOG75103; -.
DR HOGENOM; HOG000246075; -.
DR HOVERGEN; HBG000025; -.
DR InParanoid; P49902; -.
DR KO; K01081; -.
DR OMA; HLENIKF; -.
DR OrthoDB; EOG7QK0BX; -.
DR PhylomeDB; P49902; -.
DR BioCyc; MetaCyc:HS01216-MONOMER; -.
DR BRENDA; 3.1.3.5; 2681.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P49902; -.
DR EvolutionaryTrace; P49902; -.
DR GenomeRNAi; 22978; -.
DR NextBio; 43793; -.
DR PRO; PR:P49902; -.
DR ArrayExpress; P49902; -.
DR Bgee; P49902; -.
DR CleanEx; HS_NT5C2; -.
DR Genevestigator; P49902; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0008253; F:5'-nucleotidase activity; EXP:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050146; F:nucleoside phosphotransferase activity; TAS:Reactome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017144; P:drug metabolic process; TAS:Reactome.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.1000; -; 3.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR016695; Pur_nucleotidase.
DR PANTHER; PTHR12103; PTHR12103; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Complete proteome; Cytoplasm;
KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 561 Cytosolic purine 5'-nucleotidase.
FT /FTId=PRO_0000064389.
FT REGION 202 210 Substrate binding (Potential).
FT COMPBIAS 549 561 Asp/Glu-rich (acidic).
FT ACT_SITE 52 52 Nucleophile.
FT ACT_SITE 54 54 Proton donor.
FT METAL 52 52 Magnesium.
FT METAL 54 54 Magnesium; via carbonyl oxygen.
FT METAL 351 351 Magnesium.
FT BINDING 127 127 Allosteric activator 1.
FT BINDING 154 154 Allosteric activator 2.
FT BINDING 354 354 Allosteric activator 2.
FT BINDING 436 436 Allosteric activator 1; via carbonyl
FT oxygen.
FT BINDING 453 453 Allosteric activator 2.
FT MOD_RES 502 502 Phosphoserine.
FT VARIANT 3 3 T -> A (in dbSNP:rs10883841).
FT /FTId=VAR_024244.
FT VARIANT 136 136 Q -> R (in dbSNP:rs12262171).
FT /FTId=VAR_030242.
FT HELIX 5 13
FT HELIX 21 28
FT HELIX 31 33
FT STRAND 36 39
FT HELIX 43 45
FT STRAND 48 51
FT TURN 55 57
FT STRAND 58 60
FT HELIX 64 79
FT HELIX 84 88
FT STRAND 101 103
FT TURN 104 107
FT STRAND 108 112
FT STRAND 117 123
FT STRAND 126 128
FT HELIX 130 136
FT TURN 147 149
FT STRAND 150 152
FT HELIX 156 158
FT HELIX 159 174
FT STRAND 178 181
FT STRAND 184 187
FT STRAND 190 193
FT HELIX 194 210
FT HELIX 214 220
FT HELIX 222 225
FT HELIX 231 242
FT STRAND 243 248
FT HELIX 253 263
FT STRAND 266 271
FT HELIX 279 282
FT STRAND 284 289
FT HELIX 294 296
FT STRAND 302 306
FT TURN 307 310
FT STRAND 327 329
FT HELIX 332 339
FT HELIX 343 345
FT STRAND 346 351
FT HELIX 353 357
FT HELIX 358 364
FT STRAND 367 371
FT HELIX 375 384
FT HELIX 386 398
FT HELIX 421 432
FT STRAND 440 443
FT HELIX 449 457
FT STRAND 459 463
FT HELIX 465 470
FT HELIX 485 487
SQ SEQUENCE 561 AA; 64970 MW; 4C27D762575E0EA2 CRC64;
MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS
CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA
HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA
PQEITHCHDE DDDEEEEEEE E
//
MIM
600417
*RECORD*
*FIELD* NO
600417
*FIELD* TI
*600417 5-PRIME-@NUCLEOTIDASE, CYTOSOLIC II; NT5C2
;;NUCLEOTIDASE, 5-PRIME, CYTOSOLIC II;;
read moreNUCLEOTIDASE, 5-PRIME, TYPE B; NT5B;;
PURINE 5-PRIME-NUCLEOTIDASE; PNT5
*FIELD* TX
DESCRIPTION
Purine 5-prime-nucleotidase (EC 3.1.3.5) preferentially hydrolyzes
inosine 5-prime-monophosphate (IMP) and other purine nucleotides, and is
allosterically activated by various compounds, including ATP. The enzyme
is exclusively located in the cytoplasmic matrix of cells and may have a
critical role in the maintenance of a constant composition of
intracellular purine/pyrimidine nucleotides in cooperation with other
nucleotidases.
CLONING
Oka et al. (1994) found 2 distinct but closely related types of cDNAs
for purine 5-prime-nucleotidase in a chicken liver cDNA library. The
encoded A- and B-type proteins were similar throughout a central core of
472 amino acids sharing 79% sequence identity. Using degenerate
oligonucleotides based on identical portions of amino acid sequences
between A- and B-type subunits of the chicken enzyme, Oka et al. (1994)
isolated human cytosolic purine 5-prime-nucleotidase cDNA clones with
PCR. The predicted open reading frame encoded a protein of 561 amino
acids with a molecular mass of 64,966 Da. The deduced amino acid
sequence exhibited 95% identity with the sequence of the B-type subunit
of chicken enzyme. Northern blot analysis of placental polyadenylated
RNA revealed a single band of 3.6 kb.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NT5C2
gene to chromosome 10 (TMAP sts-D38524).
*FIELD* RF
1. Oka, J.; Matsumoto, A.; Hosokawa, Y.; Inoue, S.: Molecular cloning
of human cytosolic purine 5-prime-nucleotidase. Biochem. Biophys.
Res. Commun. 205: 917-922, 1994.
*FIELD* CN
Joanna S. Amberger - updated: 4/19/2002
*FIELD* CD
Victor A. McKusick: 2/17/1995
*FIELD* ED
carol: 10/12/2004
joanna: 4/19/2002
mgross: 7/17/2000
carol: 2/17/1995
*RECORD*
*FIELD* NO
600417
*FIELD* TI
*600417 5-PRIME-@NUCLEOTIDASE, CYTOSOLIC II; NT5C2
;;NUCLEOTIDASE, 5-PRIME, CYTOSOLIC II;;
read moreNUCLEOTIDASE, 5-PRIME, TYPE B; NT5B;;
PURINE 5-PRIME-NUCLEOTIDASE; PNT5
*FIELD* TX
DESCRIPTION
Purine 5-prime-nucleotidase (EC 3.1.3.5) preferentially hydrolyzes
inosine 5-prime-monophosphate (IMP) and other purine nucleotides, and is
allosterically activated by various compounds, including ATP. The enzyme
is exclusively located in the cytoplasmic matrix of cells and may have a
critical role in the maintenance of a constant composition of
intracellular purine/pyrimidine nucleotides in cooperation with other
nucleotidases.
CLONING
Oka et al. (1994) found 2 distinct but closely related types of cDNAs
for purine 5-prime-nucleotidase in a chicken liver cDNA library. The
encoded A- and B-type proteins were similar throughout a central core of
472 amino acids sharing 79% sequence identity. Using degenerate
oligonucleotides based on identical portions of amino acid sequences
between A- and B-type subunits of the chicken enzyme, Oka et al. (1994)
isolated human cytosolic purine 5-prime-nucleotidase cDNA clones with
PCR. The predicted open reading frame encoded a protein of 561 amino
acids with a molecular mass of 64,966 Da. The deduced amino acid
sequence exhibited 95% identity with the sequence of the B-type subunit
of chicken enzyme. Northern blot analysis of placental polyadenylated
RNA revealed a single band of 3.6 kb.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NT5C2
gene to chromosome 10 (TMAP sts-D38524).
*FIELD* RF
1. Oka, J.; Matsumoto, A.; Hosokawa, Y.; Inoue, S.: Molecular cloning
of human cytosolic purine 5-prime-nucleotidase. Biochem. Biophys.
Res. Commun. 205: 917-922, 1994.
*FIELD* CN
Joanna S. Amberger - updated: 4/19/2002
*FIELD* CD
Victor A. McKusick: 2/17/1995
*FIELD* ED
carol: 10/12/2004
joanna: 4/19/2002
mgross: 7/17/2000
carol: 2/17/1995