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Cytosolic 5'-nucleotidase 3A (EC 3.1.3.5) (7-methylguanosine phosphate-specific 5'-nucleotidase) (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase 3) (Cytosolic 5'-nucleotidase III) (cN-III) (Pyrimidine 5'-nucleotidase 1) (P5'N-1) (P5N-1) (PN-I) (Uridine 5'-monophosphate hydrolase 1) (p36)

 5NT3A_HUMAN             Reviewed;         336 AA.
Q9H0P0; A8K253; B2RAA5; B8ZZC4; Q6IPZ1; Q6NXS6; Q7L3G6; Q9P0P5;
Q9UC42; Q9UC43; Q9UC44; Q9UC45;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
14-NOV-2006, sequence version 3.
12-SEP-2018, entry version 163.
RecName: Full=Cytosolic 5'-nucleotidase 3A {ECO:0000305|PubMed:15968458, ECO:0000305|PubMed:24603684};
EC=3.1.3.5 {ECO:0000269|PubMed:15968458, ECO:0000269|PubMed:24603684};
AltName: Full=7-methylguanosine phosphate-specific 5'-nucleotidase {ECO:0000305|PubMed:24603684};
Short=7-methylguanosine nucleotidase;
EC=3.1.3.91 {ECO:0000269|PubMed:24603684};
AltName: Full=Cytosolic 5'-nucleotidase 3;
AltName: Full=Cytosolic 5'-nucleotidase III;
Short=cN-III;
AltName: Full=Pyrimidine 5'-nucleotidase 1;
Short=P5'N-1;
Short=P5N-1;
Short=PN-I;
AltName: Full=Uridine 5'-monophosphate hydrolase 1;
AltName: Full=p36;
Name=NT5C3A; Synonyms=NT5C3, P5N1, UMPH1; ORFNames=HSPC233;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF
92-111; 131-155; 226-240; 268-296 AND 313-332.
TISSUE=Placenta;
PubMed=10942414;
Amici A., Emanuelli M., Raffaelli N., Ruggieri S., Saccucci F.,
Magni G.;
"Human erythrocyte pyrimidine 5'-nucleotidase, PN-I, is identical to
p36, a protein associated to lupus inclusion formation in response to
alpha-interferon.";
Blood 96:1596-1598(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
VARIANT P5ND VAL-137.
PubMed=11369620; DOI=10.1182/blood.V97.11.3327;
Marinaki A.M., Escuredo E., Duley J.A., Simmonds H.A., Amici A.,
Naponelli V., Magni G., Seip M., Ben-Bassat I., Harley E.H.,
Thein S.L., Rees D.C.;
"Genetic basis of hemolytic anemia caused by pyrimidine 5'
nucleotidase deficiency.";
Blood 97:3327-3332(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain cortex, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Lung, Muscle, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-336 (ISOFORM 2).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[10]
PROTEIN SEQUENCE OF 83-95; 131-147; 226-240; 268-296 AND 311-329,
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=8557639; DOI=10.1074/jbc.271.20.11595;
Rich S.A., Bose M., Tempst P., Rudofsky U.H.;
"Purification, microsequencing, and immunolocalization of p36, a new
interferon-alpha-induced protein that is associated with human lupus
inclusions.";
J. Biol. Chem. 271:1118-1126(1996).
[11]
CHARACTERIZATION OF P5ND VAL-137; PRO-181; SER-229 AND ARG-280.
PubMed=15604219; DOI=10.1182/blood-2004-10-3895;
Chiarelli L.R., Bianchi P., Fermo E., Galizzi A., Iadarola P.,
Mattevi A., Zanella A., Valentini G.;
"Functional analysis of pyrimidine 5'-nucleotidase mutants causing
nonspherocytic hemolytic anemia.";
Blood 105:3340-3345(2005).
[12]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY,
CHARACTERIZATION OF VARIANTS P5ND SER-229 AND ARG-280, AND MUTAGENESIS
OF ASP-88; PHE-89; ASP-90; GLU-135; ASP-232; PHE-233 AND ASP-234.
PubMed=15968458; DOI=10.1007/s00018-005-5135-y;
Amici A., Ciccioli K., Naponelli V., Raffaelli N., Magni G.;
"Evidence for essential catalytic determinants for human erythrocyte
pyrimidine 5'-nucleotidase.";
Cell. Mol. Life Sci. 62:1613-1620(2005).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=24603684; DOI=10.1371/journal.pone.0090915;
Monecke T., Buschmann J., Neumann P., Wahle E., Ficner R.;
"Crystal structures of the novel cytosolic 5'-nucleotidase IIIB
explain its preference for m7GMP.";
PLoS ONE 9:90915-90915(2014).
[16]
X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 64-336 IN COMPLEX WITH
PHOSPHATE AND MAGNESIUM IONS, ACTIVE SITE, AND METAL BINDING.
PubMed=17405878; DOI=10.1074/jbc.M700917200;
Wallden K., Stenmark P., Nyman T., Flodin S., Graeslund S.,
Loppnau P., Bianchi V., Nordlund P.;
"Crystal structure of human cytosolic 5'-nucleotidase II: insights
into allosteric regulation and substrate recognition.";
J. Biol. Chem. 282:17828-17836(2007).
[17]
VARIANT P5ND SER-229.
PubMed=12930399; DOI=10.1046/j.1365-2141.2003.04532.x;
Bianchi P., Fermo E., Alfinito F., Vercellati C., Baserga M.,
Ferraro F., Guzzo I., Rotoli B., Zanella A.;
"Molecular characterization of six unrelated Italian patients affected
by pyrimidine 5'-nucleotidase deficiency.";
Br. J. Haematol. 122:847-851(2003).
[18]
VARIANTS P5ND PRO-181 AND ARG-280, IDENTIFICATION OF ISOFORM 4, TISSUE
SPECIFICITY, AND CHARACTERIZATION OF VARIANTS P5ND PRO-181 AND
ARG-280.
PubMed=15238149; DOI=10.1111/j.1365-2141.2004.05029.x;
Kanno H., Takizawa T., Miwa S., Fujii H.;
"Molecular basis of Japanese variants of pyrimidine 5'-nucleotidase
deficiency.";
Br. J. Haematol. 126:265-271(2004).
[19]
VARIANTS P5ND PRO-181; ARG-207 AND THR-297.
PubMed=16461318;
Manco L., Relvas L., Silva Pinto C., Pereira J., Almeida A.B.,
Ribeiro M.L.;
"Molecular characterization of five Portuguese patients with
pyrimidine 5'-nucleotidase deficient hemolytic anemia showing three
new P5'N-I mutations.";
Haematologica 91:266-267(2006).
[20]
CHARACTERIZATION OF VARIANTS P5ND ARG-113; ARG-207 AND THR-297.
PubMed=18499901; DOI=10.1016/j.bcmd.2007.10.005;
Chiarelli L.R., Morera S.M., Galizzi A., Fermo E., Zanella A.,
Valentini G.;
"Molecular basis of pyrimidine 5'-nucleotidase deficiency caused by 3
newly identified missense mutations (c.187T>C, c.469G>C and c.740T>C)
and a tabulation of known mutations.";
Blood Cells Mol. Dis. 40:295-301(2008).
[21]
VARIANT P5ND GLY-95.
PubMed=25153905; DOI=10.1016/j.bcmd.2014.05.009;
Dos Santos A., Dantas L.E., Traina F., Albuquerque D.M., Chaim E.A.,
Saad S.T.;
"Pyrimidine-5'-nucleotidase Campinas, a new mutation (p.R56G) in the
NT5C3 gene associated with pyrimidine-5'-nucleotidase type I
deficiency and influence of Gilbert's Syndrome on clinical
expression.";
Blood Cells Mol. Dis. 53:246-252(2014).
-!- FUNCTION: Nucleotidase which shows specific activity towards
cytidine monophosphate (CMP) and 7-methylguanosine monophosphate
(m(7)GMP) (PubMed:24603684). CMP seems to be the preferred
substrate (PubMed:15968458). {ECO:0000269|PubMed:15968458,
ECO:0000269|PubMed:24603684}.
-!- CATALYTIC ACTIVITY: N(7)-methyl-GMP + H(2)O = N(7)-methyl-
guanosine + phosphate. {ECO:0000269|PubMed:24603684}.
-!- CATALYTIC ACTIVITY: CMP + H(2)O = cytidine + phosphate.
{ECO:0000269|PubMed:15968458}.
-!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
+ phosphate. {ECO:0000269|PubMed:15968458}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15 uM for m(7)GMP (at 37 degrees Celsius)
{ECO:0000269|PubMed:24603684};
KM=66 uM for CMP {ECO:0000269|PubMed:15968458};
KM=80 uM for CMP (at 37 degrees Celsius)
{ECO:0000269|PubMed:24603684};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17405878}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=2;
IsoId=Q9H0P0-4; Sequence=Displayed;
Name=1; Synonyms=P5N-I;
IsoId=Q9H0P0-1; Sequence=VSP_021565;
Name=3; Synonyms=p36;
IsoId=Q9H0P0-2; Sequence=VSP_015623;
Name=4; Synonyms=P5N-R;
IsoId=Q9H0P0-3; Sequence=VSP_015624;
-!- TISSUE SPECIFICITY: Isoforms 1, 3 and 4 are expressed in
reticulocytes. Isoform 4 is hardly detectable in bone marrow and
fetal liver. {ECO:0000269|PubMed:11369620,
ECO:0000269|PubMed:15238149}.
-!- INDUCTION: Isoform 2 is induced by interferon alpha in Raji cells
in association with lupus inclusions.
{ECO:0000269|PubMed:8557639}.
-!- DISEASE: P5N deficiency (P5ND) [MIM:266120]: Autosomal recessive
condition causing hemolytic anemia characterized by marked
basophilic stippling and the accumulation of high concentrations
of pyrimidine nucleotides within the erythrocyte. It is implicated
in the anemia of lead poisoning and is possibly associated with
learning difficulties. {ECO:0000269|PubMed:11369620,
ECO:0000269|PubMed:12930399, ECO:0000269|PubMed:15238149,
ECO:0000269|PubMed:15604219, ECO:0000269|PubMed:15968458,
ECO:0000269|PubMed:16461318, ECO:0000269|PubMed:18499901,
ECO:0000269|PubMed:25153905}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF36153.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAG33630.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; AF312735; AAG33630.1; ALT_SEQ; mRNA.
EMBL; AL136716; CAB66650.1; -; mRNA.
EMBL; AK290118; BAF82807.1; -; mRNA.
EMBL; AK314109; BAG36802.1; -; mRNA.
EMBL; CR533518; CAG38549.1; -; mRNA.
EMBL; AC074338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC083863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471073; EAW94007.1; -; Genomic_DNA.
EMBL; CH471073; EAW94008.1; -; Genomic_DNA.
EMBL; BC013292; AAH13292.2; -; mRNA.
EMBL; BC015856; AAH15856.2; -; mRNA.
EMBL; BC066914; AAH66914.1; -; mRNA.
EMBL; BC071652; AAH71652.2; -; mRNA.
EMBL; AF151067; AAF36153.1; ALT_INIT; mRNA.
CCDS; CCDS34617.1; -. [Q9H0P0-1]
CCDS; CCDS55101.1; -. [Q9H0P0-3]
RefSeq; NP_001002009.1; NM_001002009.2. [Q9H0P0-1]
RefSeq; NP_001002010.1; NM_001002010.2.
RefSeq; NP_001159590.1; NM_001166118.2. [Q9H0P0-3]
RefSeq; NP_057573.2; NM_016489.12. [Q9H0P0-1]
RefSeq; XP_011513711.1; XM_011515409.2.
UniGene; Hs.487933; -.
PDB; 2CN1; X-ray; 2.67 A; A=64-336.
PDB; 2JGA; X-ray; 3.01 A; A=64-336.
PDB; 2VKQ; X-ray; 2.50 A; A=64-336.
PDBsum; 2CN1; -.
PDBsum; 2JGA; -.
PDBsum; 2VKQ; -.
ProteinModelPortal; Q9H0P0; -.
SMR; Q9H0P0; -.
BioGrid; 119408; 24.
IntAct; Q9H0P0; 11.
STRING; 9606.ENSP00000242210; -.
DEPOD; Q9H0P0; -.
iPTMnet; Q9H0P0; -.
PhosphoSitePlus; Q9H0P0; -.
BioMuta; NT5C3A; -.
DMDM; 117949804; -.
EPD; Q9H0P0; -.
PaxDb; Q9H0P0; -.
PeptideAtlas; Q9H0P0; -.
PRIDE; Q9H0P0; -.
ProteomicsDB; 80305; -.
ProteomicsDB; 80306; -. [Q9H0P0-1]
ProteomicsDB; 80307; -. [Q9H0P0-2]
ProteomicsDB; 80308; -. [Q9H0P0-3]
DNASU; 51251; -.
Ensembl; ENST00000381626; ENSP00000371039; ENSG00000122643. [Q9H0P0-3]
Ensembl; ENST00000396152; ENSP00000379456; ENSG00000122643. [Q9H0P0-1]
Ensembl; ENST00000405342; ENSP00000385261; ENSG00000122643. [Q9H0P0-1]
Ensembl; ENST00000409467; ENSP00000387166; ENSG00000122643. [Q9H0P0-3]
Ensembl; ENST00000620705; ENSP00000484415; ENSG00000122643. [Q9H0P0-4]
Ensembl; ENST00000643244; ENSP00000496364; ENSG00000122643. [Q9H0P0-1]
GeneID; 51251; -.
KEGG; hsa:51251; -.
UCSC; uc003tdi.5; human. [Q9H0P0-4]
CTD; 51251; -.
DisGeNET; 51251; -.
EuPathDB; HostDB:ENSG00000122643.18; -.
GeneCards; NT5C3A; -.
HGNC; HGNC:17820; NT5C3A.
HPA; HPA010630; -.
HPA; HPA029058; -.
MalaCards; NT5C3A; -.
MIM; 266120; phenotype.
MIM; 606224; gene.
neXtProt; NX_Q9H0P0; -.
OpenTargets; ENSG00000122643; -.
Orphanet; 35120; Hemolytic anemia due to pyrimidine 5' nucleotidase deficiency.
PharmGKB; PA31802; -.
eggNOG; KOG3128; Eukaryota.
eggNOG; ENOG410ZQJ8; LUCA.
GeneTree; ENSGT00390000012959; -.
HOVERGEN; HBG059750; -.
KO; K01081; -.
OMA; HNVIDNC; -.
OrthoDB; EOG091G0BCN; -.
PhylomeDB; Q9H0P0; -.
TreeFam; TF314663; -.
BRENDA; 3.1.3.91; 2681.
Reactome; R-HSA-73621; Pyrimidine catabolism.
SABIO-RK; Q9H0P0; -.
ChiTaRS; NT5C3A; human.
EvolutionaryTrace; Q9H0P0; -.
GeneWiki; NT5C3; -.
GenomeRNAi; 51251; -.
PRO; PR:Q9H0P0; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000122643; Expressed in 98 organ(s), highest expression level in quadriceps femoris.
ExpressionAtlas; Q9H0P0; baseline and differential.
Genevisible; Q9H0P0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0008253; F:5'-nucleotidase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; TAS:UniProtKB.
GO; GO:0046085; P:adenosine metabolic process; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
GO; GO:0046135; P:pyrimidine nucleoside catabolic process; TAS:Reactome.
GO; GO:0006213; P:pyrimidine nucleoside metabolic process; NAS:UniProtKB.
CDD; cd07504; HAD_5NT; 1.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
Pfam; PF05822; UMPH-1; 1.
SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01544; HAD-SF-IE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Endoplasmic reticulum;
Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 336 Cytosolic 5'-nucleotidase 3A.
/FTId=PRO_0000064387.
REGION 203 204 Substrate binding.
{ECO:0000269|PubMed:17405878}.
ACT_SITE 88 88 Nucleophile.
{ECO:0000269|PubMed:17405878}.
ACT_SITE 90 90 Proton donor.
{ECO:0000269|PubMed:17405878}.
METAL 88 88 Magnesium. {ECO:0000269|PubMed:17405878}.
METAL 90 90 Magnesium; via carbonyl oxygen.
{ECO:0000269|PubMed:17405878}.
METAL 277 277 Magnesium. {ECO:0000269|PubMed:17405878}.
BINDING 135 135 CMP. {ECO:0000250|UniProtKB:Q9W197}.
BINDING 135 135 N(7)-methyl-GMP.
{ECO:0000250|UniProtKB:Q9W197}.
BINDING 156 156 N(7)-methyl-GMP.
{ECO:0000250|UniProtKB:Q9W197}.
BINDING 252 252 Substrate.
{ECO:0000250|UniProtKB:Q9D020}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D020}.
VAR_SEQ 1 51 Missing (in isoform 4).
{ECO:0000303|PubMed:15238149}.
/FTId=VSP_015624.
VAR_SEQ 1 50 MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRK
TGRKTKIIE -> MTNQESAVHVK (in isoform 1).
{ECO:0000303|PubMed:11369620,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_021565.
VAR_SEQ 1 50 Missing (in isoform 3).
{ECO:0000303|PubMed:11369620,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_015623.
VARIANT 95 95 R -> G (in P5ND).
{ECO:0000269|PubMed:25153905}.
/FTId=VAR_073160.
VARIANT 113 113 C -> R (in P5ND; reduced catalytic
activity especially towards UMP).
{ECO:0000269|PubMed:18499901}.
/FTId=VAR_073161.
VARIANT 137 137 D -> V (in P5ND; reduced catalytic
activity; dbSNP:rs104894025).
{ECO:0000269|PubMed:11369620,
ECO:0000269|PubMed:15604219}.
/FTId=VAR_023511.
VARIANT 181 181 L -> P (in P5ND; reduced catalytic
activity in vitro; reduced protein
stability in vivo, probably through
increased proteasomal degradation).
{ECO:0000269|PubMed:15238149,
ECO:0000269|PubMed:15604219,
ECO:0000269|PubMed:16461318}.
/FTId=VAR_023512.
VARIANT 207 207 G -> R (in P5ND; reduced catalytic
activity especially towards UMP).
{ECO:0000269|PubMed:16461318,
ECO:0000269|PubMed:18499901}.
/FTId=VAR_073162.
VARIANT 229 229 N -> S (in P5ND; almost complete loss of
catalytic activity; dbSNP:rs104894028).
{ECO:0000269|PubMed:12930399,
ECO:0000269|PubMed:15604219,
ECO:0000269|PubMed:15968458}.
/FTId=VAR_023513.
VARIANT 280 280 G -> R (in P5ND; greatly reduced
catalytic activity; dbSNP:rs104894029).
{ECO:0000269|PubMed:15238149,
ECO:0000269|PubMed:15604219,
ECO:0000269|PubMed:15968458}.
/FTId=VAR_023514.
VARIANT 297 297 I -> T (in P5ND).
{ECO:0000269|PubMed:16461318,
ECO:0000269|PubMed:18499901}.
/FTId=VAR_073163.
MUTAGEN 88 88 D->N: Loss of nucleotidase and
phosphotransferase activity.
{ECO:0000269|PubMed:15968458}.
MUTAGEN 89 89 F->A: Almost complete loss of
nucleotidase and phosphotransferase
activity. {ECO:0000269|PubMed:15968458}.
MUTAGEN 90 90 D->N: Loss of nucleotidase and
phosphotransferase activity.
{ECO:0000269|PubMed:15968458}.
MUTAGEN 135 135 E->D: No effect on nucleotidase activity.
Almost complete loss of
phosphotransferase activity.
{ECO:0000269|PubMed:15968458}.
MUTAGEN 232 232 D->N: No effect on nucleotidase and
phosphotransferase activity.
{ECO:0000269|PubMed:15968458}.
MUTAGEN 233 233 F->A: Almost complete loss of
nucleotidase and phosphotransferase
activity. {ECO:0000269|PubMed:15968458}.
MUTAGEN 234 234 D->N: No effect on nucleotidase and
phosphotransferase activity.
{ECO:0000269|PubMed:15968458}.
CONFLICT 95 95 R -> K (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 144 144 E -> Q (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 329 329 N -> R (in Ref. 10; AA sequence).
{ECO:0000305}.
HELIX 65 78 {ECO:0000244|PDB:2VKQ}.
HELIX 80 82 {ECO:0000244|PDB:2VKQ}.
STRAND 83 87 {ECO:0000244|PDB:2VKQ}.
TURN 90 92 {ECO:0000244|PDB:2VKQ}.
STRAND 96 98 {ECO:0000244|PDB:2VKQ}.
HELIX 106 111 {ECO:0000244|PDB:2VKQ}.
HELIX 118 135 {ECO:0000244|PDB:2VKQ}.
STRAND 138 140 {ECO:0000244|PDB:2VKQ}.
HELIX 142 163 {ECO:0000244|PDB:2VKQ}.
HELIX 167 169 {ECO:0000244|PDB:2VKQ}.
HELIX 170 175 {ECO:0000244|PDB:2VKQ}.
HELIX 185 194 {ECO:0000244|PDB:2VKQ}.
STRAND 199 206 {ECO:0000244|PDB:2VKQ}.
HELIX 207 216 {ECO:0000244|PDB:2VKQ}.
STRAND 224 229 {ECO:0000244|PDB:2VKQ}.
STRAND 231 233 {ECO:0000244|PDB:2VKQ}.
STRAND 237 242 {ECO:0000244|PDB:2VKQ}.
HELIX 252 258 {ECO:0000244|PDB:2VKQ}.
HELIX 260 264 {ECO:0000244|PDB:2VKQ}.
TURN 265 268 {ECO:0000244|PDB:2VKQ}.
STRAND 271 279 {ECO:0000244|PDB:2VKQ}.
HELIX 280 283 {ECO:0000244|PDB:2VKQ}.
TURN 284 287 {ECO:0000244|PDB:2VKQ}.
STRAND 292 300 {ECO:0000244|PDB:2VKQ}.
HELIX 304 312 {ECO:0000244|PDB:2VKQ}.
STRAND 315 320 {ECO:0000244|PDB:2VKQ}.
HELIX 326 335 {ECO:0000244|PDB:2VKQ}.
SEQUENCE 336 AA; 37948 MW; C5D75CCF1BB61021 CRC64;
MRAPSMDRAA VARVGAVASA SVCALVAGVV LAQYIFTLKR KTGRKTKIIE MMPEFQKSSV
RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG KRCPTCHNII DNCKLVTDEC
RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV EWYTKSHGLL VQQALPKAKL KEIVAESDVM
LKEGYENFFD KLQQHSIPVF IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF MDFDETGVLK
GFKGELIHVF NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN VEHILKIGYL
NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL


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