Q9H0P0 (5NT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytosolic 5'-nucleotidase 3
EC=3.1.3.5

Alternative name(s):
Cytosolic 5'-nucleotidase III
Short name=cN-III
Pyrimidine 5'-nucleotidase 1
Short name=P5'N-1
Short name=P5N-1
Short name=PN-I
Uridine 5'-monophosphate hydrolase 1
p36

Gene names

Name:	NT5C3
Synonyms:	P5N1, UMPH1
ORF Names:	HSPC233

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Can act both as nucleotidase and as phosphotransferase.
Catalytic activity	A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Subunit structure	Monomer. Ref.12
Subcellular location	Cytoplasm Potential Ref.11. Isoform 2: Endoplasmic reticulum Ref.11.
Tissue specificity	Isoform 1 and isoform 3 are expressed in reticulocytes and lymphocytes. Isoform 4 is expressed only in reticulocytes. Ref.2 Ref.3
Induction	Isoform 2 is induced by interferon alpha in Raji cells in association with lupus inclusions. Ref.11
Involvement in disease	P5N deficiency (P5ND) [MIM:266120]: Autosomal recessive condition causing hemolytic anemia characterized by marked basophilic stipplig 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. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the pyrimidine 5'-nucleotidase family.
Biophysicochemical properties	Kinetic parameters: KM=66 µM for CMP Ref.12
Sequence caution	The sequence AAF36153.1 differs from that shown. Reason: Erroneous initiation. The sequence AAG33630.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cytoplasm Endoplasmic reticulum
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	nucleotide metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleobase metabolic process Traceable author statement. Source: Reactome pyrimidine nucleoside catabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome endoplasmic reticulum Inferred from direct assay Ref.11. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	2'-phosphotransferase activity Non-traceable author statement PubMed 9428647. Source: UniProtKB 5'-nucleotidase activity Inferred from direct assay Ref.1. Source: UniProtKB magnesium ion binding Non-traceable author statement PubMed 11795870. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q9H0P0-4)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: Q9H0P0-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIE → MTNQESAVHVK

Isoform 3 (identifier: Q9H0P0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Isoform 4 (identifier: Q9H0P0-3)

Also known as: P5N-R;

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 336

336

Cytosolic 5'-nucleotidase 3

PRO_0000064387

Regions

Region

203 – 204

2

Substrate binding

Sites

Active site

88

1

Nucleophile

Active site

90

1

Proton donor

Metal binding

88

1

Magnesium

Metal binding

90

1

Magnesium; via carbonyl oxygen

Metal binding

277

1

Magnesium

Binding site

252

1

Substrate

Natural variations

Alternative sequence

1 – 51

51

Missing in isoform 4.

VSP_015624

Alternative sequence

1 – 50

50

MRAPS…TKIIE → MTNQESAVHVK in isoform 1.

VSP_021565

Alternative sequence

1 – 50

50

Missing in isoform 3.

VSP_015623

Natural variant

137

1

D → V in P5N deficiency; may alter protein structure. Ref.2 Ref.12

VAR_023511

Natural variant

181

1

L → P in P5N deficiency; may alter protein structure and markedly decreases activity. Ref.3 Ref.12

VAR_023512

Natural variant

229

1

N → S in P5N deficiency; markedly decreases activity. Ref.12 Ref.15

VAR_023513

Natural variant

280

1

G → R in P5N deficiency; markedly decreases activity. Ref.3 Ref.12

VAR_023514

Experimental info

Mutagenesis

88

1

D → N: Loss of nucleotidase and phosphotransferase activity. Ref.12

Mutagenesis

89

1

F → A: Increases Km for CMP 45-fold. Reduces nucleotidase and phosphotransferase activity by 99%. Ref.12

Mutagenesis

90

1

D → N: Loss of nucleotidase and phosphotransferase activity. Ref.12

Mutagenesis

135

1

E → D: No effect on nucleotidase activity. Reduces phosphotransferase activity by 99%. Ref.12

Mutagenesis

233

1

F → A: Reduces nucleotidase and phosphotransferase activity by 97%. Ref.12

Sequence conflict

95

1

R → K AA sequence Ref.11

Sequence conflict

144

1

E → Q AA sequence Ref.11

Sequence conflict

329

1

N → R AA sequence Ref.11

Secondary structure

1

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336

Helix Strand Turn

Details...

Helix

65 – 78

14

Helix

80 – 82

3

Beta strand

83 – 87

5

Turn

90 – 92

3

Beta strand

96 – 98

3

Helix

106 – 111

6

Helix

118 – 135

18

Beta strand

138 – 140

3

Helix

142 – 163

22

Helix

167 – 169

3

Helix

170 – 175

6

Helix

185 – 194

10

Beta strand

199 – 206

8

Helix

207 – 216

10

Beta strand

224 – 229

6

Beta strand

231 – 233

3

Beta strand

237 – 242

6

Helix

252 – 258

7

Helix

260 – 264

5

Turn

265 – 268

4

Beta strand

271 – 279

9

Helix

280 – 283

4

Turn

284 – 287

4

Beta strand

292 – 300

9

Helix

304 – 312

9

Beta strand

315 – 320

6

Helix

326 – 335

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified November 14, 2006. Version 3. Checksum: C5D75CCF1BB61021	FASTA	336	37,948
	10 20 30 40 50 60 MRAPSMDRAA VARVGAVASA SVCALVAGVV LAQYIFTLKR KTGRKTKIIE MMPEFQKSSV 70 80 90 100 110 120 RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG KRCPTCHNII DNCKLVTDEC 130 140 150 160 170 180 RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV EWYTKSHGLL VQQALPKAKL KEIVAESDVM 190 200 210 220 230 240 LKEGYENFFD KLQQHSIPVF IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF MDFDETGVLK 250 260 270 280 290 300 GFKGELIHVF NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN VEHILKIGYL 310 320 330 NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL
	Isoform 1 [UniParc]. Checksum: FB91A66DD2273598	FASTA	297	33,915
	10 20 30 40 50 60 MTNQESAVHV KMMPEFQKSS VRIKNPTRVE EIICGLIKGG AAKLQIITDF DMTLSRFSYK 70 80 90 100 110 120 GKRCPTCHNI IDNCKLVTDE CRKKLLQLKE KYYAIEVDPV LTVEEKYPYM VEWYTKSHGL 130 140 150 160 170 180 LVQQALPKAK LKEIVAESDV MLKEGYENFF DKLQQHSIPV FIFSAGIGDV LEEVIRQAGV 190 200 210 220 230 240 YHPNVKVVSN FMDFDETGVL KGFKGELIHV FNKHDGALRN TEYFNQLKDN SNIILLGDSQ 250 260 270 280 290 GDLRMADGVA NVEHILKIGY LNDRVDELLE KYMDSYDIVL VQDESLEVAN SILQKIL
	Isoform 3 [UniParc]. Checksum: 29313E2790194ED9	FASTA	286	32,690
	10 20 30 40 50 60 MMPEFQKSSV RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG KRCPTCHNII 70 80 90 100 110 120 DNCKLVTDEC RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV EWYTKSHGLL VQQALPKAKL 130 140 150 160 170 180 KEIVAESDVM LKEGYENFFD KLQQHSIPVF IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF 190 200 210 220 230 240 MDFDETGVLK GFKGELIHVF NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN 250 260 270 280 VEHILKIGYL NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL
	Isoform 4 (P5N-R) [UniParc]. Checksum: CB3B6812C90A5578	FASTA	285	32,559
	10 20 30 40 50 60 MPEFQKSSVR IKNPTRVEEI ICGLIKGGAA KLQIITDFDM TLSRFSYKGK RCPTCHNIID 70 80 90 100 110 120 NCKLVTDECR KKLLQLKEKY YAIEVDPVLT VEEKYPYMVE WYTKSHGLLV QQALPKAKLK 130 140 150 160 170 180 EIVAESDVML KEGYENFFDK LQQHSIPVFI FSAGIGDVLE EVIRQAGVYH PNVKVVSNFM 190 200 210 220 230 240 DFDETGVLKG FKGELIHVFN KHDGALRNTE YFNQLKDNSN IILLGDSQGD LRMADGVANV 250 260 270 280 EHILKIGYLN DRVDELLEKY MDSYDIVLVQ DESLEVANSI LQKIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human erythrocyte pyrimidine 5'-nucleotidase, PN-I, is identical to p36, a protein associated to lupus inclusion formation in response to alpha-interferon." Amici A., Emanuelli M., Raffaelli N., Ruggieri S., Saccucci F., Magni G. Blood 96:1596-1598(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE. Tissue: Placenta.
[2]	"Genetic basis of hemolytic anemia caused by pyrimidine 5' nucleotidase deficiency." 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. Blood 97:3327-3332(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, VARIANT P5N DEFICIENCY VAL-137.
[3]	"Molecular basis of Japanese variants of pyrimidine 5'-nucleotidase deficiency." Kanno H., Takizawa T., Miwa S., Fujii H. Br. J. Haematol. 126:265-271(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, VARIANTS P5N DEFICIENCY PRO-181 AND ARG-280, CHARACTERIZATION OF VARIANTS P5N DEFICIENCY PRO-181 AND ARG-280.
[4]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." 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. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Kidney.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Brain cortex and Thalamus.
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]	"The DNA sequence of human chromosome 7." 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. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORMS 1 AND 2). Tissue: Brain, Lung, Muscle and Prostate.
[10]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." 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. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-336 (ISOFORM 2). Tissue: Umbilical cord blood.
[11]	"Purification, microsequencing, and immunolocalization of p36, a new interferon-alpha-induced protein that is associated with human lupus inclusions." Rich S.A., Bose M., Tempst P., Rudofsky U.H. J. Biol. Chem. 271:1118-1126(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-95; 131-147; 226-240; 268-296 AND 311-329, INDUCTION, SUBCELLULAR LOCATION.
[12]	"Evidence for essential catalytic determinants for human erythrocyte pyrimidine 5'-nucleotidase." Amici A., Ciccioli K., Naponelli V., Raffaelli N., Magni G. Cell. Mol. Life Sci. 62:1613-1620(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS P5N DEFICIENCY VAL-137; PRO-181; SER-229 AND ARG-280, MUTAGENESIS OF ASP-88; PHE-89; ASP-90; GLU-135 AND PHE-233.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 64-336 IN COMPLEX WITH PHOSPHATE AND MAGNESIUM IONS.
[15]	"Molecular characterization of six unrelated Italian patients affected by pyrimidine 5'-nucleotidase deficiency." Bianchi P., Fermo E., Alfinito F., Vercellati C., Baserga M., Ferraro F., Guzzo I., Rotoli B., Zanella A. Br. J. Haematol. 122:847-851(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT P5N DEFICIENCY SER-229.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF312735 mRNA. Translation: AAG33630.1. Sequence problems.
AL136716 mRNA. Translation: CAB66650.1.
AK290118 mRNA. Translation: BAF82807.1.
AK314109 mRNA. Translation: BAG36802.1.
CR533518 mRNA. Translation: CAG38549.1.
AC074338 Genomic DNA. No translation available.
AC083863 Genomic DNA. No translation available.
CH471073 Genomic DNA. Translation: EAW94007.1.
CH471073 Genomic DNA. Translation: EAW94008.1.
BC013292 mRNA. Translation: AAH13292.2.
BC015856 mRNA. Translation: AAH15856.2.
BC066914 mRNA. Translation: AAH66914.1.
BC071652 mRNA. Translation: AAH71652.2.
AF151067 mRNA. Translation: AAF36153.1. Different initiation.

IPI

IPI00100192.
IPI00619911.
IPI00647805.
IPI00807412.

RefSeq

NP_001002009.1. NM_001002009.2.
NP_001002010.1. NM_001002010.2.
NP_001159590.1. NM_001166118.2.
NP_057573.2. NM_016489.12.

UniGene

Hs.487933.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CN1	X-ray	2.67	A	64-336	[»]
2JGA	X-ray	3.01	A	64-336	[»]
2VKQ	X-ray	2.50	A	64-336	[»]

ProteinModelPortal

Q9H0P0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H0P0. 3 interactions.

PTM databases

PhosphoSite

Q9H0P0.

Polymorphism databases

DMDM

117949804.

Proteomic databases

PaxDb

Q9H0P0.

PRIDE

Q9H0P0.

Protocols and materials databases

DNASU

51251.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000242210; ENSP00000242210; ENSG00000122643.
ENST00000381626; ENSP00000371039; ENSG00000122643.
ENST00000396152; ENSP00000379456; ENSG00000122643.
ENST00000405342; ENSP00000385261; ENSG00000122643.
ENST00000409467; ENSP00000387166; ENSG00000122643.

GeneID

51251.

KEGG

hsa:51251.

UCSC

uc003tdi.3. human.
uc003tdk.3. human.

Organism-specific databases

CTD

51251.

GeneCards

GC07M033053.

HGNC

HGNC:17820. NT5C3.

HPA

HPA029058.

MIM

266120. phenotype.
606224. gene.

neXtProt

NX_Q9H0P0.

Orphanet

35120. Hemolytic anemia due to pyrimidine 5' nucleotidase deficiency.

PharmGKB

PA31802.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG266578.

HOVERGEN

HBG059750.

InParanoid

Q9H0P0.

KO

K01081.

OMA

NTEYFKQ.

PhylomeDB

Q9H0P0.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

Q9H0P0.

Gene expression databases

ArrayExpress

Q9H0P0.

Bgee

Q9H0P0.

Genevestigator

Q9H0P0.

GermOnline

ENSG00000122643. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1000. 2 hits.

InterPro

IPR023214. HAD-like_dom.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]

PANTHER

PTHR13045. PTHR13045. 1 hit.

Pfam

PF05822. UMPH-1. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01544. HAD-SF-IE. 1 hit.

ProtoNet

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Other

EvolutionaryTrace

Q9H0P0.

GenomeRNAi

51251.

NextBio

54391.

SOURCE

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Entry information

Entry name

5NT3_HUMAN

Accession

Primary (citable) accession number: Q9H0P0
Secondary accession number(s): A8K253 , B2RAA5, B8ZZC4, Q6IPZ1, Q6NXS6, Q7L3G6, Q9P0P5, Q9UC42, Q9UC43, Q9UC44, Q9UC45

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.