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Protein

Cytosolic 5'-nucleotidase 3A

Gene

NT5C3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Can act both as nucleotidase and as phosphotransferase.

Catalytic activityi

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

Kineticsi

  1. KM=66 µM for CMP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Nucleophile
Metal bindingi88 – 881Magnesium
Active sitei90 – 901Proton donor
Metal bindingi90 – 901Magnesium; via carbonyl oxygen
Binding sitei252 – 2521Substrate
Metal bindingi277 – 2771Magnesium

GO - Molecular functioni

  1. 2'-phosphotransferase activity Source: UniProtKB
  2. 5'-nucleotidase activity Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB
  4. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. adenosine metabolic process Source: Ensembl
  2. dephosphorylation Source: GOC
  3. nucleobase-containing small molecule metabolic process Source: Reactome
  4. nucleotide metabolic process Source: UniProtKB-KW
  5. pyrimidine nucleobase metabolic process Source: Reactome
  6. pyrimidine nucleoside catabolic process Source: Reactome
  7. pyrimidine nucleoside metabolic process Source: UniProtKB
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.3.91. 2681.
ReactomeiREACT_1023. Pyrimidine catabolism.
SABIO-RKQ9H0P0.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic 5'-nucleotidase 3A (EC:3.1.3.5)
Alternative name(s):
Cytosolic 5'-nucleotidase 3
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 namesi
Name:NT5C3A
Synonyms:NT5C3, P5N1, UMPH1
ORF Names:HSPC233
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:17820. NT5C3A.

Subcellular locationi

  1. Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. endoplasmic reticulum Source: UniProtKB
  4. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

P5N deficiency (P5ND)8 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal 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.

See also OMIM:266120
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951R → G in P5ND. 1 Publication
VAR_073160
Natural varianti113 – 1131C → R in P5ND; reduced catalytic activity especially towards UMP. 1 Publication
VAR_073161
Natural varianti137 – 1371D → V in P5ND; reduced catalytic activity. 2 Publications
VAR_023511
Natural varianti181 – 1811L → P in P5ND; reduced catalytic activity in vitro; reduced protein stability in vivo, probably through increased proteasomal degradation. 3 Publications
VAR_023512
Natural varianti207 – 2071G → R in P5ND; reduced catalytic activity especially towards UMP. 2 Publications
VAR_073162
Natural varianti229 – 2291N → S in P5ND; almost complete loss of catalytic activity. 3 Publications
VAR_023513
Natural varianti280 – 2801G → R in P5ND; greatly reduced catalytic activity. 3 Publications
VAR_023514
Natural varianti297 – 2971I → T in P5ND. 2 Publications
VAR_073163

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi88 – 881D → N: Loss of nucleotidase and phosphotransferase activity. 1 Publication
Mutagenesisi89 – 891F → A: Almost complete loss of nucleotidase and phosphotransferase activity. 1 Publication
Mutagenesisi90 – 901D → N: Loss of nucleotidase and phosphotransferase activity. 1 Publication
Mutagenesisi135 – 1351E → D: No effect on nucleotidase activity. Almost complete loss of phosphotransferase activity. 1 Publication
Mutagenesisi232 – 2321D → N: No effect on nucleotidase and phosphotransferase activity. 1 Publication
Mutagenesisi233 – 2331F → A: Almost complete loss of nucleotidase and phosphotransferase activity. 1 Publication
Mutagenesisi234 – 2341D → N: No effect on nucleotidase and phosphotransferase activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi266120. phenotype.
Orphaneti35120. Hemolytic anemia due to pyrimidine 5' nucleotidase deficiency.
PharmGKBiPA31802.

Polymorphism and mutation databases

BioMutaiNT5C3A.
DMDMi117949804.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Cytosolic 5'-nucleotidase 3APRO_0000064387Add
BLAST

Proteomic databases

MaxQBiQ9H0P0.
PaxDbiQ9H0P0.
PRIDEiQ9H0P0.

PTM databases

DEPODiQ9H0P0.
PhosphoSiteiQ9H0P0.

Expressioni

Tissue specificityi

Isoforms 1, 3 and 4 are expressed in reticulocytes. Isoform 4 is hardly detectable in bone marrow and fetal liver.2 Publications

Inductioni

Isoform 2 is induced by interferon alpha in Raji cells in association with lupus inclusions.1 Publication

Gene expression databases

BgeeiQ9H0P0.
ExpressionAtlasiQ9H0P0. baseline and differential.
GenevestigatoriQ9H0P0.

Organism-specific databases

HPAiHPA010630.
HPA029058.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi119408. 10 interactions.
IntActiQ9H0P0. 3 interactions.
MINTiMINT-3065844.

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 7814Combined sources
Helixi80 – 823Combined sources
Beta strandi83 – 875Combined sources
Turni90 – 923Combined sources
Beta strandi96 – 983Combined sources
Helixi106 – 1116Combined sources
Helixi118 – 13518Combined sources
Beta strandi138 – 1403Combined sources
Helixi142 – 16322Combined sources
Helixi167 – 1693Combined sources
Helixi170 – 1756Combined sources
Helixi185 – 19410Combined sources
Beta strandi199 – 2068Combined sources
Helixi207 – 21610Combined sources
Beta strandi224 – 2296Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi237 – 2426Combined sources
Helixi252 – 2587Combined sources
Helixi260 – 2645Combined sources
Turni265 – 2684Combined sources
Beta strandi271 – 2799Combined sources
Helixi280 – 2834Combined sources
Turni284 – 2874Combined sources
Beta strandi292 – 3009Combined sources
Helixi304 – 3129Combined sources
Beta strandi315 – 3206Combined sources
Helixi326 – 33510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CN1X-ray2.67A64-336[»]
2JGAX-ray3.01A64-336[»]
2VKQX-ray2.50A64-336[»]
ProteinModelPortaliQ9H0P0.
SMRiQ9H0P0. Positions 64-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H0P0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni203 – 2042Substrate binding

Sequence similaritiesi

Belongs to the pyrimidine 5'-nucleotidase family.Curated

Phylogenomic databases

eggNOGiNOG266578.
GeneTreeiENSGT00390000012959.
HOVERGENiHBG059750.
KOiK01081.
OMAiPRTIVEM.
PhylomeDBiQ9H0P0.
TreeFamiTF314663.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]
PANTHERiPTHR13045. PTHR13045. 1 hit.
PfamiPF05822. UMPH-1. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01544. HAD-SF-IE. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 2 (identifier: Q9H0P0-4) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRAPSMDRAA VARVGAVASA SVCALVAGVV LAQYIFTLKR KTGRKTKIIE
60 70 80 90 100
MMPEFQKSSV RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG
110 120 130 140 150
KRCPTCHNII DNCKLVTDEC RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV
160 170 180 190 200
EWYTKSHGLL VQQALPKAKL KEIVAESDVM LKEGYENFFD KLQQHSIPVF
210 220 230 240 250
IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF MDFDETGVLK GFKGELIHVF
260 270 280 290 300
NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN VEHILKIGYL
310 320 330
NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL
Length:336
Mass (Da):37,948
Last modified:November 14, 2006 - v3
Checksum:iC5D75CCF1BB61021
GO
Isoform 1 (identifier: Q9H0P0-1) [UniParc]FASTAAdd to basket

Also known as: P5N-I

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

Show »
Length:297
Mass (Da):33,915
Checksum:iFB91A66DD2273598
GO
Isoform 3 (identifier: Q9H0P0-2) [UniParc]FASTAAdd to basket

Also known as: p36

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

Show »
Length:286
Mass (Da):32,690
Checksum:i29313E2790194ED9
GO
Isoform 4 (identifier: Q9H0P0-3) [UniParc]FASTAAdd to basket

Also known as: P5N-R

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

Show »
Length:285
Mass (Da):32,559
Checksum:iCB3B6812C90A5578
GO

Sequence cautioni

The sequence AAF36153.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAG33630.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951R → K AA sequence (PubMed:8557639).Curated
Sequence conflicti144 – 1441E → Q AA sequence (PubMed:8557639).Curated
Sequence conflicti329 – 3291N → R AA sequence (PubMed:8557639).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951R → G in P5ND. 1 Publication
VAR_073160
Natural varianti113 – 1131C → R in P5ND; reduced catalytic activity especially towards UMP. 1 Publication
VAR_073161
Natural varianti137 – 1371D → V in P5ND; reduced catalytic activity. 2 Publications
VAR_023511
Natural varianti181 – 1811L → P in P5ND; reduced catalytic activity in vitro; reduced protein stability in vivo, probably through increased proteasomal degradation. 3 Publications
VAR_023512
Natural varianti207 – 2071G → R in P5ND; reduced catalytic activity especially towards UMP. 2 Publications
VAR_073162
Natural varianti229 – 2291N → S in P5ND; almost complete loss of catalytic activity. 3 Publications
VAR_023513
Natural varianti280 – 2801G → R in P5ND; greatly reduced catalytic activity. 3 Publications
VAR_023514
Natural varianti297 – 2971I → T in P5ND. 2 Publications
VAR_073163

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151Missing in isoform 4. 1 PublicationVSP_015624Add
BLAST
Alternative sequencei1 – 5050MRAPS…TKIIE → MTNQESAVHVK in isoform 1. 2 PublicationsVSP_021565Add
BLAST
Alternative sequencei1 – 5050Missing in isoform 3. 2 PublicationsVSP_015623Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34616.1. [Q9H0P0-4]
CCDS34617.1. [Q9H0P0-1]
CCDS55101.1. [Q9H0P0-3]
RefSeqiNP_001002009.1. NM_001002009.2. [Q9H0P0-1]
NP_001002010.1. NM_001002010.2. [Q9H0P0-4]
NP_001159590.1. NM_001166118.2. [Q9H0P0-3]
NP_057573.2. NM_016489.12. [Q9H0P0-1]
UniGeneiHs.487933.

Genome annotation databases

EnsembliENST00000242210; ENSP00000242210; ENSG00000122643. [Q9H0P0-4]
ENST00000381626; ENSP00000371039; ENSG00000122643. [Q9H0P0-3]
ENST00000396152; ENSP00000379456; ENSG00000122643. [Q9H0P0-1]
ENST00000405342; ENSP00000385261; ENSG00000122643. [Q9H0P0-1]
ENST00000409467; ENSP00000387166; ENSG00000122643. [Q9H0P0-3]
ENST00000620705; ENSP00000484415; ENSG00000122643. [Q9H0P0-4]
GeneIDi51251.
KEGGihsa:51251.
UCSCiuc003tdi.4. human. [Q9H0P0-1]
uc003tdk.4. human. [Q9H0P0-4]

Polymorphism and mutation databases

BioMutaiNT5C3A.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34616.1. [Q9H0P0-4]
CCDS34617.1. [Q9H0P0-1]
CCDS55101.1. [Q9H0P0-3]
RefSeqiNP_001002009.1. NM_001002009.2. [Q9H0P0-1]
NP_001002010.1. NM_001002010.2. [Q9H0P0-4]
NP_001159590.1. NM_001166118.2. [Q9H0P0-3]
NP_057573.2. NM_016489.12. [Q9H0P0-1]
UniGeneiHs.487933.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CN1X-ray2.67A64-336[»]
2JGAX-ray3.01A64-336[»]
2VKQX-ray2.50A64-336[»]
ProteinModelPortaliQ9H0P0.
SMRiQ9H0P0. Positions 64-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119408. 10 interactions.
IntActiQ9H0P0. 3 interactions.
MINTiMINT-3065844.

PTM databases

DEPODiQ9H0P0.
PhosphoSiteiQ9H0P0.

Polymorphism and mutation databases

BioMutaiNT5C3A.
DMDMi117949804.

Proteomic databases

MaxQBiQ9H0P0.
PaxDbiQ9H0P0.
PRIDEiQ9H0P0.

Protocols and materials databases

DNASUi51251.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242210; ENSP00000242210; ENSG00000122643. [Q9H0P0-4]
ENST00000381626; ENSP00000371039; ENSG00000122643. [Q9H0P0-3]
ENST00000396152; ENSP00000379456; ENSG00000122643. [Q9H0P0-1]
ENST00000405342; ENSP00000385261; ENSG00000122643. [Q9H0P0-1]
ENST00000409467; ENSP00000387166; ENSG00000122643. [Q9H0P0-3]
ENST00000620705; ENSP00000484415; ENSG00000122643. [Q9H0P0-4]
GeneIDi51251.
KEGGihsa:51251.
UCSCiuc003tdi.4. human. [Q9H0P0-1]
uc003tdk.4. human. [Q9H0P0-4]

Organism-specific databases

CTDi51251.
GeneCardsiGC07M033056.
HGNCiHGNC:17820. NT5C3A.
HPAiHPA010630.
HPA029058.
MIMi266120. phenotype.
606224. gene.
neXtProtiNX_Q9H0P0.
Orphaneti35120. Hemolytic anemia due to pyrimidine 5' nucleotidase deficiency.
PharmGKBiPA31802.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266578.
GeneTreeiENSGT00390000012959.
HOVERGENiHBG059750.
KOiK01081.
OMAiPRTIVEM.
PhylomeDBiQ9H0P0.
TreeFamiTF314663.

Enzyme and pathway databases

BRENDAi3.1.3.91. 2681.
ReactomeiREACT_1023. Pyrimidine catabolism.
SABIO-RKQ9H0P0.

Miscellaneous databases

EvolutionaryTraceiQ9H0P0.
GeneWikiiNT5C3.
GenomeRNAii51251.
NextBioi54391.
PROiQ9H0P0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H0P0.
ExpressionAtlasiQ9H0P0. baseline and differential.
GenevestigatoriQ9H0P0.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]
PANTHERiPTHR13045. PTHR13045. 1 hit.
PfamiPF05822. UMPH-1. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01544. HAD-SF-IE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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), PROTEIN SEQUENCE OF 92-111; 131-155; 226-240; 268-296 AND 313-332.
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, VARIANT P5ND VAL-137.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Kidney.
  4. "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.
  5. "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).
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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.
  9. "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.
  10. "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.
  11. "Functional analysis of pyrimidine 5'-nucleotidase mutants causing nonspherocytic hemolytic anemia."
    Chiarelli L.R., Bianchi P., Fermo E., Galizzi A., Iadarola P., Mattevi A., Zanella A., Valentini G.
    Blood 105:3340-3345(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF P5ND VAL-137; PRO-181; SER-229 AND ARG-280.
  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: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS P5ND SER-229 AND ARG-280, MUTAGENESIS OF ASP-88; PHE-89; ASP-90; GLU-135; ASP-232; PHE-233 AND ASP-234.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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.
  16. "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 P5ND SER-229.
  17. "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: VARIANTS P5ND PRO-181 AND ARG-280, IDENTIFICATION OF ISOFORM 4, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANTS P5ND PRO-181 AND ARG-280.
  18. "Molecular characterization of five Portuguese patients with pyrimidine 5'-nucleotidase deficient hemolytic anemia showing three new P5'N-I mutations."
    Manco L., Relvas L., Silva Pinto C., Pereira J., Almeida A.B., Ribeiro M.L.
    Haematologica 91:266-267(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS P5ND PRO-181; ARG-207 AND THR-297.
  19. "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."
    Chiarelli L.R., Morera S.M., Galizzi A., Fermo E., Zanella A., Valentini G.
    Blood Cells Mol. Dis. 40:295-301(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS P5ND ARG-113; ARG-207 AND THR-297.
  20. "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."
    Dos Santos A., Dantas L.E., Traina F., Albuquerque D.M., Chaim E.A., Saad S.T.
    Blood Cells Mol. Dis. 53:246-252(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT P5ND GLY-95.

Entry informationi

Entry namei5NT3A_HUMAN
AccessioniPrimary (citable) accession number: Q9H0P0
Secondary accession number(s): A8K253
, B2RAA5, B8ZZC4, Q6IPZ1, Q6NXS6, Q7L3G6, Q9P0P5, Q9UC42, Q9UC43, Q9UC44, Q9UC45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: November 14, 2006
Last modified: April 29, 2015
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.