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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

    • 2'-phosphotransferase activity Source: UniProtKB
    • 5'-nucleotidase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    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

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • endoplasmic reticulum Source: UniProtKB
    • 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.
    GenevisibleiQ9H0P0. HS.

    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]

    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.
    GenevisibleiQ9H0P0. HS.

    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: June 24, 2015
    This is version 133 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.