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P49902

- 5NTC_HUMAN

UniProt

P49902 - 5NTC_HUMAN

Protein

Cytosolic purine 5'-nucleotidase

Gene

NT5C2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium ion per subunit.

    Enzyme regulationi

    Allosterically activated by various compounds, including ATP.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei52 – 521Nucleophile
    Metal bindingi52 – 521Magnesium
    Active sitei54 – 541Proton donor
    Metal bindingi54 – 541Magnesium; via carbonyl oxygen
    Binding sitei127 – 1271Allosteric activator 1
    Binding sitei154 – 1541Allosteric activator 2
    Metal bindingi351 – 3511Magnesium
    Binding sitei354 – 3541Allosteric activator 2
    Binding sitei436 – 4361Allosteric activator 1; via carbonyl oxygen
    Binding sitei453 – 4531Allosteric activator 2

    GO - Molecular functioni

    1. 5'-nucleotidase activity Source: Reactome
    2. metal ion binding Source: UniProtKB-KW
    3. nucleoside phosphotransferase activity Source: Reactome
    4. nucleotide binding Source: UniProtKB-KW
    5. protein binding Source: IntAct

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. dephosphorylation Source: GOC
    3. drug metabolic process Source: Reactome
    4. nucleobase-containing small molecule metabolic process Source: Reactome
    5. phosphorylation Source: GOC
    6. purine nucleobase metabolic process Source: Reactome
    7. purine nucleotide catabolic process Source: Reactome
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01216-MONOMER.
    BRENDAi3.1.3.5. 2681.
    ReactomeiREACT_121388. Abacavir metabolism.
    REACT_2086. Purine catabolism.
    SABIO-RKP49902.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytosolic purine 5'-nucleotidase (EC:3.1.3.5)
    Alternative name(s):
    Cytosolic 5'-nucleotidase II
    Gene namesi
    Name:NT5C2
    Synonyms:NT5B, NT5CP, PNT5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8022. NT5C2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Spastic paraplegia 45, autosomal recessive (SPG45) [MIM:613162]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. Some SPG45 patients manifest mental retardation, contractures and learning disability.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Hereditary spastic paraplegia, Neurodegeneration

    Organism-specific databases

    MIMi613162. phenotype.
    Orphaneti320396. Autosomal recessive spastic paraplegia type 45.
    PharmGKBiPA31801.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 561561Cytosolic purine 5'-nucleotidasePRO_0000064389Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei502 – 5021Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49902.
    PaxDbiP49902.
    PeptideAtlasiP49902.
    PRIDEiP49902.

    PTM databases

    PhosphoSiteiP49902.

    Expressioni

    Gene expression databases

    ArrayExpressiP49902.
    BgeeiP49902.
    CleanExiHS_NT5C2.
    GenevestigatoriP49902.

    Organism-specific databases

    HPAiHPA003751.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FXR2P511163EBI-742084,EBI-740459
    MOB3BQ86TA13EBI-742084,EBI-751703
    NUDT18Q6ZVK83EBI-742084,EBI-740486

    Protein-protein interaction databases

    BioGridi116627. 20 interactions.
    IntActiP49902. 7 interactions.
    MINTiMINT-1436872.
    STRINGi9606.ENSP00000339479.

    Structurei

    Secondary structure

    1
    561
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 139
    Helixi21 – 288
    Helixi31 – 333
    Beta strandi36 – 394
    Helixi43 – 453
    Beta strandi48 – 514
    Turni55 – 573
    Beta strandi58 – 603
    Helixi64 – 7916
    Helixi84 – 885
    Beta strandi101 – 1033
    Turni104 – 1074
    Beta strandi108 – 1125
    Beta strandi117 – 1237
    Beta strandi126 – 1283
    Helixi130 – 1367
    Turni147 – 1493
    Beta strandi150 – 1523
    Helixi156 – 1583
    Helixi159 – 17416
    Beta strandi178 – 1814
    Beta strandi184 – 1874
    Beta strandi190 – 1934
    Helixi194 – 21017
    Helixi214 – 2207
    Helixi222 – 2254
    Helixi231 – 24212
    Beta strandi243 – 2486
    Helixi253 – 26311
    Beta strandi266 – 2716
    Helixi279 – 2824
    Beta strandi284 – 2896
    Helixi294 – 2963
    Beta strandi302 – 3065
    Turni307 – 3104
    Beta strandi327 – 3293
    Helixi332 – 3398
    Helixi343 – 3453
    Beta strandi346 – 3516
    Helixi353 – 3575
    Helixi358 – 3647
    Beta strandi367 – 3715
    Helixi375 – 38410
    Helixi386 – 39813
    Helixi421 – 43212
    Beta strandi440 – 4434
    Helixi449 – 4579
    Beta strandi459 – 4635
    Helixi465 – 4706
    Helixi485 – 4873

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J2CX-ray2.20A1-536[»]
    2JC9X-ray1.50A1-536[»]
    2JCMX-ray2.15A1-536[»]
    2XCVX-ray2.30A1-536[»]
    2XCWX-ray1.90A1-536[»]
    2XCXX-ray2.30A1-536[»]
    2XJBX-ray2.30A1-536[»]
    2XJCX-ray2.00A1-536[»]
    2XJDX-ray2.00A1-536[»]
    2XJEX-ray2.30A1-536[»]
    2XJFX-ray2.10A1-536[»]
    4H4BX-ray2.90A1-536[»]
    ProteinModelPortaliP49902.
    SMRiP49902. Positions 3-488.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49902.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni202 – 2109Substrate bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi549 – 56113Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG75103.
    HOGENOMiHOG000246075.
    HOVERGENiHBG000025.
    InParanoidiP49902.
    KOiK01081.
    OMAiHLENIKF.
    OrthoDBiEOG7QK0BX.
    PhylomeDBiP49902.
    TreeFamiTF315266.

    Family and domain databases

    Gene3Di3.40.50.1000. 3 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR008380. HAD-SF_hydro_IG_5-nucl.
    IPR016695. Pur_nucleotidase.
    [Graphical view]
    PANTHERiPTHR12103. PTHR12103. 1 hit.
    PfamiPF05761. 5_nucleotid. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017434. Purine_5'-nucleotidase. 1 hit.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR02244. HAD-IG-Ncltidse. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49902-1) [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

    MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG    50
    FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL 100
    VFDTLYGNLL KVDAYGNLLV CAHGFNFIRG PETREQYPNK FIQRDDTERF 150
    YILNTLFNLP ETYLLACLVD FFTNCPRYTS CETGFKDGDL FMSYRSMFQD 200
    VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK EVGKVFLATN 250
    SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT 300
    VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG 350
    DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA 400
    ELYKHLDSSS NERPDISSIQ RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF 450
    ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHTHVDINEM 500
    ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA PQEITHCHDE 550
    DDDEEEEEEE E 561
    Length:561
    Mass (Da):64,970
    Last modified:October 1, 1996 - v1
    Checksum:i4C27D762575E0EA2
    GO
    Isoform 2 (identifier: P49902-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MSTSWSDRLQNAADMPANMDKHALKKYRREAYHR → MSKEG

    Note: No experimental confirmation available.

    Show »
    Length:532
    Mass (Da):61,441
    Checksum:iE0DA487A03BC5F7E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31T → A.1 Publication
    Corresponds to variant rs10883841 [ dbSNP | Ensembl ].
    VAR_024244
    Natural varianti136 – 1361Q → R.
    Corresponds to variant rs12262171 [ dbSNP | Ensembl ].
    VAR_030242

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434MSTSW…EAYHR → MSKEG in isoform 2. 1 PublicationVSP_054235Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38524 mRNA. Translation: BAA07529.1.
    AK295593 mRNA. Translation: BAH12118.1.
    AL139817, AL360001 Genomic DNA. Translation: CAI40080.1.
    AL360001, AL139817 Genomic DNA. Translation: CAI13473.1.
    CH471066 Genomic DNA. Translation: EAW49656.1.
    CH471066 Genomic DNA. Translation: EAW49657.1.
    BC001595 mRNA. Translation: AAH01595.1.
    CCDSiCCDS7544.1. [P49902-1]
    PIRiJC2436.
    RefSeqiNP_001127845.1. NM_001134373.2. [P49902-1]
    NP_036361.1. NM_012229.4. [P49902-1]
    XP_005269693.1. XM_005269636.2. [P49902-1]
    XP_005269696.1. XM_005269639.2. [P49902-2]
    UniGeneiHs.97439.

    Genome annotation databases

    EnsembliENST00000343289; ENSP00000339479; ENSG00000076685. [P49902-1]
    ENST00000404739; ENSP00000383960; ENSG00000076685. [P49902-1]
    GeneIDi22978.
    KEGGihsa:22978.
    UCSCiuc001kwo.3. human. [P49902-1]

    Polymorphism databases

    DMDMi1703012.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38524 mRNA. Translation: BAA07529.1 .
    AK295593 mRNA. Translation: BAH12118.1 .
    AL139817 , AL360001 Genomic DNA. Translation: CAI40080.1 .
    AL360001 , AL139817 Genomic DNA. Translation: CAI13473.1 .
    CH471066 Genomic DNA. Translation: EAW49656.1 .
    CH471066 Genomic DNA. Translation: EAW49657.1 .
    BC001595 mRNA. Translation: AAH01595.1 .
    CCDSi CCDS7544.1. [P49902-1 ]
    PIRi JC2436.
    RefSeqi NP_001127845.1. NM_001134373.2. [P49902-1 ]
    NP_036361.1. NM_012229.4. [P49902-1 ]
    XP_005269693.1. XM_005269636.2. [P49902-1 ]
    XP_005269696.1. XM_005269639.2. [P49902-2 ]
    UniGenei Hs.97439.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2J2C X-ray 2.20 A 1-536 [» ]
    2JC9 X-ray 1.50 A 1-536 [» ]
    2JCM X-ray 2.15 A 1-536 [» ]
    2XCV X-ray 2.30 A 1-536 [» ]
    2XCW X-ray 1.90 A 1-536 [» ]
    2XCX X-ray 2.30 A 1-536 [» ]
    2XJB X-ray 2.30 A 1-536 [» ]
    2XJC X-ray 2.00 A 1-536 [» ]
    2XJD X-ray 2.00 A 1-536 [» ]
    2XJE X-ray 2.30 A 1-536 [» ]
    2XJF X-ray 2.10 A 1-536 [» ]
    4H4B X-ray 2.90 A 1-536 [» ]
    ProteinModelPortali P49902.
    SMRi P49902. Positions 3-488.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116627. 20 interactions.
    IntActi P49902. 7 interactions.
    MINTi MINT-1436872.
    STRINGi 9606.ENSP00000339479.

    Chemistry

    DrugBanki DB00171. Adenosine triphosphate.
    DB00811. Ribavirin.

    PTM databases

    PhosphoSitei P49902.

    Polymorphism databases

    DMDMi 1703012.

    Proteomic databases

    MaxQBi P49902.
    PaxDbi P49902.
    PeptideAtlasi P49902.
    PRIDEi P49902.

    Protocols and materials databases

    DNASUi 22978.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343289 ; ENSP00000339479 ; ENSG00000076685 . [P49902-1 ]
    ENST00000404739 ; ENSP00000383960 ; ENSG00000076685 . [P49902-1 ]
    GeneIDi 22978.
    KEGGi hsa:22978.
    UCSCi uc001kwo.3. human. [P49902-1 ]

    Organism-specific databases

    CTDi 22978.
    GeneCardsi GC10M104837.
    HGNCi HGNC:8022. NT5C2.
    HPAi HPA003751.
    MIMi 600417. gene.
    613162. phenotype.
    neXtProti NX_P49902.
    Orphaneti 320396. Autosomal recessive spastic paraplegia type 45.
    PharmGKBi PA31801.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG75103.
    HOGENOMi HOG000246075.
    HOVERGENi HBG000025.
    InParanoidi P49902.
    KOi K01081.
    OMAi HLENIKF.
    OrthoDBi EOG7QK0BX.
    PhylomeDBi P49902.
    TreeFami TF315266.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS01216-MONOMER.
    BRENDAi 3.1.3.5. 2681.
    Reactomei REACT_121388. Abacavir metabolism.
    REACT_2086. Purine catabolism.
    SABIO-RK P49902.

    Miscellaneous databases

    EvolutionaryTracei P49902.
    GenomeRNAii 22978.
    NextBioi 35479172.
    PROi P49902.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49902.
    Bgeei P49902.
    CleanExi HS_NT5C2.
    Genevestigatori P49902.

    Family and domain databases

    Gene3Di 3.40.50.1000. 3 hits.
    InterProi IPR023214. HAD-like_dom.
    IPR008380. HAD-SF_hydro_IG_5-nucl.
    IPR016695. Pur_nucleotidase.
    [Graphical view ]
    PANTHERi PTHR12103. PTHR12103. 1 hit.
    Pfami PF05761. 5_nucleotid. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017434. Purine_5'-nucleotidase. 1 hit.
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR02244. HAD-IG-Ncltidse. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of human cytosolic purine 5'-nucleotidase."
      Oka J., Matsumoto A., Hosokawa Y., Inoue S.
      Biochem. Biophys. Res. Commun. 205:917-922(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "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] (ISOFORM 2).
      Tissue: Hippocampus.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-3.
    5. "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] (ISOFORM 1).
      Tissue: Lymph.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: INVOLVEMENT IN SPG45.
    9. "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 (1.5 ANGSTROMS) OF 1-536 IN COMPLEX WITH ALLOSTERIC EFFECTOR AND MAGNESIUM IONS, SUBUNIT.

    Entry informationi

    Entry namei5NTC_HUMAN
    AccessioniPrimary (citable) accession number: P49902
    Secondary accession number(s): B7Z382, D3DR91, Q5JUV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 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, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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