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Q969T7

- 5NT3B_HUMAN

UniProt

Q969T7 - 5NT3B_HUMAN

Protein

7-methylguanosine phosphate-specific 5'-nucleotidase

Gene

NT5C3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 4 (03 Apr 2013)
      Previous versions | rss
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    Functioni

    Specifically hydrolyzes 7-methylguanosine monophosphate (m7GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m7GMP may protect cells against undesired salvage of m7GMP and its incorporation into nucleic acids. Also has weak activity for CMP. UMP and purine nucleotides are poor substrates.1 Publication

    Catalytic activityi

    N(7)-methyl-GMP + H2O = N(7)-methyl-guanosine + phosphate.1 Publication
    CMP + H2O = cytidine + phosphate.1 Publication
    A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.1 Publication

    Kineticsi

    kcat is 0.24 sec(-1) with m7GMP. kcat is 7 sec(-1) with CMP. kcat is 0.07 sec(-1) with GMP. kcat is 0.04 sec(-1) with AMP. kcat is 6.2 sec(-1) with UMP.

    1. KM=7.8 µM for m7GMP1 Publication
    2. KM=79 µM for CMP1 Publication
    3. KM=355 µM for GMP1 Publication
    4. KM=456 µM for AMP1 Publication
    5. KM=439 µM for UMP1 Publication

    Vmax=0.41 µmol/min/mg enzyme with m7GMP as substrate1 Publication

    Vmax=12 µmol/min/mg enzyme with CMP as substrate1 Publication

    Vmax=0.13 µmol/min/mg enzyme with GMP as substrate1 Publication

    Vmax=0.07 µmol/min/mg enzyme with AMP as substrate1 Publication

    Vmax=10.7 µmol/min/mg enzyme with UMP as substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei41 – 411NucleophileBy similarity
    Metal bindingi41 – 411MagnesiumBy similarity
    Active sitei43 – 431Proton donorBy similarity
    Metal bindingi43 – 431Magnesium; via carbonyl oxygenBy similarity
    Binding sitei205 – 2051SubstrateBy similarity
    Metal bindingi230 – 2301MagnesiumBy similarity

    GO - Molecular functioni

    1. 5'-nucleotidase activity Source: UniProtKB-EC
    2. magnesium ion binding Source: InterPro
    3. nucleotide binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. nucleotide metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ969T7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    7-methylguanosine phosphate-specific 5'-nucleotidase (EC:3.1.3.91)
    Short name:
    7-methylguanosine nucleotidase
    Alternative name(s):
    Cytosolic 5'-nucleotidase 3B
    Cytosolic 5'-nucleotidase III-like protein (EC:3.1.3.5)
    Short name:
    cN-III-like protein
    N(7)-methylguanylate 5'-phosphatase
    Gene namesi
    Name:NT5C3B
    Synonyms:NT5C3L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:28300. NT5C3B.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3003007-methylguanosine phosphate-specific 5'-nucleotidasePRO_0000328948Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei256 – 2561N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ969T7.
    PaxDbiQ969T7.
    PRIDEiQ969T7.

    PTM databases

    PhosphoSiteiQ969T7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ969T7.
    BgeeiQ969T7.
    CleanExiHS_NT5C3L.
    GenevestigatoriQ969T7.

    Organism-specific databases

    HPAiHPA030786.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MLH1P406923EBI-2932564,EBI-744248

    Protein-protein interaction databases

    IntActiQ969T7. 1 interaction.
    STRINGi9606.ENSP00000269534.

    Structurei

    3D structure databases

    ProteinModelPortaliQ969T7.
    SMRiQ969T7. Positions 18-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni156 – 1572Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the pyrimidine 5'-nucleotidase family.Curated

    Phylogenomic databases

    eggNOGiNOG266578.
    HOVERGENiHBG059750.
    InParanoidiQ969T7.
    KOiK01081.
    OMAiNDKVEEQ.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q969T7-1) [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

    MAEEVSTLMK ATVLMRQPGR VQEIVGALRK GGGDRLQVIS DFDMTLSRFA    50
    YNGKRCPSSY NILDNSKIIS EECRKELTAL LHHYYPIEID PHRTVKEKLP 100
    HMVEWWTKAH NLLCQQKIQK FQIAQVVRES NAMLREGYKT FFNTLYHNNI 150
    PLFIFSAGIG DILEEIIRQM KVFHPNIHIV SNYMDFNEDG FLQGFKGQLI 200
    HTYNKNSSAC ENSGYFQQLE GKTNVILLGD SIGDLTMADG VPGVQNILKI 250
    GFLNDKVEER RERYMDSYDI VLEKDETLDV VNGLLQHILC QGVQLEMQGP 300
    Length:300
    Mass (Da):34,389
    Last modified:April 3, 2013 - v4
    Checksum:i3E221583153381F8
    GO
    Isoform 2 (identifier: Q969T7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-8: Missing.

    Show »
    Length:292
    Mass (Da):33,528
    Checksum:i8ACC59D5F25E629A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti209 – 2091A → V.2 Publications
    Corresponds to variant rs1046403 [ dbSNP | Ensembl ].
    VAR_042582
    Natural varianti213 – 2131S → C.2 Publications
    Corresponds to variant rs1046404 [ dbSNP | Ensembl ].
    VAR_042583

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 88Missing in isoform 2. 1 PublicationVSP_046297

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC091172 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60771.1.
    BC013742 mRNA. Translation: AAH13742.2.
    BC014132 mRNA. Translation: AAH14132.2.
    BC016971 mRNA. Translation: AAH16971.2.
    BC067788 mRNA. Translation: AAH67788.1.
    CCDSiCCDS11410.2. [Q969T7-1]
    RefSeqiNP_443167.4. NM_052935.4. [Q969T7-1]
    UniGeneiHs.237536.

    Genome annotation databases

    EnsembliENST00000435506; ENSP00000389948; ENSG00000141698. [Q969T7-1]
    GeneIDi115024.
    KEGGihsa:115024.
    UCSCiuc002hxy.4. human. [Q969T7-1]

    Polymorphism databases

    DMDMi476007845.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC091172 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60771.1 .
    BC013742 mRNA. Translation: AAH13742.2 .
    BC014132 mRNA. Translation: AAH14132.2 .
    BC016971 mRNA. Translation: AAH16971.2 .
    BC067788 mRNA. Translation: AAH67788.1 .
    CCDSi CCDS11410.2. [Q969T7-1 ]
    RefSeqi NP_443167.4. NM_052935.4. [Q969T7-1 ]
    UniGenei Hs.237536.

    3D structure databases

    ProteinModelPortali Q969T7.
    SMRi Q969T7. Positions 18-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q969T7. 1 interaction.
    STRINGi 9606.ENSP00000269534.

    PTM databases

    PhosphoSitei Q969T7.

    Polymorphism databases

    DMDMi 476007845.

    Proteomic databases

    MaxQBi Q969T7.
    PaxDbi Q969T7.
    PRIDEi Q969T7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000435506 ; ENSP00000389948 ; ENSG00000141698 . [Q969T7-1 ]
    GeneIDi 115024.
    KEGGi hsa:115024.
    UCSCi uc002hxy.4. human. [Q969T7-1 ]

    Organism-specific databases

    CTDi 115024.
    GeneCardsi GC17M039982.
    HGNCi HGNC:28300. NT5C3B.
    HPAi HPA030786.
    neXtProti NX_Q969T7.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266578.
    HOVERGENi HBG059750.
    InParanoidi Q969T7.
    KOi K01081.
    OMAi NDKVEEQ.
    TreeFami TF314663.

    Enzyme and pathway databases

    SABIO-RK Q969T7.

    Miscellaneous databases

    GenomeRNAii 115024.
    NextBioi 13644547.
    PROi Q969T7.

    Gene expression databases

    ArrayExpressi Q969T7.
    Bgeei Q969T7.
    CleanExi HS_NT5C3L.
    Genevestigatori Q969T7.

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    InterProi IPR023214. HAD-like_dom.
    IPR006434. Pyrimidine_nucleotidase_eu.
    [Graphical view ]
    PANTHERi PTHR13045. PTHR13045. 1 hit.
    Pfami PF05822. UMPH-1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR01544. HAD-SF-IE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS VAL-209 AND CYS-213.
    3. "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 2), VARIANTS VAL-209 AND CYS-213.
      Tissue: Liver, Lung and Testis.
    4. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Identification of Drosophila and Human 7-Methyl GMP-specific Nucleotidases."
      Buschmann J., Moritz B., Jeske M., Lilie H., Schierhorn A., Wahle E.
      J. Biol. Chem. 288:2441-2451(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry namei5NT3B_HUMAN
    AccessioniPrimary (citable) accession number: Q969T7
    Secondary accession number(s): A8MWB9, C9JKC4, Q7L3B7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: April 3, 2013
    Last modified: October 1, 2014
    This is version 108 of the entry and version 4 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3