NUDT2: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS)
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]''' is an [[enzyme]] that in humans is encoded by the ''NUDT2'' [[gene]].<ref name="pmid7487923">{{cite journal | vauthors = Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG | title = Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases | journal = Biochem J | volume = 311 | issue =  3| pages = 717–21 |date=Dec 1995 | pmid = 7487923 | pmc = 1136061 | doi =  }}</ref><ref name="pmid9479504">{{cite journal | vauthors = McLennan AG, Flannery AV, Morten JE, Ridanpaa M | title = Chromosomal localization of the human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase) gene (APAH1) to 9p13 | journal = Genomics | volume = 47 | issue = 2 | pages = 307–9 |date=Apr 1998 | pmid = 9479504 | pmc =  | doi = 10.1006/geno.1997.5092 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NUDT2 nudix (nucleoside diphosphate linked moiety X)-type motif 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=318| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NUDT2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xsa.
| PDB = {{PDB2|1xsa}}, {{PDB2|1xsb}}, {{PDB2|1xsc}}
| Name = Nudix (nucleoside diphosphate linked moiety X)-type motif 2
| HGNCid = 8049
| Symbol = NUDT2
| AltSymbols =; APAH1; MGC10404
  | OMIM = 602852
| ECnumber =
| Homologene = 896
| MGIid = 1913651
| GeneAtlas_image1 = PBB_GE_NUDT2_218609_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0004081 |text = bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity}} {{GNF_GO|id=GO:0008803 |text = bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =  
| Process = {{GNF_GO|id=GO:0006139 |text = nucleobase, nucleoside, nucleotide and nucleic acid metabolic process}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 318
    | Hs_Ensembl = ENSG00000164978
    | Hs_RefseqProtein = NP_001152
    | Hs_RefseqmRNA = NM_001161
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 34319504
    | Hs_GenLoc_end = 34333709
    | Hs_Uniprot = P50583
    | Mm_EntrezGene = 66401
    | Mm_Ensembl = ENSMUSG00000028443
    | Mm_RefseqmRNA = NM_025539
    | Mm_RefseqProtein = NP_079815
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 41653819
    | Mm_GenLoc_end = 41669597
    | Mm_Uniprot = Q3V1C8
  }}
}}
'''Nudix (nucleoside diphosphate linked moiety X)-type motif 2''', also known as '''NUDT2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NUDT2 nudix (nucleoside diphosphate linked moiety X)-type motif 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=318| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a member of the MutT family of nucleotide pyrophosphatases, a subset of the larger NUDIX hydrolase family. The gene product possesses a modification of the MutT sequence motif found in certain nucleotide pyrophosphatases. The enzyme asymmetrically hydrolyzes Ap4A to yield AMP and ATP and is responsible for maintaining the intracellular level of the dinucleotide Ap4A, the function of which has yet to be established. This gene may be a candidate tumor suppressor gene. Alternative splicing has been observed at this locus and three transcript variants, all encoding the same protein, have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: NUDT2 nudix (nucleoside diphosphate linked moiety X)-type motif 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=318| accessdate = }}</ref>
| summary_text = This gene encodes a member of the MutT family of nucleotide pyrophosphatases, a subset of the larger NUDIX hydrolase family. The gene product possesses a modification of the MutT sequence motif found in certain nucleotide pyrophosphatases. The enzyme asymmetrically hydrolyzes Ap4A to yield AMP and ATP and is responsible for maintaining the intracellular level of the dinucleotide [[Ap4A]], the function of which has yet to be established. This gene may be a candidate tumor suppressor gene. Alternative splicing has been observed at this locus and three transcript variants, all encoding the same protein, have been identified.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Bessman MJ, Frick DN, O'Handley SF |title=The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25059-62 |year= 1996 |pmid= 8810257 |doi=  }}
*{{cite journal  | vauthors=Bessman MJ, Frick DN, O'Handley SF |title=The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25059–62 |year= 1996 |pmid= 8810257 |doi=10.1074/jbc.271.41.25059 }}
*{{cite journal | author=Pinto RM, Costas MJ, Fernández A, ''et al.'' |title=Dinucleoside tetraphosphatase from human blood cells. Purification and characterization as a high specific activity enzyme recognized by an anti-rat tetraphosphatase antibody. |journal=FEBS Lett. |volume=287 |issue= 1-2 |pages= 85-8 |year= 1991 |pmid= 1652465 |doi= }}
*{{cite journal   |vauthors=Pinto RM, Costas MJ, Fernández A, etal |title=Dinucleoside tetraphosphatase from human blood cells. Purification and characterization as a high specific activity enzyme recognized by an anti-rat tetraphosphatase antibody. |journal=FEBS Lett. |volume=287 |issue= 1–2 |pages= 85–8 |year= 1991 |pmid= 1652465 |doi=10.1016/0014-5793(91)80021-T }}
*{{cite journal  | author=Thorne NM, Hankin S, Wilkinson MC, ''et al.'' |title=Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases. |journal=Biochem. J. |volume=311 ( Pt 3) |issue=  |pages= 717-21 |year= 1995 |pmid= 7487923 |doi= }}
*{{cite journal  | vauthors=Hankin S, Matthew N, Thorne H, McLennan AG |title=Diadenosine 5',5"'-P1,P4-tetraphosphate hydrolase is present in human erythrocytes, leukocytes and platelets |journal=Int. J. Biochem. Cell Biol. |volume=27 |issue= 2 |pages= 201–6 |year= 1995 |pmid= 7767787 |doi=10.1016/1357-2725(94)00076-N }}
*{{cite journal  | author=Hankin S, Matthew N, Thorne H, McLennan AG |title=Diadenosine 5',5"'-P1,P4-tetraphosphate hydrolase is present in human erythrocytes, leukocytes and platelets. |journal=Int. J. Biochem. Cell Biol. |volume=27 |issue= 2 |pages= 201-6 |year= 1995 |pmid= 7767787 |doi=  }}
*{{cite journal  | vauthors=Lazewska D, Starzyńska E, Guranowski A |title=Human placental (Asymmetrical) diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase: purification to homogeneity and some properties |journal=Protein Expr. Purif. |volume=4 |issue= 1 |pages= 45–51 |year= 1993 |pmid= 8381042 |doi= 10.1006/prep.1993.1007 }}
*{{cite journal  | author=Lazewska D, Starzyńska E, Guranowski A |title=Human placental (Asymmetrical) diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase: purification to homogeneity and some properties. |journal=Protein Expr. Purif. |volume=4 |issue= 1 |pages= 45-51 |year= 1993 |pmid= 8381042 |doi= 10.1006/prep.1993.1007 }}
*{{cite journal  | vauthors=Rotllán P, Rodríguez-Ferrer CR, Asensio AC, Oaknin S |title=Potent inhibition of specific diadenosine polyphosphate hydrolases by suramin |journal=FEBS Lett. |volume=429 |issue= 2 |pages= 143–6 |year= 1998 |pmid= 9650578 |doi=10.1016/S0014-5793(98)00579-1 }}
*{{cite journal  | author=McLennan AG, Flannery AV, Morten JE, Ridanpää M |title=Chromosomal localization of the human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase) gene (APAH1) to 9p13. |journal=Genomics |volume=47 |issue= 2 |pages= 307-9 |year= 1998 |pmid= 9479504 |doi= 10.1006/geno.1997.5092 }}
*{{cite journal   |vauthors=Vartanian A, Alexandrov I, Prudowski I, etal |title=Ap4A induces apoptosis in human cultured cells |journal=FEBS Lett. |volume=456 |issue= 1 |pages= 175–80 |year= 1999 |pmid= 10452553 |doi=10.1016/S0014-5793(99)00956-4 }}
*{{cite journal  | author=Rotllán P, Rodríguez-Ferrer CR, Asensio AC, Oaknin S |title=Potent inhibition of specific diadenosine polyphosphate hydrolases by suramin. |journal=FEBS Lett. |volume=429 |issue= 2 |pages= 143-6 |year= 1998 |pmid= 9650578 |doi=  }}
*{{cite journal  | vauthors=Guranowski A, Galbas M, Hartmann R, Justesen J |title=Selective degradation of 2'-adenylated diadenosine tri- and tetraphosphates, Ap(3)A and Ap(4)A, by two specific human dinucleoside polyphosphate hydrolases |journal=Arch. Biochem. Biophys. |volume=373 |issue= 1 |pages= 218–24 |year= 2000 |pmid= 10620341 |doi= 10.1006/abbi.1999.1556 }}
*{{cite journal | author=Vartanian A, Alexandrov I, Prudowski I, ''et al.'' |title=Ap4A induces apoptosis in human cultured cells. |journal=FEBS Lett. |volume=456 |issue= 1 |pages= 175-80 |year= 1999 |pmid= 10452553 |doi=  }}
*{{cite journal   |vauthors=Abdelghany HM, Gasmi L, Cartwright JL, etal |title=Cloning, characterisation and crystallisation of a diadenosine 5',5"'-P(1),P(4)-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans |journal=Biochim. Biophys. Acta |volume=1550 |issue= 1 |pages= 27–36 |year= 2002 |pmid= 11738085 |doi=  10.1016/S0167-4838(01)00263-1}}
*{{cite journal  | author=Guranowski A, Galbas M, Hartmann R, Justesen J |title=Selective degradation of 2'-adenylated diadenosine tri- and tetraphosphates, Ap(3)A and Ap(4)A, by two specific human dinucleoside polyphosphate hydrolases. |journal=Arch. Biochem. Biophys. |volume=373 |issue= 1 |pages= 218-24 |year= 2000 |pmid= 10620341 |doi= 10.1006/abbi.1999.1556 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Abdelghany HM, Gasmi L, Cartwright JL, ''et al.'' |title=Cloning, characterisation and crystallisation of a diadenosine 5',5"'-P(1),P(4)-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans. |journal=Biochim. Biophys. Acta |volume=1550 |issue= 1 |pages= 27-36 |year= 2002 |pmid= 11738085 |doi=  }}
*{{cite journal  | vauthors=Guranowski A, Sillero A, Günther Sillero MA |title=Selective splitting of 3'-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates |journal=Acta Biochim. Pol. |volume=50 |issue= 1 |pages= 123–30 |year= 2003 |pmid= 12673352 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Pitcher WH, Kirby TW, DeRose EF, London RE |title=Metabolic transformation of AZTp4A by Ap4A hydrolase regenerates AZT triphosphate |journal=Antiviral Res. |volume=58 |issue= 3 |pages= 227–33 |year= 2003 |pmid= 12767470 |doi=10.1016/S0166-3542(03)00003-2 }}
*{{cite journal  | author=Guranowski A, Sillero A, Günther Sillero MA |title=Selective splitting of 3'-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates. |journal=Acta Biochim. Pol. |volume=50 |issue= 1 |pages= 123-30 |year= 2003 |pmid= 12673352 |doi= 035001123 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal  | author=Pitcher WH, Kirby TW, DeRose EF, London RE |title=Metabolic transformation of AZTp4A by Ap4A hydrolase regenerates AZT triphosphate. |journal=Antiviral Res. |volume=58 |issue= 3 |pages= 227-33 |year= 2003 |pmid= 12767470 |doi=  }}
*{{cite journal   |vauthors=Swarbrick JD, Buyya S, Gunawardana D, etal |title=Structure and substrate-binding mechanism of human Ap4A hydrolase |journal=J. Biol. Chem. |volume=280 |issue= 9 |pages= 8471–81 |year= 2005 |pmid= 15596429 |doi= 10.1074/jbc.M412318200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Swarbrick JD, Buyya S, Gunawardana D, etal |title=1H, 13C, and 15N resonance assignments of the 17 kDa Ap4A hydrolase from Homo sapiens in the presence and absence of ATP |journal=J. Biomol. NMR |volume=31 |issue= 2 |pages= 181–2 |year= 2005 |pmid= 15772762 |doi= 10.1007/s10858-004-7440-4 }}
*{{cite journal | author=Swarbrick JD, Buyya S, Gunawardana D, ''et al.'' |title=Structure and substrate-binding mechanism of human Ap4A hydrolase. |journal=J. Biol. Chem. |volume=280 |issue= 9 |pages= 8471-81 |year= 2005 |pmid= 15596429 |doi= 10.1074/jbc.M412318200 }}
*{{cite journal | author=Swarbrick JD, Buyya S, Gunawardana D, ''et al.'' |title=1H, 13C, and 15N resonance assignments of the 17 kDa Ap4A hydrolase from Homo sapiens in the presence and absence of ATP. |journal=J. Biomol. NMR |volume=31 |issue= 2 |pages= 181-2 |year= 2005 |pmid= 15772762 |doi= 10.1007/s10858-004-7440-4 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=318}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
{{gene-9-stub}}


{{protein-stub}}
[[Category:Nudix hydrolases]]
{{WikiDoc Sources}}

Latest revision as of 13:20, 5 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] is an enzyme that in humans is encoded by the NUDT2 gene.[1][2][3]

This gene encodes a member of the MutT family of nucleotide pyrophosphatases, a subset of the larger NUDIX hydrolase family. The gene product possesses a modification of the MutT sequence motif found in certain nucleotide pyrophosphatases. The enzyme asymmetrically hydrolyzes Ap4A to yield AMP and ATP and is responsible for maintaining the intracellular level of the dinucleotide Ap4A, the function of which has yet to be established. This gene may be a candidate tumor suppressor gene. Alternative splicing has been observed at this locus and three transcript variants, all encoding the same protein, have been identified.[3]

References

  1. ↑ Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG (Dec 1995). "Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases". Biochem J. 311 (3): 717–21. PMC 1136061. PMID 7487923.
  2. ↑ McLennan AG, Flannery AV, Morten JE, Ridanpaa M (Apr 1998). "Chromosomal localization of the human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase) gene (APAH1) to 9p13". Genomics. 47 (2): 307–9. doi:10.1006/geno.1997.5092. PMID 9479504.
  3. ↑ 3.0 3.1 "Entrez Gene: NUDT2 nudix (nucleoside diphosphate linked moiety X)-type motif 2".

Further reading



Retrieved from "https://www.wikidoc.org/index.php?title=NUDT2&oldid=1422665"