Full text data of NUDT2
NUDT2
(APAH1)
[Confidence: low (only semi-automatic identification from reviews)]
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]; 3.6.1.17 (Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase; Ap4A hydrolase; Ap4Aase; Diadenosine tetraphosphatase; Nucleoside diphosphate-linked moiety X motif 2; Nudix motif 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]; 3.6.1.17 (Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase; Ap4A hydrolase; Ap4Aase; Diadenosine tetraphosphatase; Nucleoside diphosphate-linked moiety X motif 2; Nudix motif 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P50583
ID AP4A_HUMAN Reviewed; 147 AA.
AC P50583; D3DRM0; Q5T589;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical];
DE EC=3.6.1.17;
DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase;
DE Short=Ap4A hydrolase;
DE Short=Ap4Aase;
DE Short=Diadenosine tetraphosphatase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 2;
DE Short=Nudix motif 2;
GN Name=NUDT2; Synonyms=APAH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver, and Spleen;
RX PubMed=7487923;
RA Thorne N.M.H., Hankin S., Wilkinson M.C., Nunez C., Barraclough R.,
RA McLennan A.G.;
RT "Human diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase is
RT a member of the MutT family of nucleotide pyrophosphatases.";
RL Biochem. J. 311:717-721(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION AT ALA-2.
RA McLennan A.G.;
RL Submitted (JAN-1997) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=15596429; DOI=10.1074/jbc.M412318200;
RA Swarbrick J.D., Buyya S., Gunawardana D., Gayler K.R., McLennan A.G.,
RA Gooley P.R.;
RT "Structure and substrate-binding mechanism of human Ap4A hydrolase.";
RL J. Biol. Chem. 280:8471-8481(2005).
CC -!- FUNCTION: Asymmetrically hydrolyzes Ap4A to yield AMP and ATP.
CC Plays a major role in maintaining homeostasis.
CC -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-guanosyl) tetraphosphate +
CC H(2)O = GTP + GMP.
CC -!- COFACTOR: Divalent ions (By similarity).
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC -!- SIMILARITY: Contains 1 nudix hydrolase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U30313; AAC50277.1; -; mRNA.
DR EMBL; AL356494; CAI15964.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58461.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58462.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58463.1; -; Genomic_DNA.
DR EMBL; BC004926; AAH04926.1; -; mRNA.
DR PIR; S60111; S60111.
DR RefSeq; NP_001152.1; NM_001161.4.
DR RefSeq; NP_001231319.1; NM_001244390.1.
DR RefSeq; NP_671701.1; NM_147172.2.
DR RefSeq; NP_671702.1; NM_147173.2.
DR UniGene; Hs.493767; -.
DR UniGene; Hs.731743; -.
DR PDB; 1XSA; NMR; -; A=1-147.
DR PDB; 1XSB; NMR; -; A=1-147.
DR PDB; 1XSC; NMR; -; A=1-147.
DR PDB; 3U53; X-ray; 2.70 A; A/B/C/D=1-147.
DR PDB; 4IJX; X-ray; 2.10 A; A/B=1-147.
DR PDBsum; 1XSA; -.
DR PDBsum; 1XSB; -.
DR PDBsum; 1XSC; -.
DR PDBsum; 3U53; -.
DR PDBsum; 4IJX; -.
DR ProteinModelPortal; P50583; -.
DR SMR; P50583; 4-147.
DR STRING; 9606.ENSP00000338397; -.
DR PhosphoSite; P50583; -.
DR DMDM; 1703326; -.
DR PaxDb; P50583; -.
DR PeptideAtlas; P50583; -.
DR PRIDE; P50583; -.
DR DNASU; 318; -.
DR Ensembl; ENST00000346365; ENSP00000344187; ENSG00000164978.
DR Ensembl; ENST00000379155; ENSP00000368452; ENSG00000164978.
DR Ensembl; ENST00000379158; ENSP00000368455; ENSG00000164978.
DR GeneID; 318; -.
DR KEGG; hsa:318; -.
DR UCSC; uc003zub.3; human.
DR CTD; 318; -.
DR GeneCards; GC09P034329; -.
DR HGNC; HGNC:8049; NUDT2.
DR HPA; CAB004684; -.
DR MIM; 602852; gene.
DR neXtProt; NX_P50583; -.
DR PharmGKB; PA31833; -.
DR eggNOG; COG0494; -.
DR HOGENOM; HOG000261976; -.
DR HOVERGEN; HBG002853; -.
DR InParanoid; P50583; -.
DR KO; K01518; -.
DR OMA; WDFPKGN; -.
DR OrthoDB; EOG7GBFZN; -.
DR PhylomeDB; P50583; -.
DR SABIO-RK; P50583; -.
DR EvolutionaryTrace; P50583; -.
DR GeneWiki; NUDT2; -.
DR GenomeRNAi; 318; -.
DR NextBio; 1299; -.
DR PRO; PR:P50583; -.
DR Bgee; P50583; -.
DR CleanEx; HS_NUDT2; -.
DR Genevestigator; P50583; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; ISS:UniProtKB.
DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; TAS:ProtInc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR Gene3D; 3.90.79.10; -; 1.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR InterPro; IPR003565; Tetra_PHTase.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR01405; TETRPHPHTASE.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; GTP-binding; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 147 Bis(5'-nucleosyl)-tetraphosphatase
FT [asymmetrical].
FT /FTId=PRO_0000057102.
FT DOMAIN 1 139 Nudix hydrolase.
FT MOTIF 43 64 Nudix box.
FT MOD_RES 2 2 N-acetylalanine.
FT STRAND 5 13
FT TURN 17 19
FT STRAND 23 33
FT STRAND 41 44
FT STRAND 47 49
FT HELIX 51 63
FT HELIX 67 69
FT STRAND 70 84
FT STRAND 87 99
FT STRAND 111 117
FT HELIX 119 126
FT HELIX 129 147
SQ SEQUENCE 147 AA; 16829 MW; 3599B12719F94AB8 CRC64;
MALRACGLII FRRCLIPKVD NNAIEFLLLQ ASDGIHHWTP PKGHVEPGED DLETALRETQ
EEAGIEAGQL TIIEGFKREL NYVARNKPKT VIYWLAEVKD YDVEIRLSHE HQAYRWLGLE
EACQLAQFKE MKAALQEGHQ FLCSIEA
//
ID AP4A_HUMAN Reviewed; 147 AA.
AC P50583; D3DRM0; Q5T589;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical];
DE EC=3.6.1.17;
DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase;
DE Short=Ap4A hydrolase;
DE Short=Ap4Aase;
DE Short=Diadenosine tetraphosphatase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 2;
DE Short=Nudix motif 2;
GN Name=NUDT2; Synonyms=APAH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver, and Spleen;
RX PubMed=7487923;
RA Thorne N.M.H., Hankin S., Wilkinson M.C., Nunez C., Barraclough R.,
RA McLennan A.G.;
RT "Human diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase is
RT a member of the MutT family of nucleotide pyrophosphatases.";
RL Biochem. J. 311:717-721(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION AT ALA-2.
RA McLennan A.G.;
RL Submitted (JAN-1997) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=15596429; DOI=10.1074/jbc.M412318200;
RA Swarbrick J.D., Buyya S., Gunawardana D., Gayler K.R., McLennan A.G.,
RA Gooley P.R.;
RT "Structure and substrate-binding mechanism of human Ap4A hydrolase.";
RL J. Biol. Chem. 280:8471-8481(2005).
CC -!- FUNCTION: Asymmetrically hydrolyzes Ap4A to yield AMP and ATP.
CC Plays a major role in maintaining homeostasis.
CC -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-guanosyl) tetraphosphate +
CC H(2)O = GTP + GMP.
CC -!- COFACTOR: Divalent ions (By similarity).
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC -!- SIMILARITY: Contains 1 nudix hydrolase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U30313; AAC50277.1; -; mRNA.
DR EMBL; AL356494; CAI15964.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58461.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58462.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58463.1; -; Genomic_DNA.
DR EMBL; BC004926; AAH04926.1; -; mRNA.
DR PIR; S60111; S60111.
DR RefSeq; NP_001152.1; NM_001161.4.
DR RefSeq; NP_001231319.1; NM_001244390.1.
DR RefSeq; NP_671701.1; NM_147172.2.
DR RefSeq; NP_671702.1; NM_147173.2.
DR UniGene; Hs.493767; -.
DR UniGene; Hs.731743; -.
DR PDB; 1XSA; NMR; -; A=1-147.
DR PDB; 1XSB; NMR; -; A=1-147.
DR PDB; 1XSC; NMR; -; A=1-147.
DR PDB; 3U53; X-ray; 2.70 A; A/B/C/D=1-147.
DR PDB; 4IJX; X-ray; 2.10 A; A/B=1-147.
DR PDBsum; 1XSA; -.
DR PDBsum; 1XSB; -.
DR PDBsum; 1XSC; -.
DR PDBsum; 3U53; -.
DR PDBsum; 4IJX; -.
DR ProteinModelPortal; P50583; -.
DR SMR; P50583; 4-147.
DR STRING; 9606.ENSP00000338397; -.
DR PhosphoSite; P50583; -.
DR DMDM; 1703326; -.
DR PaxDb; P50583; -.
DR PeptideAtlas; P50583; -.
DR PRIDE; P50583; -.
DR DNASU; 318; -.
DR Ensembl; ENST00000346365; ENSP00000344187; ENSG00000164978.
DR Ensembl; ENST00000379155; ENSP00000368452; ENSG00000164978.
DR Ensembl; ENST00000379158; ENSP00000368455; ENSG00000164978.
DR GeneID; 318; -.
DR KEGG; hsa:318; -.
DR UCSC; uc003zub.3; human.
DR CTD; 318; -.
DR GeneCards; GC09P034329; -.
DR HGNC; HGNC:8049; NUDT2.
DR HPA; CAB004684; -.
DR MIM; 602852; gene.
DR neXtProt; NX_P50583; -.
DR PharmGKB; PA31833; -.
DR eggNOG; COG0494; -.
DR HOGENOM; HOG000261976; -.
DR HOVERGEN; HBG002853; -.
DR InParanoid; P50583; -.
DR KO; K01518; -.
DR OMA; WDFPKGN; -.
DR OrthoDB; EOG7GBFZN; -.
DR PhylomeDB; P50583; -.
DR SABIO-RK; P50583; -.
DR EvolutionaryTrace; P50583; -.
DR GeneWiki; NUDT2; -.
DR GenomeRNAi; 318; -.
DR NextBio; 1299; -.
DR PRO; PR:P50583; -.
DR Bgee; P50583; -.
DR CleanEx; HS_NUDT2; -.
DR Genevestigator; P50583; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; ISS:UniProtKB.
DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; TAS:ProtInc.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR Gene3D; 3.90.79.10; -; 1.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR InterPro; IPR003565; Tetra_PHTase.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR01405; TETRPHPHTASE.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; GTP-binding; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 147 Bis(5'-nucleosyl)-tetraphosphatase
FT [asymmetrical].
FT /FTId=PRO_0000057102.
FT DOMAIN 1 139 Nudix hydrolase.
FT MOTIF 43 64 Nudix box.
FT MOD_RES 2 2 N-acetylalanine.
FT STRAND 5 13
FT TURN 17 19
FT STRAND 23 33
FT STRAND 41 44
FT STRAND 47 49
FT HELIX 51 63
FT HELIX 67 69
FT STRAND 70 84
FT STRAND 87 99
FT STRAND 111 117
FT HELIX 119 126
FT HELIX 129 147
SQ SEQUENCE 147 AA; 16829 MW; 3599B12719F94AB8 CRC64;
MALRACGLII FRRCLIPKVD NNAIEFLLLQ ASDGIHHWTP PKGHVEPGED DLETALRETQ
EEAGIEAGQL TIIEGFKREL NYVARNKPKT VIYWLAEVKD YDVEIRLSHE HQAYRWLGLE
EACQLAQFKE MKAALQEGHQ FLCSIEA
//
MIM
602852
*RECORD*
*FIELD* NO
602852
*FIELD* TI
*602852 NUCLEOSIDE DIPHOSPHATE-LINKED MOIETY X MOTIF 2; NUDT2
;;NUDIX MOTIF 2;;
AP4A HYDROLASE 1; APAH1
read more*FIELD* TX
AP4A hydrolase is the enzyme responsible for maintaining the
intracellular level of the dinucleoside AP4A (diadenosine
5-prime,5-triple prime-P(1),P(4)-tetraphosphate). Human AP4A hydrolase
is a member of the MutT (600312) motif, or 'nudix,' family of nucleotide
hydrolases, whose function may be to rid the cell of toxic nucleotide
metabolites. Thorne et al. (1995) isolated an AP4A hydrolase cDNA from a
human fetal liver and spleen normalized cDNA library. The gene,
designated APAH1, encodes a 147-amino acid polypeptide containing a MutT
sequence motif.
McLennan et al. (1998) used fluorescence in situ hybridization to map
the APAH1 gene to human chromosome 9p13. They further localized the gene
relative to other genes and markers in the region and obtained the order
tel--D9S165--D9S1878--CNTFR (118946)--IL11RA (600939)--APAH1--GALT
(606999)--D9S163--CHH (250250)--D9S50--cen.
McLennan et al. (1998) suggested that, in light of evidence for the
existence of several tumor suppressor genes in the 9p13 region, and also
given that the mammalian AP3A hydrolase gene (FHIT; 601153) is a
possible tumor suppressor gene, APAH1 may be a candidate tumor
suppressor gene as well.
*FIELD* RF
1. McLennan, A. G.; Flannery, A. V.; Morten, J. E. N.; Ridanpaa, M.
: Chromosomal localization of the human diadenosine 5-prime,5-triple
prime-P(1),P(4)-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase)
gene (APAH1) to 9p13. Genomics 47: 307-309, 1998.
2. Thorne, M. H.; Hankin, S.; Wilkinson, M. C.; Nunez, C.; Barraclough,
R.; McLennan, A. G.: Human diadenosine 5-prime,5-triple prime-P(1),P(4)-tetraphosphate
pyrophosphohydrolase is a member of the MutT family of nucleotide
pyrophosphatases. Biochem. J. 311: 717-721, 1995.
*FIELD* CD
Jennifer P. Macke: 7/15/1998
*FIELD* ED
mgross: 02/25/2005
carol: 6/7/2002
alopez: 9/5/1999
alopez: 7/15/1998
*RECORD*
*FIELD* NO
602852
*FIELD* TI
*602852 NUCLEOSIDE DIPHOSPHATE-LINKED MOIETY X MOTIF 2; NUDT2
;;NUDIX MOTIF 2;;
AP4A HYDROLASE 1; APAH1
read more*FIELD* TX
AP4A hydrolase is the enzyme responsible for maintaining the
intracellular level of the dinucleoside AP4A (diadenosine
5-prime,5-triple prime-P(1),P(4)-tetraphosphate). Human AP4A hydrolase
is a member of the MutT (600312) motif, or 'nudix,' family of nucleotide
hydrolases, whose function may be to rid the cell of toxic nucleotide
metabolites. Thorne et al. (1995) isolated an AP4A hydrolase cDNA from a
human fetal liver and spleen normalized cDNA library. The gene,
designated APAH1, encodes a 147-amino acid polypeptide containing a MutT
sequence motif.
McLennan et al. (1998) used fluorescence in situ hybridization to map
the APAH1 gene to human chromosome 9p13. They further localized the gene
relative to other genes and markers in the region and obtained the order
tel--D9S165--D9S1878--CNTFR (118946)--IL11RA (600939)--APAH1--GALT
(606999)--D9S163--CHH (250250)--D9S50--cen.
McLennan et al. (1998) suggested that, in light of evidence for the
existence of several tumor suppressor genes in the 9p13 region, and also
given that the mammalian AP3A hydrolase gene (FHIT; 601153) is a
possible tumor suppressor gene, APAH1 may be a candidate tumor
suppressor gene as well.
*FIELD* RF
1. McLennan, A. G.; Flannery, A. V.; Morten, J. E. N.; Ridanpaa, M.
: Chromosomal localization of the human diadenosine 5-prime,5-triple
prime-P(1),P(4)-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase)
gene (APAH1) to 9p13. Genomics 47: 307-309, 1998.
2. Thorne, M. H.; Hankin, S.; Wilkinson, M. C.; Nunez, C.; Barraclough,
R.; McLennan, A. G.: Human diadenosine 5-prime,5-triple prime-P(1),P(4)-tetraphosphate
pyrophosphohydrolase is a member of the MutT family of nucleotide
pyrophosphatases. Biochem. J. 311: 717-721, 1995.
*FIELD* CD
Jennifer P. Macke: 7/15/1998
*FIELD* ED
mgross: 02/25/2005
carol: 6/7/2002
alopez: 9/5/1999
alopez: 7/15/1998