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Description:
7,8-dihydro-8-oxoguanine triphosphatase (EC 3.1.6.-) (8-oxo-dGTPase)(Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1).
Molecular weight: 22552
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
30-AUG-2002, sequence version 2.
07-FEB-2006, entry version 51.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein 8ODP_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | D16581 | BAA04013.1 | - |
| EMBL | D38594 | BAA07601.1 | - |
| EMBL | AB025233 | BAA83791.1 | - |
| EMBL | AB025234 | BAA83792.1 | - |
| EMBL | AB025235 | BAA83793.1 | - |
| EMBL | AB025236 | BAA83794.1 | - |
| EMBL | AB025237 | BAA83795.1 | - |
| EMBL | AB025238 | BAA83796.1 | - |
| EMBL | AB025239 | BAA83797.1 | - |
| EMBL | AB025240 | BAA83798.1 | - |
| EMBL | AB025241 | BAA83799.1 | - |
| EMBL | AB025242 | BAA83800.1 | - |
| EMBL | DQ230907 | ABB02181.1 | - |
| EMBL | BC014618 | AAH14618.1 | - |
| EMBL | BC065367 | AAH65367.1 | - |
| PDB | 1IRY | NMR | A=42-197. |
| Ensembl | ENSG00000106268 | Homo sapiens.1 | |
| H-InvDB | HIX0006427 | -.1 | |
| HGNC | HGNC:8048 | NUDT1.1 | |
| MIM | 600312 | gene. | |
| GO | GO:0003924 | F:GTPase activity | TAS. |
| GO | GO:0006979 | P:response to oxidative stress | TAS. |
| InterPro | IPR003563 | 8Ox_triPHTase. | |
| InterPro | IPR000086 | NUDIX_hydrolase. | |
| Pfam | PF00293 | NUDIX | 1. |
| PRINTS | PR01403 | 8OXTPHPHTASE. | |
| PRINTS | PR00502 | NUDIXFAMILY. | |
| PROSITE | PS00893 | NUDIX | 1. |
Keywords:
3D-structure; Alternative initiation; Direct protein sequencing; Hydrolase; Polymorphism.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), AND PARTIAL PROTEIN
RP SEQUENCE.
RX MEDLINE=94043152; PubMed=8226881;
RA Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H.,
RA Sekiguchi M.;
RT "Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-
RT oxo-dGTP, a mutagenic substrate for DNA synthesis.";
RL J. Biol. Chem. 268:23524-23530(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=95229148; PubMed=7713500;
RA Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y.,
RA Tsuzuki T., Sekiguchi M.;
RT "Genomic structure and chromosome location of the human mutT homologue
RT gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G
RT transversion.";
RL Genomics 24:485-490(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX MEDLINE=97362283; PubMed=9211940; DOI=10.1074/jbc.272.28.17843;
RA Oda H., Nakabeppu Y., Furuichi M., Sekiguchi M.;
RT "Regulation of expression of the human MTH1 gene encoding 8-oxo-
RT dGTPase. Alternative splicing of transcription products.";
RL J. Biol. Chem. 272:17843-17850(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE INITIATION, AND VARIANT
RP VAL-124.
RX MEDLINE=20007875; PubMed=10536140; DOI=10.1093/nar/27.22.4335;
RA Oda H., Taketomi A., Maruyama R., Itoh R., Nishioka K., Yakushiji H.,
RA Suzuki T., Sekiguchi M., Nakabeppu Y.;
RT "Multi-forms of human MTH1 polypeptides produced by alternative
RT translation initiation and single nucleotide polymorphism.";
RL Nucleic Acids Res. 27:4335-4343(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-124.
RA Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N.,
RA Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B.,
RA Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J.,
RA Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department
RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P22), AND VARIANT
RP VAL-124.
RC TISSUE=Lymph, and Muscle;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
Feature:
CHAIN 1 197 7,8-dihydro-8-oxoguanine triphosphatase,
isoform p26.
/FTId=PRO_0000019944.
CHAIN 19 197 7,8-dihydro-8-oxoguanine triphosphatase,
isoform p22.
/FTId=PRO_0000019945.
INIT_MET 19 19 For isoform p22.
CHAIN 27 197 7,8-dihydro-8-oxoguanine triphosphatase,
isoform p21.
/FTId=PRO_0000019946.
INIT_MET 27 27 For isoform p21.
CHAIN 42 197 7,8-dihydro-8-oxoguanine triphosphatase,
isoform p18.
/FTId=PRO_0000019947.
INIT_MET 42 42 For isoform p18.
MOTIF 78 99 Nudix box.
VARIANT 124 124 M -> V (in dbSNP:4866).
/FTId=VAR_013757.
STRAND 46 51
STRAND 53 54
STRAND 56 70
TURN 71 71
STRAND 73 74
STRAND 76 76
STRAND 79 79
TURN 82 83
HELIX 86 98
STRAND 99 99
STRAND 102 103
STRAND 107 115
TURN 116 117
STRAND 119 119
STRAND 121 127
STRAND 132 132
STRAND 134 134
STRAND 140 148
TURN 149 150
STRAND 154 154
TURN 155 157
STRAND 159 160
HELIX 161 170
TURN 171 171
STRAND 173 184
STRAND 186 194
Comments:
-!- FUNCTION: Antimutagenic. Responsible for preventing
misincorporation of 8-oxo-dGTP into DNA thus preventing A:T to C:G
transversions.
-!- CATALYTIC ACTIVITY: 8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation;
Comment=4 isoforms, p26 (shown here), p22, p21 and p18, are
produced by alternative initiation. Isoform p26 is derived from
a B-type mRNA with a polymorphic alteration (GU-->GC) at the
beginning of exon 2c that converts an in-frame UGA to CGA
yielding another in-frame AUG further upstream;
-!- TISSUE SPECIFICITY: Widely expressed with highest expression in
thymus, testis, embryo and proliferating blood lymphocytes.
-!- DEVELOPMENTAL STAGE: In peripheral blood lymphocytes, expressed at
much higher levels in proliferating cells than in resting cells.
-!- PTM: The N-terminus is blocked.
-!- POLYMORPHISM: A polymorphism between Met-1 and Met-19 removes a
stop codon before the initiation codon for isoform p22 and gives
rise to the production of isoform p26. The allele frequency of
isoform p26 is about 20%.
-!- SIMILARITY: Belongs to the Nudix hydrolase family.
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Sequence length: 197
MYWSNQITRR LGERVQGFMS GISPQQMGEP EGSWSGKNPG TMGASRLYTL VLVLQPQRVL
LGMKKRGFGA GRWNGFGGKV QEGETIEDGA RRELQEESGL TVDALHKVGQ IVFEFVGEPE
LMDMHVFCTD SIQGTPVESD EMRPCWFQLD QIPFKDMWPD DSYWFPLLLQ KKKFHGYFKF
QGQDTILDYT LREVDTV