NUDT6_HUMAN
ID NUDT6_HUMAN Reviewed; 316 AA.
AC P53370; A8K756; O95097; Q9UQD9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Nucleoside diphosphate-linked moiety X motif 6;
DE Short=Nudix motif 6;
DE EC=3.6.1.-;
DE AltName: Full=Antisense basic fibroblast growth factor;
DE AltName: Full=Protein GFG;
GN Name=NUDT6; Synonyms=FGF2AS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RX PubMed=10022609;
RX DOI=10.1002/(sici)1097-4644(19990315)72:4<492::aid-jcb5>3.0.co;2-h;
RA Gagnon M.L., Moy G.K., Klagsbrun M.;
RT "Characterization of the promoter for the human antisense fibroblast growth
RT factor-2 gene; regulation by Ets in Jurkat T cells.";
RL J. Cell. Biochem. 72:492-506(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 170-269.
RC TISSUE=Astrocytoma;
RX PubMed=7984147; DOI=10.1210/mend.8.7.7984147;
RA Murphy P.R., Knee R.S.;
RT "Identification and characterization of an antisense RNA transcript (gfg)
RT from the human basic fibroblast growth factor gene.";
RL Mol. Endocrinol. 8:852-859(1994).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11266510; DOI=10.1210/mend.15.4.0626;
RA Asa S.L., Ramyar L., Murphy P.R., Li A.W., Ezzat S.;
RT "The endogenous fibroblast growth factor-2 antisense gene product regulates
RT pituitary cell growth and hormone production.";
RL Mol. Endocrinol. 15:589-599(2001).
RN [6]
RP ALTERNATIVE SPLICING, ABSENCE OF ANTI-MUTATOR FUNCTION IN DNA REPAIR,
RP SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=17569023; DOI=10.1007/s00109-007-0219-9;
RA Zhang S.C., Barclay C., Alexander L.A., Geldenhuys L., Porter G.A.,
RA Casson A.G., Murphy P.R.;
RT "Alternative splicing of the FGF antisense gene: differential subcellular
RT localization in human tissues and esophageal adenocarcinoma.";
RL J. Mol. Med. 85:1215-1228(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 45-316.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the N-terminal domain and of nudix domain of human
RT NUDT6.";
RL Submitted (JUL-2009) to the PDB data bank.
CC -!- FUNCTION: May contribute to the regulation of cell proliferation.
CC {ECO:0000269|PubMed:11266510}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000305|PubMed:17569023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion.
CC Note=Subcellular location may vary between isoforms.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=B;
CC IsoId=P53370-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=P53370-2; Sequence=VSP_003729;
CC -!- TISSUE SPECIFICITY: Detected in liver, kidney and esophagus (at protein
CC level). Ubiquitous. {ECO:0000269|PubMed:11266510,
CC ECO:0000269|PubMed:17569023}.
CC -!- MISCELLANEOUS: This protein is coded from a FGF2 (BFGF) gene antisense
CC transcript.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- CAUTION: The rat protein was reported to play a role in DNA repair
CC (PubMed:9406864), based on its ability to complement E.coli deficient
CC in the DNA repair enzyme mutT that hydrolyzes oxidized guanine
CC nucleotides. PubMed:17569023 found no such activity, neither for the
CC human nor the rat protein. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NUDT6ID41593ch4q28.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF019633; AAD01636.2; -; mRNA.
DR EMBL; AF019632; AAD01635.1; -; mRNA.
DR EMBL; AK291871; BAF84560.1; -; mRNA.
DR EMBL; BC009842; AAH09842.1; -; mRNA.
DR EMBL; L31408; AAA67062.1; -; mRNA.
DR CCDS; CCDS3729.1; -. [P53370-2]
DR CCDS; CCDS43268.1; -. [P53370-1]
DR RefSeq; NP_009014.2; NM_007083.4. [P53370-1]
DR RefSeq; NP_932158.1; NM_198041.2. [P53370-2]
DR PDB; 3FXT; X-ray; 2.30 A; A/B/C/D/E/F/G/H=45-134.
DR PDB; 3H95; X-ray; 1.70 A; A=141-316.
DR PDBsum; 3FXT; -.
DR PDBsum; 3H95; -.
DR AlphaFoldDB; P53370; -.
DR SMR; P53370; -.
DR BioGRID; 116333; 18.
DR IntAct; P53370; 13.
DR STRING; 9606.ENSP00000306070; -.
DR iPTMnet; P53370; -.
DR PhosphoSitePlus; P53370; -.
DR BioMuta; NUDT6; -.
DR DMDM; 17380446; -.
DR EPD; P53370; -.
DR MassIVE; P53370; -.
DR MaxQB; P53370; -.
DR PaxDb; P53370; -.
DR PeptideAtlas; P53370; -.
DR PRIDE; P53370; -.
DR ProteomicsDB; 56577; -. [P53370-1]
DR ProteomicsDB; 56578; -. [P53370-2]
DR Antibodypedia; 26864; 297 antibodies from 27 providers.
DR DNASU; 11162; -.
DR Ensembl; ENST00000304430.10; ENSP00000306070.5; ENSG00000170917.14. [P53370-1]
DR Ensembl; ENST00000339154.6; ENSP00000344011.2; ENSG00000170917.14. [P53370-2]
DR Ensembl; ENST00000502270.5; ENSP00000424117.1; ENSG00000170917.14. [P53370-2]
DR GeneID; 11162; -.
DR KEGG; hsa:11162; -.
DR MANE-Select; ENST00000304430.10; ENSP00000306070.5; NM_007083.5; NP_009014.2.
DR UCSC; uc003iew.3; human. [P53370-1]
DR CTD; 11162; -.
DR DisGeNET; 11162; -.
DR GeneCards; NUDT6; -.
DR HGNC; HGNC:8053; NUDT6.
DR HPA; ENSG00000170917; Tissue enhanced (liver).
DR MIM; 606261; gene.
DR neXtProt; NX_P53370; -.
DR OpenTargets; ENSG00000170917; -.
DR PharmGKB; PA31839; -.
DR VEuPathDB; HostDB:ENSG00000170917; -.
DR eggNOG; KOG0648; Eukaryota.
DR GeneTree; ENSGT00390000008458; -.
DR HOGENOM; CLU_054299_4_0_1; -.
DR InParanoid; P53370; -.
DR OMA; GTFGCSD; -.
DR OrthoDB; 835461at2759; -.
DR PhylomeDB; P53370; -.
DR TreeFam; TF106346; -.
DR PathwayCommons; P53370; -.
DR SignaLink; P53370; -.
DR BioGRID-ORCS; 11162; 15 hits in 1091 CRISPR screens.
DR ChiTaRS; NUDT6; human.
DR EvolutionaryTrace; P53370; -.
DR GeneWiki; NUDT6; -.
DR GenomeRNAi; 11162; -.
DR Pharos; P53370; Tbio.
DR PRO; PR:P53370; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P53370; protein.
DR Bgee; ENSG00000170917; Expressed in tendon of biceps brachii and 184 other tissues.
DR ExpressionAtlas; P53370; baseline and differential.
DR Genevisible; P53370; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR003293; Nudix_hydrolase6-like.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR040618; Pre-Nudix.
DR PANTHER; PTHR13994; PTHR13994; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF18290; Nudix_hydro; 1.
DR PRINTS; PR01356; GFGPROTEIN.
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; Alternative splicing; Cytoplasm; Hydrolase; Mitochondrion;
KW Nucleus; Reference proteome.
FT CHAIN 1..316
FT /note="Nucleoside diphosphate-linked moiety X motif 6"
FT /id="PRO_0000057107"
FT DOMAIN 141..273
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 176..197
FT /note="Nudix box"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003729"
FT VARIANT 114
FT /note="C -> R (in dbSNP:rs12648093)"
FT /id="VAR_050412"
FT VARIANT 209
FT /note="R -> Q (in dbSNP:rs1048201)"
FT /id="VAR_021909"
FT CONFLICT 181
FT /note="E -> G (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="I -> V (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="V -> L (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..214
FT /note="TN -> RS (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> R (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="K -> M (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="I -> L (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..232
FT /note="KPY -> QPR (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="E -> Q (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="R -> K (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..253
FT /note="ND -> ES (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT CONFLICT 256..259
FT /note="KTEN -> RTKH (in Ref. 4; AAA67062)"
FT /evidence="ECO:0000305"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3FXT"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:3FXT"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3FXT"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:3FXT"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:3FXT"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:3FXT"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:3FXT"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3FXT"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:3FXT"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:3H95"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3H95"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:3H95"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:3H95"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3H95"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:3H95"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:3H95"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:3H95"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:3H95"
SQ SEQUENCE 316 AA; 35679 MW; 41EC95893B52180A CRC64;
MRQPLSWGRW RAMLARTYGP GPSAGYRWAS GAQGYVRNPP VGACDLQGEL DRFGGISVRL
ARLDALDRLD AAAFQKGLQA AVQQWRSEGR TAVWLHIPIL QSRFIAPAAS LGFCFHHAES
DSSTLTLWLR EGPSRLPGYA SHQVGVAGAV FDESTRKILV VQDRNKLKNM WKFPGGLSEP
EEDIGDTAVR EVFEETGIKS EFRSVLSIRQ QHTNPGAFGK SDMYIICRLK PYSFTINFCQ
EECLRCEWMD LNDLAKTENT TPITSRVARL LLYGYREGFD KIDLTVEELP AVYTGLFYKL
YHKELPENYK TMKGID
