NUD13_HUMAN
ID NUD13_HUMAN Reviewed; 352 AA.
AC Q86X67; B4DV90; O95650; Q5SQM4; Q5SQM5; Q5SQM6; Q9Y3X2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=NAD(P)H pyrophosphatase NUDT13, mitochondrial {ECO:0000305};
DE EC=3.6.1.22 {ECO:0000250|UniProtKB:Q8JZU0};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 13;
DE Short=Nudix motif 13;
DE AltName: Full=Protein KiSS-16;
DE Flags: Precursor;
GN Name=NUDT13 {ECO:0000312|HGNC:HGNC:18827};
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAB43279.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH46173.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Eye {ECO:0000312|EMBL:AAH46173.2};
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-352 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6] {ECO:0000305, ECO:0000312|EMBL:CAB43279.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 156-236, AND TISSUE SPECIFICITY.
RC TISSUE=Melanoma;
RA Welch D.R., Lee J.-H.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and
CC AMP, and NADPH into NMNH and 2',5'-ADP. Has a marked preference for the
CC reduced pyridine nucleotides. Does not show activity toward NAD-capped
CC RNAs; the NAD-cap is an atypical cap present at the 5'-end of some
CC RNAs. {ECO:0000250|UniProtKB:Q8JZU0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-
CC ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832,
CC ChEBI:CHEBI:456215; EC=3.6.1.22;
CC Evidence={ECO:0000250|UniProtKB:Q8JZU0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48869;
CC Evidence={ECO:0000250|UniProtKB:Q8JZU0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2
CC H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC EC=3.6.1.22; Evidence={ECO:0000250|UniProtKB:Q8JZU0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11801;
CC Evidence={ECO:0000250|UniProtKB:Q8JZU0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADPH = adenosine 3',5'-bisphosphate + 2 H(+) + reduced
CC beta-nicotinamide D-ribonucleotide; Xref=Rhea:RHEA:60820,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:90832;
CC Evidence={ECO:0000250|UniProtKB:Q8JZU0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60821;
CC Evidence={ECO:0000250|UniProtKB:Q8JZU0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8JZU0};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8JZU0};
CC Note=Divalent metal cations. Mg(2+) or Mn(2+).
CC {ECO:0000250|UniProtKB:Q8JZU0};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8JZU0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86X67-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86X67-2; Sequence=VSP_011417;
CC Name=3;
CC IsoId=Q86X67-3; Sequence=VSP_054559;
CC Name=4;
CC IsoId=Q86X67-4; Sequence=VSP_055695, VSP_055696;
CC -!- TISSUE SPECIFICITY: Highly expressed in metastasis-suppressed
CC chromosome 6 melanoma hybrids. {ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD00649.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK300980; BAG62602.1; -; mRNA.
DR EMBL; AC016394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54472.1; -; Genomic_DNA.
DR EMBL; BC038833; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC046173; AAH46173.2; -; mRNA.
DR EMBL; AL050114; CAB43279.1; -; mRNA.
DR EMBL; U88048; AAD00649.1; ALT_FRAME; mRNA.
DR CCDS; CCDS31220.1; -. [Q86X67-1]
DR CCDS; CCDS60551.1; -. [Q86X67-4]
DR CCDS; CCDS60552.1; -. [Q86X67-2]
DR CCDS; CCDS60553.1; -. [Q86X67-3]
DR PIR; T08762; T08762.
DR RefSeq; NP_001269943.1; NM_001283014.1. [Q86X67-2]
DR RefSeq; NP_001269944.1; NM_001283015.1. [Q86X67-4]
DR RefSeq; NP_001269945.1; NM_001283016.1. [Q86X67-3]
DR RefSeq; NP_001269946.1; NM_001283017.1.
DR RefSeq; NP_001269948.1; NM_001283019.1.
DR RefSeq; NP_056985.3; NM_015901.5. [Q86X67-1]
DR RefSeq; XP_016871522.1; XM_017016033.1. [Q86X67-4]
DR AlphaFoldDB; Q86X67; -.
DR SMR; Q86X67; -.
DR BioGRID; 117451; 16.
DR IntAct; Q86X67; 1.
DR STRING; 9606.ENSP00000349874; -.
DR iPTMnet; Q86X67; -.
DR PhosphoSitePlus; Q86X67; -.
DR BioMuta; NUDT13; -.
DR DMDM; 51701672; -.
DR EPD; Q86X67; -.
DR jPOST; Q86X67; -.
DR MassIVE; Q86X67; -.
DR PaxDb; Q86X67; -.
DR PeptideAtlas; Q86X67; -.
DR PRIDE; Q86X67; -.
DR ProteomicsDB; 5254; -.
DR ProteomicsDB; 63810; -.
DR ProteomicsDB; 70247; -. [Q86X67-1]
DR ProteomicsDB; 70248; -. [Q86X67-2]
DR Antibodypedia; 29309; 73 antibodies from 20 providers.
DR DNASU; 25961; -.
DR Ensembl; ENST00000349051.9; ENSP00000335326.6; ENSG00000166321.14. [Q86X67-2]
DR Ensembl; ENST00000357321.9; ENSP00000349874.4; ENSG00000166321.14. [Q86X67-1]
DR Ensembl; ENST00000372997.3; ENSP00000362088.3; ENSG00000166321.14. [Q86X67-4]
DR Ensembl; ENST00000544879.5; ENSP00000440760.1; ENSG00000166321.14. [Q86X67-3]
DR GeneID; 25961; -.
DR KEGG; hsa:25961; -.
DR MANE-Select; ENST00000357321.9; ENSP00000349874.4; NM_015901.6; NP_056985.3.
DR UCSC; uc001jtj.5; human. [Q86X67-1]
DR CTD; 25961; -.
DR DisGeNET; 25961; -.
DR GeneCards; NUDT13; -.
DR HGNC; HGNC:18827; NUDT13.
DR HPA; ENSG00000166321; Low tissue specificity.
DR MIM; 609233; gene.
DR neXtProt; NX_Q86X67; -.
DR OpenTargets; ENSG00000166321; -.
DR PharmGKB; PA38700; -.
DR VEuPathDB; HostDB:ENSG00000166321; -.
DR eggNOG; KOG3084; Eukaryota.
DR GeneTree; ENSGT00940000158879; -.
DR HOGENOM; CLU_037162_0_0_1; -.
DR InParanoid; Q86X67; -.
DR OMA; CDMGENV; -.
DR OrthoDB; 1436400at2759; -.
DR PhylomeDB; Q86X67; -.
DR TreeFam; TF106352; -.
DR PathwayCommons; Q86X67; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR SignaLink; Q86X67; -.
DR BioGRID-ORCS; 25961; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; NUDT13; human.
DR GenomeRNAi; 25961; -.
DR Pharos; Q86X67; Tdark.
DR PRO; PR:Q86X67; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86X67; protein.
DR Bgee; ENSG00000166321; Expressed in right lobe of liver and 116 other tissues.
DR ExpressionAtlas; Q86X67; baseline and differential.
DR Genevisible; Q86X67; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; ISS:UniProtKB.
DR GO; GO:0016462; F:pyrophosphatase activity; TAS:Reactome.
DR GO; GO:0006734; P:NADH metabolic process; ISS:UniProtKB.
DR GO; GO:0006742; P:NADP catabolic process; ISS:UniProtKB.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR InterPro; IPR015375; NADH_PPase-like_N.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015376; Znr_NADH_PPase.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF09296; NUDIX-like; 1.
DR Pfam; PF09297; zf-NADH-PPase; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Mitochondrion; NAD; NADP; Reference proteome; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..352
FT /note="NAD(P)H pyrophosphatase NUDT13, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000057111"
FT DOMAIN 196..323
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 216..240
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT VAR_SEQ 1..126
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054559"
FT VAR_SEQ 198..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011417"
FT VAR_SEQ 198..235
FT /note="MAPVAITLVSDGTRCLLARQSSFPKGMYSALAGFCDIG -> VKVWKRPSAE
FT KLQKRWDWRWKACSTMHPSIGPSLVAHS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055695"
FT VAR_SEQ 236..352
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055696"
FT VARIANT 81
FT /note="G -> D (in dbSNP:rs34284214)"
FT /id="VAR_034160"
FT VARIANT 273
FT /note="M -> V (in dbSNP:rs17658872)"
FT /id="VAR_050413"
SQ SEQUENCE 352 AA; 39688 MW; 1FBBDB1ECD50BCAE CRC64;
MSLYCGIACR RKFFWCYRLL STYVTKTRYL FELKEDDDAC KKAQQTGAFY LFHSLAPLLQ
TSAHQYLAPR HSLLELERLL GKFGQDAQRI EDSVLIGCSE QQEAWFALDL GLDSSFSISA
SLHKPEMETE LKGSFIELRK ALFQLNARDA SLLSTAQALL RWHDAHQFCS RSGQPTKKNV
AGSKRVCPSN NIIYYPQMAP VAITLVSDGT RCLLARQSSF PKGMYSALAG FCDIGESVEE
TIRREVAEEV GLEVESLQYY ASQHWPFPSG SLMIACHATV KPGQTEIQVN LRELETAAWF
SHDEVATALK RKGPYTQQQN GTFPFWLPPK LAISHQLIKE WVEKQTCSSL PA
