Phytin Fytiini: november 2018

fredag 30 november 2018

Human NUDIX genes

https://www.ncbi.nlm.nih.gov/pubmed/29142246

Abstract

The NUDIX enzymes are involved in cellular metabolism and homeostasis, as well as mRNA processing. Although highly conserved throughout all organisms, their biological roles and biochemical redundancies remain largely unclear. To address this, we globally resolve their individual properties and inter-relationships. We purify 18 of the human NUDIX proteins and screen 52 substrates, providing a substrate redundancy map. Using crystal structures, we generate sequence alignment analyses revealing four major structural classes. To a certain extent, their substrate preference redundancies correlate with structural classes, thus linking structure and activity relationships. To elucidate interdependence among the NUDIX hydrolases, we pairwise deplete them generating an epistatic interaction map, evaluate cell cycle perturbations upon knockdown in normal and cancer cells, and analyse their protein and mRNA expression in normal and cancer tissues. Using a novel FUSION algorithm, we integrate all data creating a comprehensive NUDIX enzyme profile map, which will prove fundamental to understanding their biological functionality.

PMID:: 29142246
PMCID:: PMC5688067
DOI:: 10.1038/s41467-017-01642-w

[Indexed for MEDLINE]

Free PMC Article

FIGURE
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5688067/figure/Fig1/

NUDT22(11q13.1) UDP-glucose- and UDP-galactose hydrolase

https://www.ncbi.nlm.nih.gov/gene/84304

Expression: Ubiquitous expression in duodenum (RPKM 16.3), spleen (RPKM 14.4) and 25 other tissues See more
Orthologs: mouse all

NUDT21 (16q13), CFIM, CPSFS , cleavage and polyadenylation specifity factor subunit 5

https://www.ncbi.nlm.nih.gov/gene/11051
The protein encoded by this gene is one subunit of a cleavage factor required for 3' RNA cleavage and polyadenylation processing. The interaction of the protein with the RNA is one of the earliest steps in the assembly of the 3' end processing complex and facilitates the recruitment of other processing factors. This gene encodes the 25kD subunit of the protein complex, which is composed of four polypeptides. [provided by RefSeq, Jul 2008]

Preferred Names: cleavage and polyadenylation specificity factor subunit 5

Names: CPSF 25 kDa subunit; cleavage and polyadenylation specific factor 5, 25 kD subunit; cleavage and polyadenylation specific factor 5, 25 kDa; cleavage and polyadenylation specificity factor 25 kDa subunit; cleavage factor Im complex 25 kDa subunit; nucleoside diphosphate-linked moiety X motif 21; nudix (nucleoside diphosphate linked moiety X)-type motif 21; nudix motif 21; pre-mRNA cleavage factor Im (25kD); pre-mRNA cleavage factor Im 25 kDa subunit; pre-mRNA cleavage factor Im 68 kDa subunit; pre-mRNA cleavage factor Im, 25kD subunit

Grudzien-Nogalska E et al. Wiley Interdiscip Rev RNA. (2017)

Abstract

Removal of the 5' end cap is a critical determinant controlling mRNA stability and efficient gene expression. Removal of the cap is exquisitely controlled by multiple direct and indirect regulators that influence association with the cap and the catalytic step. A subset of these factors directly stimulate activity of the decapping enzyme, while others influence remodeling of factors bound to mRNA and indirectly stimulate decapping. Furthermore, the components of the general decapping machinery can also be recruited by mRNA-specific regulatory proteins to activate decapping.

The Nudix hydrolase, Dcp2, identified as a first decapping enzyme, cleaves capped mRNA and initiates 5'-3' degradation. Extensive studies on Dcp2 led to broad understanding of its activity and the regulation of transcript specific decapping and decay.
Interestingly, seven additional Nudix proteins possess intrinsic decapping activity in vitro and at least two, Nudt16 and Nudt3, are decapping enzymes that regulate mRNA stability in cells.

Furthermore, a new class of decapping proteins within the DXO family preferentially function on incompletely capped mRNAs. Importantly, it is now evident that each of the characterized decapping enzymes predominantly modulates only a subset of mRNAs, suggesting the existence of multiple decapping enzymes functioning in distinct cellular pathways.
WIREs RNA 2017, 8:e1379. doi: 10.1002/wrna.1379 For further resources related to this article, please visit the WIREs website.PMID:27425147PMCID:PMC5179306DOI:10.1002/wrna.1379

A human microprotein that interacts with the mRNA decapping complex.

D'Lima NG et al. Nat Chem Biol. (2017)

Mille viae in eukaryotic mRNA decapping.

Valkov E et al. Curr Opin Struct Biol. (2017)

NUDT20 (5q22.2), DCP2 , mRNA decapping enzyme 2

https://www.ncbi.nlm.nih.gov/gene

DCP2 decapping mRNA 2 [ Homo sapiens (human) ]

Gene ID: 167227, updated on 22-Nov-2018

RefSeq status: REVIEWED
Organism: Homo sapiens
Also known as: NUDT20
Summary: The protein encoded by this gene is a key component of an mRNA-decapping complex required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). It removes the 7-methyl guanine cap structure from mRNA, prior to its degradation from the 5' end. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene.[provided by RefSeq, Jun 2011]
Expression: Ubiquitous expression in lymph node (RPKM 7.7), placenta (RPKM 6.8) and 24 other tissues See more
Orthologs: mouse all

Preferred Names: m7GpppN-mRNA hydrolase

Names: DCP2 decapping enzyme homolog; hDpc; mRNA-decapping enzyme 2; nudix (nucleoside diphosphate linked moiety X)-type motif 20

NP_001229306.1

EC 3.6.1.62

Structure, history

NM_001242377.1 → NP_001229306.1 m7GpppN-mRNA hydrolase isoform 2

Conserved Domains (2) summary

cd03672 Location:97 → 246 https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=239644: Dcp2p; mRNA decapping enzyme 2 (Dcp2p), the catalytic subunit, and Dcp1p are the two components of the decapping enzyme complex. Decapping is a key step in both general and nonsense-mediated 5'->3' mRNA-decay pathways. Dcp2p contains an all-alpha helical N-terminal domain and a C-terminal domain which has the Nudix fold. While decapping is not dependent on the N-terminus of Dcp2p, it does affect its efficiency. Dcp1p binds the N-terminal domain of Dcp2p stimulating the decapping activity of Dcp2p. Decapping permits the degradation of the transcript and is a site of numerous control inputs. It is responsible for nonsense-mediated decay as well as AU-rich element (ARE)-mediated decay. In addition, it may also play a role in the levels of mRNA. Enzymes belonging to the Nudix superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and are recognized by a highly conserved 23-residue nudix motif

pfam05026 Location:12 → 93: DCP2; Dcp2, box A domain

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

torsdag 29 november 2018

NUDT19 (19q13.11) , mitchondrial , nucleoside diphosphate-linked moiety X motif 9

https://www.ncbi.nlm.nih.gov/gene/390916
Also known as: RP2
Expression: Ubiquitous expression in adrenal (RPKM 3.2), prostate (RPKM 2.7) and 25 other tissues See more
Orthologs: mouse all

Preferred Names: nucleoside diphosphate-linked moiety X motif 19

Names: CTC-379B2.4; nucleoside diphosphate-linked moiety X motif 19, mitochondrial; nudix (nucleoside diphosphate linked moiety X)-type motif 19; nudix motif 19

Structure, history

Go to:

LOCUS

 XP_016882295             300 aa            linear   PRI 26-MAR-2018
DEFINITION

 nucleoside diphosphate-linked moiety X motif 19 isoform X1 [Homo
            sapiens].
ACCESSION   XP_016882295
VERSION     XP_016882295.1
DBLINK      BioProject: PRJNA168
DBSOURCE    REFSEQ: accession XM_017026806.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT

 MODEL REFSEQ:  This record is predicted by automated computational
            analysis. This record is derived from a genomic sequence
            (NC_000019.10) annotated using gene prediction method: Gnomon,
            supported by EST evidence.
            Also see:
                Documentation of NCBI's Annotation Process
            
            ##Genome-Annotation-Data-START##
            Annotation Provider         :: NCBI
            Annotation Status           :: Full annotation
            Annotation Name             :: Homo sapiens Annotation Release 109
            Annotation Version          :: 109
            Annotation Pipeline         :: NCBI eukaryotic genome annotation
                                           pipeline
            Annotation Software Version :: 8.0
            Annotation Method           :: Best-placed RefSeq; Gnomon
            Features Annotated          :: Gene; mRNA; CDS; ncRNA
            ##Genome-Annotation-Data-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
     Protein         1..300
                     /product="nucleoside diphosphate-linked moiety X motif 19
                     isoform X1"
                     /calculated_mol_wt=32487
     CDS             1..300
                     /gene="NUDT19"
                     /gene_synonym="RP2"
                     /coded_by="XM_017026806.2:599..1501"
                     /db_xref="GeneID:390916"
                     /db_xref="HGNC:HGNC:32036"
ORIGIN      
        1 mssslrpgps rwrraasivl aagwsrpeta tppsrpppae gfrllllqrs phqgfmpgah
       61 vfsggvldaa drsadwlglf aphhgpprfg lgpapfsrta fpslpdtddh ktdntgtlpe
      121 dvafricavr eafeeagvll lrprtsppgp apgpglalep ppglaswrdr vrqdprhflr
      181 lcahldctpd iwalhnwsaw ltpflrgttr rfdtafflcc lrepppvypd laevvgyqnl
      241 qrsldpadrn scahqcssrn tscprtcnsp rtlligvvvl tnaaaettpa qepatvpgpc
//

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

NUDT18 (8p21.3), 8-oxo-dGDP phosphatase, MTH3

https://www.ncbi.nlm.nih.gov/gene/79873

MTH3
Summary: The protein encoded by this gene is a member of the Nudix hydrolase family. Nudix hydrolases eliminate potentially toxic nucleotide metabolites from the cell and regulate the concentrations and availability of many different nucleotide substrates, cofactors, and signaling molecules. This protein contains a Nudix hydrolase domain and hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates. [provided by RefSeq, Sep 2012]
Expression: Ubiquitous expression in spleen (RPKM 3.1), lymph node (RPKM 2.8) and 25 other tissues See more
Orthologs mouse all

Preferred Names: 8-oxo-dGDP phosphatase NUDT18

Names: 2-hydroxy-dADP phosphatase; 7,8-dihydro-8-oxoguanine phosphatase; mutT homolog 3; mutT human homolog 3; nucleoside diphosphate-linked moiety X motif 18; nudix (nucleoside diphosphate linked moiety X)-type motif 18; nudix motif 18

NP_079091.3

EC 3.6.1.58

Structure, history

2012:

Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine
            and deoxyguanosine diphosphates: comparison with MTH1 and MTH2

GeneRIF: MTH3 is specifically active against 8-oxo-dGDP and hardly
            cleaves 8-oxo-dGTP. Other types of oxidized nucleoside
            diphosphates, 2-hydroxy-dADP and 8-hydroxy-dADP, were also
            hydrolyzed by MTH3.

NM_024815.4 → NP_079091.3 8-oxo-dGDP phosphatase NUDT18
aminoacids 1..323
44..166 "NUDIX hydrolase_13"
https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=240028
76..98, Nudix, motif
76..97 Nudix box

ORIGIN      
        1 maseglagal asvlagqgss vhscdsapag eppapvrlrk nvcyvvlavf lseqdevlli
       61 qeakrecrgs wylpagrmep getivealqr evkeeaglhc epetllsvee rgpswvrfvf
      121 larptggilk tskeadaesl qaawyprtsl ptplrahdil hlvelaaqyr qqarhplilp
      181 qelpcdlvcq rlvatftsaq tvwvlvgtvg mphlpvtacg ldpmeqrggm kmavlrllqe
      241 cltlhhlvve ikgllglqhl grdhsdgicl nvlvtvafrs pgiqdeppkv rgenfswwkv
      301 meedlqsqll qrlqgssvvp vnr
//

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

MTH3 is specifically active against 8-oxo-dGDP and hardly cleaves 8-oxo-dGTP. Other types of oxidized nucleoside diphosphates, 2-hydroxy-dADP and 8-hydroxy-dADP, were also hydrolyzed by MTH3.

NUDT17 (1q21.1)

https://www.ncbi.nlm.nih.gov/gene/200035

Expression: Ubiquitous expression in skin (RPKM 3.7), endometrium (RPKM 3.3) and 25 other tissues See more
Orthologs: mouse all

Preferred Names: nucleoside diphosphate-linked moiety X motif 17

Names: nudix (nucleoside diphosphate linked moiety X)-type motif 17; nudix motif 17

NM_001012758.3 → NP_001012776.1 nucleoside diphosphate-linked moiety X motif 17

    CDS             1..328
                     /gene="NUDT17"
                     /coded_by="NM_001012758.3:12..998"
                     /db_xref="CCDS:CCDS72865.1"
                     /db_xref="GeneID:200035"
                     /db_xref="HGNC:HGNC:26618"
ORIGIN      
        1 maevrvqlll srrpesvsfa rsvcgllgag pglgtwpihc slkrgrlvls srpfpgasar
       61 lplqrppfcp faaleerprv pgaelptdrg vdlgvavilq ssdktvlltr rartlsvspn
      121 lwvppgghve leeelldggl relweesglh lpqgqfswvp lglwesaypp rlswglpkyh
      181 hivlyllvis qesqqqlqar iqpnpnevsa lmwltpdvaa avaaaedgte tpgllpqdlp
      241 psvlavelee dgrarplvlh mstllrmipt maedkervst gtkfalklwl qhlgrtpppc
      301 ksaayldpgp akeewnmdpl ppnqgsgk
//

NUDT16 (3q22.1), RNA decapping pathway, IDPphosphatase

https://www.ncbi.nlm.nih.gov/gene/131870

Preferred Names: U8 snoRNA-decapping enzyme

Names: IDP phosphatase; IDPase; U8 snoRNA-binding protein H29K; inosine diphosphate phosphatase; m7GpppN-mRNA hydrolase; nucleoside diphosphate-linked moiety X motif 16; nudix (nucleoside diphosphate linked moiety X)-type motif 16; nudix motif 16; testicular tissue protein Li 129

NP_001165376.1

EC 3.6.1.62

EC 3.6.1.64

Structure, history

Conserved Domains (1) summary

cl00447 Location:7 → 36: Nudix_Hydrolase; Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ ...

GeneRIFs: Gene References Into Functions

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(1) Citate

2018 May;24(5):633-642. doi: 10.1261/rna.065698.118. Epub 2018 Feb 26.

Hydrolytic activity of human Nudt16 enzyme on dinucleotide cap analogs and short capped oligonucleotides.

Grzela R¹, Nasilowska K², Lukaszewicz M², Tyras M¹, Stepinski J¹, Jankowska-Anyszka M³, Bojarska E¹, Darzynkiewicz E^1,². Abstract

Human Nudt16 (hNudt16) is a member of the Nudix family of hydrolases, comprising enzymes catabolizing various substrates including canonical (d)NTPs, oxidized (d)NTPs, nonnucleoside polyphosphates, and capped mRNAs.
Decapping activity of the Xenopus laevis (X29) Nudt16 homolog was observed in the nucleolus, with a high specificity toward U8 snoRNA. Subsequent studies have reported cytoplasmic localization of mammalian Nudt16 with cap hydrolysis activity initiating RNA turnover, similar to Dcp2. The present study focuses on hNudt16 and its hydrolytic activity toward dinucleotide cap analogs and short capped oligonucleotides.
We performed a screening assay for potential dinucleotide and oligonucleotide substrates for hNudt16. Our data indicate that dinucleotide cap analogs and capped oligonucleotides containing guanine base in the first transcribed nucleotide are more susceptible to enzymatic digestion by hNudt16 than their counterparts containing adenine. Furthermore, unmethylated dinucleotides (GpppG and ApppG) and respective oligonucleotides (GpppG-16nt and GpppA-16nt) were hydrolyzed by hNudt16 with greater efficiency than were m⁷GpppG and m⁷GpppG-16nt. In conclusion, we found that hNudt16 hydrolysis of dinucleotide cap analogs and short capped oligonucleotides displayed a broader spectrum specificity than is currently known.

KEYWORDS: cap analogs; cap hydrolysis; capped oligonucleotides; decapping enzymes; nudix hydrolasesPMID:29483298 PMCID: PMC5900562[Available on 2019-05-01] DOI:10.1261/rna.065698.118

2007 Aug 24;282(34):24792-805. Epub 2007 Jun 13.

Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16).

Peculis BA¹, Reynolds K, Cleland M. Abstract

The Xenopus X29 protein was identified by its high affinity binding to U8 small nucleolar RNA, a small nucleolar RNA required for ribosome biogenesis. X29 and its human homologue H29K (Nudt16) are nuclear nucleoside diphosphatase proteins localized within foci in the nucleolus and nucleoplasm. These proteins can remove m(7)G and m(227)G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. Here, a more complete characterization of these metal-dependent decapping proteins demonstrates that the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg(+2) the proteins hydrolyze the 5' cap from only one RNA substrate: U8 small nucleolar RNA. However, in the presence of Mn(+2) or Co(+2) all RNAs are substrates and the decapping efficiency is higher. The x-ray crystal structure of X29 facilitated structure-based mutagenesis. Mutation of single amino acids coordinating metal in the active site yielded mutant proteins confirming essential residues. In vitro assays with purified components are consistent with a lack of protein turnover, apparently due to an inability of the protein to release the decapped RNA, implicating critical in vivo interacting factors. Collectively, these studies indicate that the metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs. With the potential broader RNA substrate specificity, X29/H29K may be the nuclear counterparts of the cytoplasmic decapping machinery, localized in specialized bodies involved in RNA decay. PMID: 17567574 DOI: 10.1074/jbc.M704179200[Indexed for MEDLINE] Free full text

NUDT15 (13q14.2), MTH2D, Nucleotide triphosphate difosfataasi

https://www.ncbi.nlm.nih.gov/gene/55270
Obs: Thiopurine induced leukemia

Also known as: MTH2; NUDT15D
Summary: This gene encodes an enzyme that belongs to the Nudix hydrolase superfamily. Members of this superfamily catalyze the hydrolysis of nucleoside diphosphates, including substrates like 8-oxo-dGTP, which are a result of oxidative damage, and can induce base mispairing during DNA replication, causing transversions. The encoded enzyme is a negative regulator of thiopurine activation and toxicity. Mutations in this gene result in poor metabolism of thiopurines, and are associated with thiopurine-induced early leukopenia. Multiple pseudogenes of this gene have been identified. [provided by RefSeq, Apr 2016]
Expression: Ubiquitous expression in colon (RPKM 4.7), duodenum (RPKM 4.1) and 25 other tissues See more

Preferred Names: nucleotide triphosphate diphosphatase NUDT15

Names: 8-oxo-dGTPase NUDT15; mutT homolog 2; nucleoside diphosphate-linked to another moiety X hydrolase 15; nudix (nucleoside diphosphate linked moiety X)-type motif 15; probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15; probable 8-oxo-dGTP diphosphatase NUDT15

NP_001291674.1

EC 3.6.1.9

GeneRIFs: Gene References Into Functions

Submit: New GeneRIF Correction See all GeneRIFs (30)

NUTD14 (14q32.33), UGPP, UGPPase, UDPG-pyrophosphatase , UDP-sugar diphosphatase

https://www.ncbi.nlm.nih.gov/gene/256281

Also known as: UGPP; UGPPase
Summary: The protein encoded by this gene is a member of the Nudix hydrolase family. Nudix hydrolases eliminate potentially toxic nucleotide metabolites from the cell and regulate the concentrations and availability of many different nucleotide substrates, cofactors, and signaling molecules. This enzyme contains a Nudix hydrolase domain and is a UDPG pyrophosphatase that hydrolyzes UDPG to produce glucose 1-phosphate and UMP. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2016]
Expression: Ubiquitous expression in fat (RPKM 8.0), kidney (RPKM 7.1) and 25 other tissues See more

Preferred Names: uridine diphosphate glucose pyrophosphatase

Names: UDP-sugar diphosphatase; UDPG pyrophosphatase; nudix (nucleoside diphosphate linked moiety X)-type motif 14

NP_001305309.1

EC 3.6.1.45

Structure, History, isoform 2

https://www.ncbi.nlm.nih.gov/protein/NP_001305309.1

Conserved Domains (1) summary

cl00447 Location:39 → 145: Nudix_Hydrolase; Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ ...

GeneRIFs: Gene References Into Functions

the interaction between the RL13 protein and NUDT14 protein may be involved in human cytomegalovirus DNA replication.

NUDT13(10q22.2) NADH pyrofosfatase

https://www.ncbi.nlm.nih.gov/gene/25961

Preferred Names: nucleoside diphosphate-linked moiety X motif 13

Names: nudix (nucleoside diphosphate linked moiety X)-type motif 13; nudix motif 13

Structure, history

Conserved Domains (3) summary

pfam09296 Location:49 → 162: NUDIX-like; NADH pyrophosphatase-like rudimentary NUDIX domain

pfam09297 Location:166 → 195: zf-NADH-PPase; NADH pyrophosphatase zinc ribbon domain

cl00447 Location:198 → 255: Nudix_Hydrolase; Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ ...

GeneRIFs: Gene References Into Functions

Observational study of gene-disease association. (HuGE Navigator)

NUDT12(5q21.2) Peroxisomal NADH pyrophosphatase

Summary: Nucleotides are involved in numerous biochemical reactions and pathways within the cell as substrates, cofactors, and effectors. Nudix hydrolases, such as NUDT12, regulate the concentrations of individual nucleotides and of nucleotide ratios in response to changing circumstances (Abdelraheim et al., 2003 [PubMed 12790796]).[supplied by OMIM, Mar 2008]
Expression: Ubiquitous expression in kidney (RPKM 12.0), thyroid (RPKM 10.7) and 24 other tissues See more
Orthologs

mouse all

Preferred Names: peroxisomal NADH pyrophosphatase NUDT12

Names: nucleoside diphosphate linked moiety X-type motif 12; nucleoside diphosphate-linked moiety X motif 12; nudix (nucleoside diphosphate linked moiety X)-type motif 12; nudix motif 12

NP_001287670.1

EC 3.6.1.22

Structure, History

https://www.ncbi.nlm.nih.gov/protein/NP_001287670.1

Conserved Domains (6) summary

COG2816 Location:108 → 437: NPY1; NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism]

cd00204 Location:14 → 80: ANK; ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ANK repeats in a protein can range from 2 to over 20 (ankyrins, for example). ANK repeats may occur in combinations with other ...

cd03429 Location:305 → 438: NADH_pyrophosphatase; NADH pyrophosphatase, a member of the Nudix hydrolase superfamily, catalyzes the cleavage of NADH into reduced nicotinamide mononucleotide (NMNH) and AMP. Like other members of the Nudix family, it requires a divalent cation, such as Mg2+ or Mn2+, for ...

pfam09296 Location:130 → 259: NUDIX-like; NADH pyrophosphatase-like rudimentary NUDIX domain

pfam09297 Location:261 → 284: zf-NADH-PPase; NADH pyrophosphatase zinc ribbon domain

pfam12796 Location:16 → 80: Ank_2; Ankyrin repeats (3 copies)

GeneRIFs: Gene References Into Functions

NUTD11 (Xp11.22), DIPP3b, DIPP3beta, APS1, ASP1

https://www.ncbi.nlm.nih.gov/gene/55190

Also known as: APS1; ASP1; DIPP3b; DIPP3beta; hDIPP3beta
Summary: NUDT11 belongs to a subgroup of phosphohydrolases that preferentially attack diphosphoinositol polyphosphates (Hidaka et al., 2002 [PubMed 12105228]).[supplied by OMIM, Mar 2008]
Expression: Biased expression in testis (RPKM 29.1), brain (RPKM 16.8) and 4 other tissues See more
Orthologs mouse all

Preferred Names: diphosphoinositol polyphosphate phosphohydrolase 3-beta

Names: DIPP-3-beta; DIPP3-beta; diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-beta; diadenosine hexaphosphate hydrolase (AMP-forming); diphosphoinositol polyphosphate phosphohydrolase 3, beta; hAps1; nucleoside diphosphate-linked moiety X motif 11; nudix (nucleoside diphosphate linked moiety X)-type motif 11; nudix motif 11

NP_060629.2

EC 3.6.1.52

EC 3.6.1.60

Structure, history

https://www.ncbi.nlm.nih.gov/protein/NP_060629.2

GeneRIFs: Gene References Into Functions

Submit: New GeneRIF Correction

NUTD10 (Xp11.22) , DIPP3a, DIPP3-alpha, APS

https://www.ncbi.nlm.nih.gov/gene/170685

lso known as: APS2; DIPP3a; DIPP3-alpha
Summary: This gene is a member of the nudix (nucleoside diphosphate linked moiety X)-type motif containing family. The encoded protein is a phosphohydrolase and may regulate the turnover of diphosphoinositol polyphosphates. The turnover of these high-energy diphosphoinositol polyphosphates represents a molecular switching activity with important regulatory consequences. Molecular switching by diphosphoinositol polyphosphates may contribute to the regulation of intracellular trafficking. In some populations putative prostate cancer susceptibility alleles have been identified for this gene. Alternatively spliced transcript variants, which differ only in the 5' UTR, have been found for this gene. [provided by RefSeq, Feb 2015]
Expression: Biased expression in testis (RPKM 20.6), brain (RPKM 8.6) and 6 other tissues See more
Orthologs all

Preferred Names: diphosphoinositol polyphosphate phosphohydrolase 3-alpha

Names: diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha; diadenosine hexaphosphate hydrolase (AMP-forming); nucleoside diphosphate-linked moiety X motif 10; nudix (nucleoside diphosphate linked moiety X)-type motif 10; nudix motif 10

NP_001291892.1

EC 3.6.1.52

EC 3.6.1.60

Structure, history

ORIGIN      
        1 mkckpnqtrt ydpegfkkra aclcfrsere devllvsssr ypdrwivpgg gmepeeepgg
       61 aavrevyeea gvkgklgrll gvfeqnqdpk hrtyvyvltv telledweds vsigrkrewf
      121 kvedaikvlq chkpvhaeyl eklklggspt ngnsmapssp dsdp
//

GeneRIFs: Gene References Into Functions

Submit: New GeneRIF Correction

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Abstract

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