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Information on EC 3.1.31.1 - micrococcal nuclease and Organism(s) Homo sapiens and UniProt Accession Q7KZF4
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3.1.31.1 micrococcal nucleaseSpecify your search results
Word Map
- 3.1.31.1
- chromatin
- nucleosomes
- histone
- nuclei
- strand
- nucleases
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mononucleosomes
- dnaase
- deoxyribonuclease
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footprint
- coagulase
- nucleoprotein
- enterotoxin
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nonhistone
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oligonucleosomes
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octamer
- ribonucleoprotein
- polycephalum
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chromatin-associated
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non-transcribed
- medicine
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protein-dna
- globin
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staphylococci
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native-like
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internucleosomal
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hyperacetylated
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snrnp
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telomeres
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nuclease-resistant
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32p-postlabeling
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decondensation
- physarum
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minichromosome
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chromatin-bound
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endonucleolytic
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coagulase-positive
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coagulase-negative
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end-labeling
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histone-dna
- beta-globin
- drug development
- molecular biology
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superhelical
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supercoiled
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exonuclease
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dielectric
- analysis
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i-hypersensitive
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ladder
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base-pairs
- biotechnology
- cscl
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heterochromatic
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nucleolytic
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
Synonyms
micrococcal nuclease, staphylococcal nuclease, mnase, snase, thermonuclease, tudor-sn, staphylococcus aureus nuclease, tudor staphylococcal nuclease, staphylococcal nuclease a, s. aureus nuclease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
micrococcal DNase
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micrococcal endonuclease
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Micrococcal nuclease
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MN
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nuclease 8V
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nuclease T
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nuclease T'
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nuclease, micrococcal
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nuclease, staphylococcal
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ribonucleate (deoxyribo-nucleate) 3'-nucleotidohydrolase
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ribonucleate (deoxyribonucleate) 3'-nucleotidohydrolase
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S. aureus nuclease
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snake venom phosphodiesterase
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SNase
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spleen endonuclease
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spleen phosphodiesterase
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staph nuclease
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staphylococcal nuclease
staphylococcus aureus nuclease
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staphylococcus aureus nuclease B
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thermonuclease
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-
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TNase
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-
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staphylococcal nuclease
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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CAS REGISTRY NUMBER
COMMENTARY
9013-53-0
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
caspase-3
Tudor staphylococcal nuclease, a multifunctional regulator of gene expression, is cleaved by caspase-3 during apoptosis, this cleavage impairs the ability of Tudor staphylococcal nuclease to activate mRNA splicing, inhibits its ribonuclease activity and is important for the execution of apoptosis, cleavage of enzyme lowers its nuclease activity by almost 50%
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deoxythymidine 3',5'-bisphosphate
nuclease activity of enzyme is highly sensitive to deoxythymidine 3',5'-bisphosphate, a specific inhibitor of staphylococcal nuclease, whereas the inactive analogue deoxythymidine 3'-phosphate has no inhibitory effect
metacaspase mcII-Pa
metacaspase mcII-Pa cleaves the phylogenetically conserved protein Tudor staphylococcal nuclease during both developmental and stress-induced programmed cell death
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additional information
induction of apoptosis in HCT116 colon carcinoma cells with 5-fluorouracil leads to increased caspase-3-like activity and cleavage of endogenous Tudor staphylococcal nuclease into 2 fragments with the same molecular mass in vitro, this effect is not cell- and drug-specific because a similar pattern of endogenous Tudor staphylococcal nuclease cleavage is detected in camptothecin-treated HeLa cells
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additional information
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induction of apoptosis in HCT116 colon carcinoma cells with 5-fluorouracil leads to increased caspase-3-like activity and cleavage of endogenous Tudor staphylococcal nuclease into 2 fragments with the same molecular mass in vitro, this effect is not cell- and drug-specific because a similar pattern of endogenous Tudor staphylococcal nuclease cleavage is detected in camptothecin-treated HeLa cells
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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expression of the enzyme and of angiotensin II type 1 receptor are positively correlated
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Staphylococcal nuclease domain containing-1 is overexpressed in human hepatocellular carcinoma patients
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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human Tudor staphylococcal nuclease interacts with the Ras-GAP SH3 domain-binding protein and is recruited into stress granules, the main type of discrete RNA-containing cytoplasmic foci structure that is formed under stress conditions
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
programmed cell death pathways, Tudor staphylococcal nuclease is a new component of the human programmed degradome and is cleaved by caspase-3 between the Tudor and SN5 domains
physiological function
malfunction
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conditioned medium from Hep3B-SND1 cells stably overexpressing SND1 augmentes, whereas that from QGYSND1si cells stably overexpressing SND1 siRNA significantly inhibits angiogenesis, as analyzed by a chicken chorioallantoic membrane assay and a human umbilical vein endothelial cell differentiation assay
physiological function
additional information
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staphylococcal nuclease domain-containing 1, SND1, is a multifunctional nuclease containing four staphylococcal nuclease domains and a tudor domain. No potential interaction between enzyme SND1 and p65 subunit of NF-kappa B
physiological function
ribonuclease activity, control of gene expression by activating transcription, subsequent mRNA splicing, regulation of RNA silencing and in the pathway that edits and destroys double-stranded RNA, uncleavable Tudor staphylococcal nuclease stimulates cell proliferation and protects cells from death
physiological function
staphylococcal nuclease domain-containing protein 1 is a component of the RNA-induced splicing complex that mediates RNA interference, leading to degradation of specific mRNAs
physiological function
the downregulated expression of Tudor-staphylococcal nuclease can decrease cancer malignancy, and the overexpression can increase viability and migration potential of various tumor cell types. Tudor-SN silencing suppresses the expression of alkylglycerone phosphate synthase (AGPS) and the activity of the mechanistic target of rapamycin (mTOR) signaling pathway. NF-kappaB and miR-127 may be the mediators of Tudor-SN-regulated alkylglycerone phosphate synthase (AGPS) via the mTOR signaling pathway
physiological function
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enzyme hepatocellular carcinoma Staphylococcal nuclease domain containing-1 promotes tumorigenesis in human hepatocellular carcinoma cells. It increases angiotensin II type 1 receptor (AT1R) levels by increasing AT1R mRNA stability. That results in activation of ERK, Smad2 and subsequently the TGFbeta signaling pathway, promoting epithelial-mesenchymal transition and migration and invasion by human hepatocellular carcinoma cells. The enzyme modulates the TGFbeta signaling pathway
physiological function
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the enzyme is a stress-related protein, enzyme Tudor-SN plays an important role in the assembly of AGTR1-3' UTR granules affecting the recovery kinetics of stress granules
physiological function
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the enzyme staphylococcal nuclease domain-containing 1, SND1, regulates a variety of cellular functions and promotes an aggressive tumorigenic phenotype in hepatocellular carcinoma cells. Role of SND1 in regulating tumor angiogenesis, a hallmark of cancer, overview. SND1 regulates NF-kappaB and miR-221, two important determinants of hepatocellular carcinoma controlling the aggressive phenotype. The enzyme induces angiogenesis by up-regulating angiogenin and CXCL16. The phosphorylation of IKKalpha and IkappaBalpha upon enzyme overexpression suggests activation of a canonical NF-kappa B signaling pathway by the enzyme
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SND1_HUMAN
910
0
101997
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D790E
by site-directed mutagenesis, proteolysis of Tudor staphylococcal nuclease does not occur either when the P1 position of the DAVD motif is mutated or after treatment with the pan-caspase inhibitor zVAD-fluoromethylketone, expression of mutant under normal conditions enhances cell proliferation in both cancer (HeLa) and non-cancer (HEK-293) cells compared with mock- and wild-type Tudor staphylococcal nuclease-transfected samples, under camptothecin-induced apoptosis, expression of Tudor staphylococcal nuclease mutant results in a 35% increment in viable HeLa cells, suggesting that caspase-mediated proteolysis of enzyme is important for the progression of apoptosis
additional information
additional information
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enzyme inactivation by siRNA expression in enzyme-expressing HeLa cells
additional information
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knockdown of SND1 in QGY-7703 cells inhibits establishment of xenografts in nude mice
additional information
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suppression in QGY-7703 cells by si RNA, SND1-17-AT1Rsi
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein is purified by anion exchange chromatography on a Q Sepharose Fast Flow column using a linear gradient of NaCl (0-500 mM) in 20 mM Tris-HCl at pH 8.0, 2 mM dithiothreitol and 10% glycerol
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the enzyme from a plsmid encoding RFP-epitope-tagged Tudor-SN in HeLa cells, localization profile of the Tudor-SN-AGTR1-3'UTR complex, GFP-MS2 fluorescence and immuno-labeling analysis, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in hyperplasia specimens and normal epithelium, protein is weakly or negatively expressed
knocked down staphylococcal nuclease domain-containing protein 1 in vitro with small interfering RNA causes a significant decrease in cell growth
staphylococcal nuclease domain-containing protein 1 is highly expressed in recurrent androgen-insensitive prostate cancer tissues, protein expression intensity increases with increasing grade and aggressiveness of the cancer, staphylococcal nuclease domain-containing protein 1 mRNA is highly expressed in the cytoplasm of cancer cells but is negative to weak in noncancerous cells
Tudor staphylococcal nuclease knockdown leads to activation of ectopic cell death during reproduction, impairing plant fertility, HeLa cells transfected with Tudor staphylococcal nuclease short interfering RNA show a dramatic increase in apoptotic response to camptothecin accompanied by a 7.9fold increase in activation of caspase-3 and increased cleavage of PARP and lamin-A (by 3.7fold and 6.7fold, respectively), moreover, reduction of Tudor staphylococcal nuclease levels induces apoptosis even in the absence camptothecin, leading to 7.7fold, 6.1fold and 11fold increases in apoptotic markers, demonstrating that Tudor staphylococcal nuclease is indispensable for the maintenance of cell viability
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
as staphylococcal nuclease domain-containing protein 1 mRNA is overexpressed in cancer cells, the growth of these cells is suppressed following staphylococcal nuclease domain-containing protein 1 knock-down in vitro, thus representing a promising prostate cancer biomarker and therapeutic target, evidence for the diagnostic potential of staphylococcal nuclease domain-containing protein 1 in prostate surgical specimens equivalent or better than that of alpha-methylacyl-CoA racemase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuruma, H.; Kamata, Y.; Takahashi, H.; Igarashi, K.; Kimura, T.; Miki, K.; Miki, J.; Sasaki, H.; Hayashi, N.; Egawa, S.
Staphylococcal nuclease domain-containing protein 1 as a potential tissue marker for prostate cancer
Am. J. Pathol.
174
2044-2050
2009
Homo sapiens (Q7KZF4), Homo sapiens
Sundstroem, J.F.; Vaculova, A.; Smertenko, A.P.; Savenkov, E.I.; Golovko, A.; Minina, E.; Tiwari, B.S.; Rodriguez-Nieto, S.; Zamyatnin, A.A.; Vaelineva, T.; Saarikettu, J.; Frilander, M.J.; Suarez, M.F.; Zavialov, A.; Stahl, U.; Hussey, P.J.; Silvennoinen, O.; Sundberg, E.; Zhivotovsky, B.; Bozhkov, P.
Tudor staphylococcal nuclease is an evolutionarily conserved component of the programmed cell death degradome
Nat. Cell Biol.
11
1347-1354
2009
Picea abies (Q0JRI3), Homo sapiens (Q7KZF4), Homo sapiens, Arabidopsis thaliana (Q8VZG7), Arabidopsis thaliana (Q9FLT0)
Gao, X.; Shi, X.; Fu, X.; Ge, L.; Zhang, Y.; Su, C.; Yang, X.; Silvennoinen, O.; Yao, Z.; He, J.; Wei, M.; Yang, J.
Human Tudor staphylococcal nuclease (Tudor-SN) protein modulates the kinetics of AGTR1-3UTR granule formation
FEBS Lett.
588
2154-2161
2014
Homo sapiens
Santhekadur, P.K.; Akiel, M.; Emdad, L.; Gredler, R.; Srivastava, J.; Rajasekaran, D.; Robertson, C.L.; Mukhopadhyay, N.D.; Fisher, P.B.; Sarkar, D.
Staphylococcal nuclease domain containing-1 (SND1) promotes migration and invasion via angiotensin II type 1 receptor (AT1R) and TGFbeta signaling
FEBS open bio
4
353-361
2014
Homo sapiens
Santhekadur, P.K.; Das, S.K.; Gredler, R.; Chen, D.; Srivastava, J.; Robertson, C.; Baldwin, A.S.; Fisher, P.B.; Sarkar, D.
Multifunction protein staphylococcal nuclease domain containing 1 (SND1) promotes tumor angiogenesis in human hepatocellular carcinoma through novel pathway that involves nuclear factor kappaB and miR-221
J. Biol. Chem.
287
13952-13958
2012
Homo sapiens
Zhang, Y.; Jia, J.; Li, Y.; Chen, Y.G.; Huang, H.; Qiao, Y.; Zhu, Y.
Tudor-staphylococcal nuclease regulates the expression and biological function of alkylglycerone phosphate synthase via nuclear factor-kappaB and microRNA-127 in human glioma U87MG cells
Oncol. Lett.
15
9553-9558
2018
Homo sapiens (Q7KZF4), Homo sapiens
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