Snd1 staphylococcal nuclease and tudor domain containing 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Snd1provided by MGI
Official Full Name: staphylococcal nuclease and tudor domain containing 1provided by MGI
Primary source: MGI:MGI:1929266
See related: Ensembl:ENSMUSG00000001424 AllianceGenome:MGI:1929266
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Tudor-SN
Summary: Predicted to enable RISC complex binding activity; RNA binding activity; and RNA endonuclease activity. Predicted to be involved in mRNA catabolic process; miRNA catabolic process; and regulation of cell cycle process. Located in dense body and nucleus. Is expressed in several structures, including central nervous system; early conceptus; limb mesenchyme; reproductive system; and sensory organ. Orthologous to human SND1 (staphylococcal nuclease and tudor domain containing 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in adrenal adult (RPKM 40.7), ovary adult (RPKM 37.4) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 6 A3.3; 6 11.99 cM

Exon count:: 27

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	6	NC_000072.7 (28480332..28935161)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	6	NC_000072.6 (28480337..28935162)

Chromosome 6 - NC_000072.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

SND1, a novel co-activator of HIF1alpha, promotes tumor initiation in PyMT-induced breast tumor.
Title: SND1, a novel co-activator of HIF1α, promotes tumor initiation in PyMT-induced breast tumor.
Vascular injury activates the ELK1/SND1/SRF pathway to promote vascular smooth muscle cell proliferative phenotype and neointimal hyperplasia.
Title: Vascular injury activates the ELK1/SND1/SRF pathway to promote vascular smooth muscle cell proliferative phenotype and neointimal hyperplasia.
SND1 binds to ERG and promotes tumor growth in genetic mouse models of prostate cancer.
Title: SND1 binds to ERG and promotes tumor growth in genetic mouse models of prostate cancer.
Loss of the methylarginine reader function of SND1 confers resistance to hepatocellular carcinoma.
Title: Loss of the methylarginine reader function of SND1 confers resistance to hepatocellular carcinoma.
FXR1 impedes the development of osteoarthritis by targeting SND1.
Title: FXR1 impedes the development of osteoarthritis by targeting SND1.
SND1 aggravates mitochondrial damage, apoptosis and extracellular matrix degradation in IL-1beta-stimulated chondrocytes via PINK1/BECN1 pathway.
Title: SND1 aggravates mitochondrial damage, apoptosis and extracellular matrix degradation in IL-1β-stimulated chondrocytes via PINK1/BECN1 pathway.
Small-molecule inhibitors that disrupt the MTDH-SND1 complex suppress breast cancer progression and metastasis.
Title: Small-molecule inhibitors that disrupt the MTDH-SND1 complex suppress breast cancer progression and metastasis.
Translation of Tudor-SN, a novel terminal oligo-pyrimidine (TOP) mRNA, is regulated by the mTORC1 pathway in cardiomyocytes.
Title: Translation of Tudor-SN, a novel terminal oligo-pyrimidine (TOP) mRNA, is regulated by the mTORC1 pathway in cardiomyocytes.
The current findings reveal SND1 as a new regulatory factor in DNA damage response.
Title: Protective effects of SND1 in retinal photoreceptor cell damage induced by ionizing radiation.
The loss-of-function of Tudor-SN attenuated the enrichment of SMARCA5, GCN5 and acetylation of histone H3 (acH3) at DNA break sites and abolished chromatin relaxation; as a result, the cells exhibited DNA repair and cell survival deficiency.
Title: Oncoprotein Tudor-SN is a key determinant providing survival advantage under DNA damaging stress.

Submit: New GeneRIF Correction See all GeneRIFs (16)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (3) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH124221 (e-PCR)
- UniSTS:161043

GDB:4585141 (e-PCR)
- UniSTS:4885

01.MMHAP18FRA7.seq (e-PCR)
- UniSTS:122646

31.MMHAP80FRC10.seq (e-PCR)
- UniSTS:123959

Snd1 (e-PCR), detects polymorphism
- UniSTS:479069

D6Mit160 (e-PCR), detects polymorphism
- UniSTS:116594

MHAa75g2.seq (e-PCR)
- UniSTS:125315

Lrrc4 (e-PCR), detects polymorphism
- UniSTS:525557

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables RISC complex binding	IEA Inferred from Electronic Annotation more info
enables RISC complex binding	ISO Inferred from Sequence Orthology more info
enables RNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables RNA binding	IEA Inferred from Electronic Annotation more info
enables RNA binding	ISO Inferred from Sequence Orthology more info
enables RNA endonuclease activity	IEA Inferred from Electronic Annotation more info
enables RNA endonuclease activity	ISO Inferred from Sequence Orthology more info
enables endonuclease activity	ISO Inferred from Sequence Orthology more info
enables endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters	IEA Inferred from Electronic Annotation more info
enables nuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in mRNA catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in miRNA catabolic process	IEA Inferred from Electronic Annotation more info
involved_in miRNA catabolic process	ISO Inferred from Sequence Orthology more info
involved_in regulation of cell cycle process	IEA Inferred from Electronic Annotation more info
involved_in regulation of cell cycle process	ISO Inferred from Sequence Orthology more info
involved_in regulatory ncRNA-mediated gene silencing	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of RNAi effector complex	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in dense body	IDA Inferred from Direct Assay more info	PubMed
located_in melanosome	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: staphylococcal nuclease domain-containing protein 1

Names: 100 kDa coactivator; p100 co-activator

NP_062750.2

EC 3.1.31.1

XP_006505205.1

EC 3.1.31.1

XP_030111373.1

EC 3.1.31.1

XP_030111374.1

EC 3.1.31.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_019776.2 → NP_062750.2 staphylococcal nuclease domain-containing protein 1

See identical proteins and their annotated locations for NP_062750.2

Status: VALIDATED

Source sequence(s)

AB021491, AC072048, AK034914, BB613775, BM944959

Consensus CDS

CCDS19953.1

UniProtKB/Swiss-Prot

Q3TT46, Q78PY7, Q922L5, Q9R0S1

UniProtKB/TrEMBL

Q3TW51, Q3UZI3

Related

ENSMUSP00000001460.7, ENSMUST00000001460.14

Conserved Domains (5) summary

smart00333
Location:728 → 784

TUDOR; Tudor domain

smart00318
Location:21 → 166

SNc; Staphylococcal nuclease homologues

cd00175
Location:26 → 166

SNc; Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.

pfam00567
Location:677 → 799

TUDOR; Tudor domain

cl00140
Location:844 → 895

SNc; Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000072.7 Reference GRCm39 C57BL/6J

Range

28480332..28935161

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006505142.4 → XP_006505205.1 staphylococcal nuclease domain-containing protein 1 isoform X1

See identical proteins and their annotated locations for XP_006505205.1

UniProtKB/TrEMBL

Q3TJ56

Related

ENSMUSP00000128737.2, ENSMUST00000167201.2

Conserved Domains (3) summary

smart00318
Location:21 → 166

SNc; Staphylococcal nuclease homologues

cd00175
Location:350 → 496

SNc; Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.

cl29560
Location:525 → 593

SNc; Staphylococcal nuclease homologues
XM_030255513.1 → XP_030111373.1 staphylococcal nuclease domain-containing protein 1 isoform X2

Conserved Domains (3) summary

smart00318
Location:127 → 262

SNc; Staphylococcal nuclease homologues

pfam00567
Location:286 → 401

TUDOR; Tudor domain

cl00140
Location:1 → 98

SNc; Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.
XM_030255514.1 → XP_030111374.1 staphylococcal nuclease domain-containing protein 1 isoform X3

Conserved Domains (3) summary

smart00318
Location:98 → 233

SNc; Staphylococcal nuclease homologues

pfam00567
Location:257 → 372

TUDOR; Tudor domain

cl00140
Location:19 → 69

SNc; Staphylococcal nuclease homologues. SNase homologues are found in bacteria, archaea, and eukaryotes. They contain no disufide bonds.