Zscan10 zinc finger and SCAN domain containing 10 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Zscan10provided by MGI
Official Full Name: zinc finger and SCAN domain containing 10provided by MGI
Primary source: MGI:MGI:3040700
See related: Ensembl:ENSMUSG00000023902 AllianceGenome:MGI:3040700
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: Zfp206; Znf206; Zkscan10
Summary: Enables DNA-binding transcription factor activity and sequence-specific DNA binding activity. Involved in negative regulation of transcription, DNA-templated. Located in nucleus. Is expressed in several structures, including early conceptus; genitourinary system; gut; limb mesenchyme; and nervous system. Orthologous to human ZSCAN10 (zinc finger and SCAN domain containing 10). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in testis adult (RPKM 1.9), cerebellum adult (RPKM 0.3) and 4 other tissues See more
Orthologs: human all
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Genomic context

Location:: 17 A3.3; 17 11.79 cM

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	17	NC_000083.7 (23819800..23829993)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	17	NC_000083.6 (23600826..23611019)

Chromosome 17 - NC_000083.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

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?

Zscan10 negatively regulates osteoclast differentiation through transcription of Hp.
Title: Zscan10 suppresses osteoclast differentiation by regulating expression of Haptoglobin.
The pluripotency factor ZSCAN10 is poorly expressed in A-iPSCs and addition of ZSCAN10 to the four Yamanaka factors (OCT4, SOX2, KLF4 and c-MYC) during A-iPSC reprogramming normalizes ROS-glutathione homeostasis and the DNA damage response, and recovers genomic stability.
Title: ZSCAN10 expression corrects the genomic instability of iPSCs from aged donors.
Our results clearly indicate that Zscan10 is dispensable for the ability of self-renewal and differentiation in ES cells.
Title: Zscan10 is dispensable for maintenance of pluripotency in mouse embryonic stem cells.
a role for Zscan10 in either maintaining progenitor cell subpopulation or impacting on fate choice decisions thereof
Title: Pleiotropic functions for transcription factor zscan10.
Optimized crystals diffracted to 1.85 A resolution and belonged to space group I422, with unit-cell parameters a = 67.57, c = 87.54 A. A Matthews analysis indicated the presence of one Zfp206SCAN molecule per asymmetric unit
Title: Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206.
Zfp206 is a key component of the transcriptional regulatory network and together with Oct4 and Sox2 regulates differentiation of embryonic stem cells.
Title: Zfp206, Oct4, and Sox2 are integrated components of a transcriptional regulatory network in embryonic stem cells.
Zfp206 is an embryonic transcription factor that plays a role in regulating pluripotency of embryonic stem cells.
Title: Zfp206 is a transcription factor that controls pluripotency of embryonic stem cells.
Zfp206 is a regulator of embryonic stem cell differentiation that controls a set of genes expressed very early in development, most of which themselves appear to be regulators.
Title: Zfp206 regulates ES cell gene expression and differentiation.

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Variation

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Alleles

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

Endonuclease-mediated (1)
Gene trapped (2) 1 citation
Targeted (2)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables DNA-binding transcription factor activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables DNA-binding transcription factor activity	TAS Traceable Author Statement more info	PubMed
enables DNA-binding transcription factor activity, RNA polymerase II-specific	IBA Inferred from Biological aspect of Ancestor more info
enables RNA polymerase II cis-regulatory region sequence-specific DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables sequence-specific DNA binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in negative regulation of DNA-templated transcription	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of transcription by RNA polymerase II	IBA Inferred from Biological aspect of Ancestor more info
involved_in stem cell differentiation	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
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: zinc finger and SCAN domain-containing protein 10

Names: zinc finger and SCAN domains 10; zinc finger protein 206; zinc finger with KRAB and SCAN domains 10

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_001033425.4 → NP_001028597.2 zinc finger and SCAN domain-containing protein 10 isoform 1

See identical proteins and their annotated locations for NP_001028597.2

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (1).

Source sequence(s)

AC154766, AK141259, BM933809, BX526901, CF896527

Consensus CDS

CCDS28451.1

UniProtKB/Swiss-Prot

B7ZP53, Q20D61, Q20D62, Q20D63, Q3URR7

Related

ENSMUSP00000093255.3, ENSMUST00000095595.9

Conserved Domains (6) summary

cd07936
Location:39 → 123

SCAN; SCAN oligomerization domain

COG5048
Location:366 → 767

COG5048; FOG: Zn-finger [General function prediction only]

sd00017
Location:639 → 659

ZF_C2H2; C2H2 Zn finger [structural motif]

pfam00096
Location:754 → 776

zf-C2H2; Zinc finger, C2H2 type

pfam13465
Location:679 → 704

zf-H2C2_2; Zinc-finger double domain

cl00195
Location:592 → 643

SIR2; SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, ...
NM_001289481.1 → NP_001276410.1 zinc finger and SCAN domain-containing protein 10 isoform 2

See identical proteins and their annotated locations for NP_001276410.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses alternate in-frame splice sites in the 3' coding region, compared to variant 1. This results in an isoform (2) that is shorter, compared to isoform 1.

Source sequence(s)

AC154766, AK141259, BM933809, BX526901, CD539380, CF896527

Consensus CDS

CCDS70766.1

UniProtKB/Swiss-Prot

Q3URR7

Related

ENSMUSP00000113386.2, ENSMUST00000120967.8

Conserved Domains (6) summary

cd07936
Location:39 → 123

SCAN; SCAN oligomerization domain

COG5048
Location:318 → 735

COG5048; FOG: Zn-finger [General function prediction only]

sd00017
Location:607 → 627

ZF_C2H2; C2H2 Zn finger [structural motif]

pfam00096
Location:722 → 744

zf-C2H2; Zinc finger, C2H2 type

pfam13465
Location:647 → 672

zf-H2C2_2; Zinc-finger double domain

cl00195
Location:560 → 611

SIR2; SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, ...
NM_001289482.1 → NP_001276411.1 zinc finger and SCAN domain-containing protein 10 isoform 3

Status: VALIDATED

Description

Transcript Variant: This variant (3) lacks two alternate in-frame exons in the coding region, compared to variant 1. This results in an isoform (3) that is shorter, compared to isoform 1.

Source sequence(s)

AC154766, AK141259, BM933809, BX526901, CF896527

Consensus CDS

CCDS79510.1

UniProtKB/Swiss-Prot

Q3URR7

Related

ENSMUSP00000111171.2, ENSMUST00000115509.8

Conserved Domains (7) summary

smart00431
Location:39 → 147

SCAN; leucine rich region

cd07936
Location:39 → 123

SCAN; SCAN oligomerization domain

COG5048
Location:256 → 657

COG5048; FOG: Zn-finger [General function prediction only]

sd00017
Location:529 → 549

ZF_C2H2; C2H2 Zn finger [structural motif]

pfam00096
Location:644 → 666

zf-C2H2; Zinc finger, C2H2 type

pfam13465
Location:569 → 594

zf-H2C2_2; Zinc-finger double domain

cl00195
Location:482 → 533

SIR2; SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, ...
NM_001289483.1 → NP_001276412.1 zinc finger and SCAN domain-containing protein 10 isoform 4

Status: VALIDATED

Description

Transcript Variant: This variant (4) uses alternate in-frame splice sites in the 5' and 3' coding region and initiates translation at a downstream start codon, compared to variant 1. This results in an isoform (4) that is shorter, compared to isoform 1.

Source sequence(s)

AC154766, AK141259, BM933809, BX526901, CD539380, CF896527

UniProtKB/Swiss-Prot

Q3URR7

Related

ENSMUSP00000118987.2, ENSMUST00000129227.8

Conserved Domains (5) summary

COG5048
Location:114 → 531

COG5048; FOG: Zn-finger [General function prediction only]

sd00017
Location:403 → 423

ZF_C2H2; C2H2 Zn finger [structural motif]

pfam00096
Location:518 → 540

zf-C2H2; Zinc finger, C2H2 type

pfam13465
Location:443 → 468

zf-H2C2_2; Zinc-finger double domain

cl00195
Location:356 → 407

SIR2; SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, ...
NM_001289484.1 → NP_001276413.1 zinc finger and SCAN domain-containing protein 10 isoform 5

Status: VALIDATED

Description

Transcript Variant: This variant (5) uses alternate in-frame splice sites in the 5' and 3' coding region, compared to variant 1. This results in an isoform (5) that is shorter, compared to isoform 1.

Source sequence(s)

AC154766, AK141259, BM933809, BX526901, CD539380, CF896527

UniProtKB/Swiss-Prot

Q3URR7

Related

ENSMUSP00000120876.2, ENSMUST00000148062.8

Conserved Domains (6) summary

cd07936
Location:39 → 127

SCAN; SCAN oligomerization domain

COG5048
Location:273 → 690

COG5048; FOG: Zn-finger [General function prediction only]

sd00017
Location:562 → 582

ZF_C2H2; C2H2 Zn finger [structural motif]

pfam00096
Location:677 → 699

zf-C2H2; Zinc finger, C2H2 type

pfam13465
Location:602 → 627

zf-H2C2_2; Zinc-finger double domain

cl00195
Location:515 → 566

SIR2; SIR2 superfamily of proteins includes silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation, where the acetyl group from the lysine epsilon-amino group is transferred to the ADP-ribose moiety of NAD+, ...