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Pias1 protein inhibitor of activated STAT, 1 [ Rattus norvegicus (Norway rat) ]

Gene ID: 300772, updated on 27-Nov-2024

Summary

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Official Symbol
Pias1provided by RGD
Official Full Name
protein inhibitor of activated STAT, 1provided by RGD
Primary source
RGD:1307843
See related
EnsemblRapid:ENSRNOG00000034272 AllianceGenome:RGD:1307843
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Rattus norvegicus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary
Enables SUMO transferase activity and protein domain specific binding activity. Involved in several processes, including G1/S transition of mitotic cell cycle; positive regulation of macromolecule metabolic process; and visual learning. Predicted to be located in PML body; chromatin; and nuclear periphery. Predicted to be active in glutamatergic synapse; postsynaptic cytosol; and presynaptic cytosol. Biomarker of focal segmental glomerulosclerosis. Orthologous to human PIAS1 (protein inhibitor of activated STAT 1). [provided by Alliance of Genome Resources, Nov 2024]
Expression
Biased expression in Testes (RPKM 162.4), Thymus (RPKM 154.5) and 9 other tissues See more
Orthologs
human mouse all
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Genomic context

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See Pias1 in Genome Data Viewer
Location:
8q24
Exon count:
18
Annotation release Status Assembly Chr Location
RS_2024_02 current GRCr8 (GCF_036323735.1) 8 NC_086026.1 (72233566..72347085, complement)
RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 8 NC_051343.1 (63338150..63451670, complement)
106 previous assembly Rnor_6.0 (GCF_000001895.5) 8 NC_005107.4 (67771720..67869015, complement)

Chromosome 8 - NC_086026.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC102546547 Neighboring gene CLN6, transmembrane ER protein Neighboring gene calmodulin-like 4 Neighboring gene uncharacterized LOC134480067 Neighboring gene U6 spliceosomal RNA Neighboring gene mitochondrial pyruvate carrier 1-like

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
  • Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
  • BioProject: PRJNA238328
  • Publication: PMID 24510058
  • Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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Related articles in PubMed

  1. NMDA receptor signaling mediates the expression of protein inhibitor of activated STAT1 (PIAS1) in rat hippocampus. Liu SY, et al. Neuropharmacology, 2013 Feb. PMID 22982248
  2. CREB SUMOylation by the E3 ligase PIAS1 enhances spatial memory. Chen YC, et al. J Neurosci, 2014 Jul 16. PMID 25031400, Free PMC Article
  3. Forkhead box protein A2 (FOXA2) protein stability and activity are regulated by sumoylation. Belaguli NS, et al. PLoS One, 2012. PMID 23118920, Free PMC Article
  4. Expression of the E3 SUMO-1 ligases PIASx and PIAS1 during spermatogenesis in the rat. Yan W, et al. Gene Expr Patterns, 2003 Jun. PMID 12799075
  5. PIAS1 activates the expression of smooth muscle cell differentiation marker genes by interacting with serum response factor and class I basic helix-loop-helix proteins. Kawai-Kowase K, et al. Mol Cell Biol, 2005 Sep. PMID 16135793, Free PMC Article

See all (37) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. This study provide the first evidence that CREB could be SUMO-modified by the E3 ligase PIAS1 and that CREB SUMOylation plays an important role in spatial memory formation
    Title: CREB SUMOylation by the E3 ligase PIAS1 enhances spatial memory.
  2. PIAS1 may function as an immediate early gene in an activity-dependent manner: its expression is rapidly induced upon NMDA receptor activation in rat hippocampus.
    Title: NMDA receptor signaling mediates the expression of protein inhibitor of activated STAT1 (PIAS1) in rat hippocampus.
  3. SUMO E3 ligases are expressed in the retina and regulate SUMOylation of the metabotropic glutamate receptor 8b.
    Title: SUMO E3 ligases are expressed in the retina and regulate SUMOylation of the metabotropic glutamate receptor 8b.
  4. PIAS1 could augment anti-inflammatory activity by inhibiting STAT1, thus attenuating the severity of SAP associated with acute lung injury
    Title: Upregulation of PIAS1 protects against sodium taurocholate-induced severe acute pancreatitis associated with acute lung injury.
  5. The results indicated that in the cerulein-stimulated PIASI silencing cells, the activity of p38 MAP kinase was enhanced, while the levels of inflammatory mediators were markedly higher than those of other cerulein-stimulated cells.
    Title: SiRNA-mediated PIAS1 silencing promotes inflammatory response and leads to injury of cerulein-stimulated pancreatic acinar cells via regulation of the P38MAPK signaling pathway.
  6. Immunohistochemistry showed that Ubc9 and PIAS1 are markedly expressed in rat adrenal glomerulosa cells
    Title: Ubc9 and Protein Inhibitor of Activated STAT 1 Activate Chicken Ovalbumin Upstream Promoter-Transcription Factor I-mediated Human CYP11B2 Gene Transcription.
  7. Pias1 binds to and sumoylates metabotropic glutamate receptor 8
    Title: Pias1 interaction and sumoylation of metabotropic glutamate receptor 8.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

Gene Ontology Provided by RGD

Function Evidence Code Pubs
enables DNA-binding transcription factor binding ISO
Inferred from Sequence Orthology
more info
  
enables SUMO ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables SUMO ligase activity ISO
Inferred from Sequence Orthology
more info
  
enables SUMO transferase activity EXP
Inferred from Experiment
more info
 PubMed 
enables SUMO transferase activity ISO
Inferred from Sequence Orthology
more info
  
enables enzyme binding ISO
Inferred from Sequence Orthology
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein domain specific binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein domain specific binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables transcription cis-regulatory region binding ISO
Inferred from Sequence Orthology
more info
  
enables transcription coregulator activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ubiquitin protein ligase binding ISO
Inferred from Sequence Orthology
more info
  
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in DNA damage response ISO
Inferred from Sequence Orthology
more info
  
involved_in G1/S transition of mitotic cell cycle IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in fat cell differentiation ISO
Inferred from Sequence Orthology
more info
  
involved_in negative regulation of apoptotic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in negative regulation of transcription by RNA polymerase II ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of DNA-templated transcription IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in positive regulation of proteasomal ubiquitin-dependent protein catabolic process ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of protein localization to cell periphery ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of protein sumoylation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in positive regulation of protein sumoylation ISO
Inferred from Sequence Orthology
more info
  
involved_in positive regulation of smooth muscle cell differentiation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein sumoylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein sumoylation IEA
Inferred from Electronic Annotation
more info
  
involved_in protein sumoylation ISO
Inferred from Sequence Orthology
more info
  
involved_in protein-DNA complex assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in regulation of cell population proliferation ISO
Inferred from Sequence Orthology
more info
  
involved_in regulation of transcription by RNA polymerase II IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in spermatogenesis IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in visual learning IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in PML body ISO
Inferred from Sequence Orthology
more info
  
located_in chromatin IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in glutamatergic synapse ISO
Inferred from Sequence Orthology
more info
  
located_in nuclear periphery ISO
Inferred from Sequence Orthology
more info
  
located_in nucleoplasm TAS
Traceable Author Statement
more info
  
located_in nucleus ISO
Inferred from Sequence Orthology
more info
  
is_active_in postsynaptic cytosol ISO
Inferred from Sequence Orthology
more info
  
is_active_in presynaptic cytosol ISO
Inferred from Sequence Orthology
more info
  

General protein information

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Preferred Names
E3 SUMO-protein ligase PIAS1
NP_001100299.3
XP_038937035.1
XP_038937037.1
XP_038937038.1
XP_038937039.1
XP_063121223.1
XP_063121224.1
XP_063121225.1

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)

  1. NM_001106829.3 → NP_001100299.3  E3 SUMO-protein ligase PIAS1

    Status: VALIDATED

    Source sequence(s)
    JAXUCZ010000008
    UniProtKB/TrEMBL
    A0A8I6AIY4, A6J591, A9UK05
    Related
    ENSRNOP00000093422.1, ENSRNOT00000100439.2
    Conserved Domains (4) summary
    smart00513
    Location:11 → 45
    SAP; Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation
    COG5222
    Location:313 → 428
    COG5222; Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
    cd16790
    Location:332 → 379
    SP-RING_PIAS; SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins
    pfam14324
    Location:137 → 285
    PINIT; PINIT domain

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

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

Reference GRCr8

Genomic

  1. NC_086026.1 Reference GRCr8

    Range
    72233566..72347085 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_039081109.2 → XP_038937037.1  E3 SUMO-protein ligase PIAS1 isoform X1

    UniProtKB/TrEMBL
    A9UK05
    Conserved Domains (4) summary
    smart00513
    Location:2 → 36
    SAP; Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation
    COG5222
    Location:304 → 419
    COG5222; Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
    cd16790
    Location:323 → 370
    SP-RING_PIAS; SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins
    pfam14324
    Location:128 → 276
    PINIT; PINIT domain

  2. XM_039081110.2 → XP_038937038.1  E3 SUMO-protein ligase PIAS1 isoform X2

    UniProtKB/TrEMBL
    A0A8I5Y680
    Related
    ENSRNOP00000077365.1, ENSRNOT00000097366.2
    Conserved Domains (4) summary
    smart00513
    Location:11 → 45
    SAP; Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation
    COG5222
    Location:313 → 428
    COG5222; Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
    cd16790
    Location:332 → 379
    SP-RING_PIAS; SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins
    pfam14324
    Location:137 → 285
    PINIT; PINIT domain

  3. XM_039081111.2 → XP_038937039.1  E3 SUMO-protein ligase PIAS1 isoform X1

    UniProtKB/TrEMBL
    A9UK05
    Conserved Domains (4) summary
    smart00513
    Location:2 → 36
    SAP; Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation
    COG5222
    Location:304 → 419
    COG5222; Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
    cd16790
    Location:323 → 370
    SP-RING_PIAS; SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins
    pfam14324
    Location:128 → 276
    PINIT; PINIT domain

  4. XM_063265155.1 → XP_063121225.1  E3 SUMO-protein ligase PIAS1 isoform X3

  5. XM_063265154.1 → XP_063121224.1  E3 SUMO-protein ligase PIAS1 isoform X3

  6. XM_063265153.1 → XP_063121223.1  E3 SUMO-protein ligase PIAS1 isoform X1

  7. XM_039081107.2 → XP_038937035.1  E3 SUMO-protein ligase PIAS1 isoform X1

    UniProtKB/TrEMBL
    A9UK05
    Conserved Domains (4) summary
    smart00513
    Location:2 → 36
    SAP; Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation
    COG5222
    Location:304 → 419
    COG5222; Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]
    cd16790
    Location:323 → 370
    SP-RING_PIAS; SP-RING finger found in protein inhibitor of activated signal transducer and activator of transcription (PIAS) proteins
    pfam14324
    Location:128 → 276
    PINIT; PINIT domain
Nucleotide Protein Strain
Heading Accession and Version

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