Q9QYE0 · PLAG1_MOUSE
- ProteinZinc finger protein PLAG1
- GenePlag1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids499 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Transcription factor whose activation results in up-regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation: when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Cooperates with CBFB-MYH11.
Miscellaneous
Mice overexpressing Plag1 develop normally with high Plag1 transgene expression in salivary glands, spleen and weak mammary gland detection. They develop salivary gland tumors with major pathological features of human pleimorphic adenomas at the age of 1-5 months.
Mice with Plag1 overexpression targeted to salivary and mammary gland develop multifocal salivary gland tumors with pathological features of human pleimorphic adenomas at the age of 5 weeks, as well as mammary gland tumors at the age of 1 year. Plag1 overexpression in salivary gland are accompanied by increased IGFII expression. Besides features characteristic of benign pleimorphic adenomas, malignant characteristics are also observed in salivary gland tumors as well as metastasis to the lungs, reinforcing the tumorigenic role of Plag1.
Neonate mice carrying a human myeloid leukemia translocation-associated fusion gene CBFB-MYH11, injected with a retrovirus (4070A), develop the pathology within 2-5 months due to few viral insertions in some genes, such as PLAG1. Insertions near the transcription start site of PLAG1 are predominant in the related tumors and probably participate in the transformation process. Plag1 is one candidate gene that can cooperate with CBFB-MYH11 for leukemogenesis in this mouse model.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytosol | |
Cellular Component | nuclear speck | |
Molecular Function | DNA-binding transcription activator activity, RNA polymerase II-specific | |
Molecular Function | DNA-binding transcription factor activity, RNA polymerase II-specific | |
Molecular Function | metal ion binding | |
Molecular Function | RNA polymerase II cis-regulatory region sequence-specific DNA binding | |
Biological Process | gland morphogenesis | |
Biological Process | multicellular organism growth | |
Biological Process | negative regulation of gene expression | |
Biological Process | organ growth | |
Biological Process | positive regulation of gene expression | |
Biological Process | positive regulation of glial cell proliferation | |
Biological Process | prostate gland growth | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameZinc finger protein PLAG1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9QYE0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Strong nucleolar localization when sumoylation is inhibited.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice exhibit growth retardation with lower birth weight and disproportionally small seminal vesicles and ventral prostate as well as decreased fertility in both male and female. However, IGFII expression is normal in embryos.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000295108 | 1-499 | Zinc finger protein PLAG1 | |||
Sequence: MATVIPGDLSEVRDTQKAPSGKRKRGESKPRKNFPCQLCDKAFNSVEKLKVHSFSHTGERPYKCTHQDCTKAFVSKYKLQRHMATHSPEKTHKCNYCEKMFHRKDHLKNHLHTHDPNKETFKCEECGKSYNTKLGFKRHLALHAATSGDLTCKVCLQNFESTGVLLEHLKSHAGKSSGGVKEKKHQCEHCERRFYTRKDVRRHMVVHTGRKDFLCQYCAQRFGRKDHLTRHMKKSHNQELLKVKTEPVDFLDPFTCNMSVPIKDELLPVMSLPSSELLSKPFTNTLQLNLYNTPFQSMQSSGSAHQMITTLPLGMTCPIDMDAVHPSHHLAFKCPFSSTSYAISIPEKEQPLKGEIESYLMELQGGAPSSSQDSPASSSKLGLEPQSGSPDDGAGDLSLSKSSISISDPLSTPALDFSQLFNFIPLNGPPYNPLSVGSLGMSYSQEEAHSSVSQLPTQTQDLQDPANTVGLSSLHSLSAAFTSSLSSSTTLPRFHQAFQ | ||||||
Cross-link | 244 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | ||||||
Cross-link | 263 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K |
Post-translational modification
Sumoylated with SUMO1; which inhibits transcriptional activity, but does not affect nuclear localization. Blockers of sumoylation pathway such as SENP3 and inactive UBE2I increases transcriptional capacity. Sumoylation is increased in the presence of PIAS1 (By similarity).
Acetylated by lysine acetyltransferase EP300; which activates transcriptional capacity. Lysine residues that are sumoylated also seem to be target for acetylation (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in heart, spleen, lung, kidney, brain, testis and epididymis but not in salivary glands.
Developmental stage
High fetal expression with a strong decline after birth. Expressed at 9.5 dpc and 10.5 dpc in nervous system with highest level in telencephalon, diencephalon, and midbrain, as well as regionalized expression in the neural tube, which is characteristic of genes involved in the specification of neuronal fates.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, motif, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-33 | Disordered | ||||
Sequence: MATVIPGDLSEVRDTQKAPSGKRKRGESKPRKN | ||||||
Region | 2-84 | Interaction with KPNA2 | ||||
Sequence: ATVIPGDLSEVRDTQKAPSGKRKRGESKPRKNFPCQLCDKAFNSVEKLKVHSFSHTGERPYKCTHQDCTKAFVSKYKLQRHMA | ||||||
Motif | 22-25 | Nuclear localization signal | ||||
Sequence: KRKR | ||||||
Zinc finger | 34-56 | C2H2-type 1 | ||||
Sequence: FPCQLCDKAFNSVEKLKVHSFSH | ||||||
Region | 41-242 | Decreased nuclear import with localization in the nucleus but also in the cytoplasm | ||||
Sequence: KAFNSVEKLKVHSFSHTGERPYKCTHQDCTKAFVSKYKLQRHMATHSPEKTHKCNYCEKMFHRKDHLKNHLHTHDPNKETFKCEECGKSYNTKLGFKRHLALHAATSGDLTCKVCLQNFESTGVLLEHLKSHAGKSSGGVKEKKHQCEHCERRFYTRKDVRRHMVVHTGRKDFLCQYCAQRFGRKDHLTRHMKKSHNQELLK | ||||||
Zinc finger | 62-86 | C2H2-type 2 | ||||
Sequence: YKCTHQDCTKAFVSKYKLQRHMATH | ||||||
Zinc finger | 92-114 | C2H2-type 3 | ||||
Sequence: HKCNYCEKMFHRKDHLKNHLHTH | ||||||
Zinc finger | 121-143 | C2H2-type 4 | ||||
Sequence: FKCEECGKSYNTKLGFKRHLALH | ||||||
Zinc finger | 150-172 | C2H2-type 5 | ||||
Sequence: LTCKVCLQNFESTGVLLEHLKSH | ||||||
Zinc finger | 185-207 | C2H2-type 6 | ||||
Sequence: HQCEHCERRFYTRKDVRRHMVVH | ||||||
Zinc finger | 213-236 | C2H2-type 7 | ||||
Sequence: FLCQYCAQRFGRKDHLTRHMKKSH | ||||||
Region | 243-383 | Repression domain; contains 3 sumoylation motifs and massively decrease transcription activity | ||||
Sequence: VKTEPVDFLDPFTCNMSVPIKDELLPVMSLPSSELLSKPFTNTLQLNLYNTPFQSMQSSGSAHQMITTLPLGMTCPIDMDAVHPSHHLAFKCPFSSTSYAISIPEKEQPLKGEIESYLMELQGGAPSSSQDSPASSSKLGL | ||||||
Region | 243-499 | Activates transcription; Inhibition of nuclear import due to lack of NLS and KPNA2 interaction | ||||
Sequence: VKTEPVDFLDPFTCNMSVPIKDELLPVMSLPSSELLSKPFTNTLQLNLYNTPFQSMQSSGSAHQMITTLPLGMTCPIDMDAVHPSHHLAFKCPFSSTSYAISIPEKEQPLKGEIESYLMELQGGAPSSSQDSPASSSKLGLEPQSGSPDDGAGDLSLSKSSISISDPLSTPALDFSQLFNFIPLNGPPYNPLSVGSLGMSYSQEEAHSSVSQLPTQTQDLQDPANTVGLSSLHSLSAAFTSSLSSSTTLPRFHQAFQ | ||||||
Compositional bias | 365-385 | Polar residues | ||||
Sequence: GGAPSSSQDSPASSSKLGLEP | ||||||
Region | 365-400 | Disordered | ||||
Sequence: GGAPSSSQDSPASSSKLGLEPQSGSPDDGAGDLSLS | ||||||
Region | 384-499 | Massively activates transcription | ||||
Sequence: EPQSGSPDDGAGDLSLSKSSISISDPLSTPALDFSQLFNFIPLNGPPYNPLSVGSLGMSYSQEEAHSSVSQLPTQTQDLQDPANTVGLSSLHSLSAAFTSSLSSSTTLPRFHQAFQ |
Domain
C2H2-type zinc fingers 3 interacts with DNA-binding site G-clusterinc fingers. C2H2-type zinc fingers 6 and 7 interact with DNA-binding site core sequence (By similarity).
Sequence similarities
Belongs to the krueppel C2H2-type zinc-finger protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length499
- Mass (Da)55,579
- Last updated2011-07-27 v2
- ChecksumA3493D2DADCB83B2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D6RES7 | D6RES7_MOUSE | Plag1 | 43 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 365-385 | Polar residues | ||||
Sequence: GGAPSSSQDSPASSSKLGLEP | ||||||
Sequence conflict | 433 | in Ref. 1; AAS86161 and 2; AAF21762 | ||||
Sequence: P → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY574219 EMBL· GenBank· DDBJ | AAS86161.1 EMBL· GenBank· DDBJ | mRNA | ||
AF057366 EMBL· GenBank· DDBJ | AAF21762.1 EMBL· GenBank· DDBJ | mRNA | ||
BC139283 EMBL· GenBank· DDBJ | AAI39284.1 EMBL· GenBank· DDBJ | mRNA | ||
BC139285 EMBL· GenBank· DDBJ | AAI39286.1 EMBL· GenBank· DDBJ | mRNA | ||
AL807387 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466538 EMBL· GenBank· DDBJ | EDL05712.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK135759 EMBL· GenBank· DDBJ | BAE22643.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |