Q3UMU9 · HDGR2_MOUSE
- ProteinHepatoma-derived growth factor-related protein 2
- GeneHdgfl2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids669 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as an epigenetic regulator of myogenesis in cooperation with DPF3a (isoform 2 of DPF3/BAF45C) (PubMed:32459350).
Associates with the BAF complex via its interaction with DPF3a and HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters (PubMed:32459350).
Promotes the repair of DNA double-strand breaks (DSBs) through the homologous recombination pathway by facilitating the recruitment of the DNA endonuclease RBBP8 to the DSBs (By similarity).
Preferentially binds to chromatin regions marked by H3K9me3, H3K27me3 and H3K36me2 (By similarity).
Involved in cellular growth control, through the regulation of cyclin D1 expression (By similarity).
Associates with chromatin (PubMed:22212508).
Associates with the BAF complex via its interaction with DPF3a and HDGFL2-DPF3a activate myogenic genes by increasing chromatin accessibility through recruitment of SMARCA4/BRG1/BAF190A (ATPase subunit of the BAF complex) to myogenic gene promoters (PubMed:32459350).
Promotes the repair of DNA double-strand breaks (DSBs) through the homologous recombination pathway by facilitating the recruitment of the DNA endonuclease RBBP8 to the DSBs (By similarity).
Preferentially binds to chromatin regions marked by H3K9me3, H3K27me3 and H3K36me2 (By similarity).
Involved in cellular growth control, through the regulation of cyclin D1 expression (By similarity).
Associates with chromatin (PubMed:22212508).
Isoform 1
Binds to condensed chromatin in mitotic cells.
Isoform 3
Binds to condensed chromatin in mitotic cells.
Isoform 4
Binds to non-condensed chromatin in the presence of HDGF.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | H3K27me3 modified histone binding | |
Molecular Function | H3K9me3 modified histone binding | |
Molecular Function | histone reader activity | |
Molecular Function | methylated histone binding | |
Biological Process | DNA recombination | |
Biological Process | DNA repair | |
Biological Process | DNA repair-dependent chromatin remodeling | |
Biological Process | muscle cell differentiation | |
Biological Process | muscle organ development | |
Biological Process | positive regulation of cell growth | |
Biological Process | positive regulation of double-strand break repair via homologous recombination | |
Biological Process | skeletal muscle tissue regeneration |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameHepatoma-derived growth factor-related protein 2
- Short namesHRP-2
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 accessionQ3UMU9
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Mice show severely impaired post-injury muscle regeneration.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 523-524 | Loss of interaction with SMARCA4. | |||
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000317644 | 1-669 | Hepatoma-derived growth factor-related protein 2 | ||
Modified residue | 114 | Phosphoserine | |||
Modified residue | 137 | Phosphoserine | |||
Modified residue | 165 | Phosphoserine | |||
Modified residue | 229 | Phosphoserine | |||
Modified residue | 231 | Phosphoserine | |||
Modified residue | 233 | Phosphoserine | |||
Modified residue | 239 | Phosphoserine | |||
Modified residue | 268 | Phosphoserine | |||
Modified residue | 307 | Phosphoserine | |||
Modified residue | 366 | Phosphoserine | |||
Modified residue | 367 | Phosphoserine | |||
Modified residue | 391 | Phosphoserine | |||
Modified residue | 392 | Phosphoserine | |||
Modified residue | 393 | Phosphoserine | |||
Modified residue | 395 | Phosphoserine | |||
Modified residue | 450 | Phosphoserine | |||
Modified residue | 454 | Phosphoserine | |||
Cross-link | 550 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | |||
Modified residue | 567 | In isoform Q3UMU9-4; Phosphoserine | |||
Modified residue | 619 | In isoform Q3UMU9-2; Phosphoserine | |||
Modified residue | 620 | Phosphoserine | |||
Modified residue | 628 | Phosphoserine | |||
Modified residue | 629 | Phosphoserine | |||
Modified residue | 635 | Phosphoserine | |||
Modified residue | 640 | Phosphoserine | |||
Modified residue | 659 | Phosphoserine | |||
Modified residue | 661 | Phosphoserine | |||
Modified residue | 669 | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with trimethylated 'Lys-36' of histone H3 (H3K36me3). Interacts with trimethylated 'Lys-79' of histone H3 (H3K79me3), but has higher affinity for H3K36me3 (By similarity).
Interacts with IWS1 (By similarity).
Interacts with H2AX, POGZ, RBBP8 and CBX1 (By similarity).
Interacts with histones H3K9me3, H3K27me3 and H3K36me2 (By similarity).
Interacts with DPF3a (isoform 2 of DPF3/BAF45C) (PubMed:32459350).
Interacts with SMARCA4/BRG1/BAF190A, in a DPF3a-dependent manner (PubMed:32459350).
Interacts with SMARCC1/BAF155 and SMARCD1/BAF60A in a DPF3a-dependent manner (By similarity).
Interacts with IWS1 (By similarity).
Interacts with H2AX, POGZ, RBBP8 and CBX1 (By similarity).
Interacts with histones H3K9me3, H3K27me3 and H3K36me2 (By similarity).
Interacts with DPF3a (isoform 2 of DPF3/BAF45C) (PubMed:32459350).
Interacts with SMARCA4/BRG1/BAF190A, in a DPF3a-dependent manner (PubMed:32459350).
Interacts with SMARCC1/BAF155 and SMARCD1/BAF60A in a DPF3a-dependent manner (By similarity).
Isoform 1
Interacts with HDGF.
Isoform 3
Interacts with HDGF.
Isoform 4
Selectively interacts with HDGF (N-terminally processed form).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | Q3UMU9 | Hdgf P51859 | 4 | EBI-7627961, EBI-2943087 | |
BINARY | Q3UMU9-1 | Hdgf P51859 | 4 | EBI-7627862, EBI-2943087 | |
BINARY | Q3UMU9-3 | Hdgf P51859 | 4 | EBI-7627932, EBI-2943087 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-64 | PWWP | |||
Region | 87-469 | Disordered | |||
Compositional bias | 111-125 | Basic and acidic residues | |||
Compositional bias | 140-158 | Basic and acidic residues | |||
Compositional bias | 190-213 | Basic and acidic residues | |||
Compositional bias | 225-243 | Basic and acidic residues | |||
Compositional bias | 249-271 | Polar residues | |||
Compositional bias | 272-299 | Basic and acidic residues | |||
Compositional bias | 309-381 | Basic and acidic residues | |||
Compositional bias | 397-411 | Basic and acidic residues | |||
Compositional bias | 421-469 | Basic and acidic residues | |||
Region | 466-548 | Interaction with DPF3/BAF45C isoform 2 | |||
Coiled coil | 550-575 | ||||
Compositional bias | 558-590 | Basic and acidic residues | |||
Region | 558-669 | Disordered | |||
Compositional bias | 605-663 | Basic and acidic residues | |||
Sequence similarities
Belongs to the HDGF family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q3UMU9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsIsoform a
- Length669
- Mass (Da)74,291
- Last updated2006-10-17 v1
- MD5 Checksum8B6FB72F6F83896CCA3C15B5BF5D5ED7
Q3UMU9-2
- Name2
Q3UMU9-3
- Name3
- SynonymsIsoform b
- Differences from canonical
- 224-225: KK → KKHPTGYACPQ
Q3UMU9-4
- Name4
- SynonymsIsoform c
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Alternative sequence | VSP_047648 | 66-118 | in isoform 4 | ||
Compositional bias | 111-125 | Basic and acidic residues | |||
Compositional bias | 140-158 | Basic and acidic residues | |||
Compositional bias | 190-213 | Basic and acidic residues | |||
Alternative sequence | VSP_031117 | 224-225 | in isoform 3 | ||
Compositional bias | 225-243 | Basic and acidic residues | |||
Alternative sequence | VSP_031118 | 226 | in isoform 2 | ||
Compositional bias | 249-271 | Polar residues | |||
Compositional bias | 272-299 | Basic and acidic residues | |||
Compositional bias | 309-381 | Basic and acidic residues | |||
Compositional bias | 397-411 | Basic and acidic residues | |||
Compositional bias | 421-469 | Basic and acidic residues | |||
Compositional bias | 558-590 | Basic and acidic residues | |||
Compositional bias | 605-663 | Basic and acidic residues | |||
Alternative sequence | VSP_031119 | 635 | in isoform 2 and isoform 4 | ||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D63850 EMBL· GenBank· DDBJ | BAA22896.1 EMBL· GenBank· DDBJ | mRNA | ||
FN687734 EMBL· GenBank· DDBJ | CBK52221.2 EMBL· GenBank· DDBJ | mRNA | ||
AK143616 EMBL· GenBank· DDBJ | BAE25467.1 EMBL· GenBank· DDBJ | mRNA | ||
AK144669 EMBL· GenBank· DDBJ | BAE25999.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146813 EMBL· GenBank· DDBJ | BAE27453.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146918 EMBL· GenBank· DDBJ | BAE27530.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003741 EMBL· GenBank· DDBJ | AAH03741.1 EMBL· GenBank· DDBJ | mRNA |