Q6DIA7 · BRME1_MOUSE
- ProteinBreak repair meiotic recombinase recruitment factor 1
- GeneBrme1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids600 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Meiotic recombination factor component of recombination bridges involved in meiotic double-strand break repair (PubMed:32460033, PubMed:32463460).
Modulates the localization of recombinases DMC1:RAD51 to meiotic double-strand break (DSB) sites through the interaction with and stabilization of the BRCA2:HSF2BP complex during meiotic recombination (PubMed:32460033, PubMed:32463460).
Indispensable for the DSB repair, homologous synapsis, and crossover formation that are needed for progression past metaphase I, is essential for spermatogenesis and male fertility (PubMed:32460033, PubMed:32463460).
Modulates the localization of recombinases DMC1:RAD51 to meiotic double-strand break (DSB) sites through the interaction with and stabilization of the BRCA2:HSF2BP complex during meiotic recombination (PubMed:32460033, PubMed:32463460).
Indispensable for the DSB repair, homologous synapsis, and crossover formation that are needed for progression past metaphase I, is essential for spermatogenesis and male fertility (PubMed:32460033, PubMed:32463460).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | site of double-strand break | |
Molecular Function | damaged DNA binding | |
Biological Process | double-strand break repair involved in meiotic recombination | |
Biological Process | female meiosis I | |
Biological Process | male meiosis I | |
Biological Process | protein localization to site of double-strand break | |
Biological Process | reciprocal meiotic recombination | |
Biological Process | spermatogenesis |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameBreak repair meiotic recombinase recruitment factor 1
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6DIA7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: During meiosis, recruited to chromosomes and localizes on recombination sites in a double-strand break-dependent manner. First appears on the chromosome axis at leptotene. Along with the progression of meiotic recombination, released from the axis to form bridge-like structures linking homolog axes before they are synapsed. Finally, located between synapsed homolog axes and on the synaptonemal complex (SC).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Male mutants are infertile (PubMed:32345962, PubMed:32460033, PubMed:32463460).
They have smaller-than-normal testes with reduced diameters of seminiferous tubules and sperm density (PubMed:32345962, PubMed:32460033).
Female mutants exhibit normal fertility with no apparent defect in adult ovaries (PubMed:32345962, PubMed:32460033).
They show a strong reduction of the follicle pool
They have smaller-than-normal testes with reduced diameters of seminiferous tubules and sperm density (PubMed:32345962, PubMed:32460033).
Female mutants exhibit normal fertility with no apparent defect in adult ovaries (PubMed:32345962, PubMed:32460033).
They show a strong reduction of the follicle pool
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 38 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000295738 | 1-600 | Break repair meiotic recombinase recruitment factor 1 | |||
Sequence: MNKKKQRNSGVGLHPSKPSKNPRLRDSQSSMMVHSHYSRESEDSSEPAPSVELGGEEPLHEAFSCPVEDTGAASDLAGSPKELVPLPPSQNSVGKFVPQFAKPRKTVTRKAKAWEEDLEGCTTSQETRPELGALKAASQPQRESLRFPPHDIRPEVQTQPDGTLSKERTISLDNRSLGNNGFEMATVQDSSSPLSDAAAEGREADSRDPQERDAQGGEAGAQHSGEPQEGEDILYTSALAPASEPTWSVAQDLSVPTYTLSSTAAAPSSTSPADASLMDTVITEVSLDPSVLQQSAPQVAKLLGSLDEQIPDGGCIGTLLSSTPLAEETTAGREEARWEERCHGDTLASFTETEPEKQEPVTEAGDSGHIAQEMDPVVKTKDSGSDEQSPGDIGMLPLPAQSMNQMLVELRGLTCDQDLEGLSTPHTSSQLEHTCAASDPPQSTKDCHSSPGIPVHLAAPCPRDQAAWQESSAMELDFLPDSQIQDALDATNMEQGFPSGSMPDLGWPVPSSQSIGGSPKAVTKPQSRSHVETWAQETYRMQDATDTVRGLVVELSGLNRLIMSTHRDLEAFKRRKTKSLPYLTKGLGSLPRGDQSWRDL | ||||||
Modified residue | 79 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 191 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 192 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 195 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in testis.
Developmental stage
Expressed in fetal ovaries but not in adult ovaries.
Gene expression databases
Interaction
Subunit
Interacts with HSF2BP (via N-terminus) and BRCA2; the interaction with HSF2BP is direct and allows the formation of a ternary complex (PubMed:32345962, PubMed:32460033, PubMed:32463460, PubMed:32845237).
The complex BRME1:HSF2BP:BRCA2 interacts with SPATA22, MEIOB and RAD51 (PubMed:32345962).
The complex BRME1:HSF2BP:BRCA2 interacts with SPATA22, MEIOB and RAD51 (PubMed:32345962).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MNKKKQRNSGVGLHP | ||||||
Region | 1-98 | Disordered | ||||
Sequence: MNKKKQRNSGVGLHPSKPSKNPRLRDSQSSMMVHSHYSRESEDSSEPAPSVELGGEEPLHEAFSCPVEDTGAASDLAGSPKELVPLPPSQNSVGKFVP | ||||||
Region | 1-150 | Required for nuclear location | ||||
Sequence: MNKKKQRNSGVGLHPSKPSKNPRLRDSQSSMMVHSHYSRESEDSSEPAPSVELGGEEPLHEAFSCPVEDTGAASDLAGSPKELVPLPPSQNSVGKFVPQFAKPRKTVTRKAKAWEEDLEGCTTSQETRPELGALKAASQPQRESLRFPPH | ||||||
Region | 117-239 | Disordered | ||||
Sequence: DLEGCTTSQETRPELGALKAASQPQRESLRFPPHDIRPEVQTQPDGTLSKERTISLDNRSLGNNGFEMATVQDSSSPLSDAAAEGREADSRDPQERDAQGGEAGAQHSGEPQEGEDILYTSAL | ||||||
Compositional bias | 158-195 | Polar residues | ||||
Sequence: TQPDGTLSKERTISLDNRSLGNNGFEMATVQDSSSPLS | ||||||
Compositional bias | 200-214 | Basic and acidic residues | ||||
Sequence: EGREADSRDPQERDA | ||||||
Region | 315-394 | Disordered | ||||
Sequence: CIGTLLSSTPLAEETTAGREEARWEERCHGDTLASFTETEPEKQEPVTEAGDSGHIAQEMDPVVKTKDSGSDEQSPGDIG | ||||||
Compositional bias | 330-363 | Basic and acidic residues | ||||
Sequence: TAGREEARWEERCHGDTLASFTETEPEKQEPVTE | ||||||
Compositional bias | 432-449 | Polar residues | ||||
Sequence: EHTCAASDPPQSTKDCHS | ||||||
Region | 432-451 | Disordered | ||||
Sequence: EHTCAASDPPQSTKDCHSSP | ||||||
Region | 475-600 | Required for interaction with HSF2BP | ||||
Sequence: ELDFLPDSQIQDALDATNMEQGFPSGSMPDLGWPVPSSQSIGGSPKAVTKPQSRSHVETWAQETYRMQDATDTVRGLVVELSGLNRLIMSTHRDLEAFKRRKTKSLPYLTKGLGSLPRGDQSWRDL |
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q6DIA7-1
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
- Length600
- Mass (Da)64,440
- Last updated2020-12-02 v2
- ChecksumFAC1EB6464F0D402
Q6DIA7-2
- Name2
- Differences from canonical
- 89-123: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3YVH8 | D3YVH8_MOUSE | Brme1 | 106 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MNKKKQRNSGVGLHP | ||||||
Sequence conflict | 28 | in Ref. 5; AAH75658 | ||||
Sequence: Q → H | ||||||
Alternative sequence | VSP_027045 | 89-123 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 158-195 | Polar residues | ||||
Sequence: TQPDGTLSKERTISLDNRSLGNNGFEMATVQDSSSPLS | ||||||
Compositional bias | 200-214 | Basic and acidic residues | ||||
Sequence: EGREADSRDPQERDA | ||||||
Sequence conflict | 285 | in Ref. 5; AAH75658 | ||||
Sequence: V → A | ||||||
Compositional bias | 330-363 | Basic and acidic residues | ||||
Sequence: TAGREEARWEERCHGDTLASFTETEPEKQEPVTE | ||||||
Compositional bias | 432-449 | Polar residues | ||||
Sequence: EHTCAASDPPQSTKDCHS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LC507101 EMBL· GenBank· DDBJ | BBO60545.1 EMBL· GenBank· DDBJ | mRNA | ||
LC532163 EMBL· GenBank· DDBJ | BCB65306.1 EMBL· GenBank· DDBJ | mRNA | ||
AC159266 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK015293 EMBL· GenBank· DDBJ | BAB29783.1 EMBL· GenBank· DDBJ | mRNA | ||
BC075658 EMBL· GenBank· DDBJ | AAH75658.1 EMBL· GenBank· DDBJ | mRNA |