Firrm
entrez
381306
canonical
uniprot
Q3TQQ9
canonical
ensembl
ENSMUSG00000041406
resolver
ensp
ENSMUSP00000043143
resolver
ensp
ENSMUSP00000095101
resolver
ensp
ENSMUSP00000321025
resolver
genesymbol
Firrm
resolver
uniprot
Q3UR98
resolver
uniprot
Q5RKU3
resolver
uniprot
Q7TMQ3
resolver
uniprot_entry
FIRRM_MOUSE
resolver
uniprot_sec
Q3UR98
resolver
uniprot_sec
Q5RKU3
resolver
uniprot_sec
Q7TMQ3
resolver
amino_acid_sequence
MSQDDAEVASGVVLEELSSWSEEMCRRELPSVLPRLLSMYQCSESWIEHIRILKIIVEMFLPHMNHLTLEETLFSQVLPKSIKLFDGMICELTSEARELSSQNLEIQVTIRNILQAMVQVIGGFTGCVRHVCATQKSVFLGSIQSLPSFILHIIKSAFVHCKNSECVYSGRLHLVSDLLQVLFKEAYSLQKQLMGLLDTVCLDPSVDENNALIMVGVIHSLLDICSVISGMDQAFHANTWKFIIKQSLKHHSVIKSQLRHKEIISSLCEDILFSFHSCLQLAEQITQPAAQGNADYRLFQKTLKLCRFFANSLLHYTKECLPFLSDSCCTLHQLYLQIHSKFLSLCAAKTSKAQQEEIASTFLVLLDPLISQLLKSQPFVQAVLASKLALPCELQLPQVLLLVVAMDKLPSQPQDVQTLWSTEDMTRMSILKGIFYNFGQCSGELSLPTHLQGTKGKGQAEVPVTLYQHVCVHLCAFVASFHSSLFPRLDAALLNAVLSTNMSTSLLAMDVWCFLARYGTAKLGAHHVTLVAHLVKSCPGKCVQLTNLSILLKRLLFFMAAPHQVQFIQKFSPKEADNLHLWQYISLQAFDADLRKPVACELVRVCRAQCRKWLSSTRTLAELDSLNTALSVVLTVCNSAGEALDSRQLTAVTEVLGELWTFINVEQIISQPYVQQAFSLLLQLLAFFIQTVDLQLISQVVNVLTSVIKLEPPDHVSLAVLDFISSLGKLYISQTIRDKVLPSLSCILTSLIVNKNWLLEQHTLEAFTQFAEGTKHEEIVPQCLGSEEIKNKVVSFLEKTESVDEAEVATVDNVKQEKGTFWEPAAKVTVEEVKTSAFQPHTKRARRVLPFEEEYRSVFKAAARALETTEFLLKHSLAPAWLLPELEALQGRIEKLKRCVLTG
uniprot
proteins
function
FUNCTION: Forms a complex with FIGL1, which regulates DNA double-strand break (DSB) repair via homologous recombination (HR) (PubMed:37256941, PubMed:37439366). The FIGNL1-FIRRM complex is essential for resolution of homologous recombination intermediates in response to DNA interstrand cross-links (ICLs) (PubMed:37256941, PubMed:37439366). The complex regulates HR by promoting disassembly of RAD51 filaments from DNA and chromatin, thereby preventing DNA damage-independent RAD51 loading and persistent DNA accumulation of RAD51 recombinases (PubMed:37439366). It also regulates HR during meiosis by promoting dissociation of DMC1 filaments from DNA (PubMed:37439366, PubMed:39147779, PubMed:39797737). Within the complex, provides the ATPase activity to disassemble DMC1 and RAD51 filaments, while FIRRM directly binds single-stranded DNA to facilitate this unloading (By similarity). Independently of FIRRM, slso acts as a regulator of PLK1 kinase activity at kinetochores that promotes faithful chromosome segregation in prometaphase by bridging kinase and phosphatase activities (By similarity). Phosphorylation of FIRRM by PLK1 negatively regulates its interaction with the phosphatase, PPP1CC, thus creating a negative feedback loop for maintaining proper PLK1 kinase activity during mitosis (By similarity). {ECO:0000250|UniProtKB:Q9NSG2, ECO:0000269|PubMed:37256941, ECO:0000269|PubMed:37439366, ECO:0000269|PubMed:39147779, ECO:0000269|PubMed:39797737}.
uniprot
proteins
mass_dalton
101222
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-101 by PLK1 strengthens FIRRM-PLK1 interaction. Phosphorylation at Ser-795 by PLK1 negatively regulates its interaction with PPP1CC. {ECO:0000250|UniProtKB:Q9NSG2}.
uniprot
proteins
protein_family
FIRRM family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
37256941
uniprot
proteins
pubmed
37439366
uniprot
proteins
pubmed
39147779
uniprot
proteins
pubmed
39797737
uniprot
proteins
sequence_length
903
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q9NSG2}. Nucleus {ECO:0000250|UniProtKB:Q9NSG2}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NSG2}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9NSG2}. Midbody {ECO:0000250|UniProtKB:Q9NSG2}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9NSG2}. Note=Enriched at DNA damage sites (By similarity). Exhibits cell-cycle-dependent distribution during mitosis (By similarity). Detected in the nucleus in interphase (By similarity). Colocalizes with PLK1 to the centromeres in a nearby prometaphase cells (By similarity). Relocates to the central spindle in anaphase and to the midbody in telophase cells (By similarity). {ECO:0000250|UniProtKB:Q9NSG2}.
uniprot
proteins