FIRRM
entrez
55732
canonical
uniprot
Q9NSG2
canonical
ensembl
ENSG00000000460
resolver
ensp
ENSP00000352276
resolver
ensp
ENSP00000389257
resolver
ensp
ENSP00000490194
resolver
ensp
ENSP00000490333
resolver
ensp
ENSP00000579989
resolver
ensp
ENSP00000579990
resolver
ensp
ENSP00000579991
resolver
ensp
ENSP00000579993
resolver
ensp
ENSP00000607617
resolver
ensp
ENSP00000607621
resolver
enst
ENST00000472795
resolver
enst
ENST00000496973
resolver
genesymbol
FIRRM
resolver
genesymbol_syn
APOLO1
resolver
genesymbol_syn
C1orf112
resolver
hgnc
HGNC:25565
resolver
uniprot
A0A1B0GUP7
resolver
uniprot
A0A1B0GV14
resolver
uniprot
A6NFP1
resolver
uniprot
B3KU42
resolver
uniprot
B4E0A9
resolver
uniprot
Q3KNQ1
resolver
uniprot
Q9H8L5
resolver
uniprot
Q9NVJ0
resolver
uniprot_entry
A0A1B0GUP7_HUMAN
resolver
uniprot_entry
A0A1B0GV14_HUMAN
resolver
uniprot_entry
B4E0A9_HUMAN
resolver
uniprot_entry
FIRRM_HUMAN
resolver
uniprot_sec
A6NFP1
resolver
uniprot_sec
B3KU42
resolver
uniprot_sec
Q3KNQ1
resolver
uniprot_sec
Q9H8L5
resolver
uniprot_sec
Q9NVJ0
resolver
amino_acid_sequence
MFLPHMNHLTLEQTFFSQVLPKTVKLFDDMMYELTSQARGLSSQNLEIQTTLRNILQTMVQLLGALTGCVQHICATQESIILENIQSLPSSVLHIIKSTFVHCKNSESVYSGCLHLVSDLLQALFKEAYSLQKQLMELLDMVCMDPLVDDNDDILNMVIVIHSLLDICSVISSMDHAFHANTWKFIIKQSLKHQSIIKSQLKHKDIITSLCEDILFSFHSCLQLAEQMTQSDAQDNADYRLFQKTLKLCRFFANSLLHYAKEFLPFLSDSCCTLHQLYLQIHSKFPPSLYATRISKAHQEEIAGAFLVTLDPLISQLLTFQPFMQVVLDSKLDLPCELQFPQCLLLVVVMDKLPSQPKEVQTLWCTDSQVSETTTRISLLKAVFYSFEQCSGELSLPVHLQGLKSKGKAEVAVTLYQHVCVHLCTFITSFHPSLFAELDAALLNAVLSANMITSLLAMDAWCFLARYGTAELCAHHVTIVAHLIKSCPGECYQLINLSILLKRLFFFMAPPHQLEFIQKFSPKEAENLPLWQHISFQALPPELREQTVHEVTTVGTAECRKWLSRSRTLGELESLNTVLSALLAVCNSAGEALDTGKQTAIIEVVSQLWAFLNIKQVADQPYVQQTFSLLLPLLGFFIQTLDPKLILQAVTLQTSLLKLELPDYVRLAMLDFVSSLGKLFIPEAIQDRILPNLSCMFALLLADRSWLLEQHTLEAFTQFAEGTNHEEIVPQCLSSEETKNKVVSFLEKTGFVDETEAAKVERVKQEKGIFWEPFANVTVEEAKRSSLQPYAKRARQEFPWEEEYRSALHTIAGALEATESLLQKGPAPAWLSMEMEALQERMDKLKRYIHTLG
uniprot
proteins
function
FUNCTION: Forms a complex with FIGL1, which regulates DNA double-strand break (DSB) repair via homologous recombination (HR) (PubMed:29608566, PubMed:37256941, PubMed:37347663, PubMed:37515771, PubMed:37556550, PubMed:38286805). The FIGNL1-FIRRM complex is essential for resolution of homologous recombination intermediates in response to DNA interstrand cross-links (ICLs) (PubMed:37256941, PubMed:37347663, PubMed:37515771, PubMed:37556550, PubMed:38286805). 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:37256941, PubMed:37347663, PubMed:37515771, PubMed:37556550, PubMed:38286805). It also regulates HR during meiosis by promoting dissociation of DMC1 filaments from DNA (By similarity). Within the complex, provides the ATPase activity to disassemble DMC1 and RAD51 filaments, while FIRRM directly binds single-stranded DNA to facilitate this unloading (PubMed:37556550). 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 (PubMed:34260926). 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 (PubMed:34260926). {ECO:0000250|UniProtKB:Q3TQQ9, ECO:0000269|PubMed:29608566, ECO:0000269|PubMed:34260926, ECO:0000269|PubMed:37256941, ECO:0000269|PubMed:37347663, ECO:0000269|PubMed:37515771, ECO:0000269|PubMed:37556550, ECO:0000269|PubMed:38286805}.
uniprot
proteins
mass_dalton
96554
uniprot
proteins
mutagenesis
MUTAGEN 43; /note="S->A: Decreased binding to PLK1."; /evidence="ECO:0000269|PubMed:34260926"; MUTAGEN 43; /note="S->D: Increased binding to PLK1."; /evidence="ECO:0000269|PubMed:34260926"; MUTAGEN 461..463; /note="Missing: Abolished interaction with FIGNL1."; /evidence="ECO:0000269|PubMed:37556550"; MUTAGEN 744; /note="S->A: Does not affect binding to PPP1CC. Rescues the mitotic defects seen in FIRRM-depleted cells."; /evidence="ECO:0000269|PubMed:34260926"; MUTAGEN 744; /note="S->D: Decreased binding to PPP1CC. Does not rescue the mitotic defects seen in FIRRM-depleted cells."; /evidence="ECO:0000269|PubMed:34260926
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-43 by PLK1 strengthens FIRRM-PLK1 interaction (PubMed:34260926). Phosphorylation at Ser-744 by PLK1 negatively regulates its interaction with PPP1CC (PubMed:34260926). {ECO:0000269|PubMed:34260926}.
uniprot
proteins
protein_family
FIRRM family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
29608566
uniprot
proteins
pubmed
34260926
uniprot
proteins
pubmed
37256941
uniprot
proteins
pubmed
37347663
uniprot
proteins
pubmed
37515771
uniprot
proteins
pubmed
37556550
uniprot
proteins
pubmed
38286805
uniprot
proteins
sequence_length
853
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:37556550, ECO:0000269|PubMed:38286805}. Nucleus {ECO:0000269|PubMed:34260926}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:34260926}. Chromosome, centromere {ECO:0000269|PubMed:34260926}. Midbody {ECO:0000269|PubMed:34260926}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:34260926}. Note=Enriched at DNA damage sites (PubMed:37556550, PubMed:38286805). Exhibits cell-cycle-dependent distribution during mitosis. Detected in the nucleus in interphase (PubMed:34260926). Colocalizes with PLK1 to the centromeres in a nearby prometaphase cells (PubMed:34260926). Relocates to the central spindle in anaphase and to the midbody in telophase cells (PubMed:34260926). {ECO:0000269|PubMed:34260926, ECO:0000269|PubMed:37556550, ECO:0000269|PubMed:38286805}.
uniprot
proteins