Q8N2Z9
uniprot
Q8N2Z9
canonical
amino_acid_sequence
MEEEAETEEQQRFSYQQRLKAAVHYTVGCLCEEVALDKEMQFSKQTIAAISELTFRQCENFAKDLEMFARHAKRTTINTEDVKLLARRSNSLLKYITDKSEEIAQINLERKAQKKKKSEDGSKNSRQPAEAGVVESEN
uniprot
proteins
function
FUNCTION: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:20347428, PubMed:20347429). In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM (PubMed:20347428, PubMed:20347429). In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks (PubMed:20347428). In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression (PubMed:19620631). As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure (PubMed:20347428, PubMed:22304917). DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (PubMed:20347428, PubMed:20347429). {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428, ECO:0000269|PubMed:20347429, ECO:0000269|PubMed:22304917}.
uniprot
proteins
mass_dalton
15893
uniprot
proteins
mutagenesis
MUTAGEN 73..74; /note="KR->AA: No effect on CENPX- and FANCM-binding; loss of double-stranded DNA-binding of the MHF heterodimer and of FANCM recruitment to fork DNA; partial decrease in FA core complex activity, as shown by lower levels of FANCD2 monoubiquitination and higher frequency of sister chromatin exchanges. Complete loss of CENPX- and FANCM-binding; when associated with 87-A-A-88."; /evidence="ECO:0000269|PubMed:20347428"; MUTAGEN 87..88; /note="RR->AA: Partial loss of CENPX- and FANCM-binding; partial decrease in FA core complex activity, as shown by lower levels of FANCD2 monoubiquitination and higher frequency of sister chromatin exchanges. Complete loss of CENPX- and FANCM-binding; when associated with 73-A-A-74."; /evidence="ECO:0000269|PubMed:20347428
uniprot
proteins
protein_family
CENP-S/MHF1 subfamily
uniprot
proteins
protein_family
TAF9 family
uniprot
proteins
pubmed
15328517
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16622419
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
19620631
uniprot
proteins
pubmed
20347428
uniprot
proteins
pubmed
20347429
uniprot
proteins
pubmed
22304917
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24522885
uniprot
proteins
sequence_length
138
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428, ECO:0000269|PubMed:24522885}. Chromosome, centromere {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:24522885}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19620631}. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPS is more stably bound at the kinetochore than CENPX (PubMed:19620631, PubMed:24522885). During S phase, rapidly recruited to DNA interstrand cross-links that block replication (PubMed:20347428). Recruited to DNA damage sites about 20 minutes following UV irradiation, reaching a plateau after approximately 40 minutes (PubMed:24522885). {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428, ECO:0000269|PubMed:24522885}.
uniprot
proteins