CENPS_XENLA
ID CENPS_XENLA Reviewed; 135 AA.
AC Q6NRI8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Centromere protein S;
DE Short=CENP-S;
DE AltName: Full=Apoptosis-inducing TAF9-like domain-containing protein 1 homolog;
DE AltName: Full=FANCM-interacting histone fold protein 1;
GN Name=cenps; Synonyms=apitd1, mhf1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-binding component of the Fanconi anemia (FA) core
CC complex. Required for the normal activation of the FA pathway, leading
CC to monoubiquitination of the FANCI-FANCD2 complex in response to DNA
CC damage, cellular resistance to DNA cross-linking drugs, and prevention
CC of chromosomal breakage. In complex with CENPX (MHF heterodimer),
CC crucial cofactor for FANCM in both binding and ATP-dependent remodeling
CC of DNA. Stabilizes FANCM. In complex with CENPX and FANCM (but not
CC other FANC proteins), rapidly recruited to blocked forks and promotes
CC gene conversion at blocked replication forks. In complex with CENPT,
CC CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the
CC formation of a functional kinetochore outer plate, which is essential
CC for kinetochore-microtubule attachment and faithful mitotic
CC progression. As a component of MHF and CENP-T-W-S-X complexes, binds
CC DNA and bends it to form a nucleosome-like structure. DNA-binding
CC function is fulfilled in the presence of CENPX, with the following
CC preference for DNA substates: Holliday junction > double-stranded >
CC splay arm > single-stranded. Does not bind DNA on its own.
CC {ECO:0000250|UniProtKB:Q8N2Z9}.
CC -!- SUBUNIT: Heterodimer with CENPX, sometimes called MHF; this interaction
CC stabilizes both partners. MHF heterodimers can assemble to form
CC tetrameric structures. MHF also coassemble with CENPT-CENPW
CC heterodimers at centromeres to form the tetrameric CENP-T-W-S-X
CC complex. Forms a discrete complex with FANCM and CENPX, called FANCM-
CC MHF; this interaction, probably mediated by direct binding between
CC CENPS and FANCM, leads to synergistic activation of double-stranded DNA
CC binding and strongly stimulates FANCM-mediated DNA remodeling.
CC Recruited by FANCM to the Fanconi anemia (FA) core complex, which
CC consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG,
CC FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with
CC Bloom syndrome (BLM) complex, which consists of at least BLM, DNA
CC topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32.
CC The super complex between FA and BLM is called BRAFT. Component of the
CC CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP,
CC CENPQ, CENPR and CENPS. The CENPA-CAD complex is probably recruited on
CC centromeres by the CENPA-NAC complex, at least composed of CENPA,
CC CENPC, CENPH, CENPM, CENPN, CENPT and CENPU.
CC {ECO:0000250|UniProtKB:Q8N2Z9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N2Z9}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q8N2Z9}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q8N2Z9}. Note=Assembly
CC of CENPS and CENPX and its partner subunits CENPT and CENPW at
CC centromeres occurs through a dynamic exchange mechanism. Although
CC exchange is continuous in the cell cycle, de novo assembly starts
CC principally during mid-late S phase and is complete by G2. CENPS is
CC more stably bound at the kinetochore than CENPX. During S phase,
CC rapidly recruited to DNA interstrand cross-links that block
CC replication. Recruited to DNA damage sites about 20 minutes following
CC UV irradiation, reaching a plateau after approximately 40 minutes.
CC {ECO:0000250|UniProtKB:Q8N2Z9}.
CC -!- SIMILARITY: Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC070762; AAH70762.1; -; mRNA.
DR RefSeq; NP_001084907.1; NM_001091438.1.
DR AlphaFoldDB; Q6NRI8; -.
DR SMR; Q6NRI8; -.
DR MaxQB; Q6NRI8; -.
DR DNASU; 431958; -.
DR GeneID; 431958; -.
DR KEGG; xla:431958; -.
DR CTD; 431958; -.
DR Xenbase; XB-GENE-5938577; cenps.L.
DR OMA; MVWAQIE; -.
DR OrthoDB; 1483465at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 431958; Expressed in blastula and 18 other tissues.
DR GO; GO:0071821; C:FANCM-MHF complex; ISS:UniProtKB.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; ISS:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR029003; CENP-S/Mhf1.
DR InterPro; IPR033554; CENPS.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR22980:SF4; PTHR22980:SF4; 1.
DR Pfam; PF15630; CENP-S; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Kinetochore; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..135
FT /note="Centromere protein S"
FT /id="PRO_0000249479"
FT REGION 103..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 135 AA; 15179 MW; 315516EC816FB7A1 CRC64;
MAEGQEEHFS RTQRLKAAVH YVVGSLCQEV ADDKEIDFSK QAIAAISEIT FRQCESFAKD
LEIFARHAKR TTINMDDVKL LARRSRSLYA HISKCSDEIA ANSLEQKEKK KKKSVSGGNV
SRNSDMDTVV PESKD
