CENPS_MOUSE
ID CENPS_MOUSE Reviewed; 142 AA.
AC Q9D084; A2AH77; Q80ZS2; Q8BH28;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
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, FAAP16, MHF1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D084-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D084-2; Sequence=VSP_020435, VSP_020436;
CC -!- SIMILARITY: Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25385.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC25387.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK011725; BAB27801.1; -; mRNA.
DR EMBL; AK012995; BAC25385.1; ALT_FRAME; mRNA.
DR EMBL; AK013038; BAC25387.1; ALT_FRAME; mRNA.
DR EMBL; AL731655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048521; AAH48521.1; -; mRNA.
DR CCDS; CCDS18954.1; -. [Q9D084-1]
DR RefSeq; NP_081539.1; NM_027263.2. [Q9D084-1]
DR AlphaFoldDB; Q9D084; -.
DR SMR; Q9D084; -.
DR BioGRID; 213761; 4.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR STRING; 10090.ENSMUSP00000030813; -.
DR PhosphoSitePlus; Q9D084; -.
DR EPD; Q9D084; -.
DR MaxQB; Q9D084; -.
DR PaxDb; Q9D084; -.
DR PRIDE; Q9D084; -.
DR ProteomicsDB; 281583; -. [Q9D084-1]
DR ProteomicsDB; 281584; -. [Q9D084-2]
DR Antibodypedia; 34792; 91 antibodies from 19 providers.
DR DNASU; 69928; -.
DR Ensembl; ENSMUST00000030813; ENSMUSP00000030813; ENSMUSG00000073705. [Q9D084-1]
DR Ensembl; ENSMUST00000105695; ENSMUSP00000101320; ENSMUSG00000073705. [Q9D084-2]
DR GeneID; 69928; -.
DR KEGG; mmu:69928; -.
DR UCSC; uc008vvt.2; mouse. [Q9D084-1]
DR UCSC; uc008vvu.2; mouse. [Q9D084-2]
DR CTD; 378708; -.
DR MGI; MGI:1917178; Cenps.
DR VEuPathDB; HostDB:ENSMUSG00000073705; -.
DR eggNOG; ENOG502S62X; Eukaryota.
DR GeneTree; ENSGT00510000048007; -.
DR HOGENOM; CLU_100369_0_0_1; -.
DR InParanoid; Q9D084; -.
DR OMA; MVWAQIE; -.
DR OrthoDB; 1483465at2759; -.
DR PhylomeDB; Q9D084; -.
DR TreeFam; TF300253; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 69928; 8 hits in 109 CRISPR screens.
DR ChiTaRS; Cenps; mouse.
DR PRO; PR:Q9D084; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D084; protein.
DR Bgee; ENSMUSG00000073705; Expressed in basioccipital bone and 161 other tissues.
DR ExpressionAtlas; Q9D084; baseline and differential.
DR Genevisible; Q9D084; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
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:0003690; F:double-stranded DNA binding; ISO:MGI.
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:0036297; P:interstrand cross-link repair; IEA:Ensembl.
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 Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA damage; DNA repair; DNA-binding; Kinetochore; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..142
FT /note="Centromere protein S"
FT /id="PRO_0000249478"
FT REGION 107..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 70..76
FT /note="HAKRSTV -> WVEKLAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020435"
FT VAR_SEQ 77..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020436"
SQ SEQUENCE 142 AA; 16335 MW; E870EFF61716017D CRC64;
MEEVEAEEPQ EFSHRQRLKA AVHYTVGCLC QEVTLNKQVN FSKQTIAAIS EVTFRQCENF
AKDLEMFARH AKRSTVTTED VKLLARRNNS LLKYITEKNE EIAQLNLKGK AKKKRKPEDE
SRSSRESMAE ELDGAEELQS ES
