ID CENPS_CHICK Reviewed; 139 AA.
AC E1BSW7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Centromere protein S;
DE Short=CENP-S;
GN Name=CENPS; Synonyms=APITD1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=White Leghorn Hisex;
RX PubMed=12445392; DOI=10.1016/s0960-9822(02)01296-4;
RA Boardman P.E., Sanz-Ezquerro J., Overton I.M., Burt D.W., Bosch E.,
RA Fong W.T., Tickle C., Brown W.R., Wilson S.A., Hubbard S.J.;
RT "A comprehensive collection of chicken cDNAs.";
RL Curr. Biol. 12:1965-1969(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3]
RP FUNCTION, INTERACTION WITH CENPX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19620631; DOI=10.1083/jcb.200903100;
RA Amano M., Suzuki A., Hori T., Backer C., Okawa K., Cheeseman I.M.,
RA Fukagawa T.;
RT "The CENP-S complex is essential for the stable assembly of outer
RT kinetochore structure.";
RL J. Cell Biol. 186:173-182(2009).
RN [4]
RP FUNCTION.
RX PubMed=20347428; DOI=10.1016/j.molcel.2010.01.039;
RA Yan Z., Delannoy M., Ling C., Daee D., Osman F., Muniandy P.A., Shen X.,
RA Oostra A.B., Du H., Steltenpool J., Lin T., Schuster B., Decaillet C.,
RA Stasiak A., Stasiak A.Z., Stone S., Hoatlin M.E., Schindler D.,
RA Woodcock C.L., Joenje H., Sen R., de Winter J.P., Li L., Seidman M.M.,
RA Whitby M.C., Myung K., Constantinousend A., Wang W.;
RT "A histone-fold complex and FANCM form a conserved DNA-remodeling complex
RT to maintain genome stability.";
RL Mol. Cell 37:865-878(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), FUNCTION, INTERACTION WITH CENPT;
RP CENPW AND CEPNX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-15; LYS-41
RP AND LYS-70.
RX PubMed=22304917; DOI=10.1016/j.cell.2011.11.061;
RA Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T.,
RA Morikawa K., Cheeseman I.M., Fukagawa T.;
RT "CENP-T-W-S-X forms a unique centromeric chromatin structure with a
RT histone-like fold.";
RL Cell 148:487-501(2012).
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 (PubMed:20347428). In complex with CENPX (MHF
CC heterodimer), crucial cofactor for FANCM in both binding and ATP-
CC dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPX
CC and FANCM (but not other FANC proteins), rapidly recruited to blocked
CC forks and promotes gene conversion at blocked replication forks. In
CC complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer),
CC involved in the formation of a functional kinetochore outer plate,
CC which is essential for kinetochore-microtubule attachment and faithful
CC mitotic progression (PubMed:19620631). As a component of MHF and CENP-
CC T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like
CC structure. DNA-binding function is fulfilled in the presence of CENPX,
CC with the following preference for DNA substates: Holliday junction >
CC double-stranded > splay arm > single-stranded. Does not bind DNA on its
CC own (By similarity). {ECO:0000250|UniProtKB:Q8N2Z9,
CC ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428}.
CC -!- SUBUNIT: Heterodimer with CENPX, sometimes called MHF; this interaction
CC stabilizes both partners. MHF heterodimers can assemble to form
CC tetrameric structures (PubMed:22304917). MHF also coassemble with
CC CENPT-CENPW heterodimers at centromeres to form the tetrameric CENP-T-
CC W-S-X complex (PubMed:22304917). Forms a discrete complex with FANCM
CC and CENPX, called FANCM-MHF; this interaction, probably mediated by
CC direct binding between CENPS and FANCM, leads to synergistic activation
CC of double-stranded DNA binding and strongly stimulates FANCM-mediated
CC DNA remodeling. Recruited by FANCM to the Fanconi anemia (FA) core
CC complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE,
CC FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100. The FA core complex
CC associates with Bloom syndrome (BLM) complex, which consists of at
CC least BLM, DNA topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70
CC and RPA2/RPA32. The super complex between FA and BLM is called BRAFT.
CC Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL,
CC CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is probably
CC recruited on centromeres by the CENPA-NAC complex, at least composed of
CC CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (By similarity).
CC {ECO:0000250|UniProtKB:Q8N2Z9, ECO:0000269|PubMed:22304917}.
CC -!- INTERACTION:
CC E1BSW7; F1NPG5: CENPT; NbExp=3; IntAct=EBI-5487792, EBI-2132248;
CC E1BSW7; P0DJH7: CENPX; NbExp=4; IntAct=EBI-5487792, EBI-5590609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19620631}.
CC Chromosome, centromere {ECO:0000269|PubMed:19620631}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:19620631}. Note=Assembly of
CC CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres
CC occurs through a dynamic exchange mechanism. Although exchange is
CC continuous in the cell cycle, de novo assembly starts principally
CC during mid-late S phase and is complete by G2. CENPS is more stably
CC bound at the kinetochore than CENPX. During S phase, rapidly recruited
CC to DNA interstrand cross-links that block replication. Recruited to DNA
CC damage sites about 20 minutes following UV irradiation, reaching a
CC plateau after approximately 40 minutes. {ECO:0000250|UniProtKB:Q8N2Z9}.
CC -!- SIMILARITY: Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BX930742; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AADN02040781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001191861.1; NM_001204932.1.
DR PDB; 3B0B; X-ray; 2.15 A; A/B=2-106.
DR PDB; 3VH5; X-ray; 2.40 A; A=2-139.
DR PDB; 3VH6; X-ray; 3.35 A; A=2-139.
DR PDB; 7DA0; X-ray; 1.25 A; B=2-106.
DR PDB; 7DA1; X-ray; 2.01 A; A/B=2-106.
DR PDB; 7DA2; X-ray; 2.79 A; A/C=2-106.
DR PDBsum; 3B0B; -.
DR PDBsum; 3VH5; -.
DR PDBsum; 3VH6; -.
DR PDBsum; 7DA0; -.
DR PDBsum; 7DA1; -.
DR PDBsum; 7DA2; -.
DR AlphaFoldDB; E1BSW7; -.
DR SMR; E1BSW7; -.
DR BioGRID; 692121; 2.
DR IntAct; E1BSW7; 3.
DR STRING; 9031.ENSGALP00000040599; -.
DR PaxDb; 9031-ENSGALP00000040599; -.
DR GeneID; 771417; -.
DR KEGG; gga:771417; -.
DR CTD; 378708; -.
DR VEuPathDB; HostDB:geneid_771417; -.
DR eggNOG; ENOG502S62X; Eukaryota.
DR HOGENOM; CLU_100369_0_0_1; -.
DR InParanoid; E1BSW7; -.
DR OMA; WTQIENV; -.
DR OrthoDB; 5395965at2759; -.
DR Reactome; R-GGA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-GGA-2467813; Separation of Sister Chromatids.
DR Reactome; R-GGA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-GGA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-GGA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-GGA-68877; Mitotic Prometaphase.
DR Reactome; R-GGA-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:E1BSW7; -.
DR Proteomes; UP000000539; Chromosome 21.
DR Bgee; ENSGALG00000024481; Expressed in spermatid and 13 other cell types or tissues.
DR GO; GO:0071821; C:FANCM-MHF complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR DisProt; DP02079; -.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR029003; CENP-S/Mhf1.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR22980:SF0; CENTROMERE PROTEIN S; 1.
DR PANTHER; PTHR22980; CORTISTATIN; 1.
DR Pfam; PF15630; CENP-S; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA damage; DNA repair; DNA-binding; Kinetochore; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..139
FT /note="Centromere protein S"
FT /id="PRO_0000417386"
FT REGION 99..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 15
FT /note="R->A: Abolishes sequence-specific DNA binding; when
FT associated with A-41 and A-70."
FT /evidence="ECO:0000269|PubMed:22304917"
FT MUTAGEN 41
FT /note="K->A: Abolishes sequence-specific DNA binding; when
FT associated with A-15 and A-70."
FT /evidence="ECO:0000269|PubMed:22304917"
FT MUTAGEN 70
FT /note="K->A: Abolishes sequence-specific DNA binding; when
FT associated with A-15 and A-41."
FT /evidence="ECO:0000269|PubMed:22304917"
FT HELIX 8..35
FT /evidence="ECO:0007829|PDB:7DA0"
FT HELIX 41..68
FT /evidence="ECO:0007829|PDB:7DA0"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:7DA0"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:7DA0"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:7DA0"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:7DA0"
SQ SEQUENCE 139 AA; 15619 MW; B81526467D9416CA CRC64;
MEAAGGEQRE LLIQRLRAAV HYTTGCLCQD VAEDKGVLFS KQTVAAISEI TFRQCENFAR
DLEMFARHAK RSTITSEDVK LLARRSNSLL KYITQKSDEL ASSNMEQKEK KKKKSSAAKG
RKTEENETPV TESEDSNMA
//
