CENPS_HUMAN
ID CENPS_HUMAN Reviewed; 138 AA.
AC Q8N2Z9; Q8NFE5; Q8NFG5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Centromere protein S;
DE Short=CENP-S;
DE AltName: Full=Apoptosis-inducing TAF9-like domain-containing protein 1;
DE AltName: Full=FANCM-associated histone fold protein 1 {ECO:0000303|PubMed:20347428};
DE AltName: Full=FANCM-interacting histone fold protein 1 {ECO:0000303|PubMed:20347429};
DE AltName: Full=Fanconi anemia-associated polypeptide of 16 kDa;
GN Name=CENPS;
GN Synonyms=APITD1, FAAP16, MHF1 {ECO:0000303|PubMed:20347428,
GN ECO:0000303|PubMed:20347429};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA Cai Q., Guo J.H., Yu L.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15328517; DOI=10.1038/sj.bjc.6602083;
RA Krona C., Ejeskaer K., Caren H., Abel F., Sjoeberg R.-M., Martinsson T.;
RT "A novel 1p36.2 located gene, APITD1, with tumour-suppressive properties
RT and a putative p53-binding domain, shows low expression in neuroblastoma
RT tumours.";
RL Br. J. Cancer 91:1119-1130(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE CENPA-CAD
RP COMPLEX WITH CENPI; CENPK; CENPL; CENPO; CENPP CENPQ AND CENPR.
RX PubMed=16622419; DOI=10.1038/ncb1397;
RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA Cleveland D.W.;
RT "The human CENP-A centromeric nucleosome-associated complex.";
RL Nat. Cell Biol. 8:458-469(2006).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CENPX, 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 [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FA
RP CORE COMPLEX, IDENTIFICATION IN THE BRAFT COMPLEX, INTERACTION WITH CENPX
RP AND FANCM, DNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 73-LYS-ARG-74 AND 87-ARG-ARG-88.
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 [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FA
RP CORE COMPLEX, INTERACTION WITH CENPX AND FANCM, SUBCELLULAR LOCATION, AND
RP DNA-BINDING.
RX PubMed=20347429; DOI=10.1016/j.molcel.2010.01.036;
RA Singh T.R., Saro D., Ali A.M., Zheng X.-F., Du C., Killen M.W.,
RA Sachpatzidis A., Wahengbam K., Pierce A.J., Xiong Y., Sung P., Meetei A.R.;
RT "MHF1-MHF2, a histone-fold-containing protein complex, participates in the
RT Fanconi anemia pathway via FANCM.";
RL Mol. Cell 37:879-886(2010).
RN [9]
RP FUNCTION, AND INTERACTION WITH CENPT; CENPW AND CEPNX.
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).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP IDENTIFICATION IN THE CENP-T-W-S-X COMPLEX, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=24522885; DOI=10.1098/rsob.130229;
RA Dornblut C., Quinn N., Monajambashi S., Prendergast L., van Vuuren C.,
RA Muench S., Deng W., Leonhardt H., Cardoso M.C., Hoischen C., Diekmann S.,
RA Sullivan K.F.;
RT "A CENP-S/X complex assembles at the centromere in S and G2 phases of the
RT human cell cycle.";
RL Open Biol. 4:130229-130229(2014).
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, PubMed:20347429). In complex
CC with CENPX (MHF heterodimer), crucial cofactor for FANCM in both
CC binding and ATP-dependent remodeling of DNA. Stabilizes FANCM
CC (PubMed:20347428, PubMed:20347429). In complex with CENPX and FANCM
CC (but not other FANC proteins), rapidly recruited to blocked forks and
CC promotes gene conversion at blocked replication forks
CC (PubMed:20347428). In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X
CC heterotetramer), involved in the formation of a functional kinetochore
CC outer plate, which is essential for kinetochore-microtubule attachment
CC and faithful mitotic progression (PubMed:19620631). As a component of
CC MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a
CC nucleosome-like structure (PubMed:20347428, PubMed:22304917). DNA-
CC binding function is fulfilled in the presence of CENPX, with the
CC following preference for DNA substates: Holliday junction > double-
CC stranded > splay arm > single-stranded. Does not bind DNA on its own
CC (PubMed:20347428, PubMed:20347429). {ECO:0000269|PubMed:19620631,
CC ECO:0000269|PubMed:20347428, ECO:0000269|PubMed:20347429,
CC ECO:0000269|PubMed:22304917}.
CC -!- SUBUNIT: Heterodimer with CENPX, sometimes called MHF; this interaction
CC stabilizes both partners (PubMed:19620631, PubMed:20347428,
CC PubMed:20347429, PubMed:24522885). MHF heterodimers can assemble to
CC form 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, PubMed:24522885). Forms a discrete
CC complex with FANCM and CENPX, called FANCM-MHF; this interaction,
CC probably mediated by direct binding between CENPS and FANCM, leads to
CC synergistic activation of double-stranded DNA binding and strongly
CC stimulates FANCM-mediated DNA remodeling (PubMed:20347428,
CC PubMed:20347429). 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 (PubMed:20347428, PubMed:20347429). Component of the CENPA-CAD complex,
CC composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS.
CC The CENPA-CAD complex is probably recruited on centromeres by the
CC CENPA-NAC complex, composed of at least CENPA, CENPC, CENPH, CENPM,
CC CENPN, CENPT and CENPU (PubMed:16622419). {ECO:0000269|PubMed:16622419,
CC ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428,
CC ECO:0000269|PubMed:20347429, ECO:0000269|PubMed:22304917,
CC ECO:0000269|PubMed:24522885}.
CC -!- INTERACTION:
CC Q8N2Z9; A8MT69: CENPX; NbExp=6; IntAct=EBI-5529649, EBI-5529694;
CC Q8N2Z9; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-5529649, EBI-11962928;
CC Q8N2Z9; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-5529649, EBI-10172004;
CC Q8N2Z9; P42858: HTT; NbExp=3; IntAct=EBI-5529649, EBI-466029;
CC Q8N2Z9; Q969G2: LHX4; NbExp=3; IntAct=EBI-5529649, EBI-2865388;
CC Q8N2Z9; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-5529649, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19620631,
CC ECO:0000269|PubMed:20347428, ECO:0000269|PubMed:24522885}. Chromosome,
CC centromere {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:24522885}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19620631}.
CC Note=Assembly of CENPS and CENPX and its partner subunits CENPT and
CC CENPW at centromeres occurs through a dynamic exchange mechanism.
CC Although exchange is continuous in the cell cycle, de novo assembly
CC starts principally during mid-late S phase and is complete by G2. CENPS
CC is more stably bound at the kinetochore than CENPX (PubMed:19620631,
CC PubMed:24522885). During S phase, rapidly recruited to DNA interstrand
CC cross-links that block replication (PubMed:20347428). Recruited to DNA
CC damage sites about 20 minutes following UV irradiation, reaching a
CC plateau after approximately 40 minutes (PubMed:24522885).
CC {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428,
CC ECO:0000269|PubMed:24522885}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N2Z9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N2Z9-2; Sequence=VSP_020434;
CC Name=3;
CC IsoId=Q8N2Z9-3; Sequence=VSP_020432, VSP_020433;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15328517}.
CC -!- DEVELOPMENTAL STAGE: Expression varies across the cell cycle, with
CC highest levels in G2 phase (at protein level). No statistically
CC significant changes at the transcript level.
CC {ECO:0000269|PubMed:24522885}.
CC -!- SIMILARITY: Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF516753; AAM61954.1; -; mRNA.
DR EMBL; AF521016; AAM70482.1; -; mRNA.
DR EMBL; AL139424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029430; AAH29430.1; -; mRNA.
DR CCDS; CCDS115.1; -. [Q8N2Z9-1]
DR RefSeq; NP_001257446.1; NM_001270517.1. [Q8N2Z9-1]
DR RefSeq; NP_940946.1; NM_198544.3. [Q8N2Z9-2]
DR RefSeq; NP_950171.2; NM_199006.2. [Q8N2Z9-3]
DR RefSeq; NP_954988.1; NM_199294.2. [Q8N2Z9-1]
DR PDB; 4DRA; X-ray; 2.41 A; A/B/C/D=1-107.
DR PDB; 4DRB; X-ray; 2.63 A; A/B/D/E/G/H=1-114.
DR PDB; 4E44; X-ray; 2.10 A; A/C=1-110.
DR PDB; 4E45; X-ray; 2.00 A; A/C/F/H/K/M=1-110.
DR PDB; 4NDY; X-ray; 7.00 A; A/C/G/I/J/K/Q/R/S/T=14-105.
DR PDB; 4NE1; X-ray; 6.50 A; A/C/G/I/J/K/Q/R/S/T/Y/a/c/e/f/g/k/l/m/n=14-118.
DR PDB; 4NE3; X-ray; 1.80 A; A=14-105.
DR PDB; 4NE5; X-ray; 2.50 A; A/C/E/G=14-105.
DR PDB; 4NE6; X-ray; 2.10 A; A/C=14-105.
DR PDBsum; 4DRA; -.
DR PDBsum; 4DRB; -.
DR PDBsum; 4E44; -.
DR PDBsum; 4E45; -.
DR PDBsum; 4NDY; -.
DR PDBsum; 4NE1; -.
DR PDBsum; 4NE3; -.
DR PDBsum; 4NE5; -.
DR PDBsum; 4NE6; -.
DR AlphaFoldDB; Q8N2Z9; -.
DR SMR; Q8N2Z9; -.
DR BioGRID; 132044; 35.
DR BioGRID; 1529300; 4.
DR ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR ComplexPortal; CPX-6266; Fanconi anemia FANCM-FAAP24-MHF anchoring complex.
DR CORUM; Q8N2Z9; -.
DR IntAct; Q8N2Z9; 10.
DR MINT; Q8N2Z9; -.
DR STRING; 9606.ENSP00000308583; -.
DR iPTMnet; Q8N2Z9; -.
DR MetOSite; Q8N2Z9; -.
DR PhosphoSitePlus; Q8N2Z9; -.
DR BioMuta; CENPS; -.
DR DMDM; 74759833; -.
DR EPD; Q8N2Z9; -.
DR jPOST; Q8N2Z9; -.
DR MassIVE; Q8N2Z9; -.
DR MaxQB; Q8N2Z9; -.
DR PaxDb; Q8N2Z9; -.
DR PeptideAtlas; Q8N2Z9; -.
DR PRIDE; Q8N2Z9; -.
DR ProteomicsDB; 71742; -. [Q8N2Z9-1]
DR ProteomicsDB; 71743; -. [Q8N2Z9-2]
DR ProteomicsDB; 71744; -. [Q8N2Z9-3]
DR Antibodypedia; 34792; 91 antibodies from 19 providers.
DR DNASU; 378708; -.
DR Ensembl; ENST00000309048.8; ENSP00000308583.2; ENSG00000175279.22. [Q8N2Z9-1]
DR GeneID; 100526739; -.
DR GeneID; 378708; -.
DR KEGG; hsa:100526739; -.
DR KEGG; hsa:378708; -.
DR MANE-Select; ENST00000309048.8; ENSP00000308583.2; NM_199294.3; NP_954988.1.
DR UCSC; uc001are.4; human. [Q8N2Z9-1]
DR CTD; 100526739; -.
DR CTD; 378708; -.
DR DisGeNET; 100526739; -.
DR DisGeNET; 378708; -.
DR GeneCards; CENPS; -.
DR HGNC; HGNC:23163; CENPS.
DR HPA; ENSG00000175279; Tissue enhanced (testis).
DR MIM; 609130; gene.
DR neXtProt; NX_Q8N2Z9; -.
DR OpenTargets; ENSG00000175279; -.
DR PharmGKB; PA134861614; -.
DR VEuPathDB; HostDB:ENSG00000175279; -.
DR eggNOG; ENOG502S62X; Eukaryota.
DR GeneTree; ENSGT00510000048007; -.
DR HOGENOM; CLU_100369_0_0_1; -.
DR InParanoid; Q8N2Z9; -.
DR OMA; MVWAQIE; -.
DR OrthoDB; 1483465at2759; -.
DR PhylomeDB; Q8N2Z9; -.
DR TreeFam; TF300253; -.
DR PathwayCommons; Q8N2Z9; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q8N2Z9; -.
DR SIGNOR; Q8N2Z9; -.
DR BioGRID-ORCS; 100526739; 23 hits in 960 CRISPR screens.
DR BioGRID-ORCS; 378708; 148 hits in 991 CRISPR screens.
DR ChiTaRS; CENPS; human.
DR Pharos; Q8N2Z9; Tbio.
DR PRO; PR:Q8N2Z9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N2Z9; protein.
DR Bgee; ENSG00000175279; Expressed in left testis and 176 other tissues.
DR ExpressionAtlas; Q8N2Z9; baseline and differential.
DR Genevisible; Q8N2Z9; HS.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0071821; C:FANCM-MHF complex; IDA:UniProtKB.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA: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; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IDA:ComplexPortal.
DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; TAS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00620; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Centromere; Chromosome; DNA damage; DNA repair; DNA-binding; Kinetochore;
KW Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..138
FT /note="Centromere protein S"
FT /id="PRO_0000249477"
FT REGION 110..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 70..77
FT /note="RHAKRTTI -> SICRKRQE (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_020432"
FT VAR_SEQ 78..138
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_020433"
FT VAR_SEQ 91..138
FT /note="SLLKYITDKSEEIAQINLERKAQKKKKSEDGSKNSRQPAEAGVVESEN ->
FT SLHMQEAAGIRKSSLLTFLAWWFEWTSQASAGPLIGEEAREVARRQEGAPPQQSARRDR
FT MPCRNFFWKTFSSCK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_020434"
FT MUTAGEN 73..74
FT /note="KR->AA: No effect on CENPX- and FANCM-binding; loss
FT of double-stranded DNA-binding of the MHF heterodimer and
FT of FANCM recruitment to fork DNA; partial decrease in FA
FT core complex activity, as shown by lower levels of FANCD2
FT monoubiquitination and higher frequency of sister chromatin
FT exchanges. Complete loss of CENPX- and FANCM-binding; when
FT associated with 87-A-A-88."
FT /evidence="ECO:0000269|PubMed:20347428"
FT MUTAGEN 87..88
FT /note="RR->AA: Partial loss of CENPX- and FANCM-binding;
FT partial decrease in FA core complex activity, as shown by
FT lower levels of FANCD2 monoubiquitination and higher
FT frequency of sister chromatin exchanges. Complete loss of
FT CENPX- and FANCM-binding; when associated with 73-A-A-74."
FT /evidence="ECO:0000269|PubMed:20347428"
FT HELIX 8..12
FT /evidence="ECO:0007829|PDB:4DRA"
FT HELIX 15..38
FT /evidence="ECO:0007829|PDB:4NE3"
FT HELIX 44..71
FT /evidence="ECO:0007829|PDB:4NE3"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4NE3"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:4NE3"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:4E44"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:4NE3"
SQ SEQUENCE 138 AA; 15893 MW; CBCD22CDDE213D87 CRC64;
MEEEAETEEQ QRFSYQQRLK AAVHYTVGCL CEEVALDKEM QFSKQTIAAI SELTFRQCEN
FAKDLEMFAR HAKRTTINTE DVKLLARRSN SLLKYITDKS EEIAQINLER KAQKKKKSED
GSKNSRQPAE AGVVESEN
