MIS18_SCHPO
ID MIS18_SCHPO Reviewed; 194 AA.
AC Q9P802;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Kinetochore protein mis18;
GN Name=mis18; ORFNames=SPCC970.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP FUNCTION, INTERACTION WITH MIS16, AND SUBCELLULAR LOCATION.
RX PubMed=15369671; DOI=10.1016/j.cell.2004.09.002;
RA Hayashi T., Fujita Y., Iwasaki O., Adachi Y., Takahashi K., Yanagida M.;
RT "Mis16 and Mis18 are required for CENP-A loading and histone deacetylation
RT at centromeres.";
RL Cell 118:715-729(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=17199038; DOI=10.1016/j.devcel.2006.11.002;
RA Fujita Y., Hayashi T., Kiyomitsu T., Toyoda Y., Kokubu A., Obuse C.,
RA Yanagida M.;
RT "Priming of centromere for CENP-A recruitment by human hMis18alpha,
RT hMis18beta, and M18BP1.";
RL Dev. Cell 12:17-30(2007).
RN [6]
RP IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
RX PubMed=24774534; DOI=10.1111/gtc.12152;
RA Hayashi T., Ebe M., Nagao K., Kokubu A., Sajiki K., Yanagida M.;
RT "Schizosaccharomyces pombe centromere protein Mis19 links Mis16 and Mis18
RT to recruit CENP-A through interacting with NMD factors and the SWI/SNF
RT complex.";
RL Genes Cells 19:541-554(2014).
RN [7]
RP IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
RX PubMed=24789708; DOI=10.1098/rsob.140043;
RA Subramanian L., Toda N.R., Rappsilber J., Allshire R.C.;
RT "Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A
RT assembly.";
RL Open Biol. 4:140043-140043(2014).
RN [8]
RP IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
RX PubMed=25375240; DOI=10.1371/journal.pone.0111905;
RA Hirai H., Arai K., Kariyazono R., Yamamoto M., Sato M.;
RT "The kinetochore protein Kis1/Eic1/Mis19 ensures the integrity of mitotic
RT spindles through maintenance of kinetochore factors Mis6/CENP-I and CENP-
RT A.";
RL PLoS ONE 9:E111905-E111905(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 1-120 IN COMPLEX WITH ZINC IONS,
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-22; ILE-31; TYR-90
RP AND TYR-114.
RX PubMed=26921242; DOI=10.15252/embr.201541520;
RA Subramanian L., Medina-Pritchard B., Barton R., Spiller F.,
RA Kulasegaran-Shylini R., Radaviciute G., Allshire R.C.,
RA Arockia Jeyaprakash A.;
RT "Centromere localization and function of Mis18 requires Yippee-like domain-
RT mediated oligomerization.";
RL EMBO Rep. 17:496-507(2016).
CC -!- FUNCTION: Component of the CENP-A recruiting complex that ensures the
CC integrity of mitotic spindles through maintenance of kinetochore
CC factors mis6/CENP-I and cnp1/CENP-A (PubMed:15369671, PubMed:24774534,
CC PubMed:24789708, PubMed:25375240). Maintains the deacetylated state of
CC histones specifically in the central core of the centromeres
CC (PubMed:15369671). {ECO:0000269|PubMed:15369671,
CC ECO:0000269|PubMed:24774534, ECO:0000269|PubMed:24789708,
CC ECO:0000269|PubMed:25375240}.
CC -!- SUBUNIT: Homotetramer (PubMed:26921242). Component of the CENP-A
CC recruiting complex composed of at least mis16, mis19, mis19 and mis20
CC (PubMed:15369671, PubMed:24774534, PubMed:24789708, PubMed:25375240).
CC {ECO:0000269|PubMed:15369671, ECO:0000269|PubMed:24774534,
CC ECO:0000269|PubMed:24789708, ECO:0000269|PubMed:25375240,
CC ECO:0000269|PubMed:26921242}.
CC -!- INTERACTION:
CC Q9P802; O94244: mis16; NbExp=2; IntAct=EBI-1148763, EBI-1148703;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:17199038}. Chromosome, centromere
CC {ECO:0000269|PubMed:15369671, ECO:0000269|PubMed:17199038,
CC ECO:0000269|PubMed:26921242}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:15369671}.
CC -!- SIMILARITY: Belongs to the mis18 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01129}.
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DR EMBL; CU329672; CAB72327.2; -; Genomic_DNA.
DR RefSeq; NP_587854.2; NM_001022847.2.
DR PDB; 5HJ0; X-ray; 2.64 A; A/B/C=1-120.
DR PDB; 5J6P; X-ray; 2.60 A; A/B/C=17-118.
DR PDBsum; 5HJ0; -.
DR PDBsum; 5J6P; -.
DR AlphaFoldDB; Q9P802; -.
DR SMR; Q9P802; -.
DR BioGRID; 275346; 18.
DR IntAct; Q9P802; 1.
DR STRING; 4896.SPCC970.12.1; -.
DR iPTMnet; Q9P802; -.
DR MaxQB; Q9P802; -.
DR PaxDb; Q9P802; -.
DR PRIDE; Q9P802; -.
DR EnsemblFungi; SPCC970.12.1; SPCC970.12.1:pep; SPCC970.12.
DR GeneID; 2538763; -.
DR KEGG; spo:SPCC970.12; -.
DR PomBase; SPCC970.12; mis18.
DR VEuPathDB; FungiDB:SPCC970.12; -.
DR eggNOG; ENOG502S9R8; Eukaryota.
DR HOGENOM; CLU_120608_0_0_1; -.
DR InParanoid; Q9P802; -.
DR OMA; WVISHRE; -.
DR PRO; PR:Q9P802; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0098654; C:CENP-A recruiting complex; IDA:PomBase.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051382; P:kinetochore assembly; IMP:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR InterPro; IPR034752; Mis18.
DR InterPro; IPR004910; Yippee/Mis18/Cereblon.
DR Pfam; PF03226; Yippee-Mis18; 1.
DR PROSITE; PS51793; MIS18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm;
KW Kinetochore; Metal-binding; Mitosis; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..194
FT /note="Kinetochore protein mis18"
FT /id="PRO_0000116562"
FT DOMAIN 20..116
FT /note="Mis18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01129"
FT REGION 174..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01129,
FT ECO:0007744|PDB:5HJ0"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01129,
FT ECO:0007744|PDB:5HJ0"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01129,
FT ECO:0007744|PDB:5HJ0"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01129,
FT ECO:0007744|PDB:5HJ0"
FT MUTAGEN 22
FT /note="V->E: Abolishes self-association."
FT /evidence="ECO:0000269|PubMed:26921242"
FT MUTAGEN 31
FT /note="I->A: Abolishes self-association. Loss of function."
FT /evidence="ECO:0000269|PubMed:26921242"
FT MUTAGEN 90
FT /note="Y->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:26921242"
FT MUTAGEN 114
FT /note="Y->A,E: Abolishes self-association. Loss of
FT function."
FT /evidence="ECO:0000269|PubMed:26921242"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:5J6P"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5J6P"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5J6P"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5J6P"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5J6P"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5J6P"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5J6P"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5J6P"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5J6P"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5HJ0"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:5J6P"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:5J6P"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:5J6P"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:5J6P"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5J6P"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5J6P"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5J6P"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:5J6P"
SQ SEQUENCE 194 AA; 22542 MW; 5D9C13F1E3D68193 CRC64;
MSQTETSHSG YIDFKKESQP SVFQCKKCFQ IVGDSNAWVI SHREYLSFTL SDAVENSVRV
EDTFKRSDDG LCVYSELSCT RCNEVIGKVY NSTPIYLDDI RDMYTFSMDK LQAYQLGNKT
VNPEGLTRYQ VDLEMREDII KLKSFCLSLY EKFELHDETL RSVKETISSL KKPKIEGKEG
KKEKARTYSK RTRK
