CENPK_YEAST
ID CENPK_YEAST Reviewed; 239 AA.
AC P47167; D6VWV3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Inner kinetochore subunit MCM22 {ECO:0000305};
DE AltName: Full=CENP-K homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Constitutive centromere-associated network protein MCM22 {ECO:0000305};
DE AltName: Full=Minichromosome maintenance protein 22;
GN Name=MCM22; OrderedLocusNames=YJR135C; ORFNames=J2122;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=9987135; DOI=10.1046/j.1365-2958.1999.01179.x;
RA Poddar A., Roy N., Sinha P.;
RT "MCM21 and MCM22, two novel genes of the yeast Saccharomyces cerevisiae are
RT required for chromosome transmission.";
RL Mol. Microbiol. 31:349-360(1999).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF CTF19 COMPLEX.
RX PubMed=12408861; DOI=10.1016/s0092-8674(02)00973-x;
RA Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,
RA Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.;
RT "Phospho-regulation of kinetochore-microtubule attachments by the Aurora
RT kinase Ipl1p.";
RL Cell 111:163-172(2002).
RN [5]
RP INTERACTION WITH CTF3; CTF19 AND MCM16, AND SUBCELLULAR LOCATION.
RX PubMed=11782448; DOI=10.1101/gad.949302;
RA Measday V., Hailey D.W., Pot I., Givan S.A., Hyland K.M., Cagney G.,
RA Fields S., Davis T.N., Hieter P.;
RT "Ctf3p, the Mis6 budding yeast homolog, interacts with Mcm22p and Mcm16p at
RT the yeast outer kinetochore.";
RL Genes Dev. 16:101-113(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP IDENTIFICATION IN CCAN, AND SUBUNIT.
RX PubMed=22561346; DOI=10.1038/ncb2493;
RA Schleiffer A., Maier M., Litos G., Lampert F., Hornung P., Mechtler K.,
RA Westermann S.;
RT "CENP-T proteins are conserved centromere receptors of the Ndc80 complex.";
RL Nat. Cell Biol. 14:604-613(2012).
CC -!- FUNCTION: Component of the kinetochore, a multiprotein complex that
CC assembles on centromeric DNA and attaches chromosomes to spindle
CC microtubules, mediating chromosome segregation and sister chromatid
CC segregation during meiosis and mitosis. Component of the inner
CC kinetochore constitutive centromere-associated network (CCAN), which
CC serves as a structural platform for outer kinetochore assembly.
CC {ECO:0000269|PubMed:9987135}.
CC -!- SUBUNIT: Component of the heterotrimeric kinetochore subcomplex CTF3,
CC which consists of CTF3, MCM16 and MCM22 (PubMed:11782448). The CTF3
CC subcomplex is part of a larger constitutive centromere-associated
CC network (CCAN) (also known as central kinetochore CTF19 complex in
CC yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19,
CC IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1
CC (PubMed:12408861, PubMed:22561346). Interacts with CTF19
CC (PubMed:11782448). {ECO:0000269|PubMed:11782448,
CC ECO:0000269|PubMed:12408861, ECO:0000269|PubMed:22561346}.
CC -!- INTERACTION:
CC P47167; Q12748: CTF3; NbExp=2; IntAct=EBI-25691, EBI-30457;
CC P47167; Q12262: MCM16; NbExp=6; IntAct=EBI-25691, EBI-31487;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Associated with kinetochores.
CC -!- MISCELLANEOUS: Present with 1026 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CENP-K/MCM22 family. {ECO:0000305}.
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DR EMBL; Z49635; CAA89666.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08919.1; -; Genomic_DNA.
DR PIR; S57158; S57158.
DR RefSeq; NP_012669.1; NM_001181793.1.
DR PDB; 6OUA; EM; 4.18 A; K=1-239.
DR PDB; 6QLD; EM; 4.15 A; K=7-128.
DR PDB; 6QLE; EM; 3.55 A; K=1-133.
DR PDB; 6WUC; EM; 3.23 A; K=1-239.
DR PDB; 6YPC; X-ray; 2.90 A; K=131-239.
DR PDB; 7L7Q; EM; 3.70 A; K=1-239.
DR PDBsum; 6OUA; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6WUC; -.
DR PDBsum; 6YPC; -.
DR PDBsum; 7L7Q; -.
DR AlphaFoldDB; P47167; -.
DR SMR; P47167; -.
DR BioGRID; 33890; 162.
DR ComplexPortal; CPX-1156; Central kinetochore CTF19 complex.
DR DIP; DIP-1431N; -.
DR IntAct; P47167; 8.
DR MINT; P47167; -.
DR STRING; 4932.YJR135C; -.
DR MaxQB; P47167; -.
DR PaxDb; P47167; -.
DR PRIDE; P47167; -.
DR EnsemblFungi; YJR135C_mRNA; YJR135C; YJR135C.
DR GeneID; 853599; -.
DR KEGG; sce:YJR135C; -.
DR SGD; S000003896; MCM22.
DR VEuPathDB; FungiDB:YJR135C; -.
DR eggNOG; ENOG502S4RM; Eukaryota.
DR HOGENOM; CLU_105159_0_0_1; -.
DR InParanoid; P47167; -.
DR OMA; MFFPERS; -.
DR BioCyc; YEAST:G3O-31752-MON; -.
DR PRO; PR:P47167; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47167; protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Kinetochore; Meiosis; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..239
FT /note="Inner kinetochore subunit MCM22"
FT /id="PRO_0000096283"
FT HELIX 7..38
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 70..128
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 139..158
FT /evidence="ECO:0007829|PDB:6YPC"
FT TURN 159..164
FT /evidence="ECO:0007829|PDB:6YPC"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6YPC"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:6YPC"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:6YPC"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:6YPC"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:6YPC"
SQ SEQUENCE 239 AA; 27568 MW; 342C2A95CDBA4878 CRC64;
MDVEKDVLDV YIKNLENQIG NKRYFLKQAQ GAIDEITKRS LDTEGKPVNS EVFTELLRKP
MFFSERADPI GFSLTSNFLS LRAQSSSEWL SLMNDQSVDQ KAMLLLQNNI NSDLKELLRK
LQHQMTIMDS KKQDHAHIRT RKARNKELWD SLADFLKGYL VPNLDDNDES IDSLTNEVML
LMKRLIEHDL NLTLNDFSSK TIPIYRLLLR ANIITVIEGS TNPGTKYIKL IDFNETSLT
