CENPH_YEAST
ID CENPH_YEAST Reviewed; 181 AA.
AC Q12262; D6W454;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Inner kinetochore subunit MCM16 {ECO:0000305};
DE AltName: Full=CENP-H homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Constitutive centromere-associated network protein MCM16 {ECO:0000305};
DE AltName: Full=Minichromosome maintenance protein 16;
GN Name=MCM16; OrderedLocusNames=YPR046W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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=9862478; DOI=10.1007/s004380050892;
RA Sanyal K., Ghosh S.K., Sinha P.;
RT "The MCM16 gene of the yeast Saccharomyces cerevisiae is required for
RT chromosome segregation.";
RL Mol. Gen. Genet. 260:242-250(1998).
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 MCM22, 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 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 [7]
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 [8]
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:9862478}.
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 Q12262; Q02732: CTF19; NbExp=2; IntAct=EBI-31487, EBI-5199;
CC Q12262; Q12748: CTF3; NbExp=3; IntAct=EBI-31487, EBI-30457;
CC Q12262; P47167: MCM22; NbExp=6; IntAct=EBI-31487, EBI-25691;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Associated with kinetochores.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CENP-H/MCM16 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z49219; CAA89166.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94993.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11470.1; -; Genomic_DNA.
DR PIR; S54070; S54070.
DR RefSeq; NP_015371.1; NM_001184143.1.
DR PDB; 6OUA; EM; 4.18 A; H=1-181.
DR PDB; 6QLD; EM; 4.15 A; H=4-136.
DR PDB; 6QLE; EM; 3.55 A; H=1-136.
DR PDB; 6WUC; EM; 3.23 A; H=1-181.
DR PDB; 6YPC; X-ray; 2.90 A; H=137-181.
DR PDB; 7L7Q; EM; 3.70 A; H=1-181.
DR PDBsum; 6OUA; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6WUC; -.
DR PDBsum; 6YPC; -.
DR PDBsum; 7L7Q; -.
DR AlphaFoldDB; Q12262; -.
DR SMR; Q12262; -.
DR BioGRID; 36222; 233.
DR ComplexPortal; CPX-1156; Central kinetochore CTF19 complex.
DR DIP; DIP-1430N; -.
DR IntAct; Q12262; 19.
DR MINT; Q12262; -.
DR STRING; 4932.YPR046W; -.
DR MaxQB; Q12262; -.
DR PaxDb; Q12262; -.
DR PRIDE; Q12262; -.
DR EnsemblFungi; YPR046W_mRNA; YPR046W; YPR046W.
DR GeneID; 856159; -.
DR KEGG; sce:YPR046W; -.
DR SGD; S000006250; MCM16.
DR VEuPathDB; FungiDB:YPR046W; -.
DR eggNOG; ENOG502S9DX; Eukaryota.
DR HOGENOM; CLU_096885_0_0_1; -.
DR InParanoid; Q12262; -.
DR OMA; QIHSGYT; -.
DR BioCyc; YEAST:G3O-34201-MON; -.
DR PRO; PR:Q12262; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12262; 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 Coiled coil; Kinetochore; Meiosis; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..181
FT /note="Inner kinetochore subunit MCM16"
FT /id="PRO_0000096281"
FT COILED 112..171
FT /evidence="ECO:0000255"
FT HELIX 4..38
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 47..65
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6WUC"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6WUC"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 110..133
FT /evidence="ECO:0007829|PDB:6WUC"
FT HELIX 151..171
FT /evidence="ECO:0007829|PDB:6YPC"
SQ SEQUENCE 181 AA; 21138 MW; 73E00DC745D54FF0 CRC64;
MTNSSEKQWE RIQQLEKEHV EVYRELLITL DRLYLIRKHN HAVILSHTQQ RLLEIRHQLQ
INLEKTALLI RLLEKPDNTN VLFTKLQNLL EESNSLDYEL LQSLGAQSSL HKQLIESRAE
RDELMSKLIE LSSKFPKPTI PPDDSDTAGK QVEVEKENET IQELMIALQI HSGYTNISYT
I