CENPQ_YEAST
ID CENPQ_YEAST Reviewed; 406 AA.
AC P53298; D6VUW3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Inner kinetochore subunit OKP1 {ECO:0000305};
DE AltName: Full=CENP-Q homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Constitutive centromere-associated network protein OKP1 {ECO:0000305};
DE AltName: Full=Outer kinetochore protein 1 {ECO:0000303|PubMed:10323865};
GN Name=OKP1 {ECO:0000303|PubMed:10323865};
GN OrderedLocusNames=YGR179C {ECO:0000312|SGD:S000003411};
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP INTERACTION WITH CTF19 AND MCM21, AND SUBCELLULAR LOCATION.
RX PubMed=10323865; DOI=10.1101/gad.13.9.1140;
RA Ortiz J., Stemmann O., Rank S., Lechner J.;
RT "A putative protein complex consisting of Ctf19, Mcm21, and Okp1 represents
RT a missing link in the budding yeast kinetochore.";
RL Genes Dev. 13:1140-1155(1999).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF COMA COMPLEX.
RX PubMed=14633972; DOI=10.1101/gad.1144403;
RA De Wulf P., McAinsh A.D., Sorger P.K.;
RT "Hierarchical assembly of the budding yeast kinetochore from multiple
RT subcomplexes.";
RL Genes Dev. 17:2902-2921(2003).
RN [7]
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 [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
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).
RN [13]
RP INTERACTION WITH NKP1 AND NKP2, AND SUBUNIT.
RX PubMed=29046335; DOI=10.15252/embj.201796636;
RA Schmitzberger F., Richter M.M., Gordiyenko Y., Robinson C.V., Dadlez M.,
RA Westermann S.;
RT "Molecular basis for inner kinetochore configuration through RWD domain-
RT peptide interactions.";
RL EMBO J. 36:3458-3482(2017).
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 COMA complex, which connects centromere-associated proteins
CC and the outer kinetochore. COMA interacts with other inner kinetochore
CC proteins to form the inner kinetochore constitutive centromere-
CC associated network (CCAN), which serves as a structural platform for
CC outer kinetochore assembly. {ECO:0000269|PubMed:10323865,
CC ECO:0000269|PubMed:14633972}.
CC -!- SUBUNIT: Component of the heterotetrameric kinetochore subcomplex COMA,
CC which consists of AME1, CTF19, MCM21 and OKP1 (PubMed:14633972). The
CC COMA 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). COMA binds the centromeric
CC nucleosome-binding protein MIF2, and to the outer kinetochore MIND
CC subcomplex. OKP1 interacts directly with AME1, with an NKP1-NKP2 dimer,
CC and with CTF19-MCM21 (PubMed:29046335). {ECO:0000269|PubMed:12408861,
CC ECO:0000269|PubMed:14633972, ECO:0000269|PubMed:22561346,
CC ECO:0000269|PubMed:29046335}.
CC -!- INTERACTION:
CC P53298; P53267: DAM1; NbExp=2; IntAct=EBI-23429, EBI-23268;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:10323865}.
CC -!- MISCELLANEOUS: Present with 2688 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CENP-Q/OKP1 family. {ECO:0000305}.
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DR EMBL; Z72964; CAA97205.1; -; Genomic_DNA.
DR EMBL; AY557837; AAS56163.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08274.1; -; Genomic_DNA.
DR PIR; S64493; S64493.
DR RefSeq; NP_011695.1; NM_001181308.1.
DR PDB; 6NUW; EM; 4.25 A; F=1-406.
DR PDB; 6QLD; EM; 4.15 A; Q=161-391.
DR PDB; 6QLE; EM; 3.55 A; Q=161-406.
DR PDB; 6QLF; EM; 3.45 A; Q=1-406.
DR PDBsum; 6NUW; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6QLE; -.
DR PDBsum; 6QLF; -.
DR AlphaFoldDB; P53298; -.
DR SMR; P53298; -.
DR BioGRID; 33431; 437.
DR ComplexPortal; CPX-1187; COMA complex.
DR DIP; DIP-2382N; -.
DR IntAct; P53298; 20.
DR MINT; P53298; -.
DR STRING; 4932.YGR179C; -.
DR iPTMnet; P53298; -.
DR MaxQB; P53298; -.
DR PaxDb; P53298; -.
DR PRIDE; P53298; -.
DR EnsemblFungi; YGR179C_mRNA; YGR179C; YGR179C.
DR GeneID; 853090; -.
DR KEGG; sce:YGR179C; -.
DR SGD; S000003411; OKP1.
DR VEuPathDB; FungiDB:YGR179C; -.
DR eggNOG; ENOG502S031; Eukaryota.
DR HOGENOM; CLU_058662_0_0_1; -.
DR InParanoid; P53298; -.
DR OMA; PSKIMIG; -.
DR BioCyc; YEAST:G3O-30872-MON; -.
DR PRO; PR:P53298; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53298; protein.
DR GO; GO:0000817; C:COMA complex; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..406
FT /note="Inner kinetochore subunit OKP1"
FT /id="PRO_0000058039"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..340
FT /note="CTF19-MCM21 binding motif"
FT /evidence="ECO:0000250|UniProtKB:Q6CJY0"
FT REGION 353..400
FT /note="Interaction with NKP1-NKP2"
FT /evidence="ECO:0000269|PubMed:29046335"
FT REGION 379..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 239..285
FT /evidence="ECO:0000255"
FT COMPBIAS 9..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 163..183
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 234..292
FT /evidence="ECO:0007829|PDB:6QLF"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6QLF"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 360..380
FT /evidence="ECO:0007829|PDB:6QLF"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:6QLF"
SQ SEQUENCE 406 AA; 47349 MW; F664346B37EEFFF5 CRC64;
MAADRDNFLQ NIENDSINNG QAMDLSPNRS SSESDSSILM NVNDIKTLRL DVAPEAKSTQ
SKKSLFYENS DDAEEGEIEE RTNKEEGQYH HKGSKQLRFE VGKESTGKLQ SHLSDGSATS
GEGNVRPWEF RKVIQAEYRE RLPRNYELKH WKKPSKIMIG SILRLLETNT VSALDSVFEK
YEKEMNQMTH GDNNEVKRIY SKKERLLEII LTKIKKKLRQ AKFPSRISER DLDIEYIYSK
RQFIQNRYSQ ELQNNERLEA ILSREQNLLE ETRKLCMNLK TNNKKRLTEK LIQKDLHPVL
NKAMEYTYGL ESTNGFMHPD GPVTFRNDSH ELNLMLNDPI KSTADVRLDK EEVLSLLPSL
KEYTKKSKEL KETMGQMISD SHEEEIKEVF VPHHESHQDK TEEDIH
