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CENPU_YEAST
ID   CENPU_YEAST             Reviewed;         324 AA.
AC   P38313; D6VQK7;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Inner kinetochore subunit AME1 {ECO:0000305};
DE   AltName: Full=Associated with microtubules and essential protein 1;
DE   AltName: Full=CENP-U homolog {ECO:0000303|PubMed:22561346};
DE   AltName: Full=Constitutive centromere-associated network protein AME1 {ECO:0000305};
GN   Name=AME1; Synonyms=ARP100; OrderedLocusNames=YBR211C; ORFNames=YBR1458;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
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   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   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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-45, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-59 AND SER-101, AND
RP   IDENTIFICATION BY 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-41; SER-45 AND SER-53, AND
RP   IDENTIFICATION BY 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   SUBCELLULAR LOCATION.
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: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, probably via AME1. AME1 interacts directly with OKP1 and an
CC       NKP1-NKP2 dimer (By similarity). {ECO:0000250|UniProtKB:Q6CUE5,
CC       ECO:0000269|PubMed:12408861, ECO:0000269|PubMed:14633972,
CC       ECO:0000269|PubMed:22561346}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC       Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:29046335}.
CC   -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CENP-U/AME1 family. {ECO:0000305}.
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DR   EMBL; Z36080; CAA85175.1; -; Genomic_DNA.
DR   EMBL; AY692799; AAT92818.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07327.1; -; Genomic_DNA.
DR   PIR; S46085; S46085.
DR   RefSeq; NP_009770.3; NM_001178559.3.
DR   PDB; 6NUW; EM; 4.25 A; I=1-324.
DR   PDB; 6QLD; EM; 4.15 A; U=131-320.
DR   PDB; 6QLE; EM; 3.55 A; U=166-324.
DR   PDB; 6QLF; EM; 3.45 A; U=1-320.
DR   PDBsum; 6NUW; -.
DR   PDBsum; 6QLD; -.
DR   PDBsum; 6QLE; -.
DR   PDBsum; 6QLF; -.
DR   AlphaFoldDB; P38313; -.
DR   SMR; P38313; -.
DR   BioGRID; 32908; 299.
DR   ComplexPortal; CPX-1187; COMA complex.
DR   DIP; DIP-1588N; -.
DR   IntAct; P38313; 9.
DR   MINT; P38313; -.
DR   STRING; 4932.YBR211C; -.
DR   iPTMnet; P38313; -.
DR   MaxQB; P38313; -.
DR   PaxDb; P38313; -.
DR   PRIDE; P38313; -.
DR   EnsemblFungi; YBR211C_mRNA; YBR211C; YBR211C.
DR   GeneID; 852512; -.
DR   KEGG; sce:YBR211C; -.
DR   SGD; S000000415; AME1.
DR   VEuPathDB; FungiDB:YBR211C; -.
DR   eggNOG; ENOG502S0ZV; Eukaryota.
DR   HOGENOM; CLU_068947_0_0_1; -.
DR   InParanoid; P38313; -.
DR   OMA; HFVDLMD; -.
DR   BioCyc; YEAST:G3O-29148-MON; -.
DR   PRO; PR:P38313; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38313; protein.
DR   GO; GO:0000817; C:COMA complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0000776; C:kinetochore; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005816; C:spindle pole body; HDA:SGD.
DR   GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0034501; P:protein localization to kinetochore; IMP:SGD.
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..324
FT                   /note="Inner kinetochore subunit AME1"
FT                   /id="PRO_0000064578"
FT   COILED          199..263
FT                   /evidence="ECO:0000255"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   HELIX           132..155
FT                   /evidence="ECO:0007829|PDB:6QLF"
FT   HELIX           171..231
FT                   /evidence="ECO:0007829|PDB:6QLF"
FT   HELIX           234..264
FT                   /evidence="ECO:0007829|PDB:6QLF"
FT   HELIX           289..298
FT                   /evidence="ECO:0007829|PDB:6QLF"
FT   STRAND          301..305
FT                   /evidence="ECO:0007829|PDB:6QLF"
FT   HELIX           306..317
FT                   /evidence="ECO:0007829|PDB:6QLF"
SQ   SEQUENCE   324 AA;  37462 MW;  C53CB31A7B42F6D5 CRC64;
     MDRDTKLAFR LRGSHSRRTD DIDDDVIVFK TPNAVYREEN SPIQSPVQPI LSSPKLANSF
     EFPITTNNVN AQDRHEHGYQ PLDAEDYPMI DSENKSLISE SPQNVRNDED LTTRYNFDDI
     PIRQLSSSIT SVTTIDVLSS LFINLFENDL IPQALKDFNK SDDDQFRKLL YKLDLRLFQT
     ISDQMTRDLK DILDINVSNN ELCYQLKQVL ARKEDLNQQI ISVRNEIQEL KAGKDWHDLQ
     NEQAKLNDKV KLNKRLNDLT STLLGKYEGD RKIMSQDSED DSIRDDSNIL DIAHFVDLMD
     PYNGLLKKIN KINENLSNEL QPSL
 
 
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