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 27-MAR-2024, entry version 164. 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; GN 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}. 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; 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 PDB; 8OVW; EM; 3.40 A; U=1-324. DR PDB; 8OVX; EM; 3.40 A; U=1-324. DR PDB; 8OW0; EM; 3.40 A; U=1-324. DR PDB; 8OW1; EM; 3.70 A; U/UU=1-324. DR PDB; 8T0P; X-ray; 1.73 A; B=125-231. DR PDBsum; 6NUW; -. DR PDBsum; 6QLD; -. DR PDBsum; 6QLE; -. DR PDBsum; 6QLF; -. DR PDBsum; 8OVW; -. DR PDBsum; 8OVX; -. DR PDBsum; 8OW0; -. DR PDBsum; 8OW1; -. DR PDBsum; 8T0P; -. DR AlphaFoldDB; P38313; -. DR EMDB; EMD-0523; -. DR EMDB; EMD-17224; -. DR EMDB; EMD-17225; -. DR EMDB; EMD-17226; -. DR EMDB; EMD-17227; -. DR EMDB; EMD-4579; -. DR EMDB; EMD-4580; -. DR EMDB; EMD-4581; -. DR SMR; P38313; -. DR BioGRID; 32908; 305. DR ComplexPortal; CPX-1187; COMA complex. DR ComplexPortal; CPX-2533; Kinetochore CCAN complex. DR DIP; DIP-1588N; -. DR IntAct; P38313; 9. DR MINT; P38313; -. DR STRING; 4932.YBR211C; -. DR GlyGen; P38313; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P38313; -. DR MaxQB; P38313; -. DR PaxDb; 4932-YBR211C; -. DR PeptideAtlas; P38313; -. DR EnsemblFungi; YBR211C_mRNA; YBR211C; YBR211C. DR GeneID; 852512; -. DR KEGG; sce:YBR211C; -. DR AGR; SGD:S000000415; -. 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 OrthoDB; 2038998at2759; -. DR BioCyc; YEAST:G3O-29148-MONOMER; -. DR BioGRID-ORCS; 852512; 7 hits in 10 CRISPR screens. 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. DR InterPro; IPR048743; AME1. DR Pfam; PF20994; CENPU; 1. 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 129..148 FT /evidence="ECO:0007829|PDB:8T0P" FT HELIX 150..159 FT /evidence="ECO:0007829|PDB:8T0P" FT HELIX 165..230 FT /evidence="ECO:0007829|PDB:8T0P" 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 //