ID   BIM1_YEAST              Reviewed;         344 AA.
AC   P40013; D3DLR4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Protein BIM1;
GN   Name=BIM1; OrderedLocusNames=YER016W;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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   CHARACTERIZATION.
RX   PubMed=9398684; DOI=10.1091/mbc.8.12.2677;
RA   Schwartz K., Richards K., Botstein D.;
RT   "BIM1 encodes a microtubule-binding protein in yeast.";
RL   Mol. Biol. Cell 8:2677-2691(1997).
RN   [4]
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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [7]
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   [8]
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   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Binds microtubules.
CC   -!- INTERACTION:
CC       P40013; P53267: DAM1; NbExp=2; IntAct=EBI-3614, EBI-23268;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- MISCELLANEOUS: Present with 3630 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
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DR   EMBL; U18778; AAB64549.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07668.1; -; Genomic_DNA.
DR   PIR; S50474; S50474.
DR   RefSeq; NP_010932.1; NM_001178907.1.
DR   PDB; 2QJX; X-ray; 1.90 A; A=1-124.
DR   PDB; 4E61; X-ray; 2.45 A; A/B=182-282.
DR   PDB; 6FC6; X-ray; 1.80 A; B=334-344.
DR   PDBsum; 2QJX; -.
DR   PDBsum; 4E61; -.
DR   PDBsum; 6FC6; -.
DR   AlphaFoldDB; P40013; -.
DR   SMR; P40013; -.
DR   BioGRID; 36749; 568.
DR   DIP; DIP-1295N; -.
DR   IntAct; P40013; 17.
DR   MINT; P40013; -.
DR   STRING; 4932.YER016W; -.
DR   iPTMnet; P40013; -.
DR   MaxQB; P40013; -.
DR   PaxDb; 4932-YER016W; -.
DR   PeptideAtlas; P40013; -.
DR   EnsemblFungi; YER016W_mRNA; YER016W; YER016W.
DR   GeneID; 856736; -.
DR   KEGG; sce:YER016W; -.
DR   AGR; SGD:S000000818; -.
DR   SGD; S000000818; BIM1.
DR   VEuPathDB; FungiDB:YER016W; -.
DR   eggNOG; KOG3000; Eukaryota.
DR   GeneTree; ENSGT00490000043329; -.
DR   HOGENOM; CLU_041744_2_0_1; -.
DR   InParanoid; P40013; -.
DR   OMA; WIKRFWD; -.
DR   OrthoDB; 11676at2759; -.
DR   BioCyc; YEAST:G3O-30201-MONOMER; -.
DR   BioGRID-ORCS; 856736; 7 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P40013; -.
DR   PRO; PR:P40013; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40013; Protein.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:SGD.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-end; IDA:SGD.
DR   GO; GO:0072686; C:mitotic spindle; IDA:SGD.
DR   GO; GO:0051233; C:spindle midzone; IDA:SGD.
DR   GO; GO:0000922; C:spindle pole; IDA:SGD.
DR   GO; GO:0051010; F:microtubule plus-end binding; IDA:SGD.
DR   GO; GO:0030543; P:2-micrometer plasmid partitioning; IMP:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007019; P:microtubule depolymerization; IMP:SGD.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR   GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IGI:SGD.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:SGD.
DR   GO; GO:0030473; P:nuclear migration along microtubule; IMP:SGD.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD.
DR   GO; GO:0035372; P:protein localization to microtubule; IBA:GO_Central.
DR   GO; GO:1904825; P:protein localization to microtubule plus-end; IMP:SGD.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   Gene3D; 1.20.5.1430; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR004953; EB1_C.
DR   InterPro; IPR036133; EB1_C_sf.
DR   InterPro; IPR027328; MAPRE.
DR   PANTHER; PTHR10623:SF6; EB1, ISOFORM F-RELATED; 1.
DR   PANTHER; PTHR10623; MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER; 1.
DR   Pfam; PF03271; EB1; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF140612; EB1 dimerisation domain-like; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51230; EB1_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Cell division; Cytoplasm;
KW   Cytoskeleton; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..344
FT                   /note="Protein BIM1"
FT                   /id="PRO_0000213432"
FT   DOMAIN          6..107
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          188..281
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT   REGION          126..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   HELIX           9..20
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   HELIX           27..32
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   HELIX           34..44
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   HELIX           59..75
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   HELIX           84..87
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   HELIX           92..109
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   TURN            121..123
FT                   /evidence="ECO:0007829|PDB:2QJX"
FT   HELIX           182..239
FT                   /evidence="ECO:0007829|PDB:4E61"
FT   HELIX           260..277
FT                   /evidence="ECO:0007829|PDB:4E61"
SQ   SEQUENCE   344 AA;  38362 MW;  C9087CB46A32BD74 CRC64;
     MSAGIGESRT ELLTWLNGLL NLNYKKIEEC GTGAAYCQIM DSIYGDLPMN RVKFNATAEY
     EFQTNYKILQ SCFSRHGIEK TVYVDKLIRC KFQDNLEFLQ WLKKHWIRHK DESVYDPDAR
     RKYRPIITNN SATKPRTVSN PTTAKRSSST GTGSAMSGGL ATRHSSLGIN GSRKTSVTQG
     QLVAIQAELT KSQETIGSLN EEIEQYKGTV STLEIEREFY FNKLRDIEIL VHTTQDLINE
     GVYKFNDETI TGHGNGNGGA LLRFVKKVES ILYATAEGFE MNDGEDELND KNLGEHGTVP
     NQGGYANSNG EVNGNEGSNH DVIMQNDEGE VGVSNNLIID EETF
//