BIM1_YEAST
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 03-AUG-2022, entry version 182.
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}.
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; 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; 562.
DR DIP; DIP-1295N; -.
DR IntAct; P40013; 17.
DR MINT; P40013; -.
DR STRING; 4932.YER016W; -.
DR iPTMnet; P40013; -.
DR MaxQB; P40013; -.
DR PaxDb; P40013; -.
DR PRIDE; P40013; -.
DR EnsemblFungi; YER016W_mRNA; YER016W; YER016W.
DR GeneID; 856736; -.
DR KEGG; sce:YER016W; -.
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; EQCGTGG; -.
DR BioCyc; YEAST:G3O-30201-MON; -.
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:0005819; C: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: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; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR036133; EB1_C_sf.
DR InterPro; IPR027328; MAPRE.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR Pfam; PF03271; EB1; 1.
DR SUPFAM; SSF140612; SSF140612; 1.
DR SUPFAM; SSF47576; SSF47576; 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
