ID   BIK1_YEAST              Reviewed;         440 AA.
AC   P11709; D6VQY6;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Nuclear fusion protein BIK1;
GN   Name=BIK1; OrderedLocusNames=YCL029C; ORFNames=YCL29C;
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 [GENOMIC DNA].
RX   PubMed=3302672; DOI=10.1128/mcb.7.7.2316-2328.1987;
RA   Trueheart J., Boeke J.D., Fink G.R.;
RT   "Two genes required for cell fusion during yeast conjugation: evidence for
RT   a pheromone-induced surface protein.";
RL   Mol. Cell. Biol. 7:2316-2328(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1897318; DOI=10.1002/yea.320070513;
RA   Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.;
RT   "The complete sequence of a 11,953 bp fragment from C1G on chromosome III
RT   encompasses four new open reading frames.";
RL   Yeast 7:533-538(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [4]
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   [5]
RP   POSSIBLE FUNCTION.
RX   PubMed=2277073; DOI=10.1083/jcb.111.6.2573;
RA   Berlin V., Styles C.A., Fink G.R.;
RT   "BIK1, a protein required for microtubule function during mating and
RT   mitosis in Saccharomyces cerevisiae, colocalizes with tubulin.";
RL   J. Cell Biol. 111:2573-2586(1990).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-110, 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).
CC   -!- FUNCTION: Required for nuclear fusion, chromosome disjunction, and
CC       nuclear segregation during mitosis. Probably required for the formation
CC       or stabilization of microtubules during mitosis and for spindle pole
CC       body fusion during conjugation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body. Cytoplasm, cytoskeleton, spindle. Cytoplasm.
CC       Note=And mitotic spindle.
CC   -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; M16717; AAA34614.1; -; Genomic_DNA.
DR   EMBL; X59720; CAA42356.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07455.1; -; Genomic_DNA.
DR   PIR; B27061; B27061.
DR   RefSeq; NP_009901.1; NM_001178674.1.
DR   PDB; 6FC5; X-ray; 1.88 A; A=1-100.
DR   PDB; 6FC6; X-ray; 1.80 A; A=1-100.
DR   PDBsum; 6FC5; -.
DR   PDBsum; 6FC6; -.
DR   AlphaFoldDB; P11709; -.
DR   SMR; P11709; -.
DR   BioGRID; 30954; 251.
DR   DIP; DIP-2341N; -.
DR   IntAct; P11709; 5.
DR   MINT; P11709; -.
DR   STRING; 4932.YCL029C; -.
DR   iPTMnet; P11709; -.
DR   MaxQB; P11709; -.
DR   PaxDb; 4932-YCL029C; -.
DR   PeptideAtlas; P11709; -.
DR   TopDownProteomics; P11709; -.
DR   EnsemblFungi; YCL029C_mRNA; YCL029C; YCL029C.
DR   GeneID; 850328; -.
DR   KEGG; sce:YCL029C; -.
DR   AGR; SGD:S000000534; -.
DR   SGD; S000000534; BIK1.
DR   VEuPathDB; FungiDB:YCL029C; -.
DR   eggNOG; KOG4568; Eukaryota.
DR   HOGENOM; CLU_031641_0_0_1; -.
DR   InParanoid; P11709; -.
DR   OMA; LWCALCE; -.
DR   OrthoDB; 5473150at2759; -.
DR   BioCyc; YEAST:G3O-29290-MONOMER; -.
DR   BioGRID-ORCS; 850328; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P11709; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P11709; Protein.
DR   GO; GO:0005938; C:cell cortex; IDA:SGD.
DR   GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IDA:SGD.
DR   GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR   GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-end; IDA:SGD.
DR   GO; GO:0005819; C:spindle; IDA:SGD.
DR   GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR   GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR   GO; GO:0008017; F:microtubule 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:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
DR   GO; GO:0000022; P:mitotic spindle elongation; IGI:SGD.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:SGD.
DR   GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:SGD.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..440
FT                   /note="Nuclear fusion protein BIK1"
FT                   /id="PRO_0000083513"
FT   DOMAIN          26..69
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT   REGION          108..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          190..397
FT                   /evidence="ECO:0000255"
FT   MOTIF           416..429
FT                   /note="CCHC-box"
FT   COMPBIAS        121..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956"
FT   HELIX           2..5
FT                   /evidence="ECO:0007829|PDB:6FC6"
FT   TURN            6..9
FT                   /evidence="ECO:0007829|PDB:6FC6"
FT   STRAND          11..14
FT                   /evidence="ECO:0007829|PDB:6FC6"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:6FC6"
FT   STRAND          18..26
FT                   /evidence="ECO:0007829|PDB:6FC6"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:6FC6"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:6FC5"
FT   STRAND          45..51
FT                   /evidence="ECO:0007829|PDB:6FC6"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:6FC6"
FT   HELIX           70..79
FT                   /evidence="ECO:0007829|PDB:6FC6"
SQ   SEQUENCE   440 AA;  51092 MW;  9E098B25C431619B CRC64;
     MDRYQRKIGC FIQIPNLGRG QLKYVGPVDT KAGMFAGVDL LANIGKNDGS FMGKKYFQTE
     YPQSGLFIQL QKVASLIEKA SISQTSRRTT MEPLSIPKNR SIVRLTNQFS PMDDPKSPTP
     MRSFRITSRH SGNQQSMDQE ASDHHQQQEF GYDNREDRME VDSILSSDRK ANHNTTSDWK
     PDNGHMNDLN SSEVTIELRE AQLTIEKLQR KQLHYKRLLD DQRMVLEEVQ PTFDRYEATI
     QEREKEIDHL KQQLELERRQ QAKQKQFFDA ENEQLLAVVS QLHEEIKENE ERNLSHNQPT
     GANEDVELLK KQLEQLRNIE DQFELHKTKW AKEREQLKMH NDSLSKEYQN LSKELFLTKP
     QDSSSEEVAS LTKKLEEANE KIKQLEQAQA QTAVESLPIF DPPAPVDTTA GRQQWCEHCD
     TMGHNTAECP HHNPDNQQFF
//