BIK1_YEAST
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 03-AUG-2022, entry version 186.
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; 242.
DR DIP; DIP-2341N; -.
DR IntAct; P11709; 5.
DR MINT; P11709; -.
DR STRING; 4932.YCL029C; -.
DR iPTMnet; P11709; -.
DR MaxQB; P11709; -.
DR PaxDb; P11709; -.
DR PRIDE; P11709; -.
DR TopDownProteomics; P11709; -.
DR EnsemblFungi; YCL029C_mRNA; YCL029C; YCL029C.
DR GeneID; 850328; -.
DR KEGG; sce:YCL029C; -.
DR SGD; S000000534; BIK1.
DR VEuPathDB; FungiDB:YCL029C; -.
DR eggNOG; KOG4568; Eukaryota.
DR HOGENOM; CLU_031641_0_0_1; -.
DR InParanoid; P11709; -.
DR OMA; QIPNVGR; -.
DR BioCyc; YEAST:G3O-29290-MON; -.
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:0005737; C:cytoplasm; 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:0005634; C:nucleus; IBA:GO_Central.
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:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0030543; P:2-micrometer plasmid partitioning; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 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
