FIN1_YEAST
ID FIN1_YEAST Reviewed; 291 AA.
AC Q03898; D6VSB6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Filament protein FIN1;
DE AltName: Full=Filaments in between nuclei protein 1;
GN Name=FIN1; OrderedLocusNames=YDR130C; ORFNames=YD9302.05C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 INDUCTION, SUBCELLULAR LOCATION, AND FILAMENT FORMATION.
RX PubMed=11929974; DOI=10.1073/pnas.072556099;
RA van Hemert M.J., Lamers G.E., Klein D.C., Oosterkamp T.H., Steensma H.Y.,
RA van Heusden G.P.;
RT "The Saccharomyces cerevisiae Fin1 protein forms cell cycle-specific
RT filaments between spindle pole bodies.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5390-5393(2002).
RN [5]
RP DEPHOSPHORYLATION.
RX PubMed=11931638; DOI=10.1042/bj20020053;
RA Mayordomo I., Sanz P.;
RT "The Saccharomyces cerevisiae 14-3-3 protein Bmh2 is required for
RT regulation of the phosphorylation status of Fin1, a novel intermediate
RT filament protein.";
RL Biochem. J. 365:51-56(2002).
RN [6]
RP DIMERIZATION, AND INTERACTION WITH BMH1 AND BMH2.
RX PubMed=12551942; DOI=10.1074/jbc.m212495200;
RA van Hemert M.J., Deelder A.M., Molenaar C., Steensma H.Y.,
RA van Heusden G.P.H.;
RT "Self-association of the spindle pole body-related intermediate filament
RT protein Fin1p and its phosphorylation-dependent interaction with 14-3-3
RT proteins in yeast.";
RL J. Biol. Chem. 278:15049-15055(2003).
RN [7]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-68; SER-74 AND
RP SER-88, AND IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP 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 [10]
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).
CC -!- FUNCTION: Forms cell-cycle specific filaments between the spindle pole
CC bodies of dividing yeast cells.
CC -!- SUBUNIT: Homooligomer; in vitro, FIN1 self-assembles into 10 nm
CC diameter filaments. Interacts with the 14-3-3 proteins BMH1 and BMH2,
CC and the protein phosphatase 1 complex catalytic subunit GLC7.
CC {ECO:0000269|PubMed:12551942}.
CC -!- INTERACTION:
CC Q03898; Q00684: CDC14; NbExp=2; IntAct=EBI-32941, EBI-4192;
CC Q03898; P24869: CLB2; NbExp=2; IntAct=EBI-32941, EBI-4515;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11929974}. Cytoplasm
CC {ECO:0000269|PubMed:11929974}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11929974}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:11929974}. Note=Nuclear during early bud formation,
CC located at the spindle poles during late mitosis, very low abundance in
CC resting cells.
CC -!- INDUCTION: Induced during G2-M transition.
CC {ECO:0000269|PubMed:11929974}.
CC -!- DOMAIN: The coiled coil domain is essential for dimerization.
CC -!- PTM: Phosphorylated by CDC28. Phosphorylation is required for BMH1 and
CC BMH2 interaction. Dephosphorylation by GLC7 depends on the presence of
CC BMH1 and BMH2. {ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Strong overexpression results in the accumulation of
CC filamentous structures resembling the neurofibrillary tangles found in
CC cells of patients with Alzheimer disease.
CC -!- MISCELLANEOUS: Overexpression is lethal in haploids and causes very
CC poor growth in diploids.
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DR EMBL; Z48179; CAA88211.1; -; Genomic_DNA.
DR EMBL; AY557684; AAS56010.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11976.1; -; Genomic_DNA.
DR PIR; S51857; S51857.
DR RefSeq; NP_010415.1; NM_001180438.1.
DR AlphaFoldDB; Q03898; -.
DR SMR; Q03898; -.
DR BioGRID; 32186; 200.
DR DIP; DIP-1342N; -.
DR IntAct; Q03898; 8.
DR MINT; Q03898; -.
DR STRING; 4932.YDR130C; -.
DR iPTMnet; Q03898; -.
DR MaxQB; Q03898; -.
DR PaxDb; Q03898; -.
DR PRIDE; Q03898; -.
DR EnsemblFungi; YDR130C_mRNA; YDR130C; YDR130C.
DR GeneID; 851708; -.
DR KEGG; sce:YDR130C; -.
DR SGD; S000002537; FIN1.
DR VEuPathDB; FungiDB:YDR130C; -.
DR eggNOG; ENOG502S4EM; Eukaryota.
DR HOGENOM; CLU_095077_0_0_1; -.
DR InParanoid; Q03898; -.
DR OMA; IMSPECL; -.
DR BioCyc; YEAST:G3O-29729-MON; -.
DR PRO; PR:Q03898; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03898; protein.
DR GO; GO:0000235; C:astral microtubule; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005882; C:intermediate filament; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0072686; C:mitotic spindle; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IPI:SGD.
DR GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:SGD.
DR GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:SGD.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IDA:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:SGD.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:SGD.
DR InterPro; IPR035260; Fin1.
DR Pfam; PF17300; FIN1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..291
FT /note="Filament protein FIN1"
FT /id="PRO_0000087257"
FT COILED 254..284
FT /evidence="ECO:0000255"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 291 AA; 33186 MW; FD4DB73A50F50172 CRC64;
MSNKSNRRSL RDIGNTIGRN NIPSDKDNVF VRLSMSPLRT TSQKEFLKPP MRISPNKTDG
MKHSIQVTPR RIMSPECLKG YVSKETQSLD RPQFKNSNKN VKIQNSDHIT NIIFPTSPTK
LTFSNENKIG GDGSLTRIRA RFKNGLMSPE RIQQQQQQHI LPSDAKSNTD LCSNTELKDA
PFENDLPRAK LKGKNLLVEL KKEEEDVGNG IESLTKSNTK LNSMLANEGK IHKASFQKSV
KFKLPDNIVT EETVELKEIK DLLLQMLRRQ REIESRLSNI ELQLTEIPKH K
