SHE1_YEAST
ID SHE1_YEAST Reviewed; 338 AA.
AC P38200; D6VPW8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Mitotic spindle-associated protein SHE1;
DE AltName: Full=Sensitive to high expression protein 1;
GN Name=SHE1; OrderedLocusNames=YBL031W; ORFNames=YBL0420;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7725803; DOI=10.1002/yea.320101217;
RA van Dyck L., Jonniaux J.-L., Barreiros T.D.M., Kleine K., Goffeau A.;
RT "Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the
RT ribosomal protein L19 as well as proteins with homologies to components of
RT the hnRNP and snRNP complexes and to the human proliferation-associated
RT p120 antigen.";
RL Yeast 10:1663-1673(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=7762298; DOI=10.1002/yea.320110104;
RA Espinet C., de la Torre M.A., Aldea M., Herrero E.;
RT "An efficient method to isolate yeast genes causing overexpression-mediated
RT growth arrest.";
RL Yeast 11:25-32(1995).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE MITOTIC SPINDLE.
RX PubMed=17634282; DOI=10.1091/mbc.e07-06-0536;
RA Wong J., Nakajima Y., Westermann S., Shang C., Kang J.S., Goodner C.,
RA Houshmand P., Fields S., Chan C.S., Drubin D., Barnes G., Hazbun T.;
RT "A protein interaction map of the mitotic spindle.";
RL Mol. Biol. Cell 18:3800-3809(2007).
RN [9]
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP 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: May have a role related to the spindle integrity function of
CC the DAM1 complex, which is essential for proper chromosome segregation.
CC Causes growth arrest when highly overexpressed.
CC {ECO:0000269|PubMed:17634282, ECO:0000269|PubMed:7762298}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC spindle. Bud neck.
CC -!- MISCELLANEOUS: Present with 264 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SHE1 family. {ECO:0000305}.
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DR EMBL; X77291; CAA54497.1; -; Genomic_DNA.
DR EMBL; Z35792; CAA84851.1; -; Genomic_DNA.
DR EMBL; AY692805; AAT92824.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07088.1; -; Genomic_DNA.
DR PIR; S45765; S45765.
DR RefSeq; NP_009522.1; NM_001178271.1.
DR AlphaFoldDB; P38200; -.
DR BioGRID; 32666; 314.
DR DIP; DIP-2968N; -.
DR IntAct; P38200; 3.
DR MINT; P38200; -.
DR STRING; 4932.YBL031W; -.
DR iPTMnet; P38200; -.
DR PaxDb; P38200; -.
DR PRIDE; P38200; -.
DR TopDownProteomics; P38200; -.
DR EnsemblFungi; YBL031W_mRNA; YBL031W; YBL031W.
DR GeneID; 852249; -.
DR KEGG; sce:YBL031W; -.
DR SGD; S000000127; SHE1.
DR VEuPathDB; FungiDB:YBL031W; -.
DR eggNOG; ENOG502S5DY; Eukaryota.
DR HOGENOM; CLU_821841_0_0_1; -.
DR InParanoid; P38200; -.
DR OMA; KINSAHR; -.
DR BioCyc; YEAST:G3O-28934-MON; -.
DR PRO; PR:P38200; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38200; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; HDA:SGD.
DR GO; GO:0005880; C:nuclear microtubule; IDA:SGD.
DR GO; GO:0005819; C:spindle; IDA:SGD.
DR GO; GO:0008017; F:microtubule binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:SGD.
DR InterPro; IPR031401; She1.
DR Pfam; PF17077; Msap1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome partition; Cytoplasm; Cytoskeleton;
KW Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..338
FT /note="Mitotic spindle-associated protein SHE1"
FT /id="PRO_0000202460"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 338 AA; 38015 MW; 85D0F093A67A9690 CRC64;
MNDKLQEEHN EKDTTSQING FTPPHMSIDF HSNNNSNIIE TIGVSKRLGN SVLSELDSRA
SSKFEFLKDQ SEQQYNGDKN NEPKSGSYNI NEFFQAKHDS QFGQMESLDT HYTLLHTPKR
KSQHAIPQDR SDSMKRSRPS RSIPYTTPVV NDITRRIRRL KLRNSLVNGN DIVARARSMQ
ANSNINSIKN TPLSKPKPFM HKPNFLMPTT NSLNKINSAH RNTSSSSTAS SIPRSKVHRS
ISIRDLHAKT KPVERTPVAQ GTNSQLKNSV SVFDRLYKQT TFSRSTSMNN LSSGTSAKSK
EHTNVKTRLV KSKTSGSLSS NLKQSTATGT KSDRPIWR
