ID   SHE1_YEAS7              Reviewed;         338 AA.
AC   A6ZKR6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Mitotic spindle-associated protein SHE1;
DE   AltName: Full=Sensitive to high expression protein 1;
GN   Name=SHE1; ORFNames=SCY_0186;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250}. Bud neck {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SHE1 family. {ECO:0000305}.
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DR   EMBL; AAFW02000011; EDN64585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZKR6; -.
DR   PRIDE; A6ZKR6; -.
DR   TopDownProteomics; A6ZKR6; -.
DR   EnsemblFungi; EDN64585; EDN64585; SCY_0186.
DR   HOGENOM; CLU_821841_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   InterPro; IPR031401; She1.
DR   Pfam; PF17077; Msap1; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm; Cytoskeleton;
KW   Mitosis; Phosphoprotein.
FT   CHAIN           1..338
FT                   /note="Mitotic spindle-associated protein SHE1"
FT                   /id="PRO_0000333423"
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          210..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        210..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:0000250|UniProtKB:P38200"
SQ   SEQUENCE   338 AA;  38003 MW;  1CC00E734874766E 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
     TSIRDLHAKT KPVERTPVAQ GTNSQLKNSV SVFDRLYKQT TFSRSTSMNN LSSGTSAKSK
     EHTNVKTRLV KSKTSGSLSS NLKQSTATGT KSDRPIWR