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MPS2_YEASZ
ID   MPS2_YEASZ              Reviewed;         387 AA.
AC   E7QET1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Monopolar spindle protein 2;
GN   Name=MPS2; Synonyms=MMC1; ORFNames=VL3_1713;
OS   Saccharomyces cerevisiae (strain Zymaflore VL3) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zymaflore VL3;
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that characterize
RT   the genome of industrial strains of Saccharomyces cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
CC   -!- FUNCTION: Component of the spindle pole body (SPB) required for
CC       insertion of the nascent SPB into the nuclear envelope and for the
CC       proper execution of spindle pole body (SPB) duplication. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with BBP1, MPS3, and SPC24. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, spindle pole body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MPS2 family. {ECO:0000305}.
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DR   EMBL; AEJS01000032; EGA86760.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7QET1; -.
DR   SMR; E7QET1; -.
DR   EnsemblFungi; EGA86760; EGA86760; VL3_1713.
DR   HOGENOM; CLU_069890_0_0_1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR   GO; GO:0071988; P:protein localization to spindle pole body; IEA:InterPro.
DR   GO; GO:0030474; P:spindle pole body duplication; IEA:InterPro.
DR   InterPro; IPR031433; Mps2.
DR   Pfam; PF17060; MPS2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Nucleus; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..387
FT                   /note="Monopolar spindle protein 2"
FT                   /id="PRO_0000409168"
FT   TRANSMEM        311..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          216..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          157..269
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        216..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  44558 MW;  CBA0CA86E633834C CRC64;
     MSNGAFDAIF EYAWGQIDKP ISGDFIYGKD LPKLIEIIEN IFQKAQKSGS YELRLPLFSE
     INKDLFRTFS NTKTFFKIHK EEFDDIFFNL VNHPLREILE NAFIGVDSIP SDFIVSMNLN
     SPSKFLVENK SKNTEGAGIS TPRKKLTESP IKLLSRNNIG KALEVQVEEL KRELTAKQSL
     LQENERQVSE LKIRLETYQE KYASIQQRFS DLQKARQVED NQNSSRTSDP GSPLVTGIDQ
     KAILEEFRRR LQRQTDTISF LKDQIRRERG LNCSNDKVSH SKRKHATTDG DGTFKNFISA
     VPSNIWVKAT IRIIVCFALL AGVLPYIRKY VYAHDTPSQN SRLQLSWWEN SGILSKIVWF
     FEDQTDLETE YRSNANVDDA YSRVFGI
 
 
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