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MPS2_ASHGO
ID   MPS2_ASHGO              Reviewed;         338 AA.
AC   Q755A9;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Monopolar spindle protein 2;
GN   Name=MPS2; OrderedLocusNames=AFL084W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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   -!- 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; AE016819; AAS53288.2; -; Genomic_DNA.
DR   RefSeq; NP_985464.2; NM_210818.2.
DR   AlphaFoldDB; Q755A9; -.
DR   SMR; Q755A9; -.
DR   STRING; 33169.AAS53288; -.
DR   EnsemblFungi; AAS53288; AAS53288; AGOS_AFL084W.
DR   GeneID; 4621691; -.
DR   KEGG; ago:AGOS_AFL084W; -.
DR   eggNOG; ENOG502RYE7; Eukaryota.
DR   HOGENOM; CLU_069890_0_0_1; -.
DR   InParanoid; Q755A9; -.
DR   OMA; FIYAKDF; -.
DR   Proteomes; UP000000591; Chromosome VI.
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; 2.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..338
FT                   /note="Monopolar spindle protein 2"
FT                   /id="PRO_0000409155"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   COILED          149..228
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   338 AA;  38451 MW;  18ABE112212BA1BF CRC64;
     MWREEAREQL RRGRCCFAAA SVVSTAKHNK SLGNCTHGSG VMTEAEGILN NVWDAVDSKQ
     QGFIYAKDMP DLVGRFGQFL AQSLTSRAND EAIAAFASEK PFYKLDKEQF KSTFQTLVGT
     SLQTAVELAG HGEPRPRLFG AIRRASATGD EQAREELERK SAELSRVRDE LDEWKSKYQF
     LEREFLFYQT HHENSVDSTQ HEFIISEMKR TIEEQTRMIG QLRRQVQGGT QVLARAGKRA
     SPVDVFMYVS RQGLLLLMRM PKAAFLLLLL GYFVWYTVMG GAVQGPDPSV ALPEPPKQPW
     WEQNNIISAL YWYLTDTFEP SQRINDTVND NYNSLFGL
 
 
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