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YPI1_VANPO
ID   YPI1_VANPO              Reviewed;         145 AA.
AC   A7TSJ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Type 1 phosphatases regulator YPI1;
GN   Name=YPI1; ORFNames=Kpol_354p3;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: Regulator of type 1 phosphatases which maintains protein
CC       phosphatase activity under strict control. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the YPI1 family. {ECO:0000305}.
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DR   EMBL; DS480514; EDO14755.1; -; Genomic_DNA.
DR   RefSeq; XP_001642613.1; XM_001642563.1.
DR   AlphaFoldDB; A7TSJ7; -.
DR   STRING; 436907.A7TSJ7; -.
DR   EnsemblFungi; EDO14755; EDO14755; Kpol_354p3.
DR   GeneID; 5542780; -.
DR   KEGG; vpo:Kpol_354p3; -.
DR   eggNOG; KOG4102; Eukaryota.
DR   HOGENOM; CLU_098333_3_0_1; -.
DR   InParanoid; A7TSJ7; -.
DR   OMA; HIQWAED; -.
DR   OrthoDB; 1599272at2759; -.
DR   PhylomeDB; A7TSJ7; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IEA:InterPro.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:InterPro.
DR   InterPro; IPR011107; PPI_Ypi1.
DR   PANTHER; PTHR20835; PTHR20835; 1.
DR   Pfam; PF07491; PPI_Ypi1; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..145
FT                   /note="Type 1 phosphatases regulator YPI1"
FT                   /id="PRO_0000333486"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   145 AA;  17020 MW;  39C34B3516F27722 CRC64;
     MQNQQEEISS TQTTTIEVLP PVLQLRASRD QPSRHDVRWG TDVIDNENMN KKKTKICCIY
     HPQDEDEEGC TSDHQHEEPP ESSSSSSSES ENDKDLGFDE RRKRRVERRR RKLRDNTDSA
     PNAYEVQPDY SEHRKKMMEK KSNNT
 
 
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