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2ABA_CANTR
ID   2ABA_CANTR              Reviewed;         508 AA.
AC   P53031;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Protein phosphatase PP2A regulatory subunit B;
DE   AltName: Full=Cell division control protein 55;
DE   AltName: Full=PR55;
GN   Name=CDC55;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCYC 2512;
RX   PubMed=8923737;
RX   DOI=10.1002/(sici)1097-0061(199610)12:13<1321::aid-yea27>3.0.co;2-6;
RA   Rodriguez P.L., Ali R., Serrano R.;
RT   "CtCdc55p and CtHa13p: two putative regulatory proteins from Candida
RT   tropicalis with long acidic domains.";
RL   Yeast 12:1321-1329(1996).
CC   -!- FUNCTION: Phosphatase 2A affects a variety of biological processes in
CC       the cell such as transcription, cell cycle progression and cellular
CC       morphogenesis, and provides an initial identification of critical
CC       substrates for this phosphatase. The regulatory subunit may direct the
CC       catalytic subunit to distinct, albeit overlapping, subsets of
CC       substrates (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: PP2A exists in several trimeric forms, all of which consist of
CC       a core composed of a catalytic subunit associated with a 65 kDa (PR65)
CC       (Subunit A) and a 55 kDa (PR55) (Subunit B) regulatory subunit.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; X88899; CAA61361.1; -; Genomic_DNA.
DR   PIR; S57751; S57751.
DR   AlphaFoldDB; P53031; -.
DR   SMR; P53031; -.
DR   VEuPathDB; FungiDB:CTMYA2_019400; -.
DR   VEuPathDB; FungiDB:CTRG_01251; -.
DR   GO; GO:0072686; C:mitotic spindle; IEA:EnsemblFungi.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:EnsemblFungi.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0031030; P:negative regulation of septation initiation signaling; IEA:EnsemblFungi.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:EnsemblFungi.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR000009; PP2A_PR55.
DR   InterPro; IPR018067; PP2A_PR55_CS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR11871; PTHR11871; 1.
DR   Pfam; PF00400; WD40; 1.
DR   PIRSF; PIRSF037309; PP2A_PR55; 1.
DR   PRINTS; PR00600; PP2APR55.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS01024; PR55_1; 1.
DR   PROSITE; PS01025; PR55_2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Repeat; WD repeat.
FT   CHAIN           1..508
FT                   /note="Protein phosphatase PP2A regulatory subunit B"
FT                   /id="PRO_0000071440"
FT   REPEAT          19..58
FT                   /note="WD 1"
FT   REPEAT          81..122
FT                   /note="WD 2"
FT   REPEAT          166..204
FT                   /note="WD 3"
FT   REPEAT          215..255
FT                   /note="WD 4"
FT   REPEAT          274..312
FT                   /note="WD 5"
FT   REPEAT          329..370
FT                   /note="WD 6"
FT   REPEAT          477..507
FT                   /note="WD 7"
FT   REGION          369..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..416
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  57914 MW;  619B4C78BBC7A324 CRC64;
     MNLDFSQCFG DKGDIENITE ADIISTVEFD HTGDFLATGD KGGRVVLFER NQSKKKQSCE
     YKFFTEFQSH DAEFDYLKSL EIEEKINKIK WLKSANDSLC LLSTNDKTIK LWKIQERQIK
     LVSENNLNGL NHLPSSNIGI ESLKLPQLQL HDKLISAQPK KIYANAHAYH INSISVNSDQ
     ETYLSADDLR INLWNLGIAD QSFNIVDIKP ANMEELTEVI TSAEFHPLQC NLFMYSSSKG
     TIKLSDMRSN SLCDSHAKIF EEYLDPSSHN FFTEITSSIS DVKFSHDGRY IASRDYMTVK
     IWDLAMENKP IKTIDVHEHL RERLCDTYEN DAIFDKFEVQ FGGDNKSVMT GSYNNQFVIY
     PNAVNTGNDD KPKFKSAFKN SSKRSKKNGF STRTTDDDDD DDDDDDDEEA DDEFDEEVPA
     TKNSPGSQLE DDDEQEEIIL QADKSAFKSK KSGQHPMRRR MTSGVGSNLG REFDDVDFKK
     SILHLSWHPR ENSVAIAATN NLYIFSTL
 
 
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