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2ABD_RAT
ID   2ABD_RAT                Reviewed;         453 AA.
AC   P56932; Q66HR7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform;
DE   AltName: Full=PP2A subunit B isoform B55-delta;
DE   AltName: Full=PP2A subunit B isoform PR55-delta;
DE   AltName: Full=PP2A subunit B isoform R2-delta;
DE   AltName: Full=PP2A subunit B isoform delta;
GN   Name=Ppp2r2d;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=10556517; DOI=10.1016/s0014-5793(99)01377-0;
RA   Strack S., Chang D., Zaucha J.A., Colbran R.J., Wadzinski B.E.;
RT   "Cloning and characterization of B delta, a novel regulatory subunit of
RT   protein phosphatase 2A.";
RL   FEBS Lett. 460:462-466(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: B regulatory subunit of protein phosphatase 2A (PP2A) that
CC       plays a key role in cell cycle by controlling mitosis entry and exit.
CC       The activity of PP2A complexes containing PPP2R2D (PR55-delta)
CC       fluctuate during the cell cycle: the activity is high in interphase and
CC       low in mitosis. During mitosis, activity of PP2A is inhibited via
CC       interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the
CC       PP2A complexes, the B regulatory subunits modulate substrate
CC       selectivity and catalytic activity, and also may direct the
CC       localization of the catalytic enzyme to a particular subcellular
CC       compartment (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC       of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC       regulatory subunit (PR65 or subunit A), that associates with a variety
CC       of regulatory subunits. Proteins that associate with the core dimer
CC       include three families of regulatory subunits B (the R2/B/PR55/B55,
CC       R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable
CC       regulatory subunit, viral proteins, and cell signaling molecules.
CC       Interacts with ENSA (when phosphorylated at 'Ser-67') and ARPP19 (when
CC       phosphorylated at 'Ser-62'), leading to inhibit PP2A activity (By
CC       similarity). Interacts with IER5 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q66LE6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10556517}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with high levels in brain, heart,
CC       placenta, skeletal muscle, testis, thymus and spleen.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; AF180350; AAF08536.1; -; mRNA.
DR   EMBL; BC081720; AAH81720.1; -; mRNA.
DR   RefSeq; NP_653347.2; NM_144746.2.
DR   AlphaFoldDB; P56932; -.
DR   SMR; P56932; -.
DR   STRING; 10116.ENSRNOP00000023139; -.
DR   jPOST; P56932; -.
DR   PaxDb; P56932; -.
DR   PRIDE; P56932; -.
DR   GeneID; 246255; -.
DR   KEGG; rno:246255; -.
DR   UCSC; RGD:708356; rat.
DR   CTD; 55844; -.
DR   RGD; 708356; Ppp2r2d.
DR   eggNOG; KOG1354; Eukaryota.
DR   InParanoid; P56932; -.
DR   OrthoDB; 810409at2759; -.
DR   PhylomeDB; P56932; -.
DR   TreeFam; TF105553; -.
DR   PRO; PR:P56932; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
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   PIRSF; PIRSF037309; PP2A_PR55; 1.
DR   PRINTS; PR00600; PP2APR55.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS01024; PR55_1; 1.
DR   PROSITE; PS01025; PR55_2; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..453
FT                   /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT                   regulatory subunit B delta isoform"
FT                   /id="PRO_0000071435"
FT   REPEAT          32..71
FT                   /note="WD 1"
FT   REPEAT          97..138
FT                   /note="WD 2"
FT   REPEAT          181..219
FT                   /note="WD 3"
FT   REPEAT          230..270
FT                   /note="WD 4"
FT   REPEAT          289..327
FT                   /note="WD 5"
FT   REPEAT          344..385
FT                   /note="WD 6"
FT   REPEAT          420..452
FT                   /note="WD 7"
FT   REGION          385..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36877"
FT   MOD_RES         305
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P36877"
FT   MOD_RES         308
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P36877"
FT   CONFLICT        330
FT                   /note="H -> Q (in Ref. 2; AAH81720)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   453 AA;  51982 MW;  733E80A93A5BC2BB CRC64;
     MAGAGGGGCP TGGNDFQWCF SQVKGAVDED VAEADIISTV EFNYSGDLLA TGDKGGRVVI
     FQREQENKGR AHSRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAHFLLST
     NDKTIKLWKI SERDKRAEGY NLKDEDGRLR DPFRITALRV PILKPMDLMV EASPRRIFAN
     AHTYHINSIS VNSDHETYLS ADDLRINLWH LEITDRSFNI VDIKPANMEE LTEVITAAEF
     HPHQCNVFVY SSSKGTIRLC DMRSSALCDR HAKFFEEPED PSSRSFFSEI ISSISDVKFS
     HSGRYMMTRD YLSVKVWDLN MEGRPVETHH VHEYLRSKLC SLYENDCIFD KFECCWNGSD
     SAIMTGSYNN FFRMFDRNTR RDVTLEASRE NSKPRASLKP RKVCSGGKRK KDEISVDSLD
     FNKKILHTAW HPMESIIAVA ATNNLYIFQD KIN
 
 
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