PP4R2_ASHGO
ID PP4R2_ASHGO Reviewed; 356 AA.
AC Q75D77;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2;
DE Short=PP4R2;
GN Name=PSY4; OrderedLocusNames=ABR147C;
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, AND SEQUENCE REVISION TO 84 AND 90.
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: Regulatory subunit of the histone H2A phosphatase complex,
CC which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced
CC from sites of DNA lesions in the double-stranded DNA break repair
CC process. Dephosphorylation is necessary for efficient recovery from the
CC DNA damage checkpoint (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Regulatory subunit (R2) of the histone H2A phosphatase complex
CC (HTP-C) consisting of PPH3, PSY2 and PSY4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP4R2 family. {ECO:0000305}.
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DR EMBL; AE016815; AAS50918.2; -; Genomic_DNA.
DR RefSeq; NP_983094.2; NM_208447.2.
DR AlphaFoldDB; Q75D77; -.
DR STRING; 33169.AAS50918; -.
DR EnsemblFungi; AAS50918; AAS50918; AGOS_ABR147C.
DR GeneID; 4619204; -.
DR KEGG; ago:AGOS_ABR147C; -.
DR eggNOG; ENOG502S2WZ; Eukaryota.
DR HOGENOM; CLU_036743_1_0_1; -.
DR InParanoid; Q75D77; -.
DR OMA; ESAPEEC; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR InterPro; IPR015267; PPP4R2.
DR PANTHER; PTHR16487; PTHR16487; 1.
DR Pfam; PF09184; PPP4R2; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome.
FT CHAIN 1..356
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 2"
FT /id="PRO_0000223652"
FT REGION 202..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 38798 MW; 10F8668A972D1BF0 CRC64;
MQSGEESRLG IKCASLHEEL TQIVIDQDVG PLQRVPASEF LARLVEHMGQ TIPREVFGAE
AETGTRDLER LGAIVAYIDE NFAAQNVLPF TIQRICELCY HPLHYFRVGE LRKFVNALEK
VCYVRSSWSA GYGAVPSPAE GTPTREASVD VSMSKIPWLP DDGGRDLRQF IEKIESIVSV
NFGYEDDEDE GRDAAIQEYY DNEGAGDDED DDQDYVDEDS ATSEDEEEDV EEEEEEEGPE
PEVGLEPVHA ESAPEECVGT NKRTTAERED CHMQPCAAAH STDGAHPCGL KRSKLQEDGA
TMASPPDIVA EGGSHDPQVV DASKPPQLTT SATNVSCNAS IEATVSLDDD STAGGE
