2A5D_YEAST
ID 2A5D_YEAST Reviewed; 757 AA.
AC P38903; D6W281;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform;
DE AltName: Full=PP2A, B subunit, B' delta isoform;
DE AltName: Full=Protein RTS1;
DE AltName: Full=Protein SCS1;
GN Name=RTS1; Synonyms=SCS1; OrderedLocusNames=YOR014W; ORFNames=OR26.04;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8846889; DOI=10.1093/genetics/142.4.1083;
RA Evangelista C.C. Jr., Rodriguez Torres A.M., Limbach M.P., Zitomer R.S.;
RT "Rox3 and Rts1 function in the global stress response pathway in baker's
RT yeast.";
RL Genetics 142:1083-1093(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=7565713; DOI=10.1128/mcb.15.10.5618;
RA Shu Y., Hallberg R.L.;
RT "SCS1, a multicopy suppressor of hsp60-ts mutant alleles, does not encode a
RT mitochondrially targeted protein.";
RL Mol. Cell. Biol. 15:5618-5626(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, SUBUNIT, AND PHOSPHORYLATION.
RX PubMed=9154823; DOI=10.1128/mcb.17.6.3242;
RA Shu Y., Yang H., Hallberg E., Hallberg R.;
RT "Molecular genetic analysis of Rts1p, a B' regulatory subunit of
RT Saccharomyces cerevisiae protein phosphatase 2A.";
RL Mol. Cell. Biol. 17:3242-3253(1997).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment.
CC {ECO:0000269|PubMed:9154823}.
CC -!- FUNCTION: Multicopy suppressor of ROX3 and HSP60.
CC {ECO:0000269|PubMed:9154823}.
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 {ECO:0000269|PubMed:9154823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7565713}. Nucleus
CC {ECO:0000269|PubMed:7565713}.
CC -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; U06630; AAB38372.1; -; Genomic_DNA.
DR EMBL; S79635; AAB35312.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60763.1; -; Genomic_DNA.
DR EMBL; Z74922; CAA99203.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10797.1; -; Genomic_DNA.
DR PIR; S54620; S54620.
DR RefSeq; NP_014657.1; NM_001183433.1.
DR AlphaFoldDB; P38903; -.
DR SMR; P38903; -.
DR BioGRID; 34419; 448.
DR ComplexPortal; CPX-1857; Serine/threonine-protein phosphatase PP2A variant 2.
DR ComplexPortal; CPX-1858; Serine/threonine-protein phosphatase PP2A variant 4.
DR DIP; DIP-4191N; -.
DR IntAct; P38903; 53.
DR MINT; P38903; -.
DR STRING; 4932.YOR014W; -.
DR iPTMnet; P38903; -.
DR MaxQB; P38903; -.
DR PaxDb; P38903; -.
DR PRIDE; P38903; -.
DR EnsemblFungi; YOR014W_mRNA; YOR014W; YOR014W.
DR GeneID; 854179; -.
DR KEGG; sce:YOR014W; -.
DR SGD; S000005540; RTS1.
DR VEuPathDB; FungiDB:YOR014W; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_1_0_1; -.
DR InParanoid; P38903; -.
DR OMA; CSHEYNE; -.
DR BioCyc; YEAST:G3O-33563-MON; -.
DR PRO; PR:P38903; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38903; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IPI:ComplexPortal.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0070199; P:establishment of protein localization to chromosome; IMP:SGD.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IMP:SGD.
DR GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IGI:SGD.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IGI:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0031107; P:septin ring disassembly; IMP:SGD.
DR GO; GO:0031134; P:sister chromatid biorientation; IGI:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..757
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit delta isoform"
FT /id="PRO_0000071471"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 95
FT /note="T -> S (in Ref. 2; AAB35312)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="L -> F (in Ref. 1; AAB38372)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="A -> R (in Ref. 1; AAB38372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 85335 MW; 5A7476C30140331C CRC64;
MMRGFKQRLI KKTTGSSSSS SSKKKDKEKE KEKSSTTSST SKKPASASSS SHGTTHSSAS
STGSKSTTEK GKQSGSVPSQ GKHHSSSTSK TKTATTPSSS SSSSRSSSVS RSGSSSTKKT
SSRKGQEQSK QSQQPSQSQK QGSSSSSAAI MNPTPVLTVT KDDKSTSGED HAHPTLLGAV
SAVPSSPISN ASGTAVSSDV ENGNSNNNNM NINTSNTQDA NHASSQSIDI PRSSHSFERL
PTPTKLNPDT DLELIKTPQR HSSSRFEPSR YTPLTKLPNF NEVSPEERIP LFIAKVDQCN
TMFDFNDPSF DIQGKEIKRS TLDELIEFLV TNRFTYTNEM YAHVVNMFKI NLFRPIPPPV
NPVGDIYDPD EDEPVNELAW PHMQAVYEFF LRFVESPDFN HQIAKQYIDQ DFILKLLELF
DSEDIRERDC LKTTLHRIYG KFLSLRSFIR RSMNNIFLQF IYETEKFNGV AELLEILGSI
INGFALPLKE EHKVFLVRIL IPLHKVRCLS LYHPQLAYCI VQFLEKDPLL TEEVVMGLLR
YWPKINSTKE IMFLNEIEDI FEVIEPLEFI KVEVPLFVQL AKCISSPHFQ VAEKVLSYWN
NEYFLNLCIE NAEVILPIIF PALYELTSQL ELDTANGEDS ISDPYMLVEQ AINSGSWNRA
IHAMAFKALK IFLETNPVLY ENCNALYLSS VKETQQRKVQ REENWSKLEE YVKNLRINND
KDQYTIKNPE LRNSFNTASE NNTLNEENEN DCDSEIQ
