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Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A, B subunit, B' delta isoform) (Protein RTS1) (Protein SCS1)

 2A5D_YEAST              Reviewed;         757 AA.
P38903; D6W281;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
12-SEP-2018, entry version 164.
RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform;
AltName: Full=PP2A, B subunit, B' delta isoform;
AltName: Full=Protein RTS1;
AltName: Full=Protein SCS1;
Name=RTS1; Synonyms=SCS1; OrderedLocusNames=YOR014W; ORFNames=OR26.04;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8846889;
Evangelista C.C. Jr., Rodriguez Torres A.M., Limbach M.P.,
Zitomer R.S.;
"Rox3 and Rts1 function in the global stress response pathway in
baker's yeast.";
Genetics 142:1083-1093(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
PubMed=7565713; DOI=10.1128/MCB.15.10.5618;
Shu Y., Hallberg R.L.;
"SCS1, a multicopy suppressor of hsp60-ts mutant alleles, does not
encode a mitochondrially targeted protein.";
Mol. Cell. Biol. 15:5618-5626(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION, SUBUNIT, AND PHOSPHORYLATION.
PubMed=9154823; DOI=10.1128/MCB.17.6.3242;
Shu Y., Yang H., Hallberg E., Hallberg R.;
"Molecular genetic analysis of Rts1p, a B' regulatory subunit of
Saccharomyces cerevisiae protein phosphatase 2A.";
Mol. Cell. Biol. 17:3242-3253(1997).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: The B regulatory subunit might modulate substrate
selectivity and catalytic activity, and also might direct the
localization of the catalytic enzyme to a particular subcellular
compartment. {ECO:0000269|PubMed:9154823}.
-!- FUNCTION: Multicopy suppressor of ROX3 and HSP60.
{ECO:0000269|PubMed:9154823}.
-!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
constant regulatory subunit (PR65 or subunit A), that associates
with a variety of regulatory subunits. Proteins that associate
with the core dimer include three families of regulatory subunits
B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
families), the 48 kDa variable regulatory subunit, viral proteins,
and cell signaling molecules. {ECO:0000269|PubMed:9154823}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7565713}.
Nucleus {ECO:0000269|PubMed:7565713}.
-!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
family. {ECO:0000305}.
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EMBL; U06630; AAB38372.1; -; Genomic_DNA.
EMBL; S79635; AAB35312.1; -; Genomic_DNA.
EMBL; X87331; CAA60763.1; -; Genomic_DNA.
EMBL; Z74922; CAA99203.1; -; Genomic_DNA.
EMBL; BK006948; DAA10797.1; -; Genomic_DNA.
PIR; S54620; S54620.
RefSeq; NP_014657.1; NM_001183433.1.
ProteinModelPortal; P38903; -.
SMR; P38903; -.
BioGrid; 34419; 441.
ComplexPortal; CPX-1857; Serine/threonine-protein phosphatase PP2A variant 2.
ComplexPortal; CPX-1858; Serine/threonine-protein phosphatase PP2A variant 4.
DIP; DIP-4191N; -.
IntAct; P38903; 53.
MINT; P38903; -.
STRING; 4932.YOR014W; -.
iPTMnet; P38903; -.
MaxQB; P38903; -.
PaxDb; P38903; -.
PRIDE; P38903; -.
EnsemblFungi; YOR014W; YOR014W; YOR014W.
GeneID; 854179; -.
KEGG; sce:YOR014W; -.
EuPathDB; FungiDB:YOR014W; -.
SGD; S000005540; RTS1.
GeneTree; ENSGT00550000074525; -.
InParanoid; P38903; -.
KO; K11584; -.
OMA; DIYTMKA; -.
OrthoDB; EOG092C35SR; -.
BioCyc; YEAST:G3O-33563-MONOMER; -.
Reactome; R-SCE-198753; ERK/MAPK targets.
Reactome; R-SCE-202670; ERKs are inactivated.
Reactome; R-SCE-389513; CTLA4 inhibitory signaling.
Reactome; R-SCE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
PRO; PR:P38903; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000776; C:kinetochore; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
GO; GO:0005816; C:spindle pole body; IDA:SGD.
GO; GO:0019888; F:protein phosphatase regulator activity; IDA:SGD.
GO; GO:0032186; P:cellular bud neck septin ring organization; IMP:SGD.
GO; GO:0034613; P:cellular protein localization; IMP:SGD.
GO; GO:0070199; P:establishment of protein localization to chromosome; IMP:SGD.
GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IMP:SGD.
GO; GO:0031578; P:mitotic spindle orientation checkpoint; IGI:SGD.
GO; GO:2000786; P:positive regulation of autophagosome assembly; IGI:SGD.
GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
GO; GO:0031107; P:septin ring disassembly; IMP:SGD.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0031134; P:sister chromatid biorientation; IGI:SGD.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002554; PP2A_B56.
PANTHER; PTHR10257; PTHR10257; 1.
Pfam; PF01603; B56; 1.
PIRSF; PIRSF028043; PP2A_B56; 1.
SUPFAM; SSF48371; SSF48371; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 757 Serine/threonine-protein phosphatase 2A
56 kDa regulatory subunit delta isoform.
/FTId=PRO_0000071471.
COMPBIAS 16 22 Poly-Ser.
COMPBIAS 46 51 Poly-Ser.
COMPBIAS 98 110 Poly-Ser.
COMPBIAS 143 147 Poly-Ser.
COMPBIAS 202 213 Poly-Asn.
MOD_RES 242 242 Phosphothreonine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 257 257 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
CONFLICT 95 95 T -> S (in Ref. 2; AAB35312).
{ECO:0000305}.
CONFLICT 529 529 L -> F (in Ref. 1; AAB38372).
{ECO:0000305}.
CONFLICT 581 581 A -> R (in Ref. 1; AAB38372).
{ECO:0000305}.
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


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