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Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform

Gene

RTS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication
Multicopy suppressor of ROX3 and HSP60.1 Publication

GO - Molecular functioni

  • protein phosphatase type 2A regulator activity Source: SGD

GO - Biological processi

  • cellular bud neck septin ring organization Source: SGD
  • cellular protein localization Source: SGD
  • establishment of protein localization to chromosome Source: SGD
  • meiotic sister chromatid cohesion, centromeric Source: SGD
  • mitotic spindle orientation checkpoint Source: SGD
  • protein dephosphorylation Source: SGD
  • regulation of protein phosphatase type 2A activity Source: GOC
  • septin ring disassembly Source: SGD
  • signal transduction Source: InterPro
  • sister chromatid biorientation Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-33563-MONOMER.
ReactomeiR-SCE-198753. ERK/MAPK targets.
R-SCE-202670. ERKs are inactivated.
R-SCE-389513. CTLA4 inhibitory signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
Alternative name(s):
PP2A, B subunit, B' delta isoform
Protein RTS1
Protein SCS1
Gene namesi
Name:RTS1
Synonyms:SCS1
Ordered Locus Names:YOR014W
ORF Names:OR26.04
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR014W.
SGDiS000005540. RTS1.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • condensed nuclear chromosome, centromeric region Source: SGD
  • cytoplasm Source: UniProtKB-SubCell
  • kinetochore Source: SGD
  • nucleus Source: SGD
  • protein phosphatase type 2A complex Source: InterPro
  • spindle pole body Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 757757Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoformPRO_0000071471Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei242 – 2421PhosphothreonineCombined sources
Modified residuei257 – 2571PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38903.
PeptideAtlasiP38903.

PTM databases

iPTMnetiP38903.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi34419. 213 interactions.
DIPiDIP-4191N.
IntActiP38903. 54 interactions.
MINTiMINT-517460.

Structurei

3D structure databases

ProteinModelPortaliP38903.
SMRiP38903. Positions 285-709.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 227Poly-Ser
Compositional biasi46 – 516Poly-Ser
Compositional biasi98 – 11013Poly-SerAdd
BLAST
Compositional biasi143 – 1475Poly-Ser
Compositional biasi202 – 21312Poly-AsnAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074525.
InParanoidiP38903.
KOiK11584.
OMAiCIENAEV.
OrthoDBiEOG7WDNC5.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 3 hits.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

P38903-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRGFKQRLI KKTTGSSSSS SSKKKDKEKE KEKSSTTSST SKKPASASSS
60 70 80 90 100
SHGTTHSSAS STGSKSTTEK GKQSGSVPSQ GKHHSSSTSK TKTATTPSSS
110 120 130 140 150
SSSSRSSSVS RSGSSSTKKT SSRKGQEQSK QSQQPSQSQK QGSSSSSAAI
160 170 180 190 200
MNPTPVLTVT KDDKSTSGED HAHPTLLGAV SAVPSSPISN ASGTAVSSDV
210 220 230 240 250
ENGNSNNNNM NINTSNTQDA NHASSQSIDI PRSSHSFERL PTPTKLNPDT
260 270 280 290 300
DLELIKTPQR HSSSRFEPSR YTPLTKLPNF NEVSPEERIP LFIAKVDQCN
310 320 330 340 350
TMFDFNDPSF DIQGKEIKRS TLDELIEFLV TNRFTYTNEM YAHVVNMFKI
360 370 380 390 400
NLFRPIPPPV NPVGDIYDPD EDEPVNELAW PHMQAVYEFF LRFVESPDFN
410 420 430 440 450
HQIAKQYIDQ DFILKLLELF DSEDIRERDC LKTTLHRIYG KFLSLRSFIR
460 470 480 490 500
RSMNNIFLQF IYETEKFNGV AELLEILGSI INGFALPLKE EHKVFLVRIL
510 520 530 540 550
IPLHKVRCLS LYHPQLAYCI VQFLEKDPLL TEEVVMGLLR YWPKINSTKE
560 570 580 590 600
IMFLNEIEDI FEVIEPLEFI KVEVPLFVQL AKCISSPHFQ VAEKVLSYWN
610 620 630 640 650
NEYFLNLCIE NAEVILPIIF PALYELTSQL ELDTANGEDS ISDPYMLVEQ
660 670 680 690 700
AINSGSWNRA IHAMAFKALK IFLETNPVLY ENCNALYLSS VKETQQRKVQ
710 720 730 740 750
REENWSKLEE YVKNLRINND KDQYTIKNPE LRNSFNTASE NNTLNEENEN

DCDSEIQ
Length:757
Mass (Da):85,335
Last modified:October 1, 1996 - v2
Checksum:i5A7476C30140331C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951T → S in AAB35312 (PubMed:7565713).Curated
Sequence conflicti529 – 5291L → F in AAB38372 (PubMed:8846889).Curated
Sequence conflicti581 – 5811A → R in AAB38372 (PubMed:8846889).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06630 Genomic DNA. Translation: AAB38372.1.
S79635 Genomic DNA. Translation: AAB35312.1.
X87331 Genomic DNA. Translation: CAA60763.1.
Z74922 Genomic DNA. Translation: CAA99203.1.
BK006948 Genomic DNA. Translation: DAA10797.1.
PIRiS54620.
RefSeqiNP_014657.1. NM_001183433.1.

Genome annotation databases

EnsemblFungiiYOR014W; YOR014W; YOR014W.
GeneIDi854179.
KEGGisce:YOR014W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06630 Genomic DNA. Translation: AAB38372.1.
S79635 Genomic DNA. Translation: AAB35312.1.
X87331 Genomic DNA. Translation: CAA60763.1.
Z74922 Genomic DNA. Translation: CAA99203.1.
BK006948 Genomic DNA. Translation: DAA10797.1.
PIRiS54620.
RefSeqiNP_014657.1. NM_001183433.1.

3D structure databases

ProteinModelPortaliP38903.
SMRiP38903. Positions 285-709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34419. 213 interactions.
DIPiDIP-4191N.
IntActiP38903. 54 interactions.
MINTiMINT-517460.

PTM databases

iPTMnetiP38903.

Proteomic databases

MaxQBiP38903.
PeptideAtlasiP38903.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR014W; YOR014W; YOR014W.
GeneIDi854179.
KEGGisce:YOR014W.

Organism-specific databases

EuPathDBiFungiDB:YOR014W.
SGDiS000005540. RTS1.

Phylogenomic databases

GeneTreeiENSGT00550000074525.
InParanoidiP38903.
KOiK11584.
OMAiCIENAEV.
OrthoDBiEOG7WDNC5.

Enzyme and pathway databases

BioCyciYEAST:G3O-33563-MONOMER.
ReactomeiR-SCE-198753. ERK/MAPK targets.
R-SCE-202670. ERKs are inactivated.
R-SCE-389513. CTLA4 inhibitory signaling.

Miscellaneous databases

NextBioi975981.
PROiP38903.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 3 hits.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rox3 and Rts1 function in the global stress response pathway in baker's yeast."
    Evangelista C.C. Jr., Rodriguez Torres A.M., Limbach M.P., Zitomer R.S.
    Genetics 142:1083-1093(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "SCS1, a multicopy suppressor of hsp60-ts mutant alleles, does not encode a mitochondrially targeted protein."
    Shu Y., Hallberg R.L.
    Mol. Cell. Biol. 15:5618-5626(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    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.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Molecular genetic analysis of Rts1p, a B' regulatory subunit of Saccharomyces cerevisiae protein phosphatase 2A."
    Shu Y., Yang H., Hallberg E., Hallberg R.
    Mol. Cell. Biol. 17:3242-3253(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, PHOSPHORYLATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry namei2A5D_YEAST
AccessioniPrimary (citable) accession number: P38903
Secondary accession number(s): D6W281
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.