P38903 (2A5D_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RTS1
Synonyms:	SCS1
Ordered Locus Names:	YOR014W
ORF Names:	OR26.04

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	757 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5 Multicopy suppressor of ROX3 and HSP60. Ref.5
Subunit structure	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. Ref.5
Subcellular location	Cytoplasm. Nucleus Ref.2.
Miscellaneous	Present with 300 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the phosphatase 2A regulatory subunit B family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular protein localization Inferred from mutant phenotype. Source: SGD meiotic sister chromatid cohesion, centromeric Inferred from mutant phenotype. Source: SGD mitotic cell cycle spindle orientation checkpoint Inferred from genetic interaction. Source: SGD protein dephosphorylation Inferred from mutant phenotype. Source: SGD signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cellular bud neck Inferred from direct assay. Source: SGD condensed nuclear chromosome, centromeric region Inferred from direct assay. Source: SGD protein phosphatase type 2A complex Inferred from electronic annotation. Source: InterPro spindle pole body Inferred from direct assay. Source: SGD
Molecular function	binding Inferred from electronic annotation. Source: InterPro protein phosphatase type 2A regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 757	757	Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform		PRO_0000071471
Regions
	Compositional bias	16 – 22	7	Poly-Ser
	Compositional bias	46 – 51	6	Poly-Ser
	Compositional bias	98 – 110	13	Poly-Ser
	Compositional bias	143 – 147	5	Poly-Ser
	Compositional bias	202 – 213	12	Poly-Asn
Amino acid modifications
	Modified residue	236	1	Phosphoserine Ref.11
	Modified residue	242	1	Phosphothreonine Ref.8 Ref.11
	Modified residue	257	1	Phosphothreonine Ref.10 Ref.11
	Modified residue	272	1	Phosphothreonine Ref.7 Ref.9 Ref.10 Ref.11
Experimental info
	Sequence conflict	95	1	T → S in AAB35312. Ref.2
	Sequence conflict	529	1	L → F in AAB38372. Ref.1
	Sequence conflict	581	1	A → R in AAB38372. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38903 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 5A7476C30140331C	FASTA	757	85,335
	10 20 30 40 50 60 MMRGFKQRLI KKTTGSSSSS SSKKKDKEKE KEKSSTTSST SKKPASASSS SHGTTHSSAS 70 80 90 100 110 120 STGSKSTTEK GKQSGSVPSQ GKHHSSSTSK TKTATTPSSS SSSSRSSSVS RSGSSSTKKT 130 140 150 160 170 180 SSRKGQEQSK QSQQPSQSQK QGSSSSSAAI MNPTPVLTVT KDDKSTSGED HAHPTLLGAV 190 200 210 220 230 240 SAVPSSPISN ASGTAVSSDV ENGNSNNNNM NINTSNTQDA NHASSQSIDI PRSSHSFERL 250 260 270 280 290 300 PTPTKLNPDT DLELIKTPQR HSSSRFEPSR YTPLTKLPNF NEVSPEERIP LFIAKVDQCN 310 320 330 340 350 360 TMFDFNDPSF DIQGKEIKRS TLDELIEFLV TNRFTYTNEM YAHVVNMFKI NLFRPIPPPV 370 380 390 400 410 420 NPVGDIYDPD EDEPVNELAW PHMQAVYEFF LRFVESPDFN HQIAKQYIDQ DFILKLLELF 430 440 450 460 470 480 DSEDIRERDC LKTTLHRIYG KFLSLRSFIR RSMNNIFLQF IYETEKFNGV AELLEILGSI 490 500 510 520 530 540 INGFALPLKE EHKVFLVRIL IPLHKVRCLS LYHPQLAYCI VQFLEKDPLL TEEVVMGLLR 550 560 570 580 590 600 YWPKINSTKE IMFLNEIEDI FEVIEPLEFI KVEVPLFVQL AKCISSPHFQ VAEKVLSYWN 610 620 630 640 650 660 NEYFLNLCIE NAEVILPIIF PALYELTSQL ELDTANGEDS ISDPYMLVEQ AINSGSWNRA 670 680 690 700 710 720 IHAMAFKALK IFLETNPVLY ENCNALYLSS VKETQQRKVQ REENWSKLEE YVKNLRINND 730 740 750 KDQYTIKNPE LRNSFNTASE NNTLNEENEN DCDSEIQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8846889] [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: 7565713] [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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 9154823] [Abstract] Cited for: FUNCTION, SUBUNIT, PHOSPHORYLATION.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-272, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, MASS SPECTROMETRY. Strain: ADR376.
[9]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-272, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 AND THR-272, MASS SPECTROMETRY.
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; THR-242; THR-257 AND THR-272, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S54620.
RefSeq	NP_014657.1. NM_001183433.1.
3D structure databases
ProteinModelPortal	P38903.
SMR	P38903. Positions 284-711.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4191N.
IntAct	P38903. 56 interactions.
MINT	MINT-517460.
STRING	P38903.
Proteomic databases
PeptideAtlas	P38903.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR014W; YOR014W; YOR014W.
GeneID	854179.
KEGG	sce:YOR014W.
NMPDR	fig|4932.3.peg.5754.
Organism-specific databases
CYGD	YOR014w.
SGD	S000005540. RTS1.
Phylogenomic databases
eggNOG	fuNOG06847.
GeneTree	EFGT00050000000169.
HOGENOM	HBG602178.
OMA	CIENAEV.
OrthoDB	EOG496317.
Gene expression databases
ArrayExpress	P38903.
Genevestigator	P38903.
GermOnline	YOR014W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR002554. PP2A_B56. [Graphical view]
KO	K11584.
PANTHER	PTHR10257. B56. 1 hit.
Pfam	PF01603. B56. 2 hits. [Graphical view]
PIRSF	PIRSF028043. PP2A_B56. 1 hit.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
NextBio	975981.

Entry information

Entry name

2A5D_YEAST

Accession

Primary (citable) accession number: P38903
Secondary accession number(s): D6W281

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program