Reviewed, UniProtKB/Swiss-Prot Q00362 (2ABA_YEAST)

Names and origin

Protein names

Recommended name:
    Protein phosphatase PP2A regulatory subunit B
Alternative name(s):
    PR55
    Cell division control protein 55

Gene names

Name:	CDC55
Ordered Locus Names:	YGL190C
ORF Names:	G1345

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates.
Subunit structure	PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa (PR65) (Subunit A) and a 55 kDa (PR55) (Subunit B) regulatory subunit. Interacts with YND1; this interaction mediates adenovirus E4orf4 (early region 4 open reading frame 4) induced toxicity and is disrupted by adenovirus E4orf4, which remains associated with both CDC55 and YND1. Ref.5
Miscellaneous	Present with 8600 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the phosphatase 2A regulatory subunit B family. Contains 7 WD repeats.

Ontologies

Keywords
Biological process	Cell cycle
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	actin filament organization Traceable author statement. Source: SGD budding cell bud growth Traceable author statement. Source: SGD cell cycle Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle spindle assembly checkpoint Inferred from genetic interaction. Source: SGD negative regulation of exit from mitosis Inferred from mutant phenotype. Source: SGD protein amino acid dephosphorylation Traceable author statement. Source: SGD pseudohyphal growth Inferred from mutant phenotype. Source: SGD regulation of translation 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 cellular bud tip Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD protein phosphatase type 2A complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct protein phosphatase type 2A regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESP1	Q03018	2	EBI-1942,EBI-6657
VID22	Q05934	1	EBI-1942,EBI-30350
ZDS2	P54786	1	EBI-1942,EBI-29637

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 526	526	Protein phosphatase PP2A regulatory subunit B		PRO_0000071442
Regions
	Repeat	23 – 62	40	WD 1
	Repeat	82 – 123	42	WD 2
	Repeat	182 – 220	39	WD 3
	Repeat	231 – 271	41	WD 4
	Repeat	290 – 328	39	WD 5
	Repeat	345 – 386	42	WD 6
	Repeat	495 – 525	31	WD 7
	Compositional bias	416 – 419	4	Poly-Ser
Amino acid modifications
	Modified residue	124	1	Phosphoserine Ref.6
	Modified residue	155	1	Phosphoserine Ref.6
	Modified residue	440	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	500	1	I → N in AAA34482. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q00362-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 6DA12C2805FA6A82	FASTA	526	59,662
	10 20 30 40 50 60 MAQNNFDFKF SQCFGDKADI VVTEADLITA VEFDYTGNYL ATGDKGGRVV LFERSNSRHC 70 80 90 100 110 120 EYKFLTEFQS HDAEFDYLKS LEIEEKINEI KWLRPTQRSH FLLSTNDKTI KLWKVYEKNI 130 140 150 160 170 180 KLVSQNNLTE GVTFAKKGKP DNHNSRGGSV RAVLSLQSLK LPQLSQHDKI IAATPKRIYS 190 200 210 220 230 240 NAHTYHINSI SLNSDQETFL SADDLRINLW NLDIPDQSFN IVDIKPTNME ELTEVITSAE 250 260 270 280 290 300 FHPQECNLFM YSSSKGTIKL CDMRQNSLCD NKTKTFEEYL DPINHNFFTE ITSSISDIKF 310 320 330 340 350 360 SPNGRYIASR DYLTVKIWDV NMDNKPLKTI NIHEQLKERL SDTYENDAIF DKFEVNFSGD 370 380 390 400 410 420 SSSVMTGSYN NNFMIYPNVV TSGDNDNGIV KTFDEHNAPN SNSNKNIHNS IQNKDSSSSG 430 440 450 460 470 480 NSHKRRSNGR NTGMVGSSNS SRSSIAGGEG ANSEDSGTEM NEIVLQADKT AFRNKRYGSL 490 500 510 520 AQRSARNKDW GDDIDFKKNI LHFSWHPREN SIAVAATNNL FIFSAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CDC55, a Saccharomyces cerevisiae gene involved in cellular morphogenesis: identification, characterization, and homology to the B subunit of mammalian type 2A protein phosphatase." Healy A.M., Zolnierowicz S., Stapleton A.E., Goebl M., Depaoli-Roach A.A., Pringle J.R. Mol. Cell. Biol. 11:5767-5780(1991) [PubMed: 1656238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII from Saccharomyces cerevisiae." Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V. Yeast 13:55-64(1997) [PubMed: 9046087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"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].
[5]	"YND1 interacts with CDC55 and is a novel mediator of E4orf4-induced toxicity." Maoz T., Koren R., Ben-Ari I., Kleinberger T. J. Biol. Chem. 280:41270-41277(2005) [PubMed: 16227198] [Abstract] Cited for: INTERACTION WITH YND1.
[6]	"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-124; SER-155 AND SER-440, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M72716 Genomic DNA. Translation: AAA34482.1. X91837 Genomic DNA. Translation: CAA62954.1. X91489 Genomic DNA. Translation: CAA62785.1. Z72712 Genomic DNA. Translation: CAA96902.1.
PIR	A41698.
RefSeq	NP_011325.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2281N.
IntAct	Q00362. 64 interactions.
STRING	Q00362.
Proteomic databases
PeptideAtlas	Q00362.
Genome annotation databases
Ensembl	YGL190C; YGL190C; YGL190C; Saccharomyces cerevisiae. [Genome view]
GeneID	852685.
KEGG	sce:YGL190C.
NMPDR	fig|4932.3.peg.2428.
Organism-specific databases
CYGD	YGL190c.
SGD	S000003158. CDC55.
Phylogenomic databases
HOGENOM	Q00362.
OMA	ENSIAVA
OrthoDB	EOG9W6QC8
Gene expression databases
ArrayExpress	Q00362.
Genevestigator	Q00362.
GermOnline	YGL190C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019578. PP2A_Bsu_A/B_central-region. IPR000009. PP2A_PR55. IPR018067. PP2A_PR55_CS. IPR019573. PP2A_suB_N. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019775. WD40_repeat_CS. IPR019781. WD40_repeat_sg. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PANTHER	PTHR11871. Pp2A_PR55. 1 hit.
Pfam	PF10586. PP2A_B_N. 1 hit. PF10594. PP2A_B_subs_rcg. 1 hit. PF00400. WD40. 1 hit. [Graphical view]
PIRSF	PIRSF037309. PP2A_PR55. 1 hit.
PRINTS	PR00600. PP2APR55.
SMART	SM00320. WD40. 5 hits. [Graphical view]
PROSITE	PS01024. PR55_1. 1 hit. PS01025. PR55_2. 1 hit. PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. False negative. PS50294. WD_REPEATS_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	972008.

Entry information

Entry name

2ABA_YEAST

Accession

Primary (citable) accession number: Q00362

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 1, 1996
Last modified:	November 24, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)