Serine/threonine-protein phosphatase 2B catalytic subunit A2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P14747 (PP2B2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 132. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit A2
EC=3.1.3.16

Alternative name(s):
Calcineurin A2
Calmodulin-binding protein 2

Gene names

Name:	CMP2
Synonyms:	CNA2
Ordered Locus Names:	YML057W
ORF Names:	YM9958.05

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	604 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate.
Cofactor	Binds 1 Fe³⁺ ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.
Miscellaneous	Present with 7110 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the PPP phosphatase family. PP-2B subfamily.
Caution	Was originally (Ref.5) thought to originate from a rabbit cDNA library and was known as protein phosphatase 2Bw (PP2Bw).

Ontologies

Keywords
Ligand	Calmodulin-binding Iron Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Inferred from mutant phenotype Ref.1. Source: SGD cellular ion homeostasis Inferred from mutant phenotype PubMed 8798496. Source: SGD
Cellular_component	calcineurin complex Inferred from direct assay PubMed 1321337. Source: SGD cytoplasm Traceable author statement PubMed 9123967. Source: SGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CNB1	P25296	6	EBI-12778,EBI-3968

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 604

604

Serine/threonine-protein phosphatase 2B catalytic subunit A2

PRO_0000058837

Regions

Region

501 – 523

Calmodulin-binding Potential

Sites

Active site

205

Proton donor By similarity

Metal binding

144

Iron By similarity

Metal binding

146

Iron By similarity

Metal binding

172

Iron By similarity

Metal binding

172

Zinc By similarity

Metal binding

204

Zinc By similarity

Metal binding

253

Zinc By similarity

Metal binding

359

Zinc By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.8

Modified residue

Phosphothreonine Ref.7 Ref.8

Modified residue

489

Phosphoserine Ref.8

Modified residue

520

Phosphoserine Potential

Experimental info

Sequence conflict

87 – 88

EL → DV in CAA38712. Ref.2

Sequence conflict

581

N → K in CAA34722. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P14747 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: 4A605598FD04207F
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FASTA

604

68,528

        10         20         30         40         50         60 
MSSDAIRNTE QINAAIKIIE NKTERPQSST TPIDSKASTV AAANSTATET SRDLTQYTLD 

        70         80         90        100        110        120 
DGRVVSTNRR IMNKVPAITS HVPTDEELFQ PNGIPRHEFL RDHFKREGKL SAAQAARIVT 

       130        140        150        160        170        180 
LATELFSKEP NLISVPAPIT VCGDIHGQYF DLLKLFEVGG DPATTSYLFL GDYVDRGSFS 

       190        200        210        220        230        240 
FECLIYLYSL KLNFNDHFWL LRGNHECKHL TSYFTFKNEM LHKYNLDIYE KCCESFNNLP 

       250        260        270        280        290        300 
LAALMNGQYL CVHGGISPEL NSLQDINNLN RFREIPSHGL MCDLLWADPI EEYDEVLDKD 

       310        320        330        340        350        360 
LTEEDIVNSK TMVPHHGKMA PSRDMFVPNS VRGCSYAFTY RAACHFLQET GLLSIIRAHE 

       370        380        390        400        410        420 
AQDAGYRMYK NTKTLGFPSL LTLFSAPNYL DTYNNKAAIL KYENNVMNIR QFNMTPHPYW 

       430        440        450        460        470        480 
LPDFMDVFTW SLPFVGEKVT EMLVAILNIC TEDELENDTP VIEELVGTDK KLPQAGKSEA 

       490        500        510        520        530        540 
TPQPATSASP KHASILDDEH RRKALRNKIL AVAKVSRMYS VLREETNKVQ FLKDHNSGVL 

       550        560        570        580        590        600 
PRGALSNGVK GLDEALSTFE RARKHDLINE KLPPSLDELK NENKKYYEKV WQKVHEHDAK 


NDSK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase." Cyert M.S., Kunisawa R., Kaim D., Thorner J. Proc. Natl. Acad. Sci. U.S.A. 88:7376-7380(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[2]	"The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B." Liu Y., Ishii S., Tokai M., Tsutsumi H., Ohki O., Akada R., Tanaka K., Tsuchiya E., Fukui S., Miyakawa T. Mol. Gen. Genet. 227:52-59(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Isolation of a cDNA likely to encode a novel Ca2+-dependent/calmodulin-stimulated protein phosphatase." da Cruz e Silva E.F., Cohen P.T.W. Biochim. Biophys. Acta 1009:293-296(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 100-604.
[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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, MASS SPECTROMETRY.
[8]	"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-30; THR-31 AND SER-489, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64840 Genomic DNA. Translation: AAA34466.1. X16804 mRNA. Translation: CAA34722.1. Z46729 Genomic DNA. Translation: CAA86718.1. X54964 Genomic DNA. Translation: CAA38712.1. BK006946 Genomic DNA. Translation: DAA09841.1.
PIR	S49804.
RefSeq	NP_013655.1. NM_001182415.1.
3D structure databases
ProteinModelPortal	P14747.
SMR	P14747. Positions 75-450.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-833N.
IntAct	P14747. 17 interactions.
MINT	MINT-519169.
STRING	4932.YML057W.
Proteomic databases
PaxDb	P14747.
PeptideAtlas	P14747.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YML057W; YML057W; YML057W.
GeneID	854946.
KEGG	sce:YML057W.
Organism-specific databases
CYGD	YML057w.
SGD	S000004521. CMP2.
Phylogenomic databases
eggNOG	COG0639.
GeneTree	ENSGT00530000063087.
HOGENOM	HOG000172699.
KO	K04348.
OMA	VIQECTS.
OrthoDB	EOG45XC4G.
Gene expression databases
Genevestigator	P14747.
GermOnline	YML057W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978007.

Entry information

Entry name

PP2B2_YEAST

Accession

Primary (citable) accession number: P14747
Secondary accession number(s): D6VZB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents