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P23287 (PP2B1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit A1

EC=3.1.3.16
Alternative name(s):
Calcineurin A1
Calmodulin-binding protein 1
Gene names
Name:CNA1
Synonyms:CMP1
Ordered Locus Names:YLR433C
ORF Names:L9753.6
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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 7040 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PPP phosphatase family. PP-2B subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CMD1P067873EBI-12771,EBI-3976

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 553552Serine/threonine-protein phosphatase 2B catalytic subunit A1
PRO_0000058836

Sites

Active site1801Proton donor By similarity
Metal binding1191Iron By similarity
Metal binding1211Iron By similarity
Metal binding1471Iron By similarity
Metal binding1471Zinc By similarity
Metal binding1791Zinc By similarity
Metal binding2281Zinc By similarity
Metal binding3171Zinc By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.8

Natural variations

Natural variant45 – 462PI → SY in strain: S288c / GRF88.

Secondary structure

..... 553
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23287 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: D5D6F91CC0BD277B

FASTA55363,002
        10         20         30         40         50         60 
MSKDLNSSRI KIIKPNDSYI KVDRKKDLTK YELENGKVIS TKDRPIASVP AITGKIPSDE 

        70         80         90        100        110        120 
EVFDSKTGLP NHSFLREHFF HEGRLSKEQA IKILNMSTVA LSKEPNLLKL KAPITICGDI 

       130        140        150        160        170        180 
HGQYYDLLKL FEVGGDPAEI DYLFLGDYVD RGAFSFECLI YLYSLKLNNL GRFWMLRGNH 

       190        200        210        220        230        240 
ECKHLTSYFT FKNEMLHKYD MEVYDACCRS FNVLPLAALM NGQYFCVHGG ISPELKSVED 

       250        260        270        280        290        300 
VNKINRFREI PSRGLMCDLL WADPVENYDD ARDGSEFDQS EDEFVPNSLR GCSFAFTFKA 

       310        320        330        340        350        360 
SCKFLKANGL LSIIRAHEAQ DAGYRMYKNN KVTGFPSLIT MFSAPNYLDT YHNKAAVLKY 

       370        380        390        400        410        420 
EENVMNIRQF HMSPHPYWLP DFMDVFTWSL PFVGEKVTSM LVSILNICSE QELDPESEPK 

       430        440        450        460        470        480 
AAEETVKARA NATKETGTPS DEKASSAILE DETRRKALRN KILAIAKVSR MFSVLREESE 

       490        500        510        520        530        540 
KVEYLKTMNA GVLPRGALAR GTEGLNETLS TFEKARKEDL INEKLPPSLS EVEQEKIKYY 

       550 
EKILKGAEKK PQL 

« Hide

References

« Hide '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]"Identification and molecular characterization of the calmodulin-binding subunit gene (CMP1) of protein phosphatase 2B from Saccharomyces cerevisiae. An alpha-factor inducible gene."
Ye R.R., Bretscher A.
Eur. J. Biochem. 204:713-723(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 20B-12.
[3]"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].
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"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].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64839 Genomic DNA. Translation: AAA34465.1.
X66490 Genomic DNA. Translation: CAA47117.1.
X54963 Genomic DNA. Translation: CAA38711.1.
U21094 Genomic DNA. Translation: AAB67518.1.
AY693079 Genomic DNA. Translation: AAT93098.1.
BK006945 Genomic DNA. Translation: DAA09734.1.
PIRS16809.
RefSeqNP_013537.1. NM_001182321.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LHINMR-A453-476[»]
ProteinModelPortalP23287.
SMRP23287. Positions 49-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31692. 65 interactions.
DIPDIP-662N.
IntActP23287. 23 interactions.
MINTMINT-397444.
STRING4932.YLR433C.

Proteomic databases

PaxDbP23287.
PeptideAtlasP23287.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR433C; YLR433C; YLR433C.
GeneID851153.
KEGGsce:YLR433C.

Organism-specific databases

CYGDYLR433c.
SGDS000004425. CNA1.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000063087.
HOGENOMHOG000172699.
KOK04348.
OMAHTIQTFE.
OrthoDBEOG77M8X9.

Enzyme and pathway databases

BioCycYEAST:G3O-32491-MONOMER.

Gene expression databases

GenevestigatorP23287.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967933.

Entry information

Entry namePP2B1_YEAST
AccessionPrimary (citable) accession number: P23287
Secondary accession number(s): D6VZ68
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references