ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q08209


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PP2BA_HUMAN
Primary accession number Q08209
Secondary accession number Q8TAW9
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 98)
Name and origin of the protein
Protein name Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
Synonyms EC 3.1.3.16
Calmodulin-dependent calcineurin A subunit alpha isoform
CAM-PRP catalytic subunit
Gene name
Name: PPP3CA
Synonyms: CALNA, CNA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
DOI=10.1016/0167-4889(93)90117-8; PubMed=8392375 [NCBI, ExPASy, EBI, Israel, Japan]
Muramatsu T., Kincaid R.L.;
"Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha).";
Biochim. Biophys. Acta 1178:117-120(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH MYOZ1 AND MYOZ2.
DOI=10.1073/pnas.260501097; PubMed=11114196 [NCBI, ExPASy, EBI, Israel, Japan]
Frey N., Richardson J.A., Olson E.N.;
"Calsarcins, a novel family of sarcomeric calcineurin-binding proteins.";
Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000).
[5]
INTERACTION WITH MYOZ3.
DOI=10.1074/jbc.M200712200; PubMed=11842093 [NCBI, ExPASy, EBI, Israel, Japan]
Frey N., Olson E.N.;
"Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins.";
J. Biol. Chem. 277:13998-14004(2002).
[6]
INTERACTION WITH CRTC2.
DOI=10.1016/j.cell.2004.09.015; PubMed=15454081 [NCBI, ExPASy, EBI, Israel, Japan]
Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., Okamoto M., Montminy M.;
"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector.";
Cell 119:61-74(2004).
[7]
FUNCTION.
DOI=10.1074/jbc.M411494200; PubMed=15671020 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y., Shibasaki F., Mizuno K.;
"Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin.";
J. Biol. Chem. 280:12683-12689(2005).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[9]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1038/378641a0; PubMed=8524402 [NCBI, ExPASy, EBI, Israel, Japan]
Kissinger C.R., Parge H.E., Knighton D.R., Lewis C.T., Pelletier L.A., Tempczyk A., Kalish V.J., Tucker K.D., Showalter R.E., Moomaw E.W., Gastinel L.N., Habuka N., Chen X., Maldonado F., Barker J.E., Bacquet R., Villafranca J.E.;
"Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex.";
Nature 378:641-644(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L14778; AAA02631.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353950; CAB89253.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025714; AAH25714.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00179415; -.
IPI00747748; -.
PIR S35067; S35067.
RefSeq NP_000935.1; -.
UniGene Hs.435512
3D structure databases
PDB
1AUI; X-ray; 2.10 A; A=1-521.[ExPASy / RCSB / EBI]
1M63; X-ray; 2.80 A; A/E=1-372.[ExPASy / RCSB / EBI]
1MF8; X-ray; 3.10 A; A=20-392.[ExPASy / RCSB / EBI]
2JOG; NMR; -; A=21-347.[ExPASy / RCSB / EBI]
2JZI; NMR; -; B=391-414.[ExPASy / RCSB / EBI]
2P6B; X-ray; 2.30 A; A/C=1-380.[ExPASy / RCSB / EBI]
2R28; X-ray; 1.86 A; C/D=389-413.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AUI; -.
1M63; -.
1MF8; -.
2JOG; -.
2JZI; -.
2P6B; -.
2R28; -.
DisProt DP00092; -.
ModBase Q08209.
Protein-protein interaction databases
DIP DIP:6095N; -.
IntAct Q08209; 4.
PTM databases
PhosphoSite Q08209; -.
Enzyme and pathway databases
BRENDA 3.1.3.16; 247.
Pathway_Interaction_DB bcr_5pathway; BCR signaling pathway.
tcrcalciumpathway; Calcium signaling in the CD4+ TCR pathway.
cd8tcrdownstreampathway; Downstream signaling in naive CD8+ T cells.
il12_stat4pathway; IL12 signaling mediated by STAT4.
il12_2pathway; IL12-mediated signaling events.
nfat_3pathway; Role of Calcineurin-dependent NFAT signaling in lymphocytes.
Organism-specific databases
GeneCards GC04M102163; -.
H-InvDB HIX0004409; -.
HGNC HGNC:9314; PPP3CA.
GenAtlas PPP3CA.
HPA HPA012778; -.
MIM 114105; gene. [NCBI / EBI]
PharmGKB PA33678; -.
Gene expression databases
ArrayExpress Q08209; -.
Bgee Q08209; -.
CleanEx HS_PPP3CA; -.
GermOnline ENSG00000138814; Homo sapiens.
Ontologies
GO
GO:0005955; Cellular component: calcineurin complex (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005509; Molecular function: calcium ion binding (non-traceable author statement from UniProtKB).
GO:0005516; Molecular function: calmodulin binding (non-traceable author statement from UniProtKB).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004722; Molecular function: protein serine/threonine phosphatase activity (non-traceable author statement from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006470; Biological process: protein amino acid dephosphorylation (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR004843; M-pesterase.
IPR006186; T_phtase_apaH.
Graphical view of domain structure.
PANTHER PTHR11668; T_phtase_apaH; 1.
Pfam PF00149; Metallophos; 1.
Pfam graphical view of domain structure.
PRINTS PR00114; STPHPHTASE.
ProDom PD000252; T_phtase_apaH; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00156; PP2Ac; 1.
SMART graphical view of domain structure.
PROSITE PS00125; SER_THR_PHOSPHATASE; 1.
Proteomic databases
PRIDE Q08209; -.
Genome annotation databases
Ensembl ENSG00000138814; Homo sapiens. [Contig view]
GeneID 5530; -.
KEGG hsa:5530; -.
Phylogenomic databases
HOGENOM Q08209; -.
HOVERGEN Q08209; -.
Other
NextBio 21422; -.
PMAP-CutDB Q08209; -.
SOURCE PPP3CA; Homo sapiens.
ProtoNet Q08209.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Calmodulin-binding; Hydrolase; Iron; Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   521  521     Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform. PRO_0000058822
REGION   1   301  301     Catalytic. 
REGION   247   253  7     Calcineurin B binding-site 1 (Potential). 
REGION   296   301  6     Calcineurin B binding-site 2 (Potential). 
REGION   392   414  23     Calmodulin-binding (Potential). 
REGION   465   487  23     Inhibitory domain. 
ACT_SITE   151   151        Proton donor (By similarity). 
METAL   90    90        Iron. 
METAL   92    92        Iron. 
METAL   118   118        Iron. 
METAL   118   118        Zinc. 
METAL   150   150        Zinc. 
METAL   199   199        Zinc. 
METAL   281   281        Zinc. 
MOD_RES   469   469        Phosphoserine (By similarity). 
VAR_SEQ   448   457        Missing (in isoform 2). VSP_018562
HELIX   31    34  4      
HELIX   43    51  9      
HELIX   58    73  16      
STRAND   77    81  5      
STRAND   83    88  6      
HELIX   95   105  11      
TURN   108   110  3      
STRAND   113   115  3      
STRAND   120   124  5      
HELIX   126   139  14      
TURN   141   143  3      
STRAND   144   146  3      
HELIX   154   159  6      
HELIX   162   169  8      
HELIX   172   182  11      
STRAND   188   191  4      
TURN   192   194  3      
STRAND   195   200  6      
HELIX   209   214  6      
STRAND   218   220  3      
STRAND   223   225  3      
HELIX   226   232  7      
TURN   237   240  4      
STRAND   248   250  3      
TURN   252   255  4      
STRAND   256   260  5      
HELIX   262   271  10      
STRAND   275   279  5      
STRAND   287   290  4      
TURN   295   297  3      
STRAND   298   305  8      
HELIX   311   313  3      
STRAND   319   325  7      
STRAND   328   334  7      
HELIX   344   346  3      
HELIX   349   369  21      
HELIX   470   477  8      
HELIX   478   481  4      
Sequence information
Length: 521 AA [This is the length of the unprocessed precursor] Molecular weight: 58688 Da [This is the MW of the unprocessed precursor] CRC64: 16480D62DDBF1F40 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV 

        70         80         90        100        110        120 
ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV 

       130        140        150        160        170        180 
DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD 

       190        200        210        220        230        240 
AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG 

       250        260        270        280        290        300 
NEKTQEHFTH NTVRGCSYFY SYPAVCEFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP 

       310        320        330        340        350        360 
SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK 

       370        380        390        400        410        420 
VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV 

       430        440        450        460        470        480 
LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN 

       490        500        510        520 
ERMPPRRDAM PSDANLNSIN KALTSETNGT DSNGSNSSNI Q 

Q08209 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!