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Reviewed, UniProtKB/Swiss-Prot Q08209 (PP2BA_HUMAN)

Last modified January 19, 2010. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
    EC=3.1.3.16
Alternative name(s):
    Calmodulin-dependent calcineurin A subunit alpha isoform
    CAM-PRP catalytic subunit
Gene names
Name: PPP3CA
Synonyms: CALNA, CNA
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates HSPB1 and SSH1. Ref.10

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 1 Fe3+ ion per subunit.

Binds 1 zinc ion per subunit.

Subunit structure

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity. Interacts with TORC2/CRTC2, MYOZ1, MYOZ2 and MYOZ3. Ref.7 Ref.8 Ref.9

Subcellular location

Nucleus By similarity. Note: Colocalizes with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle By similarity.

Sequence similarities

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

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Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandCalmodulin-binding
Iron
Metal-binding
Zinc
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein amino acid dephosphorylation Ref.1

Non-traceable author statement. Source: UniProtKB

   Cellular componentcalcineurin complex Ref.1

Non-traceable author statement. Source: UniProtKB

cytosol

Inferred from Experiment. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular functioncalcium ion binding Ref.1

Non-traceable author statement. Source: UniProtKB

calmodulin binding Ref.1

Non-traceable author statement. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABL1P005191EBI-352922,EBI-375543
GRB2P629931EBI-352922,EBI-401755
PPP3R1P630981EBI-352922,EBI-915984

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08209-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q08209-2)

The sequence of this isoform differs from the canonical sequence as follows:
     448-457: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
PRO_0000058822

Regions

Region1 – 301301Catalytic
Region247 – 2537Calcineurin B binding-site 1 Potential
Region296 – 3016Calcineurin B binding-site 2 Potential
Region392 – 41423Calmodulin-binding Potential
Region465 – 48723Inhibitory domain

Sites

Active site1511Proton donor By similarity
Metal binding901Iron
Metal binding921Iron
Metal binding1181Iron
Metal binding1181Zinc
Metal binding1501Zinc
Metal binding1991Zinc
Metal binding2811Zinc

Amino acid modifications

Modified residue4691Phosphoserine By similarity

Natural variations

Alternative sequence448 – 45710Missing in isoform 2.
VSP_018562

Secondary structure

1 ...................................................................... 521
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 16480D62DDBF1F40

FASTA52158,688
        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

« Hide

Isoform 2.

Checksum: B1E98CC0D6034CCC
Show »

FASTA51157,659

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References

« Hide 'large scale' references
[1]"Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha)."
Muramatsu T., Kincaid R.L.
Biochim. Biophys. Acta 1178:117-120(1993) [PubMed: 8392375] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Amygdala.
[4]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Pancreas.
[7]"Calsarcins, a novel family of sarcomeric calcineurin-binding proteins."
Frey N., Richardson J.A., Olson E.N.
Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000) [PubMed: 11114196] [Abstract]
Cited for: INTERACTION WITH MYOZ1 AND MYOZ2.
[8]"Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins."
Frey N., Olson E.N.
J. Biol. Chem. 277:13998-14004(2002) [PubMed: 11842093] [Abstract]
Cited for: INTERACTION WITH MYOZ3.
[9]"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector."
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.
Cell 119:61-74(2004) [PubMed: 15454081] [Abstract]
Cited for: INTERACTION WITH CRTC2.
[10]"Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin."
Wang Y., Shibasaki F., Mizuno K.
J. Biol. Chem. 280:12683-12689(2005) [PubMed: 15671020] [Abstract]
Cited for: FUNCTION.
[11]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]"Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex."
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.
Nature 378:641-644(1995) [PubMed: 8524402] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

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Web resources

Wikipedia

Calcineurin entry

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L14778 mRNA. Translation: AAA02631.1.
AK290532 mRNA. Translation: BAF83221.1.
AL353950 mRNA. Translation: CAB89253.1.
AB451338 mRNA. Translation: BAG70152.1.
AB451487 mRNA. Translation: BAG70301.1.
CH471057 Genomic DNA. Translation: EAX06125.1.
CH471057 Genomic DNA. Translation: EAX06124.1.
BC025714 mRNA. Translation: AAH25714.1.
IPIIPI00179415.
IPI00747748.
PIRS35067.
RefSeqNP_000935.1.
NP_001124163.1.
UniGeneHs.435512

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AUIX-ray2.10A1-521[»]
1M63X-ray2.80A/E1-372[»]
1MF8X-ray3.10A20-392[»]
2JOGNMR-A21-347[»]
2JZINMR-B391-414[»]
2P6BX-ray2.30A/C1-380[»]
2R28X-ray1.86C/D389-413[»]
2W73X-ray1.45K/L/M/O395-411[»]
DisProtDP00092.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29315N.
DIP-6095N.
IntActQ08209. 4 interactions.
STRINGQ08209.

PTM databases

PhosphoSiteQ08209.

Proteomic databases

PRIDEQ08209.

Genome annotation databases

EnsemblENST00000394854; ENSP00000378323; ENSG00000138814; Homo sapiens. [Genome view]
GeneID5530.
KEGGhsa:5530.
UCSCuc003hvu.1. human.
uc003hvv.1. human.

Organism-specific databases

CTD5530.
GeneCardsGC04M102163.
H-InvDBHIX0004409.
HGNCHGNC:9314. PPP3CA.
HPACAB018581.
HPA012778.
MIM114105. gene.
PharmGKBPA33678.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG716770.
HOVERGENQ08209.
InParanoidQ08209.
OMAEMSEPKA.
PhylomeDBQ08209.

Enzyme and pathway databases

BRENDA3.1.3.16. 247.
Pathway_Interaction_DBbcr_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.
ReactomeREACT_15295. Opioid Signalling.

Gene expression databases

ArrayExpressQ08209.
BgeeQ08209.
CleanExHS_PPP3CA.
GenevestigatorQ08209.
GermOnlineENSG00000138814. Homo sapiens.

Family and domain databases

InterProIPR004843. M-pesterase.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PANTHERPTHR11668. T_phtase_apaH. 1 hit.
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio21422.
PMAP-CutDBQ08209.
SOURCESearch...

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Entry information

Entry namePP2BA_HUMAN
AccessionPrimary (citable) accession number: Q08209
Secondary accession number(s): A8K3B7, B5BUA2, Q8TAW9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 19, 2010
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents