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P63328

- PP2BA_MOUSE

UniProt

P63328 - PP2BA_MOUSE

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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform

Gene

Ppp3ca

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase. Many of the substrates contain a PxIxIT motif. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L and HSPB1 (By similarity). Dephosphorylates SSH1.By similarity1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe(3+) ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901IronBy similarity
Metal bindingi92 – 921IronBy similarity
Metal bindingi118 – 1181IronBy similarity
Metal bindingi118 – 1181ZincBy similarity
Metal bindingi150 – 1501ZincBy similarity
Active sitei151 – 1511Proton donorBy similarity
Metal bindingi199 – 1991ZincBy similarity
Metal bindingi281 – 2811ZincBy similarity

GO - Molecular functioni

  1. calcium-dependent protein serine/threonine phosphatase activity Source: Reactome
  2. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  3. drug binding Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW
  5. phosphoprotein phosphatase activity Source: MGI

GO - Biological processi

  1. calcineurin-NFAT signaling cascade Source: MGI
  2. calcium ion transport Source: MGI
  3. calcium-mediated signaling Source: MGI
  4. cellular response to drug Source: Ensembl
  5. cellular response to glucose stimulus Source: Ensembl
  6. dephosphorylation Source: MGI
  7. G1/S transition of mitotic cell cycle Source: MGI
  8. multicellular organismal response to stress Source: MGI
  9. negative regulation of insulin secretion Source: Ensembl
  10. positive regulation of cardiac muscle hypertrophy in response to stress Source: BHF-UCL
  11. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  12. protein dephosphorylation Source: MGI
  13. protein import into nucleus Source: MGI
  14. regulation of excitatory postsynaptic membrane potential Source: MGI
  15. regulation of synaptic transmission Source: MGI
  16. response to amphetamine Source: Ensembl
  17. response to calcium ion Source: UniProtKB
  18. skeletal muscle fiber development Source: MGI
  19. transition between fast and slow fiber Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_188202. FCERI mediated Ca+2 mobilization.
REACT_203795. DARPP-32 events.
REACT_221970. Ca2+ pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC:3.1.3.16)
Alternative name(s):
CAM-PRP catalytic subunit
Calmodulin-dependent calcineurin A subunit alpha isoform
Gene namesi
Name:Ppp3ca
Synonyms:Calna
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:107164. Ppp3ca.

Subcellular locationi

Cell membrane. Cell membranesarcolemma. Nucleus
Note: Colocalizes with ACTN1 and MYOZ2 at the Z line in heart and skeletal muscle.

GO - Cellular componenti

  1. calcineurin complex Source: MGI
  2. cytosol Source: MGI
  3. mitochondrion Source: MGI
  4. nucleus Source: MGI
  5. plasma membrane Source: UniProtKB-KW
  6. Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi477 – 4771D → N: Greatly reduces inhibition of calcineurin phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 521520Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoformPRO_0000058823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei224 – 2241Nitrated tyrosine1 Publication

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiP63328.
PaxDbiP63328.
PRIDEiP63328.

PTM databases

PhosphoSiteiP63328.

Expressioni

Gene expression databases

BgeeiP63328.
ExpressionAtlasiP63328. baseline and differential.
GenevestigatoriP63328.

Interactioni

Subunit structurei

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity. Interacts with CRTC2, MYOZ1, MYOZ2 and MYOZ3. Interacts with DNM1L; the interaction dephosphorylates DNM1L and regulates its translocation to mitochondria. Interacts with CHP1 and CHP2 (By similarity). Interacts with CMYA5; this interaction represses calcineurin activity in muscle. Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy.By similarity2 Publications

Protein-protein interaction databases

BioGridi202344. 8 interactions.
DIPiDIP-31543N.
IntActiP63328. 8 interactions.
MINTiMINT-135995.

Structurei

3D structure databases

ProteinModelPortaliP63328.
SMRiP63328. Positions 1-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 301300CatalyticAdd
BLAST
Regioni247 – 2537Calcineurin B binding-site 1Sequence Analysis
Regioni296 – 3016Calcineurin B binding-site 2Sequence Analysis
Regioni392 – 41423Calmodulin-bindingSequence AnalysisAdd
BLAST
Regioni465 – 48723Inhibitory domainAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
HOGENOMiHOG000172699.
HOVERGENiHBG002819.
InParanoidiP63328.
KOiK04348.
OMAiMFWSPED.
OrthoDBiEOG7BZVSC.
PhylomeDBiP63328.
TreeFamiTF105557.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P63328-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL
60 70 80 90 100
MKEGRLEESV ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK
110 120 130 140 150
LFEVGGSPAN TRYLFLGDYV DRGYFSIECV LYLWALKILY PKTLFLLRGN
160 170 180 190 200
HECRHLTEYF TFKQECKIKY SERVYDACMD AFDCLPLAAL MNQQFLCVHG
210 220 230 240 250
GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG NEKTQEHFTH
260 270 280 290 300
NTVRGCSYFY SYPAVCDFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP
310 320 330 340 350
SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF
360 370 380 390 400
TWSLPFVGEK VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI
410 420 430 440 450
RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLSGG KQTLQSATVE
460 470 480 490 500
AIEADEAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDAM PSDANLNSIN
510 520
KALASETNGT DSNGSNSSNI Q
Length:521
Mass (Da):58,644
Last modified:October 11, 2004 - v1
Checksum:i16530C27DDBF1F05
GO
Isoform 2 (identifier: P63328-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:511
Mass (Da):57,615
Checksum:i01428D70D67450BD
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei448 – 45710Missing in isoform 2. 1 PublicationVSP_018563

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05479 mRNA. Translation: AAA37359.1.
AK146387 mRNA. Translation: BAE27131.1.
AK150393 mRNA. Translation: BAE29521.1.
J04134 mRNA. Translation: AAA37432.1.
S78668 mRNA. Translation: AAB34675.1.
CCDSiCCDS17860.1. [P63328-1]
PIRiA42232. A31257.
RefSeqiNP_001280551.1. NM_001293622.1. [P63328-2]
NP_032939.1. NM_008913.5. [P63328-1]
UniGeneiMm.331389.
Mm.486983.

Genome annotation databases

EnsembliENSMUST00000056758; ENSMUSP00000053101; ENSMUSG00000028161. [P63328-1]
ENSMUST00000070198; ENSMUSP00000071040; ENSMUSG00000028161. [P63328-2]
GeneIDi19055.
KEGGimmu:19055.
UCSCiuc008rmg.1. mouse. [P63328-1]
uc008rmh.1. mouse. [P63328-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05479 mRNA. Translation: AAA37359.1 .
AK146387 mRNA. Translation: BAE27131.1 .
AK150393 mRNA. Translation: BAE29521.1 .
J04134 mRNA. Translation: AAA37432.1 .
S78668 mRNA. Translation: AAB34675.1 .
CCDSi CCDS17860.1. [P63328-1 ]
PIRi A42232. A31257.
RefSeqi NP_001280551.1. NM_001293622.1. [P63328-2 ]
NP_032939.1. NM_008913.5. [P63328-1 ]
UniGenei Mm.331389.
Mm.486983.

3D structure databases

ProteinModelPortali P63328.
SMRi P63328. Positions 1-411.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202344. 8 interactions.
DIPi DIP-31543N.
IntActi P63328. 8 interactions.
MINTi MINT-135995.

PTM databases

PhosphoSitei P63328.

Proteomic databases

MaxQBi P63328.
PaxDbi P63328.
PRIDEi P63328.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000056758 ; ENSMUSP00000053101 ; ENSMUSG00000028161 . [P63328-1 ]
ENSMUST00000070198 ; ENSMUSP00000071040 ; ENSMUSG00000028161 . [P63328-2 ]
GeneIDi 19055.
KEGGi mmu:19055.
UCSCi uc008rmg.1. mouse. [P63328-1 ]
uc008rmh.1. mouse. [P63328-2 ]

Organism-specific databases

CTDi 5530.
MGIi MGI:107164. Ppp3ca.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000063087.
HOGENOMi HOG000172699.
HOVERGENi HBG002819.
InParanoidi P63328.
KOi K04348.
OMAi MFWSPED.
OrthoDBi EOG7BZVSC.
PhylomeDBi P63328.
TreeFami TF105557.

Enzyme and pathway databases

Reactomei REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_203795. DARPP-32 events.
REACT_221970. Ca2+ pathway.

Miscellaneous databases

ChiTaRSi Ppp3ca. mouse.
NextBioi 295542.
PROi P63328.
SOURCEi Search...

Gene expression databases

Bgeei P63328.
ExpressionAtlasi P63328. baseline and differential.
Genevestigatori P63328.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of molecular isoforms of the catalytic subunit of calcineurin using nonisotopic methods."
    Kincaid R.L., Giri P.R., Higuchi S., Tamura J., Dixon S.C., Marietta C.A., Amorese D.A., Martin B.M.
    J. Biol. Chem. 265:11312-11319(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: BALB/c and C57BL/6J.
    Tissue: Bone marrow.
  3. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 64-73; 101-122 AND 425-459, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  4. "Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain."
    Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.
    J. Biol. Chem. 269:22586-22592(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 95-116.
  5. "Characterization of a cDNA clone encoding the calmodulin-binding domain of mouse brain calcineurin."
    Kincaid R.L., Nightingale M.S., Martin B.M.
    Proc. Natl. Acad. Sci. U.S.A. 85:8983-8987(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 215-521 (ISOFORM 1).
  6. "Characterization of a mutant calcineurin A alpha gene expressed by EL4 lymphoma cells."
    Fruman D.A., Pai S.-Y., Burakoff S.J., Bierer B.E.
    Mol. Cell. Biol. 15:3857-3863(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 467-491, MUTAGENESIS OF ASP-477.
  7. "Dephosphorylation of the small heat shock protein hsp25 by calcium/calmodulin-dependent (type 2B) protein phosphatase."
    Gaestel M., Benndorf R., Hayess K., Priemer E., Engel K.
    J. Biol. Chem. 267:21607-21611(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. Cited for: INTERACTION WITH CIB1, SUBCELLULAR LOCATION.
  11. "Myospryn is a calcineurin-interacting protein that negatively modulates slow-fiber-type transformation and skeletal muscle regeneration."
    Kielbasa O.M., Reynolds J.G., Wu C.L., Snyder C.M., Cho M.Y., Weiler H., Kandarian S., Naya F.J.
    FASEB J. 25:2276-2286(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CMYA5.

Entry informationi

Entry nameiPP2BA_MOUSE
AccessioniPrimary (citable) accession number: P63328
Secondary accession number(s): P12816
, P20652, Q3UCU1, Q64135
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 26, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3