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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, Calna
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 SSH1.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 Fe3+ ion per subunit By similarity.
Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901Iron By similarity
Metal bindingi92 – 921Iron By similarity
Metal bindingi118 – 1181Iron By similarity
Metal bindingi118 – 1181Zinc By similarity
Metal bindingi150 – 1501Zinc By similarity
Active sitei151 – 1511Proton donor By similarity
Metal bindingi199 – 1991Zinc By similarity
Metal bindingi281 – 2811Zinc By 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
  6. protein binding Source: BHF-UCL

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 transcription from RNA polymerase II promoter Source: MGI
  11. protein dephosphorylation Source: MGI
  12. protein import into nucleus Source: MGI
  13. regulation of excitatory postsynaptic membrane potential Source: MGI
  14. regulation of synaptic transmission Source: MGI
  15. response to amphetamine Source: Ensembl
  16. response to calcium ion Source: UniProtKB
  17. skeletal muscle fiber development Source: MGI
  18. 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.2 Publications

GO - Cellular componenti

  1. calcineurin complex Source: MGI
  2. cytosol Source: MGI
  3. mitochondrion Source: MGI
  4. nucleus Source: MGI
  5. sarcolemma Source: UniProtKB-SubCell
  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 – 11Removed By 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-acetylserine By similarity
Modified residuei224 – 2241Nitrated tyrosine1 Publication

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiP63328.
PaxDbiP63328.
PRIDEiP63328.

PTM databases

PhosphoSiteiP63328.

Expressioni

Gene expression databases

ArrayExpressiP63328.
BgeeiP63328.
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.2 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP63328.
SMRiP63328. Positions 1-411.

Family & Domainsi

Region

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

Sequence similaritiesi

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

MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL    50
MKEGRLEESV ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK 100
LFEVGGSPAN TRYLFLGDYV DRGYFSIECV LYLWALKILY PKTLFLLRGN 150
HECRHLTEYF TFKQECKIKY SERVYDACMD AFDCLPLAAL MNQQFLCVHG 200
GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG NEKTQEHFTH 250
NTVRGCSYFY SYPAVCDFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP 300
SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF 350
TWSLPFVGEK VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI 400
RAIGKMARVF SVLREESESV LTLKGLTPTG MLPSGVLSGG KQTLQSATVE 450
AIEADEAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDAM PSDANLNSIN 500
KALASETNGT DSNGSNSSNI Q 521
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. VSP_018563

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_032939.1. NM_008913.5. [P63328-1]
UniGeneiMm.331389.

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:
EMBL
GenBank
DDBJ
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_032939.1. NM_008913.5. [P63328-1 ]
UniGenei Mm.331389.

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

ArrayExpressi P63328.
Bgeei P63328.
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: September 3, 2014
This is version 110 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

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