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Q08209 (PP2BA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PPP3CA
Synonyms:CALNA, CNA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length521 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. Many of the substrates contain a PxIxIT motif. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1. Ref.13 Ref.14 Ref.18

Catalytic activity

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

Cofactor

Binds 1 Fe3+ ion per subunit.

Binds 1 zinc ion per subunit.

Subunit structure

Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy By similarity. Interacts with CHP1 and CHP2 By similarity. 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 CMYA5; this interaction represses calcineurin activity in muscle By similarity. Ref.10 Ref.11 Ref.12 Ref.14

Subcellular location

Cell membrane By similarity. Cell membranesarcolemma By similarity. 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.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandCalmodulin-binding
Iron
Metal-binding
Zinc
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Nitration
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

T cell activation

Traceable author statement PubMed 11005320. Source: UniProtKB

calcineurin-NFAT signaling cascade

Inferred from electronic annotation. Source: Ensembl

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from direct assay PubMed 11005320. Source: UniProtKB

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

dephosphorylation

Traceable author statement PubMed 2556704. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

multicellular organismal response to stress

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from direct assay PubMed 18815128. Source: UniProtKB

protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic transmission

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from direct assay PubMed 18815128. Source: UniProtKB

skeletal muscle fiber development

Inferred from electronic annotation. Source: Ensembl

transition between fast and slow fiber

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

calcineurin complex

Non-traceable author statement Ref.1. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

sarcolemma

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Non-traceable author statement Ref.1. Source: UniProtKB

calmodulin binding

Inferred from direct assay PubMed 11005320. Source: UniProtKB

calmodulin-dependent protein phosphatase activity

Inferred from direct assay PubMed 18815128. Source: UniProtKB

drug binding

Inferred from direct assay PubMed 11005320. Source: UniProtKB

enzyme binding

Inferred from direct assay PubMed 11005320. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10Ref.11Ref.14. Source: UniProtKB

protein dimerization activity

Inferred from physical interaction PubMed 11005320. Source: UniProtKB

protein serine/threonine phosphatase activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cacng8Q8VHW52EBI-352922,EBI-9086576From a different organism.
GRB2P629933EBI-352922,EBI-401755
PPP3R1P630982EBI-352922,EBI-915984
USP14P545783EBI-352922,EBI-1048016

Alternative products

This entry describes 5 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.
Isoform 3 (identifier: Q08209-3)

The sequence of this isoform differs from the canonical sequence as follows:
     318-359: Missing.
     448-457: Missing.
Isoform 4 (identifier: Q08209-4)

The sequence of this isoform differs from the canonical sequence as follows:
     87-318: Missing.
Isoform 5 (identifier: Q08209-5)

The sequence of this isoform differs from the canonical sequence as follows:
     20-86: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.16
Chain2 – 521520Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
PRO_0000058822

Regions

Region2 – 301300Catalytic
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 residue21N-acetylserine Ref.16
Modified residue2241Nitrated tyrosine By similarity

Natural variations

Alternative sequence20 – 8667Missing in isoform 5.
VSP_054467
Alternative sequence87 – 318232Missing in isoform 4.
VSP_047755
Alternative sequence318 – 35942Missing in isoform 3.
VSP_043378
Alternative sequence448 – 45710Missing in isoform 2 and isoform 3.
VSP_018562

Secondary structure

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

Details...

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 [UniParc].

Checksum: B1E98CC0D6034CCC
Show »

FASTA51157,659
Isoform 3 [UniParc].

Checksum: A3365471746633B7
Show »

FASTA46952,672
Isoform 4 [UniParc].

Checksum: B3AEE20F6A4F19B7
Show »

FASTA28931,736
Isoform 5 [UniParc].

Checksum: E28DCB758984D380
Show »

FASTA45451,245

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Fine mapping of calcineurin (PPP3CA) gene reveals novel alternative splicing patterns, association of 5'UTR trinucleotide repeat with addiction vulnerability, and differential isoform expression in Alzheimer's disease."
Chiocco M.J., Zhu X., Walther D., Pletnikova O., Troncoso J.C., Uhl G.R., Liu Q.R.
Subst. Use Misuse 45:1809-1826(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING.
[3]"Identification of differentially expressed genes in uveal melanoma using suppressive subtractive hybridization."
Landreville S., Lupien C.B., Vigneault F., Gaudreault M., Mathieu M., Rousseau A.P., Guerin S.L., Salesse C.
Mol. Vis. 17:1324-1333(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Amygdala.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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].
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Pancreas.
[10]"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: INTERACTION WITH MYOZ1 AND MYOZ2.
[11]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYOZ3.
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRTC2.
[13]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria."
Cereghetti G.M., Stangherlin A., Martins de Brito O., Chang C.R., Blackstone C., Bernardi P., Scorrano L.
Proc. Natl. Acad. Sci. U.S.A. 105:15803-15808(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DMN1L, FUNCTION.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
[17]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[18]"Structure of calcineurin in complex with PVIVIT peptide: portrait of a low-affinity signalling interaction."
Li H., Zhang L., Rao A., Harrison S.C., Hogan P.G.
J. Mol. Biol. 369:1296-1306(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-380 IN COMPLEX WITH SUBSTRATE PEPTIDE, FUNCTION, METAL-BINDING SITES.
+Additional computationally mapped references.

Web resources

Wikipedia

Calcineurin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14778 mRNA. Translation: AAA02631.1.
EU192652 mRNA. Translation: ABW74484.1.
EU192653 mRNA. Translation: ABW74485.1.
AY904364 mRNA. Translation: AAY17314.1.
AK290532 mRNA. Translation: BAF83221.1.
AL353950 mRNA. Translation: CAB89253.1.
AB451338 mRNA. Translation: BAG70152.1.
AB451487 mRNA. Translation: BAG70301.1.
AC092671 Genomic DNA. No translation available.
AP001816 Genomic DNA. No translation available.
AP001870 Genomic DNA. No translation available.
AP001939 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06125.1.
CH471057 Genomic DNA. Translation: EAX06124.1.
BC025714 mRNA. Translation: AAH25714.1.
CCDSCCDS34037.1. [Q08209-1]
CCDS47113.1. [Q08209-3]
CCDS47114.1. [Q08209-2]
PIRS35067.
RefSeqNP_000935.1. NM_000944.4. [Q08209-1]
NP_001124163.1. NM_001130691.1. [Q08209-2]
NP_001124164.1. NM_001130692.1. [Q08209-3]
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[»]
3LL8X-ray2.00A/C14-370[»]
4F0ZX-ray1.70A1-370[»]
DisProtDP00092.
ProteinModelPortalQ08209.
SMRQ08209. Positions 14-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111522. 40 interactions.
DIPDIP-6095N.
IntActQ08209. 13 interactions.
MINTMINT-1037516.
STRING9606.ENSP00000378323.

Chemistry

BindingDBQ08209.
ChEMBLCHEMBL4445.

PTM databases

PhosphoSiteQ08209.

Polymorphism databases

DMDM1352673.

Proteomic databases

MaxQBQ08209.
PaxDbQ08209.
PRIDEQ08209.

Protocols and materials databases

DNASU5530.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323055; ENSP00000320580; ENSG00000138814. [Q08209-3]
ENST00000394853; ENSP00000378322; ENSG00000138814. [Q08209-2]
ENST00000394854; ENSP00000378323; ENSG00000138814. [Q08209-1]
ENST00000512215; ENSP00000422781; ENSG00000138814. [Q08209-4]
ENST00000523694; ENSP00000429350; ENSG00000138814.
GeneID5530.
KEGGhsa:5530.
UCSCuc003hvt.2. human. [Q08209-2]
uc010ilj.2. human. [Q08209-3]
uc011cen.1. human. [Q08209-1]

Organism-specific databases

CTD5530.
GeneCardsGC04M101944.
HGNCHGNC:9314. PPP3CA.
HPACAB018581.
HPA012778.
MIM114105. gene.
neXtProtNX_Q08209.
PharmGKBPA33678.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172699.
HOVERGENHBG002819.
InParanoidQ08209.
KOK04348.
OMAXATAAAR.
OrthoDBEOG7PCJJX.
PhylomeDBQ08209.
TreeFamTF105557.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118664. Calcineurin dephosphorylates NFATC1,2,3.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ08209.
BgeeQ08209.
CleanExHS_PPP3CA.
GenevestigatorQ08209.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP3CA. human.
EvolutionaryTraceQ08209.
GeneWikiPPP3CA.
GenomeRNAi5530.
NextBio21422.
PMAP-CutDBQ08209.
PROQ08209.
SOURCESearch...

Entry information

Entry namePP2BA_HUMAN
AccessionPrimary (citable) accession number: Q08209
Secondary accession number(s): A1A441 expand/collapse secondary AC list , A8K3B7, A8W6Z7, A8W6Z8, B5BUA2, Q8TAW9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 4

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