Q08209 (PP2BA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PPP3CA
Synonyms:	CALNA, CNA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1. Ref.12 Ref.13
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 1 Fe3+ ion per subunit. Binds 1 zinc ion per subunit.
Subunit structure	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.9 Ref.10 Ref.11 Ref.13
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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Calmodulin-binding Iron Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara T cell activation Traceable author statement PubMed 11005320. Source: UniProtKB calcineurin-NFAT signaling cascade Inferred from electronic annotation. Source: Compara calcium ion transport Inferred from electronic annotation. Source: Compara cellular response to drug Inferred from direct assay PubMed 11005320. Source: UniProtKB cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara negative regulation of insulin secretion Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara protein dephosphorylation Inferred from direct assay PubMed 18815128. Source: UniProtKB protein import into nucleus Inferred from electronic annotation. Source: Compara regulation of excitatory postsynaptic membrane potential Inferred from electronic annotation. Source: Compara regulation of synaptic transmission Inferred from electronic annotation. Source: Compara response to amphetamine Inferred from electronic annotation. Source: Compara response to calcium ion Inferred from direct assay PubMed 18815128. Source: UniProtKB response to stress Inferred from electronic annotation. Source: Compara skeletal muscle fiber development Inferred from electronic annotation. Source: Compara transition between fast and slow fiber Inferred from electronic annotation. Source: Compara
Cellular_component	Z disc Inferred from electronic annotation. Source: Compara calcineurin complex Non-traceable author statement Ref.1. Source: UniProtKB cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA
Molecular_function	calcium 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	2	EBI-352922,EBI-401755

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 521

521

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

PRO_0000058822

Regions

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

Sites

Active site

151

1

Proton donor By similarity

Metal binding

90

1

Iron

Metal binding

92

1

Iron

Metal binding

118

1

Iron

Metal binding

118

1

Zinc

Metal binding

150

1

Zinc

Metal binding

199

1

Zinc

Metal binding

281

1

Zinc

Amino acid modifications

Modified residue

469

1

Phosphoserine By similarity

Natural variations

Alternative sequence

318 – 359

42

Missing in isoform 3.

VSP_043378

Alternative sequence

448 – 457

10

Missing in isoform 2 and isoform 3.

VSP_018562

Secondary structure

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521

Helix Strand Turn

Details...

Beta strand

11 – 13

3

Helix

31 – 34

4

Helix

43 – 51

9

Helix

58 – 73

16

Beta strand

77 – 81

5

Beta strand

83 – 88

6

Helix

95 – 105

11

Turn

108 – 110

3

Beta strand

113 – 115

3

Beta strand

120 – 123

4

Helix

126 – 139

14

Turn

141 – 143

3

Beta strand

144 – 146

3

Helix

154 – 159

6

Helix

162 – 169

8

Helix

172 – 183

12

Beta strand

187 – 191

5

Turn

192 – 194

3

Beta strand

195 – 197

3

Beta strand

206 – 208

3

Helix

209 – 213

5

Beta strand

218 – 220

3

Beta strand

223 – 225

3

Helix

226 – 232

7

Turn

237 – 240

4

Beta strand

247 – 250

4

Turn

252 – 255

4

Beta strand

256 – 260

5

Helix

262 – 271

10

Beta strand

275 – 279

5

Beta strand

287 – 290

4

Turn

295 – 297

3

Beta strand

298 – 305

8

Helix

311 – 313

3

Beta strand

319 – 325

7

Beta strand

328 – 334

7

Helix

344 – 346

3

Helix

349 – 369

21

Helix

396 – 409

14

Helix

470 – 477

8

Helix

478 – 481

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 16480D62DDBF1F40	FASTA	521	58,688
	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
	Isoform 2 [UniParc]. Checksum: B1E98CC0D6034CCC	FASTA	511	57,659
	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 KQTLQSAIKG FSPQHKITSF EEAKGLDRIN ERMPPRRDAM 490 500 510 PSDANLNSIN KALTSETNGT DSNGSNSSNI Q
	Isoform 3 [UniParc]. Checksum: A3365471746633B7	FASTA	469	52,672
	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 YLDVYNNKVT EMLVNVLNIC SDDELGSEED GFDGATAAAR KEVIRNKIRA 370 380 390 400 410 420 IGKMARVFSV LREESESVLT LKGLTPTGML PSGVLSGGKQ TLQSAIKGFS PQHKITSFEE 430 440 450 460 AKGLDRINER MPPRRDAMPS DANLNSINKA LTSETNGTDS NGSNSSNIQ

References

	« Hide 'large scale' referencesShow '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] (ISOFORM 3), ALTERNATIVE SPLICING.
[3]	"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. , 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.
[4]	"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.
[5]	"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. , 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).
[6]	"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. , 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].
[7]	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. , 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].
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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].
[15]	"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).
+	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.
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.

IPI

IPI00179415.
IPI00747748.
IPI00910825.

PIR

S35067.

RefSeq

NP_000935.1. NM_000944.4.
NP_001124163.1. NM_001130691.1.
NP_001124164.1. NM_001130692.1.

UniGene

Hs.435512.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AUI	X-ray	2.10	A	1-521	[»]
1M63	X-ray	2.80	A/E	1-372	[»]
1MF8	X-ray	3.10	A	20-392	[»]
2JOG	NMR	-	A	21-347	[»]
2JZI	NMR	-	B	391-414	[»]
2P6B	X-ray	2.30	A/C	1-380	[»]
2R28	X-ray	1.86	C/D	389-413	[»]
2W73	X-ray	1.45	K/L/M/O	395-411	[»]
3LL8	X-ray	2.00	A/C	14-370	[»]
4F0Z	X-ray	1.70	A	1-370	[»]

DisProt

DP00092.

ProteinModelPortal

Q08209.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29315N.
DIP-6095N.

IntAct

Q08209. 8 interactions.

MINT

MINT-1037516.

STRING

9606.ENSP00000378323.

PTM databases

PhosphoSite

Q08209.

Polymorphism databases

DMDM

1352673.

Proteomic databases

PaxDb

Q08209.

PRIDE

Q08209.

Protocols and materials databases

DNASU

5530.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000323055; ENSP00000320580; ENSG00000138814.
ENST00000394853; ENSP00000378322; ENSG00000138814.
ENST00000394854; ENSP00000378323; ENSG00000138814.

GeneID

5530.

KEGG

hsa:5530.

UCSC

uc003hvt.2. human.
uc011cen.1. human.

Organism-specific databases

CTD

5530.

GeneCards

GC04M101944.

HGNC

HGNC:9314. PPP3CA.

HPA

CAB018581.
HPA012778.

MIM

114105. gene.

neXtProt

NX_Q08209.

PharmGKB

PA33678.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0639.

HOGENOM

HOG000172699.

HOVERGEN

HBG002819.

InParanoid

Q08209.

KO

K04348.

OMA

NKPNDEP.

OrthoDB

EOG4PVNZK.

Enzyme and pathway databases

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.

Reactome

REACT_111102. Signal Transduction.
REACT_118664. Calcineurin Dephosphorylates NFATC1/2/3.

Gene expression databases

ArrayExpress

Q08209.

Bgee

Q08209.

CleanEx

HS_PPP3CA.

Genevestigator

Q08209.

GermOnline

ENSG00000138814. Homo sapiens.

Family and domain databases

InterPro

IPR004843. Metallo_PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]

Pfam

PF00149. Metallophos. 1 hit.
[Graphical view]

PRINTS

PR00114. STPHPHTASE.

SMART

SM00156. PP2Ac. 1 hit.
[Graphical view]

PROSITE

PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q08209.

ChEMBL

CHEMBL4445.

ChiTaRS

PPP3CA. human.

EvolutionaryTrace

Q08209.

GenomeRNAi

5530.

NextBio

21422.

PMAP-CutDB

Q08209.

SOURCE

Search...

Entry information

Entry name

PP2BA_HUMAN

Accession

Primary (citable) accession number: Q08209
Secondary accession number(s): A8K3B7 , A8W6Z7, B5BUA2, Q8TAW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.