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Q08209

- PP2BA_HUMAN

UniProt

Q08209 - PP2BA_HUMAN

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Protein

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

Gene

PPP3CA

Organism
Homo sapiens (Human)
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, HSPB1 and SSH1.3 Publications

Catalytic activityi

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

Cofactori

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

Sites

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

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. calmodulin binding Source: UniProtKB
  3. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  4. drug binding Source: UniProtKB
  5. enzyme binding Source: UniProtKB
  6. protein dimerization activity Source: UniProtKB
  7. protein serine/threonine phosphatase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15334. DARPP-32 events.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_172761. 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, CNA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:9314. PPP3CA.

Subcellular locationi

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

GO - Cellular componenti

  1. calcineurin complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. mitochondrion Source: Ensembl
  5. nucleoplasm Source: Reactome
  6. nucleus Source: HPA
  7. plasma membrane Source: UniProtKB-KW
  8. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33678.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 521520Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoformPRO_0000058822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei224 – 2241Nitrated tyrosineBy similarity

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

MaxQBiQ08209.
PaxDbiQ08209.
PRIDEiQ08209.

PTM databases

PhosphoSiteiQ08209.

Miscellaneous databases

PMAP-CutDBQ08209.

Expressioni

Gene expression databases

BgeeiQ08209.
CleanExiHS_PPP3CA.
ExpressionAtlasiQ08209. baseline and differential.
GenevestigatoriQ08209.

Organism-specific databases

HPAiCAB018581.
HPA012778.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111522. 50 interactions.
DIPiDIP-6095N.
IntActiQ08209. 13 interactions.
MINTiMINT-1037516.
STRINGi9606.ENSP00000378323.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133Combined sources
Helixi31 – 344Combined sources
Helixi43 – 519Combined sources
Helixi58 – 7316Combined sources
Beta strandi77 – 815Combined sources
Beta strandi83 – 886Combined sources
Helixi95 – 10511Combined sources
Turni108 – 1103Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi120 – 1234Combined sources
Helixi126 – 13914Combined sources
Turni141 – 1433Combined sources
Beta strandi144 – 1463Combined sources
Helixi154 – 1596Combined sources
Helixi162 – 1698Combined sources
Helixi172 – 18312Combined sources
Beta strandi188 – 1914Combined sources
Turni192 – 1943Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi206 – 2083Combined sources
Helixi210 – 2134Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2253Combined sources
Helixi226 – 2327Combined sources
Turni237 – 2404Combined sources
Beta strandi247 – 2504Combined sources
Turni252 – 2543Combined sources
Beta strandi255 – 2606Combined sources
Helixi262 – 27110Combined sources
Beta strandi276 – 2794Combined sources
Beta strandi287 – 2904Combined sources
Turni295 – 2973Combined sources
Beta strandi298 – 3069Combined sources
Helixi311 – 3133Combined sources
Beta strandi319 – 3257Combined sources
Beta strandi328 – 3347Combined sources
Helixi344 – 3463Combined sources
Helixi349 – 36921Combined sources
Helixi396 – 40914Combined sources
Helixi470 – 4778Combined sources
Helixi478 – 4814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4Q5UX-ray1.95C391-414[»]
DisProtiDP00092.
ProteinModelPortaliQ08209.
SMRiQ08209. Positions 14-411.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08209.

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.
InParanoidiQ08209.
KOiK04348.
OMAiXATAAAR.
OrthoDBiEOG7PCJJX.
PhylomeDBiQ08209.
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 (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q08209-1) [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 SYPAVCEFLQ 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
KALTSETNGT DSNGSNSSNI Q
Length:521
Mass (Da):58,688
Last modified:February 1, 1996 - v1
Checksum:i16480D62DDBF1F40
GO
Isoform 2 (identifier: Q08209-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:511
Mass (Da):57,659
Checksum:iB1E98CC0D6034CCC
GO
Isoform 3 (identifier: Q08209-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     318-359: Missing.
     448-457: Missing.

Show »
Length:469
Mass (Da):52,672
Checksum:iA3365471746633B7
GO
Isoform 4 (identifier: Q08209-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-318: Missing.

Show »
Length:289
Mass (Da):31,736
Checksum:iB3AEE20F6A4F19B7
GO
Isoform 5 (identifier: Q08209-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:454
Mass (Da):51,245
Checksum:iE28DCB758984D380
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei20 – 8667Missing in isoform 5. 1 PublicationVSP_054467Add
BLAST
Alternative sequencei87 – 318232Missing in isoform 4. 1 PublicationVSP_047755Add
BLAST
Alternative sequencei318 – 35942Missing in isoform 3. 1 PublicationVSP_043378Add
BLAST
Alternative sequencei448 – 45710Missing in isoform 2 and isoform 3. 3 PublicationsVSP_018562

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34037.1. [Q08209-1]
CCDS47113.1. [Q08209-3]
CCDS47114.1. [Q08209-2]
PIRiS35067.
RefSeqiNP_000935.1. NM_000944.4. [Q08209-1]
NP_001124163.1. NM_001130691.1. [Q08209-2]
NP_001124164.1. NM_001130692.1. [Q08209-3]
UniGeneiHs.435512.

Genome annotation databases

EnsembliENST00000323055; ENSP00000320580; ENSG00000138814. [Q08209-3]
ENST00000394853; ENSP00000378322; ENSG00000138814. [Q08209-2]
ENST00000394854; ENSP00000378323; ENSG00000138814. [Q08209-1]
ENST00000512215; ENSP00000422781; ENSG00000138814. [Q08209-4]
GeneIDi5530.
KEGGihsa:5530.
UCSCiuc003hvt.2. human. [Q08209-2]
uc010ilj.2. human. [Q08209-3]
uc011cen.1. human. [Q08209-1]

Polymorphism databases

DMDMi1352673.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Calcineurin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS34037.1. [Q08209-1 ]
CCDS47113.1. [Q08209-3 ]
CCDS47114.1. [Q08209-2 ]
PIRi S35067.
RefSeqi NP_000935.1. NM_000944.4. [Q08209-1 ]
NP_001124163.1. NM_001130691.1. [Q08209-2 ]
NP_001124164.1. NM_001130692.1. [Q08209-3 ]
UniGenei Hs.435512.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
4Q5U X-ray 1.95 C 391-414 [» ]
DisProti DP00092.
ProteinModelPortali Q08209.
SMRi Q08209. Positions 14-411.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111522. 50 interactions.
DIPi DIP-6095N.
IntActi Q08209. 13 interactions.
MINTi MINT-1037516.
STRINGi 9606.ENSP00000378323.

Chemistry

BindingDBi Q08209.
ChEMBLi CHEMBL4445.

PTM databases

PhosphoSitei Q08209.

Polymorphism databases

DMDMi 1352673.

Proteomic databases

MaxQBi Q08209.
PaxDbi Q08209.
PRIDEi Q08209.

Protocols and materials databases

DNASUi 5530.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323055 ; ENSP00000320580 ; ENSG00000138814 . [Q08209-3 ]
ENST00000394853 ; ENSP00000378322 ; ENSG00000138814 . [Q08209-2 ]
ENST00000394854 ; ENSP00000378323 ; ENSG00000138814 . [Q08209-1 ]
ENST00000512215 ; ENSP00000422781 ; ENSG00000138814 . [Q08209-4 ]
GeneIDi 5530.
KEGGi hsa:5530.
UCSCi uc003hvt.2. human. [Q08209-2 ]
uc010ilj.2. human. [Q08209-3 ]
uc011cen.1. human. [Q08209-1 ]

Organism-specific databases

CTDi 5530.
GeneCardsi GC04M101944.
HGNCi HGNC:9314. PPP3CA.
HPAi CAB018581.
HPA012778.
MIMi 114105. gene.
neXtProti NX_Q08209.
PharmGKBi PA33678.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000063087.
HOGENOMi HOG000172699.
HOVERGENi HBG002819.
InParanoidi Q08209.
KOi K04348.
OMAi XATAAAR.
OrthoDBi EOG7PCJJX.
PhylomeDBi Q08209.
TreeFami TF105557.

Enzyme and pathway databases

Reactomei REACT_15334. DARPP-32 events.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_172761. Ca2+ pathway.

Miscellaneous databases

ChiTaRSi PPP3CA. human.
EvolutionaryTracei Q08209.
GeneWikii PPP3CA.
GenomeRNAii 5530.
NextBioi 21422.
PMAP-CutDB Q08209.
PROi Q08209.
SOURCEi Search...

Gene expression databases

Bgeei Q08209.
CleanExi HS_PPP3CA.
ExpressionAtlasi Q08209. baseline and differential.
Genevestigatori Q08209.

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. "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.
    , 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. 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.
    , 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.
    , 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. 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. Cited for: INTERACTION WITH DMN1L, FUNCTION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. 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.

Entry informationi

Entry nameiPP2BA_HUMAN
AccessioniPrimary (citable) accession number: Q08209
Secondary accession number(s): A1A441
, A8K3B7, A8W6Z7, A8W6Z8, B5BUA2, Q8TAW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3