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Q08209

- PP2BA_HUMAN

UniProt

Q08209 - PP2BA_HUMAN

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
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    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

    Binds 1 Fe3+ ion per subunit.
    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 binding Source: UniProtKB
    7. protein dimerization activity Source: UniProtKB
    8. 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

    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. sarcolemma Source: UniProtKB-SubCell
    8. Z disc Source: Ensembl

    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

    ArrayExpressiQ08209.
    BgeeiQ08209.
    CleanExiHS_PPP3CA.
    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. 40 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 – 133
    Helixi31 – 344
    Helixi43 – 519
    Helixi58 – 7316
    Beta strandi77 – 815
    Beta strandi83 – 886
    Helixi95 – 10511
    Turni108 – 1103
    Beta strandi113 – 1153
    Beta strandi120 – 1234
    Helixi126 – 13914
    Turni141 – 1433
    Beta strandi144 – 1463
    Helixi154 – 1596
    Helixi162 – 1698
    Helixi172 – 18312
    Beta strandi188 – 1914
    Turni192 – 1943
    Beta strandi195 – 2006
    Beta strandi206 – 2083
    Helixi210 – 2134
    Beta strandi218 – 2203
    Beta strandi223 – 2253
    Helixi226 – 2327
    Turni237 – 2404
    Beta strandi247 – 2504
    Turni252 – 2543
    Beta strandi255 – 2606
    Helixi262 – 27110
    Beta strandi276 – 2794
    Beta strandi287 – 2904
    Turni295 – 2973
    Beta strandi298 – 3069
    Helixi311 – 3133
    Beta strandi319 – 3257
    Beta strandi328 – 3347
    Helixi344 – 3463
    Helixi349 – 36921
    Helixi396 – 40914
    Helixi470 – 4778
    Helixi478 – 4814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    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

    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 SYPAVCEFLQ 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
    KALTSETNGT DSNGSNSSNI Q 521
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    DisProti DP00092.
    ProteinModelPortali Q08209.
    SMRi Q08209. Positions 14-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111522. 40 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.
    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

    ArrayExpressi Q08209.
    Bgeei Q08209.
    CleanExi HS_PPP3CA.
    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

    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: October 1, 2014
    This is version 155 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