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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit 2

Gene

Pp2B-14D

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.2 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi156 – 1561IronBy similarity
Metal bindingi158 – 1581IronBy similarity
Metal bindingi184 – 1841IronBy similarity
Metal bindingi184 – 1841ZincBy similarity
Metal bindingi216 – 2161ZincBy similarity
Active sitei217 – 2171Proton donorBy similarity
Metal bindingi265 – 2651ZincBy similarity
Metal bindingi347 – 3471ZincBy similarity

GO - Molecular functioni

  1. calcium-dependent protein serine/threonine phosphatase activity Source: FlyBase
  2. calmodulin binding Source: FlyBase
  3. calmodulin-dependent protein phosphatase activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. protein serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  1. female meiotic division Source: FlyBase
  2. meiotic nuclear division Source: FlyBase
  3. protein dephosphorylation Source: FlyBase
  4. sleep Source: FlyBase
  5. wing disc development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calcium, Calmodulin-binding, Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_184321. Ca2+ pathway.
REACT_203584. FCERI mediated Ca+2 mobilization.
REACT_213958. DARPP-32 events.
SignaLinkiQ27889.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit 2 (EC:3.1.3.16)
Alternative name(s):
Calmodulin-dependent calcineurin A2 subunit
Gene namesi
Name:Pp2B-14D
ORF Names:CG9842
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0011826. Pp2B-14D.

Subcellular locationi

GO - Cellular componenti

  1. calcineurin complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 570570Serine/threonine-protein phosphatase 2B catalytic subunit 2PRO_0000058831Add
BLAST

Proteomic databases

PaxDbiQ27889.
PRIDEiQ27889.

Expressioni

Tissue specificityi

Expressed in CNS and PNS.1 Publication

Developmental stagei

Expressed both maternally and zygotically in embryos, larvae and adults.2 Publications

Gene expression databases

BgeeiQ27889.

Interactioni

Subunit structurei

Interacts with sra in a complex that contains CanA-14F.2 Publications

Protein-protein interaction databases

BioGridi58962. 33 interactions.
DIPiDIP-17529N.
IntActiQ27889. 10 interactions.
MINTiMINT-809182.

Structurei

3D structure databases

ProteinModelPortaliQ27889.
SMRiQ27889. Positions 86-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 405Poly-Asn

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2B subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
InParanoidiQ27889.
KOiK04348.
OMAiIRVIQEC.
OrthoDBiEOG7BZVSC.
PhylomeDBiQ27889.

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]

Sequencei

Sequence statusi: Complete.

Q27889-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSNNQSSSV AQAATSARTV SAGSAEATDA NSTASNNNNN SSSTAAAGNN
60 70 80 90 100
SDNSSPTTGT GTGASTGKLH GGHTAVNTKE RVVDSVPFPP SHKLTLAEVF
110 120 130 140 150
DQRTGKPNHE LLKQHFILEG RIEEAPALKI IQDGAALLRQ EKTMIDIEAP
160 170 180 190 200
VTVCGDIHGQ FYDLMKLFEV GGSPASTKYL FLGDYVDRGY FSIECVLYLW
210 220 230 240 250
SLKITYPQTL FLLRGNHECR HLTEYFTFKQ ECKIKYSERV YDACMDAFDC
260 270 280 290 300
LPLAALMNQQ FLCVHGGLSP EIHELEDIRR LDRFKEPPAF GPMCDLLWSD
310 320 330 340 350
PLEDFGNEKN SDFYTHNSVR GCSYFYSYAA CCDFLQNNNL LSIIRAHEAQ
360 370 380 390 400
DAGYRMYRKS QTTGFPSLIT IFSAPNYLDV YNNKAAVLKY ENNVMNIRQF
410 420 430 440 450
NCSPHPYWLP NFMDVFTWSL PFVGEKVTEM LVNVLNICSD DELMTEESEE
460 470 480 490 500
PLSDDEAALR KEVIRNKIRA IGKMARVFSV LREESESVLQ LKGLTPTGAL
510 520 530 540 550
PLGALSGGKQ SLKNAMQGFS PNHKITSFAE AKGLDAVNER MPPRRDQPPT
560 570
PSEDPNQHSQ QGGKNGAGHG
Length:570
Mass (Da):63,101
Last modified:August 30, 2005 - v2
Checksum:i4A5429A620C0C275
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111Missing(PubMed:8849894)Curated
Sequence conflicti133 – 1331D → E in CAA54807. (PubMed:8313960)Curated
Sequence conflicti175 – 1751A → Q in CAA54807. (PubMed:8313960)Curated
Sequence conflicti175 – 1751A → Q in AAB29893. (PubMed:8849894)Curated
Sequence conflicti323 – 33311SYFYSYAACCD → CY in CAA54807. (PubMed:8313960)CuratedAdd
BLAST
Sequence conflicti407 – 4071Y → I in CAA54807. (PubMed:8313960)Curated
Sequence conflicti459 – 4591L → V in CAA54807. (PubMed:8313960)Curated
Sequence conflicti491 – 4911Missing in CAA54807. (PubMed:8313960)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77768 mRNA. Translation: CAA54807.1.
S68806 mRNA. Translation: AAB29893.1.
AE014298 Genomic DNA. Translation: AAF48622.1.
BT010083 mRNA. Translation: AAQ22552.1.
PIRiS41743.
S70551.
RefSeqiNP_001245715.1. NM_001258786.3.
NP_001245716.1. NM_001258787.2.
NP_523373.2. NM_078649.4.
UniGeneiDm.33340.

Genome annotation databases

EnsemblMetazoaiFBtr0074294; FBpp0074069; FBgn0011826.
FBtr0305593; FBpp0294044; FBgn0011826.
FBtr0309793; FBpp0301546; FBgn0011826.
GeneIDi32624.
KEGGidme:Dmel_CG9842.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77768 mRNA. Translation: CAA54807.1.
S68806 mRNA. Translation: AAB29893.1.
AE014298 Genomic DNA. Translation: AAF48622.1.
BT010083 mRNA. Translation: AAQ22552.1.
PIRiS41743.
S70551.
RefSeqiNP_001245715.1. NM_001258786.3.
NP_001245716.1. NM_001258787.2.
NP_523373.2. NM_078649.4.
UniGeneiDm.33340.

3D structure databases

ProteinModelPortaliQ27889.
SMRiQ27889. Positions 86-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58962. 33 interactions.
DIPiDIP-17529N.
IntActiQ27889. 10 interactions.
MINTiMINT-809182.

Proteomic databases

PaxDbiQ27889.
PRIDEiQ27889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074294; FBpp0074069; FBgn0011826.
FBtr0305593; FBpp0294044; FBgn0011826.
FBtr0309793; FBpp0301546; FBgn0011826.
GeneIDi32624.
KEGGidme:Dmel_CG9842.

Organism-specific databases

CTDi32624.
FlyBaseiFBgn0011826. Pp2B-14D.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000063087.
InParanoidiQ27889.
KOiK04348.
OMAiIRVIQEC.
OrthoDBiEOG7BZVSC.
PhylomeDBiQ27889.

Enzyme and pathway databases

ReactomeiREACT_184321. Ca2+ pathway.
REACT_203584. FCERI mediated Ca+2 mobilization.
REACT_213958. DARPP-32 events.
SignaLinkiQ27889.

Miscellaneous databases

GenomeRNAii32624.
NextBioi779520.

Gene expression databases

BgeeiQ27889.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a cDNA encoding a Drosophila calcium/calmodulin regulated protein phosphatase, which has its most abundant expression in the early embryo."
    Brown L., Chen M.X., Cohen P.T.W.
    FEBS Lett. 339:124-128(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
    Strain: Oregon-R.
    Tissue: Eye imaginal disk.
  2. "Molecular characterization of neurally expressing genes in the para sodium channel gene cluster of Drosophila."
    Hong C.-S., Ganetzky B.
    Genetics 142:879-892(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "The calcineurin regulator sra plays an essential role in female meiosis in Drosophila."
    Takeo S., Tsuda M., Akahori S., Matsuo T., Aigaki T.
    Curr. Biol. 16:1435-1440(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SRA.
  7. "Shaggy/glycogen synthase kinase 3beta and phosphorylation of Sarah/regulator of calcineurin are essential for completion of Drosophila female meiosis."
    Takeo S., Swanson S.K., Nandanan K., Nakai Y., Aigaki T., Washburn M.P., Florens L., Hawley R.S.
    Proc. Natl. Acad. Sci. U.S.A. 109:6382-6389(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRA.

Entry informationi

Entry nameiPP2B2_DROME
AccessioniPrimary (citable) accession number: Q27889
Secondary accession number(s): Q26248, Q9VXF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 30, 2005
Last modified: January 7, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.