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Protein

Serine/threonine-protein phosphatase beta isoform

Gene

flw

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

Functioni

Required for cell adhesion in non-muscle tissues and in maintenance of muscle attachment. Vital for larval development.1 Publication

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Manganese 1By similarity
Metal bindingi65 – 651Manganese 1By similarity
Metal bindingi91 – 911Manganese 1By similarity
Metal bindingi91 – 911Manganese 2By similarity
Metal bindingi123 – 1231Manganese 2By similarity
Active sitei124 – 1241Proton donorBy similarity
Metal bindingi172 – 1721Manganese 2By similarity
Metal bindingi247 – 2471Manganese 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • myosin phosphatase activity Source: FlyBase
  • protein serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • chromosome segregation Source: FlyBase
  • female germline ring canal formation Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • mesoderm development Source: FlyBase
  • negative regulation of JNK cascade Source: FlyBase
  • oocyte nucleus migration involved in oocyte dorsal/ventral axis specification Source: FlyBase
  • ovarian nurse cell to oocyte transport Source: FlyBase
  • protein dephosphorylation Source: FlyBase
  • regulation of actomyosin contractile ring contraction Source: FlyBase
  • striated muscle tissue development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_290875. Regulation of PLK1 Activity at G2/M Transition.
REACT_292430. Circadian Clock.
REACT_358651. RHO GTPases Activate ROCKs.
SignaLinkiP48462.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase beta isoform (EC:3.1.3.16)
Alternative name(s):
Protein flap wing
Gene namesi
Name:flw
Synonyms:PP1-9C, PP1-BETA-9C
ORF Names:CG2096
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000711. flw.

Subcellular locationi

GO - Cellular componenti

  • protein phosphatase type 1 complex Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi133 – 1331Y → F: Semi lethal, adult escapers exhibit muscle and wing mutant phenotype; allele flw-6. 1 Publication
Mutagenesisi284 – 2841V → A: Muscle and wing mutant phenotype; allele flw-1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Serine/threonine-protein phosphatase beta isoformPRO_0000058794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151Phosphothreonine1 Publication
Modified residuei316 – 3161Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP48462.
PRIDEiP48462.

Expressioni

Gene expression databases

BgeeiP48462.

Interactioni

Subunit structurei

Interacts with Nop17l.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Nop17lQ0E9G33EBI-869621,EBI-150380

Protein-protein interaction databases

BioGridi68952. 26 interactions.
IntActiP48462. 28 interactions.

Structurei

3D structure databases

ProteinModelPortaliP48462.
SMRiP48462. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000263972.
InParanoidiP48462.
KOiK06269.
OrthoDBiEOG7TJ3K3.
PhylomeDBiP48462.

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.

P48462-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDFDLNVDS LIQRLLEMRS CRTGKQVQMT EAEVRGLCLK SREIFLQQPI
60 70 80 90 100
LLELEAPLII CGDIHGQYTD LLRLFEYGGF PPAANYLFLG DYVDRGKQSL
110 120 130 140 150
ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRYNVKLWKT
160 170 180 190 200
FTDCFNCLPV AAIIDEKIFC CHGGLSPDLQ GMEQIRRLMR PTDVPDTGLL
210 220 230 240 250
CDLLWSDPDK DVQGWGENDR GVSFTFGVDV VSKFLNRHEL DLICRAHQVV
260 270 280 290 300
EDGYEFFARR QLVTLFSAPN YCGEFDNAGG MMTVDDTLMC SFQILKPSEK
310 320 330
KAKYLYSGMN SSRPTTPQRS APMLATNKKK
Length:330
Mass (Da):37,740
Last modified:February 1, 1996 - v1
Checksum:i9233DFC06EAE17AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56439 mRNA. Translation: CAA39821.1.
AJ249214, AJ249215 Genomic DNA. Translation: CAB59732.1.
AE014298 Genomic DNA. Translation: AAF46583.2.
PIRiS13828.
RefSeqiNP_001259407.1. NM_001272478.1.
NP_524738.1. NM_079999.3.
UniGeneiDm.7222.

Genome annotation databases

EnsemblMetazoaiFBtr0071447; FBpp0071382; FBgn0000711.
FBtr0333305; FBpp0305497; FBgn0000711.
GeneIDi44289.
KEGGidme:Dmel_CG2096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56439 mRNA. Translation: CAA39821.1.
AJ249214, AJ249215 Genomic DNA. Translation: CAB59732.1.
AE014298 Genomic DNA. Translation: AAF46583.2.
PIRiS13828.
RefSeqiNP_001259407.1. NM_001272478.1.
NP_524738.1. NM_079999.3.
UniGeneiDm.7222.

3D structure databases

ProteinModelPortaliP48462.
SMRiP48462. Positions 1-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68952. 26 interactions.
IntActiP48462. 28 interactions.

Proteomic databases

PaxDbiP48462.
PRIDEiP48462.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071447; FBpp0071382; FBgn0000711.
FBtr0333305; FBpp0305497; FBgn0000711.
GeneIDi44289.
KEGGidme:Dmel_CG2096.

Organism-specific databases

CTDi44289.
FlyBaseiFBgn0000711. flw.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
HOGENOMiHOG000263972.
InParanoidiP48462.
KOiK06269.
OrthoDBiEOG7TJ3K3.
PhylomeDBiP48462.

Enzyme and pathway databases

ReactomeiREACT_290875. Regulation of PLK1 Activity at G2/M Transition.
REACT_292430. Circadian Clock.
REACT_358651. RHO GTPases Activate ROCKs.
SignaLinkiP48462.

Miscellaneous databases

ChiTaRSiflw. fly.
GenomeRNAii44289.
NextBioi837117.
PROiP48462.

Gene expression databases

BgeeiP48462.

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. "Drosophila contains three genes that encode distinct isoforms of protein phosphatase 1."
    Dombradi V., Axton J.M., Brewis N.D., da Cruz e Silva E.F., Alphey L., Cohen P.T.W.
    Eur. J. Biochem. 194:739-745(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "Protein phosphatase 1beta is required for the maintenance of muscle attachments."
    Raghavan S., Williams I., Aslam H., Thomas D., Szoor B., Morgan G., Gross S., Turner J., Fernandes J., VijayRaghavan K., Alphey L.
    Curr. Biol. 10:269-272(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF TYR-133 AND VAL-284.
  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. "Towards a comprehensive analysis of the protein phosphatase 1 interactome in Drosophila."
    Bennett D., Lyulcheva E., Alphey L.
    J. Mol. Biol. 364:196-212(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOP17L.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315 AND THR-316, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiPP1B_DROME
AccessioniPrimary (citable) accession number: P48462
Secondary accession number(s): Q9W2V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 27, 2015
This is version 135 of the entry and version 1 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.