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P48462

- PP1B_DROME

UniProt

P48462 - PP1B_DROME

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Protein
Serine/threonine-protein phosphatase beta isoform
Gene
flw, PP1-9C, PP1-BETA-9C, CG2096
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

Binds 2 manganese ions per subunit By similarity.

Sites

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

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. myosin phosphatase activity Source: FlyBase
  3. protein binding Source: IntAct
  4. protein serine/threonine phosphatase activity Source: FlyBase
Complete GO annotation...

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. chromosome segregation Source: FlyBase
  3. female germline ring canal formation Source: FlyBase
  4. imaginal disc-derived wing morphogenesis Source: FlyBase
  5. mesoderm development Source: FlyBase
  6. negative regulation of JNK cascade Source: FlyBase
  7. oocyte nucleus migration involved in oocyte dorsal/ventral axis specification Source: FlyBase
  8. ovarian nurse cell to oocyte transport Source: FlyBase
  9. protein dephosphorylation Source: FlyBase
  10. regulation of actomyosin contractile ring contraction Source: FlyBase
  11. 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_184294. Regulation of PLK1 Activity at G2/M Transition.
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: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000711. flw.

Subcellular locationi

GO - Cellular componenti

  1. 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 isoform
PRO_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.

Family & Domainsi

Sequence similaritiesi

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

MGDFDLNVDS LIQRLLEMRS CRTGKQVQMT EAEVRGLCLK SREIFLQQPI    50
LLELEAPLII CGDIHGQYTD LLRLFEYGGF PPAANYLFLG DYVDRGKQSL 100
ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRYNVKLWKT 150
FTDCFNCLPV AAIIDEKIFC CHGGLSPDLQ GMEQIRRLMR PTDVPDTGLL 200
CDLLWSDPDK DVQGWGENDR GVSFTFGVDV VSKFLNRHEL DLICRAHQVV 250
EDGYEFFARR QLVTLFSAPN YCGEFDNAGG MMTVDDTLMC SFQILKPSEK 300
KAKYLYSGMN SSRPTTPQRS APMLATNKKK 330
Length:330
Mass (Da):37,740
Last modified:February 1, 1996 - v1
Checksum:i9233DFC06EAE17AD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X56439 mRNA. Translation: CAA39821.1 .
AJ249214 , AJ249215 Genomic DNA. Translation: CAB59732.1 .
AE014298 Genomic DNA. Translation: AAF46583.2 .
PIRi S13828.
RefSeqi NP_001259407.1. NM_001272478.1.
NP_524738.1. NM_079999.3.
UniGenei Dm.7222.

3D structure databases

ProteinModelPortali P48462.
SMRi P48462. Positions 1-308.
ModBasei Search...

Protein-protein interaction databases

BioGridi 68952. 26 interactions.
IntActi P48462. 28 interactions.

Proteomic databases

PaxDbi P48462.
PRIDEi P48462.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0071447 ; FBpp0071382 ; FBgn0000711 .
FBtr0333305 ; FBpp0305497 ; FBgn0000711 .
GeneIDi 44289.
KEGGi dme:Dmel_CG2096.

Organism-specific databases

CTDi 44289.
FlyBasei FBgn0000711. flw.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00530000062911.
HOGENOMi HOG000263972.
InParanoidi P48462.
KOi K06269.
OrthoDBi EOG7TJ3K3.
PhylomeDBi P48462.

Enzyme and pathway databases

Reactomei REACT_184294. Regulation of PLK1 Activity at G2/M Transition.
SignaLinki P48462.

Miscellaneous databases

ChiTaRSi flw. drosophila.
GenomeRNAii 44289.
NextBioi 837117.
PROi P48462.

Gene expression databases

Bgeei P48462.

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. "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: September 3, 2014
This is version 129 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