Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P48462 (PP1B_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase beta isoform

EC=3.1.3.16
Alternative name(s):
Protein flap wing
Gene names
Name:flw
Synonyms:PP1-9C, PP1-BETA-9C
ORF Names:CG2096
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for cell adhesion in non-muscle tissues and in maintenance of muscle attachment. Vital for larval development. Ref.2

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subunit structure

Interacts with Nop17l. Ref.5

Sequence similarities

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

Ontologies

Keywords
   Biological processCell adhesion
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

chromosome segregation

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

female germline ring canal formation

Inferred from mutant phenotype PubMed 15269282PubMed 23936219. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 15269282. Source: FlyBase

mesoderm development

Non-traceable author statement PubMed 11486054. Source: FlyBase

negative regulation of JNK cascade

Inferred from genetic interaction PubMed 17277363. Source: FlyBase

oocyte nucleus migration involved in oocyte dorsal/ventral axis specification

Inferred from mutant phenotype PubMed 21490061. Source: FlyBase

ovarian nurse cell to oocyte transport

Inferred from mutant phenotype PubMed 15269282. Source: FlyBase

protein dephosphorylation

Inferred from sequence or structural similarity PubMed 2550221. Source: FlyBase

regulation of actomyosin contractile ring contraction

Inferred from mutant phenotype PubMed 23936219. Source: FlyBase

striated muscle tissue development

Inferred from mutant phenotype PubMed 410901. Source: FlyBase

   Cellular_componentprotein phosphatase type 1 complex

Inferred from sequence or structural similarity PubMed 2550221. Source: FlyBase

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin phosphatase activity

Inferred from direct assay PubMed 15269282. Source: FlyBase

protein binding

Inferred from physical interaction Ref.5. Source: IntAct

protein serine/threonine phosphatase activity

Inferred from sequence or structural similarity PubMed 2550221. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Nop17lQ0E9G33EBI-869621,EBI-150380

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Serine/threonine-protein phosphatase beta isoform
PRO_0000058794

Sites

Active site1241Proton donor By similarity
Metal binding631Manganese 1 By similarity
Metal binding651Manganese 1 By similarity
Metal binding911Manganese 1 By similarity
Metal binding911Manganese 2 By similarity
Metal binding1231Manganese 2 By similarity
Metal binding1721Manganese 2 By similarity
Metal binding2471Manganese 2 By similarity

Amino acid modifications

Modified residue3151Phosphothreonine Ref.6
Modified residue3161Phosphothreonine Ref.6

Experimental info

Mutagenesis1331Y → F: Semi lethal, adult escapers exhibit muscle and wing mutant phenotype; allele flw-6. Ref.2
Mutagenesis2841V → A: Muscle and wing mutant phenotype; allele flw-1. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48462 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9233DFC06EAE17AD

FASTA33037,740
        10         20         30         40         50         60 
MGDFDLNVDS LIQRLLEMRS CRTGKQVQMT EAEVRGLCLK SREIFLQQPI LLELEAPLII 

        70         80         90        100        110        120 
CGDIHGQYTD LLRLFEYGGF PPAANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL 

       130        140        150        160        170        180 
RGNHECASIN RIYGFYDECK RRYNVKLWKT FTDCFNCLPV AAIIDEKIFC CHGGLSPDLQ 

       190        200        210        220        230        240 
GMEQIRRLMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGVDV VSKFLNRHEL 

       250        260        270        280        290        300 
DLICRAHQVV EDGYEFFARR QLVTLFSAPN YCGEFDNAGG MMTVDDTLMC SFQILKPSEK 

       310        320        330 
KAKYLYSGMN SSRPTTPQRS APMLATNKKK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56439 mRNA. Translation: CAA39821.1.
AJ249214, AJ249215 Genomic DNA. Translation: CAB59732.1.
AE014298 Genomic DNA. Translation: AAF46583.2.
PIRS13828.
RefSeqNP_001259407.1. NM_001272478.1.
NP_524738.1. NM_079999.3.
UniGeneDm.7222.

3D structure databases

ProteinModelPortalP48462.
SMRP48462. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68952. 26 interactions.
IntActP48462. 28 interactions.

Proteomic databases

PaxDbP48462.
PRIDEP48462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071447; FBpp0071382; FBgn0000711.
FBtr0333305; FBpp0305497; FBgn0000711.
GeneID44289.
KEGGdme:Dmel_CG2096.

Organism-specific databases

CTD44289.
FlyBaseFBgn0000711. flw.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000062911.
HOGENOMHOG000263972.
InParanoidP48462.
KOK06269.
OrthoDBEOG7TJ3K3.
PhylomeDBP48462.

Enzyme and pathway databases

SignaLinkP48462.

Gene expression databases

BgeeP48462.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSflw. drosophila.
GenomeRNAi44289.
NextBio837117.
PROP48462.

Entry information

Entry namePP1B_DROME
AccessionPrimary (citable) accession number: P48462
Secondary accession number(s): Q9W2V5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase