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O76932 (PP4C_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 4 catalytic subunit

Short name=PP4C
EC=3.1.3.16
Gene names
Name:Pp4-19C
Synonyms:pp4
ORF Names:CG32505
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Protein phosphatase that regulates many processes such as microtubule organization at centrosomes. The probable PP4 complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase-induced cell death (in vitro). Ref.1 Ref.5

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Subunit structure

Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits By similarity. Probably part of a PP4 PPP4C-PPP4R2-PPP4R3 complex containing Pp4-19C, PPP4R2r and flfl.

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome Ref.1.

Sequence similarities

Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307Serine/threonine-protein phosphatase 4 catalytic subunit
PRO_0000353208

Sites

Active site1151Proton donor By similarity
Metal binding541Iron By similarity
Metal binding561Iron By similarity
Metal binding821Iron By similarity
Metal binding821Manganese By similarity
Metal binding1141Manganese By similarity
Metal binding1641Manganese By similarity
Metal binding2381Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
O76932 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 514FCCB93A345E2E

FASTA30735,341
        10         20         30         40         50         60 
MSDYSDLDRQ IEQLKRCEII KENEVKALCA KAREILVEEG NVQRVDSPVT VCGDIHGQFY 

        70         80         90        100        110        120 
DLKELFKVGG DVPEKNYLFM GDFVDRGYYS VETFLLLLAL KVRYPDRITL IRGNHESRQI 

       130        140        150        160        170        180 
TQVYGFYDEC LRKYGSTAVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IQYLDQIRSI 

       190        200        210        220        230        240 
DRKQEVPHDG PMCDLLWSDP EDQTGWGVSP RGAGYLFGSD VVSQFNRTND IDMICRAHQL 

       250        260        270        280        290        300 
VMEGFKWHFN ETVLTVWSAP NYCYRCGNVA AILELNEYLH RDFVIFEAAP QESRGIPSKK 


PQADYFL 

« Hide

References

« Hide 'large scale' references
[1]"Protein phosphatase 4 is an essential enzyme required for organisation of microtubules at centrosomes in Drosophila embryos."
Helps N.R., Brewis N.D., Lineruth K., Davis T., Kaiser K., Cohen P.T.W.
J. Cell Sci. 111:1331-1340(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: Oregon-R.
[2]"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.
[3]"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.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Depletion of protein phosphatase 4 in human cells reveals essential roles in centrosome maturation, cell migration and the regulation of Rho GTPases."
Martin-Granados C., Philp A., Oxenham S.K., Prescott A.R., Cohen P.T.W.
Int. J. Biochem. Cell Biol. 40:2315-2332(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE COMPONENT OF A COMPLEX WITH PPP4R2R AND FLFL, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14213 Genomic DNA. Translation: CAA74606.1.
AE014298 Genomic DNA. Translation: AAF50905.1.
AE014298 Genomic DNA. Translation: AAN09547.1.
AY113503 mRNA. Translation: AAM29508.1.
RefSeqNP_524803.1. NM_080064.2.
NP_728342.1. NM_167703.3.
UniGeneDm.1809.

3D structure databases

ProteinModelPortalO76932.
SMRO76932. Positions 6-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid69445. 10 interactions.
IntActO76932. 5 interactions.
MINTMINT-1643247.
STRING7227.FBpp0077017.

Proteomic databases

PaxDbO76932.
PRIDEO76932.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0077324; FBpp0077016; FBgn0023177.
FBtr0077325; FBpp0077017; FBgn0023177.
GeneID45031.
KEGGdme:Dmel_CG32505.

Organism-specific databases

CTD45031.
FlyBaseFBgn0023177. Pp4-19C.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074618.
InParanoidO76932.
KOK15423.
OMAVFNHRND.
OrthoDBEOG74N5H2.
PhylomeDBO76932.

Enzyme and pathway databases

SignaLinkO76932.

Gene expression databases

BgeeO76932.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi45031.
NextBio837889.
PROO76932.

Entry information

Entry namePP4C_DROME
AccessionPrimary (citable) accession number: O76932
Secondary accession number(s): Q9VR98
Entry history
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 104 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