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O76932

- PP4C_DROME

UniProt

O76932 - PP4C_DROME

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Protein
Serine/threonine-protein phosphatase 4 catalytic subunit
Gene
Pp4-19C, pp4, CG32505
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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).2 Publications

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 bindingi54 – 541Manganese 1 By similarity
Metal bindingi56 – 561Manganese 1 By similarity
Metal bindingi82 – 821Manganese 1 By similarity
Metal bindingi82 – 821Manganese 2 By similarity
Metal bindingi114 – 1141Manganese 2 By similarity
Active sitei115 – 1151Proton donor By similarity
Metal bindingi164 – 1641Manganese 2 By similarity
Metal bindingi238 – 2381Manganese 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  1. microtubule-based process Source: FlyBase
  2. mitotic cell cycle Source: FlyBase
  3. neurogenesis Source: FlyBase
  4. protein dephosphorylation Source: FlyBase
  5. regulation of mitotic cell cycle Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

SignaLinkiO76932.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 4 catalytic subunit (EC:3.1.3.16)
Short name:
PP4C
Gene namesi
Name:Pp4-19C
Synonyms:pp4
ORF Names:CG32505
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0023177. Pp4-19C.

Subcellular locationi

Cytoplasm. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication

GO - Cellular componenti

  1. centrosome Source: FlyBase
  2. cytoplasm Source: FlyBase
  3. nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Serine/threonine-protein phosphatase 4 catalytic subunit
PRO_0000353208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei307 – 3071Leucine methyl ester By similarity

Post-translational modificationi

Reversibly methyl esterified on Leu-307 by leucine carboxyl methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1 (PPME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization By similarity.

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiO76932.
PRIDEiO76932.

Expressioni

Gene expression databases

BgeeiO76932.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi69445. 10 interactions.
IntActiO76932. 5 interactions.
MINTiMINT-1643247.
STRINGi7227.FBpp0077017.

Structurei

3D structure databases

ProteinModelPortaliO76932.
SMRiO76932. Positions 6-291.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
InParanoidiO76932.
KOiK15423.
OMAiVFNHRND.
OrthoDBiEOG74N5H2.
PhylomeDBiO76932.

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.

O76932-1 [UniParc]FASTAAdd to Basket

« Hide

MSDYSDLDRQ IEQLKRCEII KENEVKALCA KAREILVEEG NVQRVDSPVT    50
VCGDIHGQFY DLKELFKVGG DVPEKNYLFM GDFVDRGYYS VETFLLLLAL 100
KVRYPDRITL IRGNHESRQI TQVYGFYDEC LRKYGSTAVW RYCTEIFDYL 150
SLSAIIDGKI FCVHGGLSPS IQYLDQIRSI DRKQEVPHDG PMCDLLWSDP 200
EDQTGWGVSP RGAGYLFGSD VVSQFNRTND IDMICRAHQL VMEGFKWHFN 250
ETVLTVWSAP NYCYRCGNVA AILELNEYLH RDFVIFEAAP QESRGIPSKK 300
PQADYFL 307
Length:307
Mass (Da):35,341
Last modified:November 1, 1998 - v1
Checksum:i514FCCB93A345E2E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y14213 Genomic DNA. Translation: CAA74606.1.
AE014298 Genomic DNA. Translation: AAF50905.1.
AE014298 Genomic DNA. Translation: AAN09547.1.
AY113503 mRNA. Translation: AAM29508.1.
RefSeqiNP_524803.1. NM_080064.2.
NP_728342.1. NM_167703.3.
UniGeneiDm.1809.

Genome annotation databases

EnsemblMetazoaiFBtr0077324; FBpp0077016; FBgn0023177.
FBtr0077325; FBpp0077017; FBgn0023177.
GeneIDi45031.
KEGGidme:Dmel_CG32505.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y14213 Genomic DNA. Translation: CAA74606.1 .
AE014298 Genomic DNA. Translation: AAF50905.1 .
AE014298 Genomic DNA. Translation: AAN09547.1 .
AY113503 mRNA. Translation: AAM29508.1 .
RefSeqi NP_524803.1. NM_080064.2.
NP_728342.1. NM_167703.3.
UniGenei Dm.1809.

3D structure databases

ProteinModelPortali O76932.
SMRi O76932. Positions 6-291.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 69445. 10 interactions.
IntActi O76932. 5 interactions.
MINTi MINT-1643247.
STRINGi 7227.FBpp0077017.

Proteomic databases

PaxDbi O76932.
PRIDEi O76932.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0077324 ; FBpp0077016 ; FBgn0023177 .
FBtr0077325 ; FBpp0077017 ; FBgn0023177 .
GeneIDi 45031.
KEGGi dme:Dmel_CG32505.

Organism-specific databases

CTDi 45031.
FlyBasei FBgn0023177. Pp4-19C.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00550000074618.
InParanoidi O76932.
KOi K15423.
OMAi VFNHRND.
OrthoDBi EOG74N5H2.
PhylomeDBi O76932.

Enzyme and pathway databases

SignaLinki O76932.

Miscellaneous databases

GenomeRNAii 45031.
NextBioi 837889.
PROi O76932.

Gene expression databases

Bgeei O76932.

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. "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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiPP4C_DROME
AccessioniPrimary (citable) accession number: O76932
Secondary accession number(s): Q9VR98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 107 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