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Q27884

- PPP6_DROME

UniProt

Q27884 - PPP6_DROME

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Protein

Serine/threonine-protein phosphatase 6 catalytic subunit

Gene

PpV

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

May be involved in controlling cellularization or in regulating transcription of the genes involved in this process.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 bindingi51 – 511Manganese 1By similarity
Metal bindingi53 – 531Manganese 1By similarity
Metal bindingi79 – 791Manganese 1By similarity
Metal bindingi79 – 791Manganese 2By similarity
Metal bindingi111 – 1111Manganese 2By similarity
Active sitei112 – 1121Proton donorBy similarity
Metal bindingi161 – 1611Manganese 2By similarity
Metal bindingi235 – 2351Manganese 2By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: FlyBase
  2. mitotic cell cycle Source: FlyBase
  3. protein dephosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

SignaLinkiQ27884.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 6 catalytic subunit (EC:3.1.3.16)
Short name:
PP6C
Alternative name(s):
Phosphatase V
Short name:
PP-V
Gene namesi
Name:PpV
Synonyms:PPPV6A
ORF Names:CG12217
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003139. PpV.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Serine/threonine-protein phosphatase 6 catalytic subunitPRO_0000058880Add
BLAST

Proteomic databases

PaxDbiQ27884.
PRIDEiQ27884.

Expressioni

Developmental stagei

Expressed at highest levels in 2-4 hours embryos.1 Publication

Gene expression databases

BgeeiQ27884.

Interactioni

Protein-protein interaction databases

BioGridi58069. 2 interactions.
DIPiDIP-20494N.
IntActiQ27884. 3 interactions.
MINTiMINT-803511.

Structurei

3D structure databases

ProteinModelPortaliQ27884.
SMRiQ27884. Positions 3-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074961.
InParanoidiQ27884.
KOiK15498.
OMAiVPETSYI.
OrthoDBiEOG74N5H2.
PhylomeDBiQ27884.

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.

Q27884-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGDVDKWIED VKKCKYLPEN ELKKLCEMVC DILLEETNIL PVSTPVTVCG
60 70 80 90 100
DIHGQFYDLE QLFRTGGQVP HTNYIFMGDF VDRGYYSLET FTRLLTLKAR
110 120 130 140 150
YPSRITLLRG NHETRQITKV YGFFDECFSK YGNANGWKYC CKVFDLLTIA
160 170 180 190 200
AIIDEEVLCV HGGLSPEIIT LDQIRTIDRN GEIPYKGAFC DLVWSDPEDM
210 220 230 240 250
EYWGQSPRGA GWLFGHNVTK DFMAINNLNL ICRAHQLVNE GIKYMFDGKL
260 270 280 290 300
VTVWSAPNYC YRCGNVAAIL SFETAEKRQT KIFLAVPDAE RVIPKQNTTP

YFL
Length:303
Mass (Da):34,759
Last modified:November 1, 1997 - v1
Checksum:i5269F971416E55EC
GO

Sequence cautioni

The sequence AAM51039.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75980 mRNA. Translation: CAA53588.1.
AE014298 Genomic DNA. Translation: AAF46163.1.
BT021230 mRNA. Translation: AAX33378.1.
AY119179 mRNA. Translation: AAM51039.1. Different initiation.
PIRiS39611.
RefSeqiNP_001259272.1. NM_001272343.1.
NP_001259273.1. NM_001272344.1.
NP_001259274.1. NM_001272345.1.
NP_511061.1. NM_078506.3.
UniGeneiDm.2624.

Genome annotation databases

EnsemblMetazoaiFBtr0070921; FBpp0070883; FBgn0003139.
FBtr0331430; FBpp0303847; FBgn0003139.
FBtr0331431; FBpp0303848; FBgn0003139.
FBtr0331432; FBpp0303849; FBgn0003139.
GeneIDi31582.
KEGGidme:Dmel_CG12217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75980 mRNA. Translation: CAA53588.1 .
AE014298 Genomic DNA. Translation: AAF46163.1 .
BT021230 mRNA. Translation: AAX33378.1 .
AY119179 mRNA. Translation: AAM51039.1 . Different initiation.
PIRi S39611.
RefSeqi NP_001259272.1. NM_001272343.1.
NP_001259273.1. NM_001272344.1.
NP_001259274.1. NM_001272345.1.
NP_511061.1. NM_078506.3.
UniGenei Dm.2624.

3D structure databases

ProteinModelPortali Q27884.
SMRi Q27884. Positions 3-277.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58069. 2 interactions.
DIPi DIP-20494N.
IntActi Q27884. 3 interactions.
MINTi MINT-803511.

Proteomic databases

PaxDbi Q27884.
PRIDEi Q27884.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0070921 ; FBpp0070883 ; FBgn0003139 .
FBtr0331430 ; FBpp0303847 ; FBgn0003139 .
FBtr0331431 ; FBpp0303848 ; FBgn0003139 .
FBtr0331432 ; FBpp0303849 ; FBgn0003139 .
GeneIDi 31582.
KEGGi dme:Dmel_CG12217.

Organism-specific databases

CTDi 31582.
FlyBasei FBgn0003139. PpV.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00550000074961.
InParanoidi Q27884.
KOi K15498.
OMAi VPETSYI.
OrthoDBi EOG74N5H2.
PhylomeDBi Q27884.

Enzyme and pathway databases

SignaLinki Q27884.

Miscellaneous databases

ChiTaRSi PpV. drosophila.
GenomeRNAii 31582.
NextBioi 774303.
PROi Q27884.

Gene expression databases

Bgeei Q27884.

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 protein phosphatase V functionally complements a SIT4 mutant in Saccharomyces cerevisiae and its amino-terminal region can confer this complementation to a heterologous phosphatase catalytic domain."
    Mann D.J., Dombradi V., Cohen P.T.W.
    EMBO J. 12:4833-4842(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Strain: Oregon-R.
    Tissue: Eye imaginal disk and Head.
  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. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-303.
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPPP6_DROME
AccessioniPrimary (citable) accession number: Q27884
Secondary accession number(s): Q5BIJ4, Q8MRZ7, Q9W3Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 1, 2014
This is version 126 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