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Protein

Protein phosphatase PHLPP-like protein

Gene

Phlpp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Protein phosphatase that specifically mediates dephosphorylation of 'Ser-586' of Akt1, a protein that regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-586' of Akt1 triggers apoptosis and suppression of tumor growth.1 Publication

Catalytic activityi

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

Cofactori

Mn2+By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. protein dephosphorylation Source: UniProtKB
  3. regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_276010. Negative regulation of the PI3K/AKT network.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase PHLPP-like protein (EC:3.1.3.16)
Alternative name(s):
PH domain leucine-rich repeat protein phosphatase
dPHLPP
Gene namesi
Name:Phlpp
ORF Names:CG10493
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0032749. Phlpp.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 954954Protein phosphatase PHLPP-like proteinPRO_0000057787Add
BLAST

Proteomic databases

PRIDEiQ9VJ07.

Expressioni

Gene expression databases

BgeeiQ9VJ07.

Interactioni

Protein-protein interaction databases

IntActiQ9VJ07. 2 interactions.
STRINGi7227.FBpp0080693.

Structurei

3D structure databases

ProteinModelPortaliQ9VJ07.
SMRiQ9VJ07. Positions 48-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati69 – 8921LRR 1Add
BLAST
Repeati90 – 10415LRR 2Add
BLAST
Repeati110 – 13122LRR 3Add
BLAST
Repeati135 – 15622LRR 4Add
BLAST
Repeati158 – 17922LRR 5Add
BLAST
Repeati183 – 20220LRR 6Add
BLAST
Repeati206 – 22722LRR 7Add
BLAST
Repeati231 – 25222LRR 8Add
BLAST
Repeati255 – 27521LRR 9Add
BLAST
Repeati279 – 30022LRR 10Add
BLAST
Repeati303 – 32422LRR 11Add
BLAST
Repeati326 – 34722LRR 12Add
BLAST
Repeati348 – 36922LRR 13Add
BLAST
Repeati372 – 39322LRR 14Add
BLAST
Domaini437 – 655219PPM-type phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 14 LRR (leucine-rich) repeats.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiNOG240924.
GeneTreeiENSGT00440000037833.
InParanoidiQ9VJ07.
KOiK16340.
OMAiVCENEME.
OrthoDBiEOG7RFTGK.
PhylomeDBiQ9VJ07.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR001932. PP2C-like_dom.
[Graphical view]
PfamiPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 1 hit.
PF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS51450. LRR. 12 hits.
PS51746. PPM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VJ07-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKATRKQAD PYKSKLKVSA SHSGPHPLPV EVTAAEEEQA ATFGQTSPQK
60 70 80 90 100
LSLKGSQLGG SILIGNYNYL TQLEVCENEM EVLDLSSLAQ LETLKCSRNK
110 120 130 140 150
LMELIINGTN LQTLVADHNY LHNISTTNTH PVPLKLQRID ISHNNFSELP
160 170 180 190 200
NWVGACASLT AINASHNRLN NVAVLLRNYR ITELVSLDLA YNDLKQLDQF
210 220 230 240 250
PEGFSSIRSL QLQSNELPSL PDNFFAVTHA RLETLNVSCN KLSTLPRYEQ
260 270 280 290 300
NNHAALVNLS LAGNHLNDSI FEPLHNAAKL RVLHLAYNRI GVLPAACVRN
310 320 330 340 350
WPELEILVLS GNMLQQLPEE VATLGQLRVL RCCNNLLLCT PQLAKLAMLK
360 370 380 390 400
VLDLSHNHLD RVNLLALVPS RNLKYLDLSG NLQLQVDEQQ FKVCQSQSQR
410 420 430 440 450
HWSLVDVSGN NRAALPTTKI RQVSAQRNQN KTSGPWTMGF AETPGSGDCR
460 470 480 490 500
KLSVYQLRAA NYGGSDEALY GMFEALEGRG RAAQEMSHLV PDLMKQEQMV
510 520 530 540 550
KDSAVRDYMK FTLLAAQQQC GSVRSAALFH LTRTRAPSKV RPLKSKRYVL
560 570 580 590 600
RMASTGGLDA YLIRRTSQLR LTKPDVIQKD QIHSMPDPHV LELILSNDDE
610 620 630 640 650
YLVVGNAQLW SVMDIDRAAR EIRKEENSLL AAKRLVDIAQ SFAAAESLSV
660 670 680 690 700
IVVRFRHLGT DVDHLIRELK QSVRKKPQPV SLPLSSGSVC KRTCCDRSNA
710 720 730 740 750
CRHRAIEQEP LAGRSSPSGQ SDRDLLAKDK DDEFVLAHAR VLQEEQQLEM
760 770 780 790 800
LDETESVSES VLSEEQFKCW EYMLEQNTQL LFDKELNTIS KSFTKQRTVP
810 820 830 840 850
NAIMAATVLP ERNDFTSNLM RTVTNKFIST STPQLPQPIT TSVPLGSYHQ
860 870 880 890 900
VKQAPPGHFG SALSFQQAHS YGYNLFDAKP RPKFHGGTVK RSAGPNSAYF
910 920 930 940 950
GSLQRLMPYN FEYDFAVTQE RERNILDEEE HDDDDFNEHE SRMRKYWGVA

TTEL
Length:954
Mass (Da):107,092
Last modified:April 30, 2000 - v1
Checksum:i7ADCF6F54F15957A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53751.1.
RefSeqiNP_001260558.1. NM_001273629.1.
NP_609938.1. NM_136094.2.
UniGeneiDm.17963.

Genome annotation databases

EnsemblMetazoaiFBtr0081149; FBpp0080693; FBgn0032749.
FBtr0336844; FBpp0307805; FBgn0032749.
GeneIDi35178.
KEGGidme:Dmel_CG10493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF53751.1.
RefSeqiNP_001260558.1. NM_001273629.1.
NP_609938.1. NM_136094.2.
UniGeneiDm.17963.

3D structure databases

ProteinModelPortaliQ9VJ07.
SMRiQ9VJ07. Positions 48-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9VJ07. 2 interactions.
STRINGi7227.FBpp0080693.

Proteomic databases

PRIDEiQ9VJ07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081149; FBpp0080693; FBgn0032749.
FBtr0336844; FBpp0307805; FBgn0032749.
GeneIDi35178.
KEGGidme:Dmel_CG10493.

Organism-specific databases

CTDi35178.
FlyBaseiFBgn0032749. Phlpp.

Phylogenomic databases

eggNOGiNOG240924.
GeneTreeiENSGT00440000037833.
InParanoidiQ9VJ07.
KOiK16340.
OMAiVCENEME.
OrthoDBiEOG7RFTGK.
PhylomeDBiQ9VJ07.

Enzyme and pathway databases

ReactomeiREACT_276010. Negative regulation of the PI3K/AKT network.

Miscellaneous databases

GenomeRNAii35178.
NextBioi792238.

Gene expression databases

BgeeiQ9VJ07.

Family and domain databases

Gene3Di3.60.40.10. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR001932. PP2C-like_dom.
[Graphical view]
PfamiPF00560. LRR_1. 2 hits.
PF13855. LRR_8. 1 hit.
PF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS51450. LRR. 12 hits.
PS51746. PPM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. "PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth."
    Gao T., Furnari F., Newton A.C.
    Mol. Cell 18:13-24(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPHLPP_DROME
AccessioniPrimary (citable) accession number: Q9VJ07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2005
Last sequence update: April 30, 2000
Last modified: March 31, 2015
This is version 102 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.