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Protein

Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit

Gene

Pp2A-29B

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

Functioni

The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.By similarity

GO - Molecular functioni

  • protein phosphatase type 2A regulator activity Source: FlyBase

GO - Biological processi

  • autophagy Source: FlyBase
  • centriole replication Source: FlyBase
  • centrosome cycle Source: FlyBase
  • centrosome duplication Source: FlyBase
  • centrosome organization Source: FlyBase
  • chromosome segregation Source: FlyBase
  • mitotic spindle assembly Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • neurogenesis Source: FlyBase
  • phagocytosis Source: FlyBase
  • protein dephosphorylation Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • spindle assembly Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-DME-1295596. Spry regulation of FGF signaling.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-196299. Beta-catenin phosphorylation cascade.
R-DME-198753. ERK/MAPK targets.
R-DME-202670. ERKs are inactivated.
R-DME-2995383. Initiation of Nuclear Envelope Reformation.
R-DME-389513. CTLA4 inhibitory signaling.
R-DME-5673000. RAF activation.
R-DME-5675221. Negative regulation of MAPK pathway.
R-DME-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-DME-69231. Cyclin D associated events in G1.
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
Alternative name(s):
PR65
Protein phosphatase PP2A regulatory subunit A
Gene namesi
ORF Names:CG17291
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0260439. Pp2A-29B.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: FlyBase
  • cytoplasm Source: FlyBase
  • protein phosphatase type 2A complex Source: FlyBase
  • protein serine/threonine phosphatase complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 591590Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunitPRO_0000071408Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP36179.
PRIDEiP36179.

Expressioni

Tissue specificityi

Expression varies in tissues throughout development. Highly distributed expression in early embryos. In late embryonal development, found at high levels in nervous system and gonads. In third instar larvae, found in brain, imaginal disks and salivary glands.1 Publication

Developmental stagei

Expressed both maternally and zygotically. Expressed at lower levels in larvae and adult.1 Publication

Gene expression databases

BgeeiFBgn0260439.
ExpressionAtlasiP36179. differential.
GenevisibleiP36179. DM.

Interactioni

Subunit structurei

PP2A exists in several trimeric forms, all of which consist of a core composed of a catalytic subunit associated with a 65 kDa regulatory subunit (PR65) (subunit A). The core complex associates with a third, variable subunit (subunit B), which confers distinct properties to the holoenzyme.

Protein-protein interaction databases

BioGridi77789. 68 interactions.
IntActiP36179. 9 interactions.
MINTiMINT-803219.
STRINGi7227.FBpp0297239.

Structurei

3D structure databases

ProteinModelPortaliP36179.
SMRiP36179. Positions 15-585.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati10 – 4839HEAT 1Add
BLAST
Repeati49 – 8638HEAT 2Add
BLAST
Repeati87 – 12539HEAT 3Add
BLAST
Repeati126 – 16338HEAT 4Add
BLAST
Repeati164 – 20239HEAT 5Add
BLAST
Repeati203 – 24139HEAT 6Add
BLAST
Repeati242 – 28039HEAT 7Add
BLAST
Repeati281 – 32343HEAT 8Add
BLAST
Repeati324 – 36239HEAT 9Add
BLAST
Repeati363 – 40139HEAT 10Add
BLAST
Repeati402 – 44039HEAT 11Add
BLAST
Repeati441 – 47939HEAT 12Add
BLAST
Repeati480 – 51839HEAT 13Add
BLAST
Repeati519 – 55739HEAT 14Add
BLAST
Repeati558 – 59134HEAT 15Add
BLAST

Domaini

Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure.

Sequence similaritiesi

Contains 15 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0211. Eukaryota.
ENOG410XQVI. LUCA.
GeneTreeiENSGT00730000110944.
InParanoidiP36179.
KOiK03456.
OrthoDBiEOG091G045V.
PhylomeDBiP36179.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021133. HEAT_type_2.
IPR031090. PP2A_A_meta.
[Graphical view]
PANTHERiPTHR10648:SF9. PTHR10648:SF9. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P36179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASDKSVDD SLYPIAVLID ELKNEDVQLR LNSIKKLSTI ALALGEERTR
60 70 80 90 100
SELIPFLTET IYDEDEVLLA LADQLGNFTS LVGGPEFAMY LIPPLESLAT
110 120 130 140 150
VEETVVRDKA VESLRTVAAE HSAQDLEIHV VPTLQRLVSG DWFTSRTSAC
160 170 180 190 200
GLFSVCYPRV TQPVKAELRA NFRKLCQDET PMVRRAAANK LGEFAKVVET
210 220 230 240 250
EYLKSDLIPN FVQLAQDDQD SVRLLAVEAC VSIAQLLPQD DVEHLVLPTL
260 270 280 290 300
RQCASDSSWR VRYMVAEKFV DLQKAVGPEI TRVDLVPAFQ YLLKDAEAEV
310 320 330 340 350
RAAVATKVKD FCANLDKVNQ VQIILSSILP YVRDLVSDPN PHVKSALASV
360 370 380 390 400
IMGLSPMLGA YQTVEQLLPL FLIQLKDECP EVRLNIISNL DCVNDVIGIQ
410 420 430 440 450
QLSQSLLPAI VELAEDSKWR VRLAIIEYMP ALAGQLGQEF FDQKLRGLCM
460 470 480 490 500
GWLNDHVYAI REAATLNMKK LVEQFGAPWA EQAIIPMILV MSRNKNYLHR
510 520 530 540 550
MTCLFCLNVL AEVCGTDITT KLLLPTVLLL AADPVANVRF NVAKTLQKIS
560 570 580 590
PFLEASVIDA QVKPTLDKLN TDTDVDVKHF AAQAIAGIAA A
Length:591
Mass (Da):65,424
Last modified:January 23, 2007 - v4
Checksum:i13948F39796662AC
GO

Sequence cautioni

The sequence AAX33553 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321S → T in AAA28304 (PubMed:1320961).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86442 mRNA. Translation: AAA28304.1.
AE014134 Genomic DNA. Translation: AAF52650.2.
AE014134 Genomic DNA. Translation: AAZ66587.1.
BT021405 mRNA. Translation: AAX33553.1. Sequence problems.
PIRiA43767.
RefSeqiNP_001027225.1. NM_001032054.3.
NP_001027226.1. NM_001032055.3.
NP_001027227.1. NM_001032056.3.
UniGeneiDm.1532.

Genome annotation databases

EnsemblMetazoaiFBtr0005088; FBpp0099974; FBgn0260439.
FBtr0100533; FBpp0099975; FBgn0260439.
FBtr0100535; FBpp0293227; FBgn0260439.
GeneIDi2768940.
KEGGidme:Dmel_CG17291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86442 mRNA. Translation: AAA28304.1.
AE014134 Genomic DNA. Translation: AAF52650.2.
AE014134 Genomic DNA. Translation: AAZ66587.1.
BT021405 mRNA. Translation: AAX33553.1. Sequence problems.
PIRiA43767.
RefSeqiNP_001027225.1. NM_001032054.3.
NP_001027226.1. NM_001032055.3.
NP_001027227.1. NM_001032056.3.
UniGeneiDm.1532.

3D structure databases

ProteinModelPortaliP36179.
SMRiP36179. Positions 15-585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi77789. 68 interactions.
IntActiP36179. 9 interactions.
MINTiMINT-803219.
STRINGi7227.FBpp0297239.

Proteomic databases

PaxDbiP36179.
PRIDEiP36179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0005088; FBpp0099974; FBgn0260439.
FBtr0100533; FBpp0099975; FBgn0260439.
FBtr0100535; FBpp0293227; FBgn0260439.
GeneIDi2768940.
KEGGidme:Dmel_CG17291.

Organism-specific databases

CTDi2768940.
FlyBaseiFBgn0260439. Pp2A-29B.

Phylogenomic databases

eggNOGiKOG0211. Eukaryota.
ENOG410XQVI. LUCA.
GeneTreeiENSGT00730000110944.
InParanoidiP36179.
KOiK03456.
OrthoDBiEOG091G045V.
PhylomeDBiP36179.

Enzyme and pathway databases

ReactomeiR-DME-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-DME-1295596. Spry regulation of FGF signaling.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-196299. Beta-catenin phosphorylation cascade.
R-DME-198753. ERK/MAPK targets.
R-DME-202670. ERKs are inactivated.
R-DME-2995383. Initiation of Nuclear Envelope Reformation.
R-DME-389513. CTLA4 inhibitory signaling.
R-DME-5673000. RAF activation.
R-DME-5675221. Negative regulation of MAPK pathway.
R-DME-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-DME-69231. Cyclin D associated events in G1.
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

GenomeRNAii2768940.
PROiP36179.

Gene expression databases

BgeeiFBgn0260439.
ExpressionAtlasiP36179. differential.
GenevisibleiP36179. DM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021133. HEAT_type_2.
IPR031090. PP2A_A_meta.
[Graphical view]
PANTHERiPTHR10648:SF9. PTHR10648:SF9. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei2AAA_DROME
AccessioniPrimary (citable) accession number: P36179
Secondary accession number(s): A4V0F7
, Q2MGK6, Q5BI19, Q9VLN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 133 of the entry and version 4 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

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 one 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.