Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform

Gene

Ppp2r1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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 - Biological processi

  1. apoptotic process involved in morphogenesis Source: MGI
  2. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_279737. Integration of energy metabolism.
REACT_281671. APC truncation mutants have impaired AXIN binding.
REACT_287097. S33 mutants of beta-catenin aren't phosphorylated.
REACT_289448. Cyclin D associated events in G1.
REACT_292325. S45 mutants of beta-catenin aren't phosphorylated.
REACT_295564. AXIN missense mutants destabilize the destruction complex.
REACT_299247. ERKs are inactivated.
REACT_303008. Beta-catenin phosphorylation cascade.
REACT_305569. S37 mutants of beta-catenin aren't phosphorylated.
REACT_306375. Mitotic Prometaphase.
REACT_307423. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_307889. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_311393. CTLA4 inhibitory signaling.
REACT_314687. Glycolysis.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_320326. truncations of AMER1 destabilize the destruction complex.
REACT_320976. T41 mutants of beta-catenin aren't phosphorylated.
REACT_321346. Separation of Sister Chromatids.
REACT_323000. ERK/MAPK targets.
REACT_324544. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_325290. DARPP-32 events.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_342444. MASTL Facilitates Mitotic Progression.
REACT_349749. Cyclin A/B1 associated events during G2/M transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
Alternative name(s):
PP2A subunit A isoform PR65-beta
PP2A subunit A isoform R1-beta
Gene namesi
Name:Ppp2r1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1920949. Ppp2r1b.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. membrane raft Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 601600Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoformPRO_0000071404Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ7TNP2.
PaxDbiQ7TNP2.
PRIDEiQ7TNP2.

PTM databases

PhosphoSiteiQ7TNP2.

Expressioni

Gene expression databases

BgeeiQ7TNP2.
ExpressionAtlasiQ7TNP2. baseline and differential.
GenevestigatoriQ7TNP2.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9 (By similarity). Interacts with SGOL1 (By similarity). Interacts with RAF1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Unc5bQ8K1S32EBI-4396871,EBI-4396886

Protein-protein interaction databases

IntActiQ7TNP2. 1 interaction.
STRINGi10090.ENSMUSP00000034560.

Structurei

3D structure databases

ProteinModelPortaliQ7TNP2.
SMRiQ7TNP2. Positions 19-601.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati20 – 5839HEAT 1Add
BLAST
Repeati59 – 9638HEAT 2Add
BLAST
Repeati97 – 13539HEAT 3Add
BLAST
Repeati136 – 17338HEAT 4Add
BLAST
Repeati174 – 21239HEAT 5Add
BLAST
Repeati213 – 25139HEAT 6Add
BLAST
Repeati252 – 29039HEAT 7Add
BLAST
Repeati291 – 33343HEAT 8Add
BLAST
Repeati334 – 37239HEAT 9Add
BLAST
Repeati373 – 41139HEAT 10Add
BLAST
Repeati412 – 45039HEAT 11Add
BLAST
Repeati451 – 48939HEAT 12Add
BLAST
Repeati490 – 52839HEAT 13Add
BLAST
Repeati529 – 56739HEAT 14Add
BLAST
Repeati568 – 60134HEAT 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

eggNOGiNOG247268.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiQ7TNP2.
KOiK03456.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
PfamiPF02985. HEAT. 3 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 12 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q7TNP2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAAGPGSG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI
60 70 80 90 100
ALALGVERTR TELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC
110 120 130 140 150
LLPPLESLAT VEETVVRDKA VESLRQISQE HTPVALEAHF VPLVKRLASG
160 170 180 190 200
DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ HFRSLCSDDT PMVRRAAASK
210 220 230 240 250
LGEFAKVLEL DSVKTEIVPL FTNLASDEQD SVRLLAVEAC VSIAQLLSQE
260 270 280 290 300
DLEALVMPTL RQAAEDKSWR VRYMVADKFS ELQKAVGPKI ALSDLIPAFQ
310 320 330 340 350
SLLRDCEAEV RAAAAHKVRE LCENLPAEGR ETVIMNQILP YIKELVSDTN
360 370 380 390 400
QHVKSALASV IMGLSTVLGK ENTIEHLLPL FLAQLKDECP EVRLNIISNL
410 420 430 440 450
DCVNEVIGIR QLSQSLLPAI VELAEDAKWR VRLAIIEYMP LLAGQLGVEF
460 470 480 490 500
FDEKLNSLCM AWLVDHVYAI REAATNNLMK LVQKFGTEWA QNTIVPKVLV
510 520 530 540 550
MANDPNYLHR MTTLFCINAL SEACGKEITT KQMLPIVLKM AGDQVANVRF
560 570 580 590 600
NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL

A
Length:601
Mass (Da):65,934
Last modified:July 27, 2011 - v2
Checksum:i801D903C90D1F15A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541T → M in AAH56218 (PubMed:15489334).Curated
Sequence conflicti193 – 1931V → E in AAH56218 (PubMed:15489334).Curated
Sequence conflicti257 – 2571M → I in AAH56218 (PubMed:15489334).Curated
Sequence conflicti350 – 3501N → S in AAH56218 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC103406 Genomic DNA. No translation available.
AC123614 Genomic DNA. No translation available.
BC056218 mRNA. Translation: AAH56218.1.
CCDSiCCDS40626.1.
RefSeqiNP_082890.2. NM_028614.3.
UniGeneiMm.7726.

Genome annotation databases

EnsembliENSMUST00000114437; ENSMUSP00000110080; ENSMUSG00000032058.
GeneIDi73699.
KEGGimmu:73699.
UCSCiuc009pkv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC103406 Genomic DNA. No translation available.
AC123614 Genomic DNA. No translation available.
BC056218 mRNA. Translation: AAH56218.1.
CCDSiCCDS40626.1.
RefSeqiNP_082890.2. NM_028614.3.
UniGeneiMm.7726.

3D structure databases

ProteinModelPortaliQ7TNP2.
SMRiQ7TNP2. Positions 19-601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7TNP2. 1 interaction.
STRINGi10090.ENSMUSP00000034560.

PTM databases

PhosphoSiteiQ7TNP2.

Proteomic databases

MaxQBiQ7TNP2.
PaxDbiQ7TNP2.
PRIDEiQ7TNP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114437; ENSMUSP00000110080; ENSMUSG00000032058.
GeneIDi73699.
KEGGimmu:73699.
UCSCiuc009pkv.1. mouse.

Organism-specific databases

CTDi5519.
MGIiMGI:1920949. Ppp2r1b.

Phylogenomic databases

eggNOGiNOG247268.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiQ7TNP2.
KOiK03456.

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_279737. Integration of energy metabolism.
REACT_281671. APC truncation mutants have impaired AXIN binding.
REACT_287097. S33 mutants of beta-catenin aren't phosphorylated.
REACT_289448. Cyclin D associated events in G1.
REACT_292325. S45 mutants of beta-catenin aren't phosphorylated.
REACT_295564. AXIN missense mutants destabilize the destruction complex.
REACT_299247. ERKs are inactivated.
REACT_303008. Beta-catenin phosphorylation cascade.
REACT_305569. S37 mutants of beta-catenin aren't phosphorylated.
REACT_306375. Mitotic Prometaphase.
REACT_307423. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_307889. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_311393. CTLA4 inhibitory signaling.
REACT_314687. Glycolysis.
REACT_317277. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_320326. truncations of AMER1 destabilize the destruction complex.
REACT_320976. T41 mutants of beta-catenin aren't phosphorylated.
REACT_321346. Separation of Sister Chromatids.
REACT_323000. ERK/MAPK targets.
REACT_324544. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_325290. DARPP-32 events.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_342444. MASTL Facilitates Mitotic Progression.
REACT_349749. Cyclin A/B1 associated events during G2/M transition.

Miscellaneous databases

NextBioi338839.
PROiQ7TNP2.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TNP2.
ExpressionAtlasiQ7TNP2. baseline and differential.
GenevestigatoriQ7TNP2.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
PfamiPF02985. HEAT. 3 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 12 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.

Entry informationi

Entry namei2AAB_MOUSE
AccessioniPrimary (citable) accession number: Q7TNP2
Secondary accession number(s): E9QNJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.