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 56 kDa regulatory subunit beta isoform

Gene

PPP2R5B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

As the regulatory component of the serine/threonine-protein phosphatase 2A (PP2A) holoenzyme, modulates substrate specificity, subcellular localization, and responsiveness to phosphorylation. The phosphorylated form mediates the interaction between PP2A and AKT1, leading to AKT1 dephosphorylation.1 Publication

GO - Molecular functioni

  • protein phosphatase regulator activity Source: ProtInc

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-196299 Beta-catenin phosphorylation cascade
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-381038 XBP1(S) activates chaperone genes
R-HSA-389513 CTLA4 inhibitory signaling
R-HSA-432142 Platelet sensitization by LDL
R-HSA-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-HSA-5339716 Misspliced GSK3beta mutants stabilize beta-catenin
R-HSA-5358747 S33 mutants of beta-catenin aren't phosphorylated
R-HSA-5358749 S37 mutants of beta-catenin aren't phosphorylated
R-HSA-5358751 S45 mutants of beta-catenin aren't phosphorylated
R-HSA-5358752 T41 mutants of beta-catenin aren't phosphorylated
R-HSA-5467337 APC truncation mutants have impaired AXIN binding
R-HSA-5467340 AXIN missense mutants destabilize the destruction complex
R-HSA-5467348 Truncations of AMER1 destabilize the destruction complex
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5673000 RAF activation
R-HSA-5675221 Negative regulation of MAPK pathway
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-68877 Mitotic Prometaphase
SignaLinkiQ15173
SIGNORiQ15173

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
Alternative name(s):
PP2A B subunit isoform B'-beta
PP2A B subunit isoform B56-beta
PP2A B subunit isoform PR61-beta
PP2A B subunit isoform R5-beta
Gene namesi
Name:PPP2R5B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000068971.13
HGNCiHGNC:9310 PPP2R5B
MIMi601644 gene
neXtProtiNX_Q15173

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52Y → S: Loss of KLHL15-binding and enhanced stability. 1 Publication1
Mutagenesisi103 – 104KR → DE: Impaired trimer formation with PP2A subunits A/C, no effect on KLHL15-binding. 1 Publication2
Mutagenesisi232 – 233RK → ED: Impaired trimer formation with PP2A subunits A/C, no effect on KLHL15-binding. 1 Publication2

Organism-specific databases

DisGeNETi5526
OpenTargetsiENSG00000068971
PharmGKBiPA33673

Polymorphism and mutation databases

BioMutaiPPP2R5B
DMDMi7387497

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000714501 – 497Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoformAdd BLAST497

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32Phosphoserine; by CLK21 Publication1
Modified residuei35Phosphoserine; by CLK21 Publication1
Modified residuei44Phosphoserine; by CLK21 Publication1
Modified residuei46Phosphoserine; by CLK21 Publication1
Modified residuei47Phosphoserine; by CLK21 Publication1
Modified residuei48Phosphoserine; by CLK21 Publication1

Post-translational modificationi

Ubiquitinated by E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15173
MaxQBiQ15173
PaxDbiQ15173
PeptideAtlasiQ15173
PRIDEiQ15173
TopDownProteomicsiQ15173-1 [Q15173-1]

PTM databases

iPTMnetiQ15173
PhosphoSitePlusiQ15173

Expressioni

Tissue specificityi

Highest expression in brain.

Inductioni

By retinoic acid; in neuroblastoma cell lines.

Gene expression databases

BgeeiENSG00000068971
CleanExiHS_PPP2R5B
ExpressionAtlasiQ15173 baseline and differential
GenevisibleiQ15173 HS

Organism-specific databases

HPAiHPA036607

Interactioni

Subunit structurei

Component of the serine/threonine-protein phosphatase 2A complex (PP2A). This complex consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant scaffold 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 (PubMed:23135275). Interacts with SGO1 (PubMed:16541025). Interacts with AKT1 (PubMed:21329884). Interacts with CUL3 and KLHL15; this interaction leads to proteasomal degradation (PubMed:23135275).3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111518, 14 interactors
ELMiQ15173
IntActiQ15173, 9 interactors
MINTiQ15173
STRINGi9606.ENSP00000164133

Structurei

3D structure databases

ProteinModelPortaliQ15173
SMRiQ15173
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2085 Eukaryota
ENOG410XQJW LUCA
GeneTreeiENSGT00550000074525
HOGENOMiHOG000067326
HOVERGENiHBG000009
InParanoidiQ15173
KOiK11584
OMAiFIYEFEH
OrthoDBiEOG091G06HU
PhylomeDBiQ15173
TreeFamiTF105556

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR002554 PP2A_B56
PANTHERiPTHR10257 PTHR10257, 1 hit
PfamiView protein in Pfam
PF01603 B56, 1 hit
PIRSFiPIRSF028043 PP2A_B56, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Beta-1 (identifier: Q15173-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METKLPPAST PTSPSSPGLS PVPPPDKVDG FSRRSLRRAR PRRSHSSSQF
60 70 80 90 100
RYQSNQQELT PLPLLKDVPA SELHELLSRK LAQCGVMFDF LDCVADLKGK
110 120 130 140 150
EVKRAALNEL VECVGSTRGV LIEPVYPDII RMISVNIFRT LPPSENPEFD
160 170 180 190 200
PEEDEPNLEP SWPHLQLVYE FFLRFLESPD FQPSVAKRYV DQKFVLMLLE
210 220 230 240 250
LFDSEDPRER EYLKTILHRV YGKFLGLRAY IRKQCNHIFL RFIYEFEHFN
260 270 280 290 300
GVAELLEILG SIINGFALPL KTEHKQFLVR VLIPLHSVKS LSVFHAQLAY
310 320 330 340 350
CVVQFLEKDA TLTEHVIRGL LKYWPKTCTQ KEVMFLGEME EILDVIEPSQ
360 370 380 390 400
FVKIQEPLFK QVARCVSSPH FQVAERALYF WNNEYILSLI EDNCHTVLPA
410 420 430 440 450
VFGTLYQVSK EHWNQTIVSL IYNVLKTFME MNGKLFDELT ASYKLEKQQE
460 470 480 490
QQKAQERQEL WQGLEELRLR RLQGTQGAKE APLQRLTPQV AASGGQS
Length:497
Mass (Da):57,393
Last modified:November 1, 1996 - v1
Checksum:i8BEF84F20A77982D
GO
Isoform Beta-2 (identifier: Q15173-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: METKLPPASTPTSPSSPGL → MITVNPPLPQDTVNLF

Show »
Length:494
Mass (Da):57,294
Checksum:i5FADF4C0DD9B5507
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti57 – 58QE → IF AA sequence (PubMed:8694763).Curated2
Sequence conflicti177 – 178ES → GA AA sequence (PubMed:8694763).Curated2
Sequence conflicti181F → M AA sequence (PubMed:8694763).Curated1
Sequence conflicti184S → M AA sequence (PubMed:8694763).Curated1
Sequence conflicti461W → E AA sequence (PubMed:8694763).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0051091 – 19METKL…SSPGL → MITVNPPLPQDTVNLF in isoform Beta-2. 1 PublicationAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42374 mRNA Translation: AAC37602.1
Z69028 mRNA Translation: CAA93152.1
BC045619 mRNA Translation: AAH45619.1
CCDSiCCDS8085.1 [Q15173-1]
PIRiI70147
RefSeqiNP_006235.1, NM_006244.3 [Q15173-1]
UniGeneiHs.75199

Genome annotation databases

EnsembliENST00000164133; ENSP00000164133; ENSG00000068971 [Q15173-1]
GeneIDi5526
KEGGihsa:5526
UCSCiuc001oby.4 human [Q15173-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry namei2A5B_HUMAN
AccessioniPrimary (citable) accession number: Q15173
Secondary accession number(s): Q13853
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 167 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health