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Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform

Gene

PPP2R5B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The phosphorylated form mediates the interaction between AKT1 and PP2A phosphatase leading to dephosphorylation of AKT1 on the 'Thr-308' and 'Ser-373' residues.1 Publication

GO - Molecular functioni

  • protein phosphatase type 2A regulator activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-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

HGNCiHGNC:9310. PPP2R5B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • protein phosphatase type 2A complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33673.

Polymorphism and mutation databases

BioMutaiPPP2R5B.
DMDMi7387497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 497497Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoformPRO_0000071450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphoserine; by CLK21 Publication
Modified residuei35 – 351Phosphoserine; by CLK21 Publication
Modified residuei44 – 441Phosphoserine; by CLK21 Publication
Modified residuei46 – 461Phosphoserine; by CLK21 Publication
Modified residuei47 – 471Phosphoserine; by CLK21 Publication
Modified residuei48 – 481Phosphoserine; by CLK21 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

PTM databases

iPTMnetiQ15173.
PhosphoSiteiQ15173.

Expressioni

Tissue specificityi

Highest expression in brain.

Inductioni

By retinoic acid; in neuroblastoma cell lines.

Gene expression databases

BgeeiQ15173.
CleanExiHS_PPP2R5B.
ExpressionAtlasiQ15173. baseline and differential.
GenevisibleiQ15173. HS.

Organism-specific databases

HPAiHPA036607.

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 SGOL1. Interacts with AKT1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHEK2O960172EBI-1369497,EBI-1180783
IER3P466954EBI-1369497,EBI-1748945
PPP2CAP677754EBI-1369497,EBI-712311

Protein-protein interaction databases

BioGridi111518. 9 interactions.
IntActiQ15173. 9 interactions.
MINTiMINT-2835290.
STRINGi9606.ENSP00000164133.

Structurei

3D structure databases

ProteinModelPortaliQ15173.
SMRiQ15173. Positions 75-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2085. Eukaryota.
ENOG410XQJW. LUCA.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ15173.
KOiK11584.
OMAiFIRIQEP.
PhylomeDBiQ15173.
TreeFamiTF105556.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 582QE → IF AA sequence (PubMed:8694763).Curated
Sequence conflicti177 – 1782ES → GA AA sequence (PubMed:8694763).Curated
Sequence conflicti181 – 1811F → M AA sequence (PubMed:8694763).Curated
Sequence conflicti184 – 1841S → M AA sequence (PubMed:8694763).Curated
Sequence conflicti461 – 4611W → E AA sequence (PubMed:8694763).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1919METKL…SSPGL → MITVNPPLPQDTVNLF in isoform Beta-2. 1 PublicationVSP_005109Add
BLAST

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ15173.
SMRiQ15173. Positions 75-443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111518. 9 interactions.
IntActiQ15173. 9 interactions.
MINTiMINT-2835290.
STRINGi9606.ENSP00000164133.

PTM databases

iPTMnetiQ15173.
PhosphoSiteiQ15173.

Polymorphism and mutation databases

BioMutaiPPP2R5B.
DMDMi7387497.

Proteomic databases

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

Protocols and materials databases

DNASUi5526.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5526.
GeneCardsiPPP2R5B.
HGNCiHGNC:9310. PPP2R5B.
HPAiHPA036607.
MIMi601644. gene.
neXtProtiNX_Q15173.
PharmGKBiPA33673.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2085. Eukaryota.
ENOG410XQJW. LUCA.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ15173.
KOiK11584.
OMAiFIRIQEP.
PhylomeDBiQ15173.
TreeFamiTF105556.

Enzyme and pathway databases

ReactomeiR-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.

Miscellaneous databases

ChiTaRSiPPP2R5B. human.
GeneWikiiPPP2R5B.
GenomeRNAii5526.
PROiQ15173.
SOURCEiSearch...

Gene expression databases

BgeeiQ15173.
CleanExiHS_PPP2R5B.
ExpressionAtlasiQ15173. baseline and differential.
GenevisibleiQ15173. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 1 hit.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a new family of protein phosphatase 2A regulatory subunits."
    McCright B., Virshup D.M.
    J. Biol. Chem. 270:26123-26128(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
    Tissue: Fetal brain.
  2. "The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
    Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
    Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2), PARTIAL PROTEIN SEQUENCE.
    Tissue: Brain.
  3. "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] (ISOFORM BETA-1).
    Tissue: Brain.
  4. "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm."
    McCright B., Rivers A.M., Audlin S., Virshup D.M.
    J. Biol. Chem. 271:22081-22089(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
  5. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
    Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
    Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGOL1.
  6. "Clk2 and B56-beta mediate insulin-regulated assembly of the PP2A phosphatase holoenzyme complex on Akt."
    Rodgers J.T., Vogel R.O., Puigserver P.
    Mol. Cell 41:471-479(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-32; SER-35; SER-44; SER-46; SER-47 AND SER-48, INTERACTION WITH AKT1.

Entry informationi

Entry namei2A5B_HUMAN
AccessioniPrimary (citable) accession number: Q15173
Secondary accession number(s): Q13853
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 151 of the entry and version 1 of the sequence. [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

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.