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Protein

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

Gene

PPP2R5A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

GO - Molecular functioni

  • kinase binding Source: BHF-UCL
  • phosphoprotein phosphatase activity Source: UniProtKB
  • protein phosphatase regulator activity Source: ProtInc

GO - Biological processi

  • negative regulation of lipid kinase activity Source: BHF-UCL
  • negative regulation of protein localization to plasma membrane Source: BHF-UCL
  • positive regulation of protein dephosphorylation Source: BHF-UCL
  • protein dephosphorylation Source: UniProtKB
  • signal transduction Source: InterPro

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-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
SignaLinkiQ15172
SIGNORiQ15172

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
Alternative name(s):
PP2A B subunit isoform B'-alpha
PP2A B subunit isoform B56-alpha
PP2A B subunit isoform PR61-alpha
Short name:
PR61alpha
PP2A B subunit isoform R5-alpha
Gene namesi
Name:PPP2R5A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000066027.11
HGNCiHGNC:9309 PPP2R5A
MIMi601643 gene
neXtProtiNX_Q15172

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

Centromere, Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5525
OpenTargetsiENSG00000066027
PharmGKBiPA33672

Chemistry databases

ChEMBLiCHEMBL4763

Polymorphism and mutation databases

BioMutaiPPP2R5A
DMDMi7387496

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000714482 – 486Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoformAdd BLAST485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei41PhosphoserineCombined sources1
Modified residuei42PhosphoserineCombined sources1
Modified residuei49PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated on serine residues.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15172
MaxQBiQ15172
PaxDbiQ15172
PeptideAtlasiQ15172
PRIDEiQ15172

2D gel databases

OGPiQ15172

PTM databases

iPTMnetiQ15172
PhosphoSitePlusiQ15172

Expressioni

Tissue specificityi

Widely expressed with the highest expression in heart and skeletal muscle.

Gene expression databases

BgeeiENSG00000066027
CleanExiHS_PPP2R5A
GenevisibleiQ15172 HS

Organism-specific databases

HPAiHPA059288

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 SGO1.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111517, 36 interactors
CORUMiQ15172
DIPiDIP-459N
ELMiQ15172
IntActiQ15172, 29 interactors
MINTiQ15172
STRINGi9606.ENSP00000261461

Chemistry databases

BindingDBiQ15172

Structurei

3D structure databases

ProteinModelPortaliQ15172
SMRiQ15172
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 5Poly-Ser4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2085 Eukaryota
ENOG410XQJW LUCA
GeneTreeiENSGT00550000074525
HOGENOMiHOG000067326
HOVERGENiHBG000009
InParanoidiQ15172
KOiK11584
OMAiFTRKSMR
OrthoDBiEOG091G06HU
PhylomeDBiQ15172
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.

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

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

Isoform 1 (identifier: Q15172-1) [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
MSSSSPPAGA ASAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ
60 70 80 90 100
AELHPLPQLK DATSNEQQEL FCQKLQQCCI LFDFMDSVSD LKSKEIKRAT
110 120 130 140 150
LNELVEYVST NRGVIVESAY SDIVKMISAN IFRTLPPSDN PDFDPEEDEP
160 170 180 190 200
TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA KRYIDQKFVQ QLLELFDSED
210 220 230 240 250
PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET EHFNGVAELL
260 270 280 290 300
EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL
310 320 330 340 350
EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE
360 370 380 390 400
PLFKQISKCV SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY
410 420 430 440 450
KISKEHWNPT IVALVYNVLK TLMEMNGKLF DDLTSSYKAE RQREKKKELE
460 470 480
REELWKKLEE LKLKKALEKQ NSAYNMHSIL SNTSAE
Length:486
Mass (Da):56,194
Last modified:November 1, 1996 - v1
Checksum:iD31407F7032A6D44
GO
Isoform 2 (identifier: Q15172-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKD → MIMN

Note: No experimental confirmation available.
Show »
Length:429
Mass (Da):50,244
Checksum:i8DF4B7962741F179
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52E → F AA sequence (PubMed:8694763).Curated1
Sequence conflicti54H → S AA sequence (PubMed:8694763).Curated1
Sequence conflicti176Q → R in AAH22474 (PubMed:15489334).Curated1
Sequence conflicti389D → N in AAH22474 (PubMed:15489334).Curated1
Sequence conflicti451R → E AA sequence (PubMed:8694763).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0428891 – 61MSSSS…PQLKD → MIMN in isoform 2. 1 PublicationAdd BLAST61

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42373 mRNA Translation: AAC37601.1
AK302202 mRNA Translation: BAH13648.1
AK312530 mRNA Translation: BAG35429.1
AL451060 Genomic DNA No translation available.
AL360091 Genomic DNA No translation available.
CH471100 Genomic DNA Translation: EAW93392.1
CH471100 Genomic DNA Translation: EAW93393.1
BC022474 mRNA Translation: AAH22474.1
BC110883 mRNA Translation: AAI10884.1
CCDSiCCDS1503.1 [Q15172-1]
CCDS55686.1 [Q15172-2]
PIRiI55449
RefSeqiNP_001186685.1, NM_001199756.1 [Q15172-2]
NP_006234.1, NM_006243.3 [Q15172-1]
UniGeneiHs.744012

Genome annotation databases

EnsembliENST00000261461; ENSP00000261461; ENSG00000066027 [Q15172-1]
ENST00000537030; ENSP00000442866; ENSG00000066027 [Q15172-2]
GeneIDi5525
KEGGihsa:5525
UCSCiuc001hjb.3 human [Q15172-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry namei2A5A_HUMAN
AccessioniPrimary (citable) accession number: Q15172
Secondary accession number(s): B2R6D2
, B7Z7L2, D3DT99, Q2NL72, Q5VVB2, Q8TBI9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 171 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

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