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Protein

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

Gene

Ppp2r1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (PubMed:10100624). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (By similarity). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • chromosome segregation Source: UniProtKB
  • female meiotic nuclear division Source: MGI
  • meiotic sister chromatid cohesion, centromeric Source: MGI
  • meiotic spindle elongation Source: MGI
  • mitotic sister chromatid separation Source: MGI
  • peptidyl-serine dephosphorylation Source: MGI
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • protein-containing complex assembly Source: InterPro
  • regulation of meiotic cell cycle process involved in oocyte maturation Source: MGI

Keywordsi

Biological processChromosome partition

Enzyme and pathway databases

ReactomeiR-MMU-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-MMU-1295596 Spry regulation of FGF signaling
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-180024 DARPP-32 events
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-196299 Beta-catenin phosphorylation cascade
R-MMU-198753 ERK/MAPK targets
R-MMU-202670 ERKs are inactivated
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-380259 Loss of Nlp from mitotic centrosomes
R-MMU-380270 Recruitment of mitotic centrosome proteins and complexes
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-389513 CTLA4 inhibitory signaling
R-MMU-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-MMU-5620912 Anchoring of the basal body to the plasma membrane
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-5673000 RAF activation
R-MMU-5675221 Negative regulation of MAPK pathway
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-68877 Mitotic Prometaphase
R-MMU-69231 Cyclin D associated events in G1
R-MMU-69273 Cyclin A/B1/B2 associated events during G2/M transition
R-MMU-8854518 AURKA Activation by TPX2
R-MMU-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Alternative name(s):
PP2A subunit A isoform PR65-alpha
PP2A subunit A isoform R1-alpha
Gene namesi
Name:Ppp2r1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1926334 Ppp2r1a

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

Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3557

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000714012 – 589Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformAdd BLAST588

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei280N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ76MZ3
MaxQBiQ76MZ3
PaxDbiQ76MZ3
PeptideAtlasiQ76MZ3
PRIDEiQ76MZ3

2D gel databases

REPRODUCTION-2DPAGEiQ76MZ3

PTM databases

iPTMnetiQ76MZ3
PhosphoSitePlusiQ76MZ3
SwissPalmiQ76MZ3

Expressioni

Gene expression databases

BgeeiENSMUSG00000007564
ExpressionAtlasiQ76MZ3 baseline and differential
GenevisibleiQ76MZ3 MM

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A 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 TP53 and SGO1 (By similarity). Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with PLA2G16; this interaction might decrease PP2A activity (By similarity). Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphorylation sites (PubMed:22417654). Interacts with CTTNBP2NL (By similarity). Interacts with GNA12; the interaction promotes protein phosphatase 2A activation causing dephosphorylation of MAPT (By similarity).Interacts with CIP2A; this interaction stabilizes CIP2A (By similarity).By similarity1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi206176, 120 interactors
CORUMiQ76MZ3
DIPiDIP-29429N
IntActiQ76MZ3, 139 interactors
MINTiQ76MZ3
STRINGi10090.ENSMUSP00000007708

Chemistry databases

BindingDBiQ76MZ3

Structurei

Secondary structure

1589
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 21Combined sources11
Helixi25 – 33Combined sources9
Helixi35 – 41Combined sources7
Helixi44 – 49Combined sources6
Helixi51 – 56Combined sources6
Helixi63 – 73Combined sources11
Turni77 – 81Combined sources5
Helixi83 – 85Combined sources3
Helixi86 – 89Combined sources4
Helixi90 – 98Combined sources9
Helixi102 – 116Combined sources15
Helixi121 – 126Combined sources6
Helixi128 – 136Combined sources9
Helixi141 – 147Combined sources7
Turni148 – 150Combined sources3
Helixi151 – 154Combined sources4
Helixi155 – 157Combined sources3
Helixi160 – 174Combined sources15
Helixi179 – 187Combined sources9
Helixi189 – 193Combined sources5
Helixi198 – 213Combined sources16
Helixi218 – 232Combined sources15
Helixi237 – 242Combined sources6
Helixi244 – 251Combined sources8
Helixi257 – 265Combined sources9
Helixi267 – 274Combined sources8
Helixi276 – 291Combined sources16
Helixi296 – 303Combined sources8
Helixi306 – 311Combined sources6
Turni315 – 317Combined sources3
Helixi318 – 324Combined sources7
Helixi327 – 334Combined sources8
Helixi339 – 346Combined sources8
Helixi349 – 352Combined sources4
Helixi353 – 373Combined sources21
Helixi378 – 385Combined sources8
Helixi386 – 388Combined sources3
Helixi389 – 394Combined sources6
Helixi397 – 403Combined sources7
Helixi405 – 411Combined sources7
Helixi417 – 424Combined sources8
Helixi427 – 434Combined sources8
Helixi436 – 442Combined sources7
Helixi444 – 451Combined sources8
Helixi456 – 473Combined sources18
Helixi475 – 481Combined sources7
Helixi483 – 488Combined sources6
Helixi489 – 491Combined sources3
Helixi495 – 520Combined sources26
Helixi522 – 528Combined sources7
Helixi534 – 547Combined sources14
Helixi548 – 550Combined sources3
Helixi553 – 558Combined sources6
Helixi560 – 568Combined sources9
Beta strandi569 – 571Combined sources3
Helixi573 – 585Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50A/D1-589[»]
2PF4X-ray3.10A/B/C/D1-589[»]
3FGAX-ray2.70A2-589[»]
ProteinModelPortaliQ76MZ3
SMRiQ76MZ3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ76MZ3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati8 – 46HEAT 1Add BLAST39
Repeati47 – 84HEAT 2Add BLAST38
Repeati85 – 123HEAT 3Add BLAST39
Repeati124 – 161HEAT 4Add BLAST38
Repeati162 – 200HEAT 5Add BLAST39
Repeati201 – 239HEAT 6Add BLAST39
Repeati240 – 278HEAT 7Add BLAST39
Repeati279 – 321HEAT 8Add BLAST43
Repeati322 – 360HEAT 9Add BLAST39
Repeati361 – 399HEAT 10Add BLAST39
Repeati400 – 438HEAT 11Add BLAST39
Repeati439 – 477HEAT 12Add BLAST39
Repeati478 – 516HEAT 13Add BLAST39
Repeati517 – 555HEAT 14Add BLAST39
Repeati556 – 589HEAT 15Add BLAST34

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0211 Eukaryota
ENOG410XQVI LUCA
GeneTreeiENSGT00730000110944
HOGENOMiHOG000078539
HOVERGENiHBG000011
InParanoidiQ76MZ3
KOiK03456
OMAiWAQNTVI
OrthoDBiEOG091G045V
PhylomeDBiQ76MZ3
TreeFamiTF105552

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000357 HEAT
IPR021133 HEAT_type_2
IPR031090 PP2A_A_meta
PANTHERiPTHR10648:SF2 PTHR10648:SF2, 1 hit
PfamiView protein in Pfam
PF02985 HEAT, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit
PROSITEiView protein in PROSITE
PS50077 HEAT_REPEAT, 11 hits

Sequencei

Sequence statusi: Complete.

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

Q76MZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE
60 70 80 90 100
LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE
110 120 130 140 150
ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL
160 170 180 190 200
FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN
210 220 230 240 250
VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ
260 270 280 290 300
AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA
310 320 330 340 350
AASHKVKEFC ENLSADCREN VIMTQILPCI KELVSDANQH VKSALASVIM
360 370 380 390 400
GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL
410 420 430 440 450
SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW
460 470 480 490 500
LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT
510 520 530 540 550
TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI
560 570 580
LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
Length:589
Mass (Da):65,323
Last modified:January 23, 2007 - v3
Checksum:i5175409E4D50A366
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021743 mRNA Translation: BAA75478.1
AK054239 mRNA Translation: BAC35700.1
AK078135 mRNA Translation: BAC37143.1
BC006606 mRNA Translation: AAH06606.1
CCDSiCCDS28432.1
RefSeqiNP_058587.1, NM_016891.3
UniGeneiMm.294138

Genome annotation databases

EnsembliENSMUST00000007708; ENSMUSP00000007708; ENSMUSG00000007564
GeneIDi51792
KEGGimmu:51792
UCSCiuc008aqi.1 mouse

Similar proteinsi

Entry informationi

Entry namei2AAA_MOUSE
AccessioniPrimary (citable) accession number: Q76MZ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 131 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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