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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: Annotation score: 5 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. Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • beta-catenin destruction complex disassembly Source: Reactome
  • chromosome segregation Source: UniProtKB
  • female meiotic 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 complex assembly Source: InterPro
  • regulation of meiotic cell cycle process involved in oocyte maturation Source: MGI
Complete GO annotation...

Keywords - Biological processi

Chromosome partition

Enzyme and pathway databases

ReactomeiR-MMU-1295596. Spry regulation of FGF signaling.
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-2995383. Initiation of Nuclear Envelope Reformation.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
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-69273. Cyclin A/B1 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1926334. Ppp2r1a.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • protein phosphatase type 2A complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm

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-2DPAGEQ76MZ3.

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. Interacts with TP53 and SGO1. 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 phosphoylation sites. Interacts with CTTNBP2NL (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
P030812EBI-400413,EBI-1266256From a different organism.
Ppp2caP633303EBI-400413,EBI-397144

GO - Molecular functioni

Protein-protein interaction databases

BioGridi206176. 114 interactors.
DIPiDIP-29429N.
IntActiQ76MZ3. 133 interactors.
MINTiMINT-135926.
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

Contains 15 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
IPR031090. PP2A_A_meta.
[Graphical view]
PANTHERiPTHR10648:SF9. PTHR10648:SF9. 1 hit.
PfamiPF02985. HEAT. 3 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi206176. 114 interactors.
DIPiDIP-29429N.
IntActiQ76MZ3. 133 interactors.
MINTiMINT-135926.
STRINGi10090.ENSMUSP00000007708.

Chemistry databases

BindingDBiQ76MZ3.
ChEMBLiCHEMBL3557.

PTM databases

iPTMnetiQ76MZ3.
PhosphoSitePlusiQ76MZ3.
SwissPalmiQ76MZ3.

2D gel databases

REPRODUCTION-2DPAGEQ76MZ3.

Proteomic databases

EPDiQ76MZ3.
MaxQBiQ76MZ3.
PaxDbiQ76MZ3.
PeptideAtlasiQ76MZ3.
PRIDEiQ76MZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5518.
MGIiMGI:1926334. Ppp2r1a.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-MMU-1295596. Spry regulation of FGF signaling.
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-2995383. Initiation of Nuclear Envelope Reformation.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
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-69273. Cyclin A/B1 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).

Miscellaneous databases

ChiTaRSiPpp2r1a. mouse.
EvolutionaryTraceiQ76MZ3.
PROiQ76MZ3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000007564.
ExpressionAtlasiQ76MZ3. baseline and differential.
GenevisibleiQ76MZ3. MM.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
IPR031090. PP2A_A_meta.
[Graphical view]
PANTHERiPTHR10648:SF9. PTHR10648:SF9. 1 hit.
PfamiPF02985. HEAT. 3 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei2AAA_MOUSE
AccessioniPrimary (citable) accession number: Q76MZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 118 of the entry and version 3 of the sequence. [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

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.