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Protein

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

Gene

PPP2R1A

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

Complete GO annotation...

Keywords - Biological processi

Chromosome partition

Enzyme and pathway databases

ReactomeiR-SSC-1295596. Spry regulation of FGF signaling.
R-SSC-180024. DARPP-32 events.
R-SSC-195253. Degradation of beta-catenin by the destruction complex.
R-SSC-196299. Beta-catenin phosphorylation cascade.
R-SSC-198753. ERK/MAPK targets.
R-SSC-202670. ERKs are inactivated.
R-SSC-2467813. Separation of Sister Chromatids.
R-SSC-2500257. Resolution of Sister Chromatid Cohesion.
R-SSC-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-SSC-2995383. Initiation of Nuclear Envelope Reformation.
R-SSC-380259. Loss of Nlp from mitotic centrosomes.
R-SSC-380270. Recruitment of mitotic centrosome proteins and complexes.
R-SSC-389513. CTLA4 inhibitory signaling.
R-SSC-5620912. Anchoring of the basal body to the plasma membrane.
R-SSC-5663220. RHO GTPases Activate Formins.
R-SSC-5673000. RAF activation.
R-SSC-5675221. Negative regulation of MAPK pathway.
R-SSC-6804757. Regulation of TP53 Degradation.
R-SSC-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-SSC-68877. Mitotic Prometaphase.
R-SSC-69273. Cyclin A/B1 associated events during G2/M transition.
R-SSC-8854518. AURKA Activation by TPX2.
R-SSC-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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 6

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000714022 – 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-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP54612.
PeptideAtlasiP54612.
PRIDEiP54612.

Expressioni

Gene expression databases

BgeeiENSSSCG00000024413.
GenevisibleiP54612. SS.

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. Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphoylation sites (By similarity). Interacts with CTTNBP2NL (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000024131.

Structurei

3D structure databases

ProteinModelPortaliP54612.
SMRiP54612.
ModBaseiSearch...
MobiDBiSearch...

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.
HOVERGENiHBG000011.
InParanoidiP54612.
KOiK03456.
OMAiMSNILPC.
OrthoDBiEOG091G045V.
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.

P54612-1 [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 - v2
Checksum:i5175409E4D50A366
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z34955 mRNA. Translation: CAA84414.1.
RefSeqiNP_999189.1. NM_214024.1.
UniGeneiSsc.102.

Genome annotation databases

EnsembliENSSSCT00000030514; ENSSSCP00000024131; ENSSSCG00000024413.
GeneIDi397088.
KEGGissc:397088.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z34955 mRNA. Translation: CAA84414.1.
RefSeqiNP_999189.1. NM_214024.1.
UniGeneiSsc.102.

3D structure databases

ProteinModelPortaliP54612.
SMRiP54612.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000024131.

Proteomic databases

PaxDbiP54612.
PeptideAtlasiP54612.
PRIDEiP54612.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000030514; ENSSSCP00000024131; ENSSSCG00000024413.
GeneIDi397088.
KEGGissc:397088.

Organism-specific databases

CTDi5518.

Phylogenomic databases

eggNOGiKOG0211. Eukaryota.
ENOG410XQVI. LUCA.
GeneTreeiENSGT00730000110944.
HOVERGENiHBG000011.
InParanoidiP54612.
KOiK03456.
OMAiMSNILPC.
OrthoDBiEOG091G045V.
TreeFamiTF105552.

Enzyme and pathway databases

ReactomeiR-SSC-1295596. Spry regulation of FGF signaling.
R-SSC-180024. DARPP-32 events.
R-SSC-195253. Degradation of beta-catenin by the destruction complex.
R-SSC-196299. Beta-catenin phosphorylation cascade.
R-SSC-198753. ERK/MAPK targets.
R-SSC-202670. ERKs are inactivated.
R-SSC-2467813. Separation of Sister Chromatids.
R-SSC-2500257. Resolution of Sister Chromatid Cohesion.
R-SSC-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-SSC-2995383. Initiation of Nuclear Envelope Reformation.
R-SSC-380259. Loss of Nlp from mitotic centrosomes.
R-SSC-380270. Recruitment of mitotic centrosome proteins and complexes.
R-SSC-389513. CTLA4 inhibitory signaling.
R-SSC-5620912. Anchoring of the basal body to the plasma membrane.
R-SSC-5663220. RHO GTPases Activate Formins.
R-SSC-5673000. RAF activation.
R-SSC-5675221. Negative regulation of MAPK pathway.
R-SSC-6804757. Regulation of TP53 Degradation.
R-SSC-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-SSC-68877. Mitotic Prometaphase.
R-SSC-69273. Cyclin A/B1 associated events during G2/M transition.
R-SSC-8854518. AURKA Activation by TPX2.
R-SSC-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Gene expression databases

BgeeiENSSSCG00000024413.
GenevisibleiP54612. SS.

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_PIG
AccessioniPrimary (citable) accession number: P54612
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.