P30154 · 2AAB_HUMAN

  • Protein
    Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
  • Gene
    PPP2R1B
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentextracellular exosome
Cellular Componentmembrane raft
Cellular Componentnucleus
Cellular Componentprotein phosphatase type 2A complex
Molecular Functionprotein phosphatase regulator activity
Biological Processapoptotic process involved in morphogenesis
Biological Processpositive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
  • Alternative names
    • PP2A subunit A isoform PR65-beta
    • PP2A subunit A isoform R1-beta

Gene names

    • Name
      PPP2R1B

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P30154
  • Secondary accessions
    • A8MY67
    • B0YJ69
    • B4DGQ6
    • B4DK91
    • B4DWW5

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_0228958in a lung cancer patient; dbSNP:rs142771326
Natural variantVAR_02289615in a colorectal cancer patient
Natural variantVAR_02289765in a lung cancer patient
Natural variantVAR_00638490in a lung cancer patient; dbSNP:rs1805076
Natural variantVAR_022898101in a colon adenocarcinoma
Natural variantVAR_022899343in a lung cancer patient
Natural variantVAR_022900365in a colorectal cancer patient; dbSNP:rs1442893893
Natural variantVAR_022901448in a colon adenocarcinoma
Natural variantVAR_022902498in a colorectal cancer patient
Natural variantVAR_022903499in a colorectal cancer patient
Natural variantVAR_022904500in a colorectal cancer patient
Natural variantVAR_022905504in a lung cancer patient; dbSNP:rs973682124
Natural variantVAR_022906545in a colon adenocarcinoma; dbSNP:rs1318084062

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 692 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00000714032-601Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

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 IPO9. Interacts with SGO1. Interacts with RAF1.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat20-58HEAT 1
Repeat59-96HEAT 2
Repeat97-135HEAT 3
Repeat136-173HEAT 4
Repeat174-212HEAT 5
Repeat213-251HEAT 6
Repeat252-290HEAT 7
Repeat291-333HEAT 8
Repeat334-372HEAT 9
Repeat373-411HEAT 10
Repeat412-450HEAT 11
Repeat451-489HEAT 12
Repeat490-528HEAT 13
Repeat529-567HEAT 14
Repeat568-601HEAT 15

Domain

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 similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

This entry describes 5 isoforms produced by Alternative splicing.

P30154-1

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.

  • Length
    601
  • Mass (Da)
    66,214
  • Last updated
    2006-10-17 v3
  • Checksum
    86AB20D7505210B0
MAGASELGTGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLENLATVEETVVRDKAVESLRQISQEHTPVALEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQQFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTSLASDEQDSVRLLAVEACVSIAQLLSQDDLETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVKELGENLPIEDRETIIMNQILPYIKELVSDTNQHVKSALASVIMGLSTILGKENTIEHLLPLFLAQLKDECPDVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGQEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA

P30154-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD

P30154-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 39-102: Missing
    • 598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD

P30154-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P30154-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YDG7H0YDG7_HUMANPPP2R1B224
E9PPI5E9PPI5_HUMANPPP2R1B83
E9PNM7E9PNM7_HUMANPPP2R1B119
E9PHZ6E9PHZ6_HUMANPPP2R1B135

Sequence caution

The sequence AAA59983.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Sequence of unknown origin in the N-terminal part.
The sequence BAG59103.1 differs from that shown. Reason: Frameshift

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_04337939-102in isoform 3
Sequence conflict74in Ref. 9; AAA59983
Alternative sequenceVSP_046684103-229in isoform 5
Sequence conflict178in Ref. 1; AAC63525, 3; AAG39644 and 9; AAA59983
Sequence conflict211in Ref. 4; BAG57867
Alternative sequenceVSP_045275344-388in isoform 4
Sequence conflict411in Ref. 9; AAA59983
Sequence conflict503in Ref. 4; BAG57867
Alternative sequenceVSP_036460598-601in isoform 2 and isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF083439
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083425
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083426
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083427
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083428
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083429
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083430
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083431
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083432
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083433
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083434
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083435
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083436
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083437
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF083438
EMBL· GenBank· DDBJ
AAC63525.1
EMBL· GenBank· DDBJ
Genomic DNA
AF087438
EMBL· GenBank· DDBJ
AAC69624.1
EMBL· GenBank· DDBJ
mRNA
AF163473
EMBL· GenBank· DDBJ
AAG39644.1
EMBL· GenBank· DDBJ
mRNA
AK294716
EMBL· GenBank· DDBJ
BAG57867.1
EMBL· GenBank· DDBJ
mRNA
AK296455
EMBL· GenBank· DDBJ
BAG59103.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AK301705
EMBL· GenBank· DDBJ
BAG63177.1
EMBL· GenBank· DDBJ
mRNA
EF445011
EMBL· GenBank· DDBJ
ACA06046.1
EMBL· GenBank· DDBJ
Genomic DNA
EF445011
EMBL· GenBank· DDBJ
ACA06047.1
EMBL· GenBank· DDBJ
Genomic DNA
AP000925
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AP001781
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471065
EMBL· GenBank· DDBJ
EAW67150.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471065
EMBL· GenBank· DDBJ
EAW67151.1
EMBL· GenBank· DDBJ
Genomic DNA
BC027596
EMBL· GenBank· DDBJ
AAH27596.1
EMBL· GenBank· DDBJ
mRNA
M65254
EMBL· GenBank· DDBJ
AAA59983.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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