P30154 · 2AAB_HUMAN
- ProteinSerine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- GenePPP2R1B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids601 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | membrane raft | |
Cellular Component | nucleus | |
Cellular Component | protein phosphatase type 2A complex | |
Molecular Function | protein phosphatase regulator activity | |
Biological Process | apoptotic process involved in morphogenesis | |
Biological Process | positive regulation of extrinsic apoptotic signaling pathway in absence of ligand |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP30154
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_022895 | 8 | in a lung cancer patient; dbSNP:rs142771326 | |||
Sequence: G → R | ||||||
Natural variant | VAR_022896 | 15 | in a colorectal cancer patient | |||
Sequence: G → A | ||||||
Natural variant | VAR_022897 | 65 | in a lung cancer patient | |||
Sequence: P → S | ||||||
Natural variant | VAR_006384 | 90 | in a lung cancer patient; dbSNP:rs1805076 | |||
Sequence: G → D | ||||||
Natural variant | VAR_022898 | 101 | in a colon adenocarcinoma | |||
Sequence: L → P | ||||||
Natural variant | VAR_022899 | 343 | in a lung cancer patient | |||
Sequence: K → E | ||||||
Natural variant | VAR_022900 | 365 | in a colorectal cancer patient; dbSNP:rs1442893893 | |||
Sequence: S → P | ||||||
Natural variant | VAR_022901 | 448 | in a colon adenocarcinoma | |||
Sequence: V → A | ||||||
Natural variant | VAR_022902 | 498 | in a colorectal cancer patient | |||
Sequence: V → E | ||||||
Natural variant | VAR_022903 | 499 | in a colorectal cancer patient | |||
Sequence: L → I | ||||||
Natural variant | VAR_022904 | 500 | in a colorectal cancer patient | |||
Sequence: V → G | ||||||
Natural variant | VAR_022905 | 504 | in a lung cancer patient; dbSNP:rs973682124 | |||
Sequence: D → G | ||||||
Natural variant | VAR_022906 | 545 | in a colon adenocarcinoma; dbSNP:rs1318084062 | |||
Sequence: V → A |
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000071403 | 2-601 | Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform | |||
Sequence: AGASELGTGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLENLATVEETVVRDKAVESLRQISQEHTPVALEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQQFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTSLASDEQDSVRLLAVEACVSIAQLLSQDDLETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVKELGENLPIEDRETIIMNQILPYIKELVSDTNQHVKSALASVIMGLSTILGKENTIEHLLPLFLAQLKDECPDVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGQEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P30154 | Clock O08785 | 2 | EBI-357094, EBI-79859 | |
BINARY | P30154 | PPP2CA P67775 | 9 | EBI-357094, EBI-712311 | |
BINARY | P30154 | PPP2R1A P30153 | 3 | EBI-357094, EBI-302388 | |
BINARY | P30154 | PPP2R2A P63151 | 5 | EBI-357094, EBI-1048931 | |
BINARY | P30154 | PPP2R5A Q15172 | 4 | EBI-357094, EBI-641666 | |
BINARY | P30154 | PPP2R5C Q13362 | 2 | EBI-357094, EBI-1266156 | |
BINARY | P30154 | PPP2R5D Q14738 | 3 | EBI-357094, EBI-396563 | |
BINARY | P30154 | PPP2R5E Q16537 | 3 | EBI-357094, EBI-968374 | |
BINARY | P30154 | RALA P11233 | 6 | EBI-357094, EBI-1036803 | |
XENO | P30154 | Unc5b O08722 | 4 | EBI-357094, EBI-4404185 | |
BINARY | P30154-2 | DNAJB6 O75190-2 | 3 | EBI-11058011, EBI-12593112 | |
BINARY | P30154-2 | KLF11 O14901 | 3 | EBI-11058011, EBI-948266 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 20-58 | HEAT 1 | ||||
Sequence: DSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVER | ||||||
Repeat | 59-96 | HEAT 2 | ||||
Sequence: TRSELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPD | ||||||
Repeat | 97-135 | HEAT 3 | ||||
Sequence: FAHCLLPPLENLATVEETVVRDKAVESLRQISQEHTPVA | ||||||
Repeat | 136-173 | HEAT 4 | ||||
Sequence: LEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNA | ||||||
Repeat | 174-212 | HEAT 5 | ||||
Sequence: VKAEIRQQFRSLCSDDTPMVRRAAASKLGEFAKVLELDS | ||||||
Repeat | 213-251 | HEAT 6 | ||||
Sequence: VKSEIVPLFTSLASDEQDSVRLLAVEACVSIAQLLSQDD | ||||||
Repeat | 252-290 | HEAT 7 | ||||
Sequence: LETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKI | ||||||
Repeat | 291-333 | HEAT 8 | ||||
Sequence: TLNDLIPAFQNLLKDCEAEVRAAAAHKVKELGENLPIEDRETI | ||||||
Repeat | 334-372 | HEAT 9 | ||||
Sequence: IMNQILPYIKELVSDTNQHVKSALASVIMGLSTILGKEN | ||||||
Repeat | 373-411 | HEAT 10 | ||||
Sequence: TIEHLLPLFLAQLKDECPDVRLNIISNLDCVNEVIGIRQ | ||||||
Repeat | 412-450 | HEAT 11 | ||||
Sequence: LSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEF | ||||||
Repeat | 451-489 | HEAT 12 | ||||
Sequence: FDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEW | ||||||
Repeat | 490-528 | HEAT 13 | ||||
Sequence: AQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGQEI | ||||||
Repeat | 529-567 | HEAT 14 | ||||
Sequence: TTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNA | ||||||
Repeat | 568-601 | HEAT 15 | ||||
Sequence: LQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA |
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
Belongs to the phosphatase 2A regulatory subunit A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length601
- Mass (Da)66,214
- Last updated2006-10-17 v3
- Checksum86AB20D7505210B0
P30154-2
- Name2
- Differences from canonical
- 598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD
P30154-3
- Name3
P30154-4
- Name4
- Differences from canonical
- 344-388: Missing
P30154-5
- Name5
- Differences from canonical
- 103-229: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043379 | 39-102 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 74 | in Ref. 9; AAA59983 | ||||
Sequence: E → V | ||||||
Alternative sequence | VSP_046684 | 103-229 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 178 | in Ref. 1; AAC63525, 3; AAG39644 and 9; AAA59983 | ||||
Sequence: I → T | ||||||
Sequence conflict | 211 | in Ref. 4; BAG57867 | ||||
Sequence: D → G | ||||||
Alternative sequence | VSP_045275 | 344-388 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 411 | in Ref. 9; AAA59983 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 503 | in Ref. 4; BAG57867 | ||||
Sequence: N → S | ||||||
Alternative sequence | VSP_036460 | 598-601 | in isoform 2 and isoform 3 | |||
Sequence: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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. |