Q14738 · 2A5D_HUMAN
- ProteinSerine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
- GenePPP2R5D
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids602 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
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 | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | protein phosphatase type 2A complex | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | protein phosphatase activator activity | |
Molecular Function | protein phosphatase regulator activity | |
Biological Process | negative regulation of peptidyl-threonine phosphorylation | |
Biological Process | nervous system development | |
Biological Process | positive regulation of protein dephosphorylation | |
Biological Process | protein dephosphorylation | |
Biological Process | signal transduction |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta 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 accessionQ14738
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Houge-Janssens syndrome 1 (HJS1)
- Note
- DescriptionAn autosomal dominant disorder characterized by global developmental delay, hypotonia, variably impaired intellectual development, poor speech, and dysmorphic facial features. Additional more variable features may include macrocephaly and seizures.
- See alsoMIM:616355
Natural variants in HJS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_073708 | 198 | E>K | in HJS1; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A; dbSNP:rs863225082 | |
VAR_074491 | 200 | E>K | in HJS1; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A; dbSNP:rs863225079 | |
VAR_073709 | 201 | P>R | in HJS1; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A; dbSNP:rs876657383 | |
VAR_074492 | 207 | W>R | in HJS1; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A; dbSNP:rs869320691 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_069414 | 53 | found in a patient with delayed psychomotor development, no speech and cataracts; no effect on binding to subunit PPP2CA; no effect on binding to subunit PPP2R1A; dbSNP:rs757369209 | |||
Sequence: P → S | ||||||
Natural variant | VAR_073708 | 198 | in HJS1; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A; dbSNP:rs863225082 | |||
Sequence: E → K | ||||||
Natural variant | VAR_074491 | 200 | in HJS1; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A; dbSNP:rs863225079 | |||
Sequence: E → K | ||||||
Natural variant | VAR_073709 | 201 | in HJS1; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A; dbSNP:rs876657383 | |||
Sequence: P → R | ||||||
Natural variant | VAR_074492 | 207 | in HJS1; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A; dbSNP:rs869320691 | |||
Sequence: W → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 445 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000071452 | 1-602 | UniProt | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform | |||
Sequence: MPYKLKKEKEPPKVAKCTAKPSSSGKDGGGENTEEAQPQPQPQPQPQAQSQPPSSNKRPSNSTPPPTQLSKIKYSGGPQIVKKERRQSSSRFNLSKNRELQKLPALKDSPTQEREELFIQKLRQCCVLFDFVSDPLSDLKFKEVKRAGLNEMVEYITHSRDVVTEAIYPEAVTMFSVNLFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLALLDLFDSEDPRERDFLKTILHRIYGKFLGLRAYIRRQINHIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKMFLIRVLLPLHKVKSLSVYHPQLAYCVVQFLEKESSLTEPVIVGLLKFWPKTHSPKEVMFLNELEEILDVIEPSEFSKVMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAARVLPIMFPALYRNSKSHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQYKAEKQKGRFRMKEREEMWQKIEELARLNPQYPMFRAPPPLPPVYSMETETPTAEDIQLLKRTVETEAVQMLKDIKKEKVLLRRKSELPQDVYTIKALEAHKRAEEFLTASQEAL | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 63 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 88 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 89 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 89 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 90 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 95 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 461 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 533 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 538 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 573 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 573 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 580 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 598 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 598 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
By retinoic acid; in neuroblastoma cell lines.
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 the PP2A A subunit PPP2R1A (PubMed:37761890).
Interacts with SGO1 (PubMed:16541025).
Interacts with ADCY8 (PubMed:22976297).
Interacts with SGO1 (PubMed:16541025).
Interacts with ADCY8 (PubMed:22976297).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q14738 | Clock O08785 | 2 | EBI-396563, EBI-79859 | |
BINARY | Q14738 | DYDC1 Q8WWB3 | 3 | EBI-396563, EBI-740680 | |
BINARY | Q14738 | FSD2 A1L4K1 | 3 | EBI-396563, EBI-5661036 | |
BINARY | Q14738 | PPFIA1 Q13136 | 5 | EBI-396563, EBI-745426 | |
BINARY | Q14738 | PPP2R1A P30153 | 14 | EBI-396563, EBI-302388 | |
BINARY | Q14738 | PPP2R1B P30154 | 3 | EBI-396563, EBI-357094 | |
BINARY | Q14738 | SGO1 Q5FBB7 | 4 | EBI-396563, EBI-989069 | |
BINARY | Q14738 | USHBP1 Q8N6Y0 | 3 | EBI-396563, EBI-739895 |
Protein-protein interaction databases
Miscellaneous
Family & Domains
Features
Showing features for compositional bias, region, repeat, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MPYKLKKEKEPPKVA | ||||||
Region | 1-96 | Disordered | ||||
Sequence: MPYKLKKEKEPPKVAKCTAKPSSSGKDGGGENTEEAQPQPQPQPQPQAQSQPPSSNKRPSNSTPPPTQLSKIKYSGGPQIVKKERRQSSSRFNLSK | ||||||
Repeat | 37-38 | 1 | ||||
Sequence: QP | ||||||
Region | 37-52 | 8 X 2 AA approximate tandem repeats of Q-P | ||||
Sequence: QPQPQPQPQPQAQSQP | ||||||
Repeat | 39-40 | 2 | ||||
Sequence: QP | ||||||
Repeat | 41-42 | 3 | ||||
Sequence: QP | ||||||
Repeat | 43-44 | 4 | ||||
Sequence: QP | ||||||
Repeat | 45-46 | 5 | ||||
Sequence: QP | ||||||
Repeat | 47-48 | 6; approximate | ||||
Sequence: QA | ||||||
Repeat | 49-50 | 7; approximate | ||||
Sequence: QS | ||||||
Compositional bias | 50-74 | Polar residues | ||||
Sequence: SQPPSSNKRPSNSTPPPTQLSKIKY | ||||||
Repeat | 51-52 | 8 | ||||
Sequence: QP | ||||||
Compositional bias | 78-92 | Basic and acidic residues | ||||
Sequence: PQIVKKERRQSSSRF | ||||||
Motif | 523-530 | SH3-binding; class I | ||||
Sequence: RAPPPLPP | ||||||
Motif | 548-565 | Nuclear localization signal | ||||
Sequence: KRTVETEAVQMLKDIKKE |
Sequence similarities
Belongs to the phosphatase 2A regulatory subunit B56 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q14738-1
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.
- NameDelta-1
- Length602
- Mass (Da)69,992
- Last updated1996-11-01 v1
- ChecksumF15F71AF4E565387
Q14738-2
- NameDelta-2
- Differences from canonical
- 85-116: Missing
Q14738-3
- NameDelta-3
- Differences from canonical
- 11-116: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MPYKLKKEKEPPKVA | ||||||
Alternative sequence | VSP_005110 | 11-116 | in isoform Delta-3 | |||
Sequence: Missing | ||||||
Compositional bias | 50-74 | Polar residues | ||||
Sequence: SQPPSSNKRPSNSTPPPTQLSKIKY | ||||||
Compositional bias | 78-92 | Basic and acidic residues | ||||
Sequence: PQIVKKERRQSSSRF | ||||||
Alternative sequence | VSP_005111 | 85-116 | in isoform Delta-2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L76702 EMBL· GenBank· DDBJ | AAB69751.1 EMBL· GenBank· DDBJ | mRNA | ||
AB000634 EMBL· GenBank· DDBJ | BAA20381.1 EMBL· GenBank· DDBJ | mRNA | ||
AB000635 EMBL· GenBank· DDBJ | BAA20382.1 EMBL· GenBank· DDBJ | mRNA | ||
D78360 EMBL· GenBank· DDBJ | BAA11372.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290604 EMBL· GenBank· DDBJ | BAF83293.1 EMBL· GenBank· DDBJ | mRNA | ||
AB451342 EMBL· GenBank· DDBJ | BAG70156.1 EMBL· GenBank· DDBJ | mRNA | ||
AB451357 EMBL· GenBank· DDBJ | BAG70171.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136304 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471081 EMBL· GenBank· DDBJ | EAX04133.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010692 EMBL· GenBank· DDBJ | AAH10692.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001095 EMBL· GenBank· DDBJ | AAH01095.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001175 EMBL· GenBank· DDBJ | AAH01175.1 EMBL· GenBank· DDBJ | mRNA |