Q9HB21 · PKHA1_HUMAN
- ProteinPleckstrin homology domain-containing family A member 1
- GenePLEKHA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids404 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane.
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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Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePleckstrin homology domain-containing family A member 1
- Short namesPH domain-containing family A member 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9HB21
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 28 | No effect on phosphatidylinositide binding. | ||||
Sequence: R → L | ||||||
Mutagenesis | 203 | Binds both PtdIns3,4P2 and PtdIns3,4,5P3. | ||||
Sequence: A → G | ||||||
Mutagenesis | 203-204 | Binds both PtdIns3,4P2 and PtdIns3,4,5P3. | ||||
Sequence: AV → GG | ||||||
Mutagenesis | 203-205 | Abolishes phosphatidylinositide binding. | ||||
Sequence: AVM → GGG | ||||||
Mutagenesis | 203-205 | Binds both PtdIns3,4P2 and PtdIns3,4,5P3. | ||||
Sequence: AVM → GLV | ||||||
Mutagenesis | 204 | No effect. | ||||
Sequence: V → L | ||||||
Mutagenesis | 205 | No effect. | ||||
Sequence: M → V | ||||||
Mutagenesis | 207 | No effect. | ||||
Sequence: N → T | ||||||
Mutagenesis | 211 | Abolishes phosphatidylinositide binding. | ||||
Sequence: R → L | ||||||
Natural variant | VAR_024562 | 320 | in dbSNP:rs1045216 | |||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 487 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
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_0000053873 | 1-404 | UniProt | Pleckstrin homology domain-containing family A member 1 | |||
Sequence: MPYVDRQNRICGFLDIEENENSGKFLRRYFILDTREDSFVWYMDNPQNLPSGSSRVGAIKLTYISKVSDATKLRPKAEFCFVMNAGMRKYFLQANDQQDLVEWVNVLNKAIKITVPKQSDSQPNSDNLSRHGECGKKQVSYRTDIVGGVPIITPTQKEEVNECGESIDRNNLKRSQSHLPYFTPKPPQDSAVIKAGYCVKQGAVMKNWKRRYFQLDENTIGYFKSELEKEPLRVIPLKEVHKVQECKQSDIMMRDNLFEIVTTSRTFYVQADSPEEMHSWIKAVSGAIVAQRGPGRSASSEHPPGPSESKHAFRPTNAATATSHSTASRSNSLVSTFTMEKRGFYESLAKVKPGNFKVQTVSPREPASKVTEQALLRPQSKNGPQEKDCDLVDLDDASLPVSDV | |||||||
Modified residue (large scale data) | 129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 166 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 181 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 332 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 362 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 380 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in skeletal muscle, thymus, pancreas, placenta and lung. Detected at low levels in brain, heart, peripheral blood leukocytes, testis, ovary, spinal cord, thyroid, kidney, liver, small intestine and colon.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with MPDZ and PTPN13.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9HB21 | MPDZ O75970 | 6 | EBI-2652984, EBI-821405 | |
BINARY | Q9HB21 | SH3BP4 Q9P0V3 | 2 | EBI-2652984, EBI-1049513 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 7-112 | PH 1 | ||||
Sequence: QNRICGFLDIEENENSGKFLRRYFILDTREDSFVWYMDNPQNLPSGSSRVGAIKLTYISKVSDATKLRPKAEFCFVMNAGMRKYFLQANDQQDLVEWVNVLNKAIK | ||||||
Domain | 191-289 | PH 2 | ||||
Sequence: AVIKAGYCVKQGAVMKNWKRRYFQLDENTIGYFKSELEKEPLRVIPLKEVHKVQECKQSDIMMRDNLFEIVTTSRTFYVQADSPEEMHSWIKAVSGAIV | ||||||
Region | 291-332 | Disordered | ||||
Sequence: QRGPGRSASSEHPPGPSESKHAFRPTNAATATSHSTASRSNS | ||||||
Compositional bias | 313-332 | Polar residues | ||||
Sequence: FRPTNAATATSHSTASRSNS | ||||||
Region | 355-404 | Disordered | ||||
Sequence: NFKVQTVSPREPASKVTEQALLRPQSKNGPQEKDCDLVDLDDASLPVSDV | ||||||
Compositional bias | 361-380 | Polar residues | ||||
Sequence: VSPREPASKVTEQALLRPQS |
Domain
Binds to membranes enriched in PtdIns3,4P2 via the C-terminal PH domain.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9HB21-1
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
- Length404
- Mass (Da)45,553
- Last updated2004-03-29 v2
- Checksum6855CD58E1A80F8A
Q9HB21-2
- Name2
- Differences from canonical
- 301-404: EHPPGPSESKHAFRPTNAATATSHSTASRSNSLVSTFTMEKRGFYESLAKVKPGNFKVQTVSPREPASKVTEQALLRPQSKNGPQEKDCDLVDLDDASLPVSDV → MRQARRLSNPCIQRYTSRAGECSTYVGSHANVPS
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043091 | 301-404 | in isoform 2 | |||
Sequence: EHPPGPSESKHAFRPTNAATATSHSTASRSNSLVSTFTMEKRGFYESLAKVKPGNFKVQTVSPREPASKVTEQALLRPQSKNGPQEKDCDLVDLDDASLPVSDV → MRQARRLSNPCIQRYTSRAGECSTYVGSHANVPS | ||||||
Compositional bias | 313-332 | Polar residues | ||||
Sequence: FRPTNAATATSHSTASRSNS | ||||||
Compositional bias | 361-380 | Polar residues | ||||
Sequence: VSPREPASKVTEQALLRPQS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF286160 EMBL· GenBank· DDBJ | AAG15197.1 EMBL· GenBank· DDBJ | mRNA | ||
AK057463 EMBL· GenBank· DDBJ | BAG51917.1 EMBL· GenBank· DDBJ | mRNA | ||
BX664700 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BX842242 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471066 EMBL· GenBank· DDBJ | EAW49315.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471066 EMBL· GenBank· DDBJ | EAW49316.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471066 EMBL· GenBank· DDBJ | EAW49318.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471066 EMBL· GenBank· DDBJ | EAW49319.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001136 EMBL· GenBank· DDBJ | AAH01136.1 EMBL· GenBank· DDBJ | mRNA | ||
BC042458 EMBL· GenBank· DDBJ | AAH42458.1 EMBL· GenBank· DDBJ | mRNA |