Q15735 · PI5PA_HUMAN
- ProteinPhosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- GeneINPP5J
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1006 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles.
Catalytic activity
- 1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol 1,4-bisphosphate + phosphateThis reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | dendritic shaft | |
Cellular Component | growth cone | |
Cellular Component | plasma membrane | |
Cellular Component | ruffle | |
Molecular Function | inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity | |
Molecular Function | inositol-1,4,5-trisphosphate 5-phosphatase activity | |
Molecular Function | inositol-polyphosphate 5-phosphatase activity | |
Molecular Function | phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity | |
Molecular Function | SH3 domain binding | |
Biological Process | inositol phosphate metabolic process | |
Biological Process | negative regulation of neuron projection development | |
Biological Process | negative regulation of peptidyl-serine phosphorylation | |
Biological Process | phosphatidylinositol biosynthetic process | |
Biological Process | phosphatidylinositol dephosphorylation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ15735
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly localized to membrane ruffles.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_028107 | 333 | in dbSNP:rs12485025 | |||
Sequence: S → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,145 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 chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000209738 | 1-1006 | UniProt | Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A | |||
Sequence: MEGQSSRGSRRPGTRAGLGSLPMPQGVAQTGAPSKVDSSFQLPAKKNAALGPSEPRLALAPVGPRAAMSASSEGPRLALASPRPILAPLCTPEGQKTATAHRSSSLAPTSVGQLVMSASAGPKPPPATTGSVLAPTSLGLVMPASAGPRSPPVTLGPNLAPTSRDQKQEPPASVGPKPTLAASGLSLALASEEQPPELPSTPSPVPSPVLSPTQEQALAPASTASGAASVGQTSARKRDAPAPRPLPASEGHLQPPAQTSGPTGSPPCIQTSPDPRLSPSFRARPEALHSSPEDPVLPRPPQTLPLDVGQGPSEPGTHSPGLLSPTFRPGAPSGQTVPPPLPKPPRSPSRSPSHSPNRSPCVPPAPDMALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPTWKSDPGFRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQISLPSSELASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALRPSSRERRGASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGLLPALRLETVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP | |||||||
Modified residue | 56 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 56 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 65 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 76 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 83 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 83 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 154 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 291 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 324 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 902 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 903 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 903 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 990 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 990 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 992 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-416 | Disordered | ||||
Sequence: MEGQSSRGSRRPGTRAGLGSLPMPQGVAQTGAPSKVDSSFQLPAKKNAALGPSEPRLALAPVGPRAAMSASSEGPRLALASPRPILAPLCTPEGQKTATAHRSSSLAPTSVGQLVMSASAGPKPPPATTGSVLAPTSLGLVMPASAGPRSPPVTLGPNLAPTSRDQKQEPPASVGPKPTLAASGLSLALASEEQPPELPSTPSPVPSPVLSPTQEQALAPASTASGAASVGQTSARKRDAPAPRPLPASEGHLQPPAQTSGPTGSPPCIQTSPDPRLSPSFRARPEALHSSPEDPVLPRPPQTLPLDVGQGPSEPGTHSPGLLSPTFRPGAPSGQTVPPPLPKPPRSPSRSPSHSPNRSPCVPPAPDMALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPT | ||||||
Compositional bias | 96-116 | Polar residues | ||||
Sequence: KTATAHRSSSLAPTSVGQLVM | ||||||
Motif | 102-107 | RSXSXX motif 1 | ||||
Sequence: RSSSLA | ||||||
Compositional bias | 210-232 | Polar residues | ||||
Sequence: LSPTQEQALAPASTASGAASVGQ | ||||||
Compositional bias | 253-267 | Polar residues | ||||
Sequence: LQPPAQTSGPTGSPP | ||||||
Compositional bias | 332-367 | Pro residues | ||||
Sequence: PSGQTVPPPLPKPPRSPSRSPSHSPNRSPCVPPAPD | ||||||
Motif | 345-350 | SH3-binding | ||||
Sequence: PRSPSR | ||||||
Motif | 350-355 | RSXSXX motif 2 | ||||
Sequence: RSPSHS | ||||||
Compositional bias | 378-416 | Polar residues | ||||
Sequence: TGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPT | ||||||
Region | 425-728 | Catalytic | ||||
Sequence: ITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAAQF | ||||||
Region | 729-840 | Required for ruffle localization | ||||
Sequence: LLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQIS | ||||||
Compositional bias | 844-863 | Polar residues | ||||
Sequence: SELASSSTDSSGTSSEGEDD | ||||||
Region | 844-1006 | Disordered | ||||
Sequence: SELASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALRPSSRERRGASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGLLPALRLETVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP | ||||||
Motif | 874-879 | RSXSXX motif 3 | ||||
Sequence: RSPSPG | ||||||
Motif | 885-890 | RSXSXX motif 4 | ||||
Sequence: RSRSPG | ||||||
Compositional bias | 908-939 | Polar residues | ||||
Sequence: GASRSPSPQSRRLSRVAPDRSSNGSSRGSSEE | ||||||
Motif | 911-916 | RSXSXX motif 5 | ||||
Sequence: RSPSPQ |
Domain
The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein.
Sequence similarities
Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type II family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q15735-1
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
- Length1,006
- Mass (Da)107,197
- Last updated2006-10-17 v3
- ChecksumADB6382AA33E15AC
Q15735-2
- Name2
- Differences from canonical
- 1-367: Missing
Q15735-3
- Name3
- Differences from canonical
- 56-423: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J0H5 | C9J0H5_HUMAN | INPP5J | 96 | ||
A0AAQ5BIH3 | A0AAQ5BIH3_HUMAN | INPP5J | 54 | ||
A0AAQ5BIH4 | A0AAQ5BIH4_HUMAN | INPP5J | 67 | ||
C9K0M5 | C9K0M5_HUMAN | INPP5J | 90 | ||
B5MBZ3 | B5MBZ3_HUMAN | INPP5J | 371 | ||
B5MCL8 | B5MCL8_HUMAN | INPP5J | 345 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007296 | 1-367 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_021017 | 56-423 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 96-116 | Polar residues | ||||
Sequence: KTATAHRSSSLAPTSVGQLVM | ||||||
Compositional bias | 210-232 | Polar residues | ||||
Sequence: LSPTQEQALAPASTASGAASVGQ | ||||||
Compositional bias | 253-267 | Polar residues | ||||
Sequence: LQPPAQTSGPTGSPP | ||||||
Compositional bias | 332-367 | Pro residues | ||||
Sequence: PSGQTVPPPLPKPPRSPSRSPSHSPNRSPCVPPAPD | ||||||
Compositional bias | 378-416 | Polar residues | ||||
Sequence: TGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPT | ||||||
Sequence conflict | 610-612 | in Ref. 5 | ||||
Sequence: SYD → ARG | ||||||
Sequence conflict | 662 | in Ref. 1; BAC86611 | ||||
Sequence: V → A | ||||||
Sequence conflict | 791 | in Ref. 4; AAI09289 | ||||
Sequence: W → R | ||||||
Compositional bias | 844-863 | Polar residues | ||||
Sequence: SELASSSTDSSGTSSEGEDD | ||||||
Compositional bias | 908-939 | Polar residues | ||||
Sequence: GASRSPSPQSRRLSRVAPDRSSNGSSRGSSEE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK092859 EMBL· GenBank· DDBJ | BAG52616.1 EMBL· GenBank· DDBJ | mRNA | ||
AK095944 EMBL· GenBank· DDBJ | BAC04657.1 EMBL· GenBank· DDBJ | mRNA | ||
AK126610 EMBL· GenBank· DDBJ | BAC86611.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005005 EMBL· GenBank· DDBJ | AAD15618.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CH471095 EMBL· GenBank· DDBJ | EAW59936.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC109288 EMBL· GenBank· DDBJ | AAI09289.1 EMBL· GenBank· DDBJ | mRNA | ||
U45975 EMBL· GenBank· DDBJ | AAB03216.1 EMBL· GenBank· DDBJ | mRNA |