P27987 · IP3KB_HUMAN
- ProteinInositol-trisphosphate 3-kinase B
- GeneITPKB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids946 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis.
Catalytic activity
- 1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H+This reaction proceeds in the forward direction.
Activity regulation
IP3K is activated by calcium and calmodulin. Form B is much more sensitive to calcium/calmodulin than form A.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.6 μM | 1D-myo-inositol 1,4,5-trisphosphate |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 679 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 690 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 730-732 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DDL | ||||||
Binding site | 743 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 745 | substrate | ||||
Sequence: K | ||||||
Binding site | 766 | substrate | ||||
Sequence: R | ||||||
Binding site | 793-800 | substrate | ||||
Sequence: KPRYMQWR | ||||||
Binding site | 817 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 897 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 900 | substrate | ||||
Sequence: K |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInositol-trisphosphate 3-kinase B
- 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 accessionP27987
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_053444 | 322 | in dbSNP:rs3754413 | |||
Sequence: A → T | ||||||
Natural variant | VAR_023768 | 408 | in dbSNP:rs6667260 | |||
Sequence: S → A | ||||||
Natural variant | VAR_022380 | 552 | in dbSNP:rs708776 | |||
Sequence: P → Q | ||||||
Mutagenesis | 897 | Loss of kinase activity. | ||||
Sequence: D → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,325 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_0000066868 | 1-946 | UniProt | Inositol-trisphosphate 3-kinase B | |||
Sequence: MAVYCYALNSLVIMNSANEMKSGGGPGPSGSETPPPPRRAVLSPGSVFSPGRGASFLFPPAESLSPEEPRSPGGWRSGRRRLNSSSGSGSGSSGSSVSSPSWAGRLRGDRQQVVAAGTLSPPGPEEAKRKLRILQRELQNVQVNQKVGMFEAHIQAQSSAIQAPRSPRLGRARSPSPCPFRSSSQPPGRVLVQGARSEERRTKSWGEQCPETSGTDSGRKGGPSLCSSQVKKGMPPLPGRAAPTGSEAQGPSAFVRMEKGIPASPRCGSPTAMEIDKRGSPTPGTRSCLAPSLGLFGASLTMATEVAARVTSTGPHRPQDLALTEPSGRARELEDLQPPEALVERQGQFLGSETSPAPERGGPRDGEPPGKMGKGYLPCGMPGSGEPEVGKRPEETTVSVQSAESSDSLSWSRLPRALASVGPEEARSGAPVGGGRWQLSDRVEGGSPTLGLLGGSPSAQPGTGNVEAGIPSGRMLEPLPCWDAAKDLKEPQCPPGDRVGVQPGNSRVWQGTMEKAGLAWTRGTGVQSEGTWESQRQDSDALPSPELLPQDPDKPFLRKACSPSNIPAVIITDMGTQEDGALEETQGSPRGNLPLRKLSSSSASSTGFSSSYEDSEEDISSDPERTLDPNSAFLHTLDQQKPRVSKSWRKIKNMVHWSPFVMSFKKKYPWIQLAGHAGSFKAAANGRILKKHCESEQRCLDRLMVDVLRPFVPAYHGDVVKDGERYNQMDDLLADFDSPCVMDCKMGIRTYLEEELTKARKKPSLRKDMYQKMIEVDPEAPTEEEKAQRAVTKPRYMQWRETISSTATLGFRIEGIKKEDGTVNRDFKKTKTREQVTEAFREFTKGNHNILIAYRDRLKAIRTTLEVSPFFKCHEVIGSSLLFIHDKKEQAKVWMIDFGKTTPLPEGQTLQHDVPWQEGNREDGYLSGLNNLVDILTEMSQDAPLA | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 43 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 49 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 71 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 166 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 174 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 204 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 204 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 228 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 264 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 269 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 269 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 271 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 280 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 355 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 449 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 456 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 562 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 621 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with DMTN.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P27987 | CEP70 Q8NHQ1 | 3 | EBI-751388, EBI-739624 | |
BINARY | P27987 | CTDSP1 Q9GZU7 | 5 | EBI-751388, EBI-751587 | |
BINARY | P27987 | GOLGA2 Q08379 | 4 | EBI-751388, EBI-618309 | |
BINARY | P27987 | IFT88 Q13099 | 3 | EBI-751388, EBI-347427 | |
BINARY | P27987 | KRT34 O76011 | 3 | EBI-751388, EBI-1047093 | |
BINARY | P27987 | PPP3CA Q08209-2 | 3 | EBI-751388, EBI-11959013 | |
BINARY | P27987 | SCAI Q8N9R8 | 3 | EBI-751388, EBI-4395514 | |
BINARY | P27987 | TRIM54 Q9BYV2 | 3 | EBI-751388, EBI-2130429 | |
BINARY | P27987 | UBQLN2 Q9UHD9 | 5 | EBI-751388, EBI-947187 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 19-128 | Disordered | ||||
Sequence: EMKSGGGPGPSGSETPPPPRRAVLSPGSVFSPGRGASFLFPPAESLSPEEPRSPGGWRSGRRRLNSSSGSGSGSSGSSVSSPSWAGRLRGDRQQVVAAGTLSPPGPEEAK | ||||||
Compositional bias | 78-102 | Polar residues | ||||
Sequence: GRRRLNSSSGSGSGSSGSSVSSPSW | ||||||
Region | 156-288 | Disordered | ||||
Sequence: AQSSAIQAPRSPRLGRARSPSPCPFRSSSQPPGRVLVQGARSEERRTKSWGEQCPETSGTDSGRKGGPSLCSSQVKKGMPPLPGRAAPTGSEAQGPSAFVRMEKGIPASPRCGSPTAMEIDKRGSPTPGTRSC | ||||||
Compositional bias | 207-224 | Polar residues | ||||
Sequence: EQCPETSGTDSGRKGGPS | ||||||
Region | 308-472 | Disordered | ||||
Sequence: ARVTSTGPHRPQDLALTEPSGRARELEDLQPPEALVERQGQFLGSETSPAPERGGPRDGEPPGKMGKGYLPCGMPGSGEPEVGKRPEETTVSVQSAESSDSLSWSRLPRALASVGPEEARSGAPVGGGRWQLSDRVEGGSPTLGLLGGSPSAQPGTGNVEAGIPS | ||||||
Compositional bias | 395-413 | Polar residues | ||||
Sequence: ETTVSVQSAESSDSLSWSR | ||||||
Region | 486-561 | Disordered | ||||
Sequence: KDLKEPQCPPGDRVGVQPGNSRVWQGTMEKAGLAWTRGTGVQSEGTWESQRQDSDALPSPELLPQDPDKPFLRKAC | ||||||
Compositional bias | 524-541 | Polar residues | ||||
Sequence: TGVQSEGTWESQRQDSDA | ||||||
Region | 580-638 | Disordered | ||||
Sequence: GALEETQGSPRGNLPLRKLSSSSASSTGFSSSYEDSEEDISSDPERTLDPNSAFLHTLD | ||||||
Compositional bias | 592-614 | Polar residues | ||||
Sequence: NLPLRKLSSSSASSTGFSSSYED | ||||||
Region | 768-776 | Calmodulin-binding | ||||
Sequence: DMYQKMIEV |
Sequence similarities
Belongs to the inositol phosphokinase (IPK) family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P27987-1
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
- Length946
- Mass (Da)102,376
- Last updated2005-04-26 v5
- Checksum2CCBCBE7AEF26848
P27987-2
- Name2
- Differences from canonical
- 645-946: Missing
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 78-102 | Polar residues | ||||
Sequence: GRRRLNSSSGSGSGSSGSSVSSPSW | ||||||
Sequence conflict | 173 | in Ref. 2; CAC40650 and 4; AAH15009 | ||||
Sequence: R → H | ||||||
Compositional bias | 207-224 | Polar residues | ||||
Sequence: EQCPETSGTDSGRKGGPS | ||||||
Sequence conflict | 210 | in Ref. 2; CAC40650 | ||||
Sequence: P → S | ||||||
Sequence conflict | 297-301 | in Ref. 2; CAC40650 | ||||
Sequence: GASLT → APSFP | ||||||
Compositional bias | 395-413 | Polar residues | ||||
Sequence: ETTVSVQSAESSDSLSWSR | ||||||
Sequence conflict | 442-443 | in Ref. 5 | ||||
Sequence: RV → IP | ||||||
Compositional bias | 524-541 | Polar residues | ||||
Sequence: TGVQSEGTWESQRQDSDA | ||||||
Compositional bias | 592-614 | Polar residues | ||||
Sequence: NLPLRKLSSSSASSTGFSSSYED | ||||||
Alternative sequence | VSP_016092 | 645-946 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y18024 EMBL· GenBank· DDBJ | CAB65055.3 EMBL· GenBank· DDBJ | mRNA | ||
AJ242780 EMBL· GenBank· DDBJ | CAC40650.1 EMBL· GenBank· DDBJ | mRNA | ||
AL365444 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC015009 EMBL· GenBank· DDBJ | AAH15009.1 EMBL· GenBank· DDBJ | mRNA | ||
X57206 EMBL· GenBank· DDBJ | CAA40491.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |