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Protein

Inositol-trisphosphate 3-kinase A

Gene

ITPKA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.

Enzyme regulationi

IP3K is activated by calmodulin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei197 – 1971ATP
Binding sitei209 – 2091ATP
Binding sitei262 – 2621ATP
Binding sitei264 – 2641Substrate1 Publication
Binding sitei285 – 2851Substrate1 Publication
Binding sitei336 – 3361ATP
Binding sitei416 – 4161ATP
Binding sitei419 – 4191Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi249 – 2513ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06405-MONOMER.
BRENDAi2.7.1.127. 2681.
ReactomeiR-HSA-1855204. Synthesis of IP3 and IP4 in the cytosol.
SIGNORiP23677.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol-trisphosphate 3-kinase A (EC:2.7.1.127)
Alternative name(s):
Inositol 1,4,5-trisphosphate 3-kinase A
Short name:
IP3 3-kinase A
Short name:
IP3K A
Short name:
InsP 3-kinase A
Gene namesi
Name:ITPKA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:6178. ITPKA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29975.

Polymorphism and mutation databases

BioMutaiITPKA.
DMDMi124807.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Inositol-trisphosphate 3-kinase APRO_0000066865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei137 – 1371PhosphoserineBy similarity
Modified residuei197 – 1971PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP23677.
MaxQBiP23677.
PaxDbiP23677.
PeptideAtlasiP23677.
PRIDEiP23677.

PTM databases

iPTMnetiP23677.
PhosphoSiteiP23677.

Expressioni

Gene expression databases

BgeeiP23677.
CleanExiHS_ITPKA.
ExpressionAtlasiP23677. baseline and differential.
GenevisibleiP23677. HS.

Organism-specific databases

HPAiHPA040454.

Interactioni

Protein-protein interaction databases

BioGridi109911. 2 interactions.
IntActiP23677. 1 interaction.
STRINGi9606.ENSP00000260386.

Chemistry

BindingDBiP23677.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi166 – 1749Combined sources
Turni177 – 1793Combined sources
Helixi188 – 1914Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi206 – 2105Combined sources
Helixi213 – 22311Combined sources
Helixi226 – 2305Combined sources
Beta strandi234 – 2407Combined sources
Beta strandi243 – 2497Combined sources
Turni251 – 2544Combined sources
Beta strandi259 – 2679Combined sources
Helixi272 – 2809Combined sources
Helixi286 – 29510Combined sources
Helixi302 – 3076Combined sources
Helixi312 – 32211Combined sources
Helixi325 – 3284Combined sources
Beta strandi329 – 3368Combined sources
Beta strandi338 – 3403Combined sources
Helixi352 – 36312Combined sources
Helixi367 – 38418Combined sources
Helixi388 – 3914Combined sources
Beta strandi393 – 3975Combined sources
Beta strandi399 – 4046Combined sources
Beta strandi410 – 4156Combined sources
Beta strandi419 – 4224Combined sources
Beta strandi431 – 4333Combined sources
Helixi444 – 45916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W2CX-ray1.95A/B197-461[»]
1W2DX-ray1.94A/B197-461[»]
1W2FX-ray1.80A/B188-461[»]
4UPUX-ray2.34B158-183[»]
ProteinModelPortaliP23677.
SMRiP23677. Positions 177-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23677.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 2959Calmodulin-bindingBy similarity
Regioni312 – 3198Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1621. Eukaryota.
ENOG410Y8AC. LUCA.
GeneTreeiENSGT00390000017438.
HOGENOMiHOG000231765.
HOVERGENiHBG052138.
InParanoidiP23677.
KOiK00911.
OMAiWLPAVGS.
PhylomeDBiP23677.
TreeFamiTF318394.

Family and domain databases

InterProiIPR005522. IPK.
[Graphical view]
PANTHERiPTHR12400. PTHR12400. 2 hits.
PfamiPF03770. IPK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLPGGPTGM ARPGGARPCS PGLERAPRRS VGELRLLFEA RCAAVAAAAA
60 70 80 90 100
AGEPRARGAK RRGGQVPNGL PRAPPAPVIP QLTVTAEEPD VPPTSPGPPE
110 120 130 140 150
RERDCLPAAG SSHLQQPRRL STSSVSSTGS SSLLEDSEDD LLSDSESRSR
160 170 180 190 200
GNVQLEAGED VGQKNHWQKI RTMVNLPVIS PFKKRYAWVQ LAGHTGSFKA
210 220 230 240 250
AGTSGLILKR CSEPERYCLA RLMADALRGC VPAFHGVVER DGESYLQLQD
260 270 280 290 300
LLDGFDGPCV LDCKMGVRTY LEEELTKARE RPKLRKDMYK KMLAVDPEAP
310 320 330 340 350
TEEEHAQRAV TKPRYMQWRE GISSSTTLGF RIEGIKKADG SCSTDFKTTR
360 370 380 390 400
SREQVLRVFE EFVQGDEEVL RRYLNRLQQI RDTLEVSEFF RRHEVIGSSL
410 420 430 440 450
LFVHDHCHRA GVWLIDFGKT TPLPDGQILD HRRPWEEGNR EDGYLLGLDN
460
LIGILASLAE R
Length:461
Mass (Da):51,009
Last modified:November 1, 1991 - v1
Checksum:i18CA214A091F5B19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711P → Q in AAH26331 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54938 mRNA. Translation: CAA38700.1.
BC026331 mRNA. Translation: AAH26331.1.
CCDSiCCDS10076.1.
PIRiJN0129.
RefSeqiNP_002211.1. NM_002220.2.
UniGeneiHs.2722.

Genome annotation databases

EnsembliENST00000260386; ENSP00000260386; ENSG00000137825.
GeneIDi3706.
KEGGihsa:3706.
UCSCiuc001znz.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54938 mRNA. Translation: CAA38700.1.
BC026331 mRNA. Translation: AAH26331.1.
CCDSiCCDS10076.1.
PIRiJN0129.
RefSeqiNP_002211.1. NM_002220.2.
UniGeneiHs.2722.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W2CX-ray1.95A/B197-461[»]
1W2DX-ray1.94A/B197-461[»]
1W2FX-ray1.80A/B188-461[»]
4UPUX-ray2.34B158-183[»]
ProteinModelPortaliP23677.
SMRiP23677. Positions 177-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109911. 2 interactions.
IntActiP23677. 1 interaction.
STRINGi9606.ENSP00000260386.

Chemistry

BindingDBiP23677.

PTM databases

iPTMnetiP23677.
PhosphoSiteiP23677.

Polymorphism and mutation databases

BioMutaiITPKA.
DMDMi124807.

Proteomic databases

EPDiP23677.
MaxQBiP23677.
PaxDbiP23677.
PeptideAtlasiP23677.
PRIDEiP23677.

Protocols and materials databases

DNASUi3706.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260386; ENSP00000260386; ENSG00000137825.
GeneIDi3706.
KEGGihsa:3706.
UCSCiuc001znz.4. human.

Organism-specific databases

CTDi3706.
GeneCardsiITPKA.
HGNCiHGNC:6178. ITPKA.
HPAiHPA040454.
MIMi147521. gene.
neXtProtiNX_P23677.
PharmGKBiPA29975.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1621. Eukaryota.
ENOG410Y8AC. LUCA.
GeneTreeiENSGT00390000017438.
HOGENOMiHOG000231765.
HOVERGENiHBG052138.
InParanoidiP23677.
KOiK00911.
OMAiWLPAVGS.
PhylomeDBiP23677.
TreeFamiTF318394.

Enzyme and pathway databases

BioCyciMetaCyc:HS06405-MONOMER.
BRENDAi2.7.1.127. 2681.
ReactomeiR-HSA-1855204. Synthesis of IP3 and IP4 in the cytosol.
SIGNORiP23677.

Miscellaneous databases

ChiTaRSiITPKA. human.
EvolutionaryTraceiP23677.
GeneWikiiITPKA.
GenomeRNAii3706.
PROiP23677.
SOURCEiSearch...

Gene expression databases

BgeeiP23677.
CleanExiHS_ITPKA.
ExpressionAtlasiP23677. baseline and differential.
GenevisibleiP23677. HS.

Family and domain databases

InterProiIPR005522. IPK.
[Graphical view]
PANTHERiPTHR12400. PTHR12400. 2 hits.
PfamiPF03770. IPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase."
    Takazawa K., Perret J., Dumont J.E., Erneux C.
    Biochem. Biophys. Res. Commun. 174:529-535(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence."
    Takazawa K., Perret J., Dumont J.E., Erneux C.
    Nucleic Acids Res. 18:7141-7141(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  5. "Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase."
    Gonzalez B., Schell M.J., Letcher A.J., Veprintsev D.B., Irvine R.F., Williams R.L.
    Mol. Cell 15:689-701(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 197-461 IN COMPLEX WITH SUBSTRATE AND ADP.

Entry informationi

Entry nameiIP3KA_HUMAN
AccessioniPrimary (citable) accession number: P23677
Secondary accession number(s): Q8TAN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: July 6, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.