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Protein

Inositol-trisphosphate 3-kinase A

Gene

Itpka

Organism
Rattus norvegicus (Rat)
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.1 Publication

Enzyme regulationi

IP3K is activated by calmodulin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei195 – 1951ATPBy similarity
Binding sitei207 – 2071ATP
Binding sitei260 – 2601ATP
Binding sitei262 – 2621SubstrateBy similarity
Binding sitei283 – 2831SubstrateBy similarity
Binding sitei334 – 3341ATPBy similarity
Binding sitei414 – 4141ATP
Binding sitei417 – 4171SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi247 – 2493ATP

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin-dependent protein kinase activity Source: RGD
  • inositol-1,4,5-trisphosphate 3-kinase activity Source: RGD
  • Rac GTPase binding Source: MGI

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • dendritic spine maintenance Source: MGI
  • inositol metabolic process Source: Ensembl
  • positive regulation of dendritic spine morphogenesis Source: MGI
  • regulation of synaptic plasticity Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.127. 5301.
ReactomeiR-RNO-1855204. Synthesis of IP3 and IP4 in the cytosol.
SABIO-RKP17105.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi619950. Itpka.

Subcellular locationi

GO - Cellular componenti

  • dendritic spine Source: MGI
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3261.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Inositol-trisphosphate 3-kinase APRO_0000066867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei195 – 1951PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP17105.
PRIDEiP17105.

PTM databases

iPTMnetiP17105.
PhosphoSiteiP17105.

Expressioni

Gene expression databases

GenevisibleiP17105. RN.

Interactioni

GO - Molecular functioni

  • Rac GTPase binding Source: MGI

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007247.

Chemistry

BindingDBiP17105.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi204 – 2063Combined sources
Helixi211 – 22010Combined sources
Helixi224 – 2285Combined sources
Beta strandi245 – 2473Combined sources
Turni249 – 2524Combined sources
Beta strandi257 – 2615Combined sources
Helixi270 – 2789Combined sources
Helixi286 – 2894Combined sources
Helixi299 – 3035Combined sources
Helixi312 – 3209Combined sources
Turni323 – 3253Combined sources
Beta strandi330 – 3345Combined sources
Beta strandi336 – 3383Combined sources
Helixi350 – 36112Combined sources
Helixi365 – 38218Combined sources
Helixi386 – 3894Combined sources
Beta strandi397 – 4026Combined sources
Beta strandi408 – 4136Combined sources
Beta strandi429 – 4313Combined sources
Helixi442 – 45615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TZDX-ray2.20A/B185-459[»]
ProteinModelPortaliP17105.
SMRiP17105. Positions 185-459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17105.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni285 – 2939Calmodulin-binding
Regioni310 – 3178Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1621. Eukaryota.
ENOG410Y8AC. LUCA.
GeneTreeiENSGT00390000017438.
HOGENOMiHOG000231765.
HOVERGENiHBG052138.
InParanoidiP17105.
KOiK00911.
OMAiWLPAVGS.
OrthoDBiEOG7DVDB7.
PhylomeDBiP17105.
TreeFamiTF318394.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P17105-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLPGHPTGM ARPRGAGPCS PGLERAPRRS VGELRLLFEA RCAAVAAAAA
60 70 80 90 100
AGEPRARGAK RRGGQVPNGL PRAAPAPVIP QLTVTSEEDV APASPGPPDR
110 120 130 140 150
EGNWLPAAGS HLQQPRRLST SSLSSTGSSS LLEDSEDDLL SDSESRSRGN
160 170 180 190 200
VQLETSEDVG QKSHWQKIRT MVNLPVMSPF KKRYSWVQLA GHTGSFKAAG
210 220 230 240 250
TSGLILKRSS EPEHYCLVRL MADVLRGCVP AFHGVVERDG ESYLQLQDLL
260 270 280 290 300
DGFDGPCVLD CKMGVRTYLE EELTKARERP KLRKDMYKKM LAVDPEAPTE
310 320 330 340 350
EEHAQRAVTK PRYMQWREGI SSSTTLGFRI EGIKKADGSC STDFKTTRSR
360 370 380 390 400
EQVTRVFEEF MQGDAEVLKR YLNRLQQIRD TLEISDFFRR HEVIGSSLLF
410 420 430 440 450
VHDHCHRAGV WLIDFGKTTP LPDGQILDHR RPWEEGNRED GYLLGLDNLI

GILANLAER
Length:459
Mass (Da):50,871
Last modified:November 1, 1991 - v3
Checksum:i8093DADC0FADC290
GO

Sequence cautioni

The sequence AAA41457.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56917 mRNA. Translation: CAA40248.1.
M29787 mRNA. Translation: AAA41457.1. Different initiation.
PIRiS13064.
RefSeqiNP_112307.2. NM_031045.2.
UniGeneiRn.9877.

Genome annotation databases

EnsembliENSRNOT00000007247; ENSRNOP00000007247; ENSRNOG00000005284.
GeneIDi81677.
KEGGirno:81677.
UCSCiRGD:619950. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56917 mRNA. Translation: CAA40248.1.
M29787 mRNA. Translation: AAA41457.1. Different initiation.
PIRiS13064.
RefSeqiNP_112307.2. NM_031045.2.
UniGeneiRn.9877.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TZDX-ray2.20A/B185-459[»]
ProteinModelPortaliP17105.
SMRiP17105. Positions 185-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007247.

Chemistry

BindingDBiP17105.
ChEMBLiCHEMBL3261.

PTM databases

iPTMnetiP17105.
PhosphoSiteiP17105.

Proteomic databases

PaxDbiP17105.
PRIDEiP17105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000007247; ENSRNOP00000007247; ENSRNOG00000005284.
GeneIDi81677.
KEGGirno:81677.
UCSCiRGD:619950. rat.

Organism-specific databases

CTDi3706.
RGDi619950. Itpka.

Phylogenomic databases

eggNOGiKOG1621. Eukaryota.
ENOG410Y8AC. LUCA.
GeneTreeiENSGT00390000017438.
HOGENOMiHOG000231765.
HOVERGENiHBG052138.
InParanoidiP17105.
KOiK00911.
OMAiWLPAVGS.
OrthoDBiEOG7DVDB7.
PhylomeDBiP17105.
TreeFamiTF318394.

Enzyme and pathway databases

BRENDAi2.7.1.127. 5301.
ReactomeiR-RNO-1855204. Synthesis of IP3 and IP4 in the cytosol.
SABIO-RKP17105.

Miscellaneous databases

EvolutionaryTraceiP17105.
PROiP17105.

Gene expression databases

GenevisibleiP17105. RN.

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. "Cloning and expression in Escherichia coli of a rat brain cDNA encoding a Ca2+/calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase."
    Takazawa K., Vandekerckhove J., Dumont J.E., Erneux C.
    Biochem. J. 272:107-112(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and expression of a complementary DNA for inositol 1,4,5-trisphosphate 3-kinase."
    Choi K.Y., Kim H.K., Lee S.Y., Moon K.H., Sim S.S., Kim J.W., Chung H.K., Rhee S.G.
    Science 248:64-66(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Brain.
  3. "Active site labelling of inositol 1,4,5-trisphosphate 3-kinase A by phenylglyoxal."
    Communi D., Lecocq R., Vanweyenberg V., Erneux C.
    Biochem. J. 310:109-115(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 315-326, CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase."
    Miller G.J., Hurley J.H.
    Mol. Cell 15:703-711(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 185-459 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiIP3KA_RAT
AccessioniPrimary (citable) accession number: P17105
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1991
Last modified: July 6, 2016
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.