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Protein

Inositol-trisphosphate 3-kinase C

Gene

ITPKC

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

Functioni

Can phosphorylate inositol 2,4,5-triphosphate to inositol 2,4,5,6-tetraphosphate.By similarity

Catalytic activityi

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

Enzyme regulationi

Activated by calcium/calmodulin. Inhibited by high concentrations of the substrate Ins(1,2,4)P3, and allosterically activated by the product Ins(1,3,4,5)P4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei431 – 4311ATPBy similarity
Binding sitei484 – 4841ATPBy similarity
Binding sitei486 – 4861Substrate
Binding sitei558 – 5581ATPBy similarity
Binding sitei638 – 6381ATPBy similarity
Binding sitei641 – 6411Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi471 – 4733ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • activation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • inositol phosphate metabolic process Source: Reactome
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS01533-MONOMER.
ReactomeiREACT_150312. Synthesis of IP3 and IP4 in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol-trisphosphate 3-kinase C (EC:2.7.1.127)
Alternative name(s):
Inositol 1,4,5-trisphosphate 3-kinase C
Short name:
IP3 3-kinase C
Short name:
IP3K C
Short name:
InsP 3-kinase C
Gene namesi
Name:ITPKC
Synonyms:IP3KC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:14897. ITPKC.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Kawasaki disease (KWD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn acute, self-limited vasculitis of infants and children characterized by prolonged fever unresponsive to antibiotics, polymorphous skin rash, erythema of the oral mucosa, lips, and tongue, erythema of the palms and soles, bilateral conjunctival injection, and cervical lymphadenopathy.

See also OMIM:611775

Organism-specific databases

MIMi611775. phenotype.
PharmGKBiPA29977.

Polymorphism and mutation databases

BioMutaiITPKC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 683683Inositol-trisphosphate 3-kinase CPRO_0000234070Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96DU7.
PaxDbiQ96DU7.
PRIDEiQ96DU7.

PTM databases

PhosphoSiteiQ96DU7.

Expressioni

Tissue specificityi

Highly expressed in pancreas, skeletal muscle, liver, placenta and weakly in kidney and brain.1 Publication

Gene expression databases

BgeeiQ96DU7.
CleanExiHS_ITPKC.
ExpressionAtlasiQ96DU7. baseline and differential.
GenevisibleiQ96DU7. HS.

Organism-specific databases

HPAiHPA050760.
HPA053003.

Interactioni

Protein-protein interaction databases

BioGridi123209. 3 interactions.
IntActiQ96DU7. 1 interaction.
STRINGi9606.ENSP00000263370.

Structurei

Secondary structure

1
683
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi427 – 4326Combined sources
Helixi435 – 44410Combined sources
Helixi450 – 4523Combined sources
Beta strandi456 – 4627Combined sources
Beta strandi465 – 4717Combined sources
Turni473 – 4764Combined sources
Beta strandi481 – 4899Combined sources
Helixi494 – 4963Combined sources
Turni500 – 5023Combined sources
Helixi508 – 5158Combined sources
Helixi524 – 5296Combined sources
Helixi534 – 54411Combined sources
Helixi547 – 5504Combined sources
Beta strandi551 – 5588Combined sources
Helixi574 – 58512Combined sources
Helixi589 – 60820Combined sources
Helixi610 – 6134Combined sources
Beta strandi615 – 6173Combined sources
Beta strandi621 – 6266Combined sources
Beta strandi632 – 6376Combined sources
Beta strandi642 – 6443Combined sources
Beta strandi653 – 6553Combined sources
Turni659 – 6613Combined sources
Helixi666 – 68116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A98X-ray2.60A425-683[»]
ProteinModelPortaliQ96DU7.
SMRiQ96DU7. Positions 395-683.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96DU7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni507 – 5137Substrate binding
Regioni509 – 5179Calmodulin-bindingBy similarity
Regioni534 – 5418Substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi324 – 3329Nuclear export signalBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG275147.
GeneTreeiENSGT00390000017438.
HOGENOMiHOG000113089.
HOVERGENiHBG081804.
InParanoidiQ96DU7.
KOiK00911.
OMAiSWKELYT.
OrthoDBiEOG7DVDB7.
PhylomeDBiQ96DU7.
TreeFamiTF318394.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q96DU7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRCPCRGSL NEAEAGALPA AARMGLEAPR GGRRRQPGQQ RPGPGAGAPA
60 70 80 90 100
GRPEGGGPWA RTEGSSLHSE PERAGLGPAP GTESPQAEFW TDGQTEPAAA
110 120 130 140 150
GLGVETERPK QKTEPDRSSL RTHLEWSWSE LETTCLWTET GTDGLWTDPH
160 170 180 190 200
RSDLQFQPEE ASPWTQPGVH GPWTELETHG SQTQPERVKS WADNLWTHQN
210 220 230 240 250
SSSLQTHPEG ACPSKEPSAD GSWKELYTDG SRTQQDIEGP WTEPYTDGSQ
260 270 280 290 300
KKQDTEAARK QPGTGGFQIQ QDTDGSWTQP STDGSQTAPG TDCLLGEPED
310 320 330 340 350
GPLEEPEPGE LLTHLYSHLK CSPLCPVPRL IITPETPEPE AQPVGPPSRV
360 370 380 390 400
EGGSGGFSSA SSFDESEDDV VAGGGGASDP EDRSGSKPWK KLKTVLKYSP
410 420 430 440 450
FVVSFRKHYP WVQLSGHAGN FQAGEDGRIL KRFCQCEQRS LEQLMKDPLR
460 470 480 490 500
PFVPAYYGMV LQDGQTFNQM EDLLADFEGP SIMDCKMGSR TYLEEELVKA
510 520 530 540 550
RERPRPRKDM YEKMVAVDPG APTPEEHAQG AVTKPRYMQW RETMSSTSTL
560 570 580 590 600
GFRIEGIKKA DGTCNTNFKK TQALEQVTKV LEDFVDGDHV ILQKYVACLE
610 620 630 640 650
ELREALEISP FFKTHEVVGS SLLFVHDHTG LAKVWMIDFG KTVALPDHQT
660 670 680
LSHRLPWAEG NREDGYLWGL DNMICLLQGL AQS
Length:683
Mass (Da):75,207
Last modified:December 1, 2001 - v1
Checksum:i58093A2A8E046458
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 823PGT → NSA in BAA22524 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ290975 mRNA. Translation: CAC40815.1.
BC060788 mRNA. Translation: AAH60788.1.
D38169 mRNA. Translation: BAA22524.1.
Y11999 mRNA. Translation: CAA72728.1.
CCDSiCCDS12563.1.
RefSeqiNP_079470.1. NM_025194.2.
XP_006723467.1. XM_006723404.1.
UniGeneiHs.515415.

Genome annotation databases

EnsembliENST00000263370; ENSP00000263370; ENSG00000086544.
GeneIDi80271.
KEGGihsa:80271.
UCSCiuc002oot.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ290975 mRNA. Translation: CAC40815.1.
BC060788 mRNA. Translation: AAH60788.1.
D38169 mRNA. Translation: BAA22524.1.
Y11999 mRNA. Translation: CAA72728.1.
CCDSiCCDS12563.1.
RefSeqiNP_079470.1. NM_025194.2.
XP_006723467.1. XM_006723404.1.
UniGeneiHs.515415.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A98X-ray2.60A425-683[»]
ProteinModelPortaliQ96DU7.
SMRiQ96DU7. Positions 395-683.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123209. 3 interactions.
IntActiQ96DU7. 1 interaction.
STRINGi9606.ENSP00000263370.

PTM databases

PhosphoSiteiQ96DU7.

Polymorphism and mutation databases

BioMutaiITPKC.

Proteomic databases

MaxQBiQ96DU7.
PaxDbiQ96DU7.
PRIDEiQ96DU7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263370; ENSP00000263370; ENSG00000086544.
GeneIDi80271.
KEGGihsa:80271.
UCSCiuc002oot.3. human.

Organism-specific databases

CTDi80271.
GeneCardsiGC19P041223.
HGNCiHGNC:14897. ITPKC.
HPAiHPA050760.
HPA053003.
MIMi606476. gene.
611775. phenotype.
neXtProtiNX_Q96DU7.
PharmGKBiPA29977.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG275147.
GeneTreeiENSGT00390000017438.
HOGENOMiHOG000113089.
HOVERGENiHBG081804.
InParanoidiQ96DU7.
KOiK00911.
OMAiSWKELYT.
OrthoDBiEOG7DVDB7.
PhylomeDBiQ96DU7.
TreeFamiTF318394.

Enzyme and pathway databases

BioCyciMetaCyc:HS01533-MONOMER.
ReactomeiREACT_150312. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

ChiTaRSiITPKC. human.
EvolutionaryTraceiQ96DU7.
GenomeRNAii80271.
NextBioi70737.
PROiQ96DU7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96DU7.
CleanExiHS_ITPKC.
ExpressionAtlasiQ96DU7. baseline and differential.
GenevisibleiQ96DU7. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C."
    Dewaste V., Pouillon V., Moreau C., Shears S., Takazawa K., Erneux C.
    Biochem. J. 352:343-351(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Thyroid.
  2. "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: Placenta.
  3. Takazawa K., Go M., Togashi S., Endo T., Erneux C., Onaya T.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-683.
    Tissue: Thyroid.
  4. Erneux C., Communi D.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 531-667.
    Tissue: Placenta.
  5. "The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show specific intracellular localization but comparable Ca2+ responses on transfection in COS-7 cells."
    Dewaste V., Moreau C., De Smedt F., Bex F., De Smedt H., Wuytack F., Missiaen L., Erneux C.
    Biochem. J. 374:41-49(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The crystal structure of the catalytic domain of human inositol 1,4,5-trisphosphate 3-kinase C."
    Structural genomics consortium (SGC)
    Submitted (OCT-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 425-683 IN COMPLEX WITH INOSITOL-1,4,5-TRIPHOSPHATE.
  8. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO KAWASAKI DISEASE.

Entry informationi

Entry nameiIP3KC_HUMAN
AccessioniPrimary (citable) accession number: Q96DU7
Secondary accession number(s): Q9UE25, Q9Y475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 106 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 19
    Human chromosome 19: 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

External Data

Dasty 3

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 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.