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Q13572 - ITPK1_HUMAN

UniProt

Q13572 - ITPK1_HUMAN

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Protein

Inositol-tetrakisphosphate 1-kinase

Gene

ITPK1

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

Functioni

Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca2+-activated Cl- channels, while Ins(1,3,4,5,6)P5 is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. Also acts as an inositol polyphosphate phosphatase that dephosphorylate Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 to Ins(1,3,4)P3, and Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also act as an isomerase that interconverts the inositol tetrakisphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP and magnesium. Probably acts as the rate-limiting enzyme of the InsP6 pathway. Modifies TNF-alpha-induced apoptosis by interfering with the activation of TNFRSF1A-associated death domain.3 Publications

Catalytic activityi

ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate.
ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.
ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate.

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit.1 Publication

Kineticsi

  1. KM=0.3 µM for Ins(1,3,4)P31 Publication
  2. KM=0.1 µM for Ins(3,4,5,6)P41 Publication

Vmax=320 pmol/min/µg enzyme with Ins(1,3,4)P3 as substrate1 Publication

Vmax=780 pmol/min/µg enzyme enzyme with Ins(3,4,5,6)P4 as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 1811D-myo-inositol 1,3,4-trisphosphateBy similarity
Binding sitei106 – 1061ATP
Binding sitei157 – 1571ATP
Binding sitei167 – 16711D-myo-inositol 1,3,4-trisphosphateBy similarity
Binding sitei199 – 19911D-myo-inositol 1,3,4-trisphosphateBy similarity
Binding sitei214 – 2141ATP
Binding sitei232 – 2321ATP
Binding sitei236 – 2361ATP
Metal bindingi281 – 2811Magnesium 1
Metal bindingi295 – 2951Magnesium 1
Metal bindingi295 – 2951Magnesium 2
Metal bindingi297 – 2971Magnesium 2
Binding sitei297 – 29711D-myo-inositol 1,3,4-trisphosphateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 19912ATPAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. catalytic activity Source: ProtInc
  3. inositol-1,3,4,5,6-pentakisphosphate 1-phosphatase activity Source: Reactome
  4. inositol-1,3,4,6-tetrakisphosphate 1-phosphatase activity Source: Reactome
  5. inositol-1,3,4,6-tetrakisphosphate 6-phosphatase activity Source: Reactome
  6. inositol-1,3,4-trisphosphate 5-kinase activity Source: Reactome
  7. inositol-1,3,4-trisphosphate 6-kinase activity Source: Reactome
  8. inositol-3,4,6-trisphosphate 1-kinase activity Source: Reactome
  9. inositol tetrakisphosphate 1-kinase activity Source: Reactome
  10. isomerase activity Source: UniProtKB-KW
  11. magnesium ion binding Source: InterPro

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. dephosphorylation Source: GOC
  3. inositol phosphate metabolic process Source: Reactome
  4. inositol trisphosphate metabolic process Source: InterPro
  5. signal transduction Source: ProtInc
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Isomerase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02123-MONOMER.
BRENDAi2.7.1.134. 2681.
ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
SABIO-RKQ13572.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol-tetrakisphosphate 1-kinase (EC:2.7.1.134)
Alternative name(s):
Inositol 1,3,4-trisphosphate 5/6-kinase (EC:2.7.1.159)
Short name:
Inositol-triphosphate 5/6-kinase
Short name:
Ins(1,3,4)P(3) 5/6-kinase
Gene namesi
Name:ITPK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 14, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:6177. ITPK1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181K → A: Loss of kinase activity. 1 Publication
Mutagenesisi58 – 581H → A: No effect. 1 Publication
Mutagenesisi59 – 591K → A: Loss of kinase activity. 1 Publication
Mutagenesisi106 – 1061R → A: Loss of kinase activity. 2 Publications
Mutagenesisi157 – 1571K → A: Loss of kinase activity. 1 Publication
Mutagenesisi162 – 1621H → Q: Loss of kinase activity. 1 Publication
Mutagenesisi163 – 1631G → A or P: Loss of kinase activity. 2 Publications
Mutagenesisi163 – 1631G → A: No effect. 2 Publications
Mutagenesisi167 – 1671H → A or Q: Loss of kinase activity. 1 Publication
Mutagenesisi188 – 1881Q → A: No effect. 1 Publication
Mutagenesisi193 – 1931H → A: Loss of kinase activity. 1 Publication
Mutagenesisi199 – 1991K → A: Loss of kinase activity. 1 Publication
Mutagenesisi212 – 2121R → A: Loss of kinase activity. 1 Publication
Mutagenesisi214 – 2141S → A: Loss of kinase activity. 1 Publication
Mutagenesisi215 – 2151L → A: No effect. 1 Publication
Mutagenesisi281 – 2811D → A: Loss of kinase activity. 1 Publication
Mutagenesisi295 – 2951D → A: Loss of kinase activity. 1 Publication
Mutagenesisi297 – 2971N → A or L: Loss of kinase activity. 2 Publications
Mutagenesisi297 – 2971N → D: Induces a strong reduction in kinase activity. 2 Publications
Mutagenesisi301 – 3011G → A: Loss of kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA29974.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Inositol-tetrakisphosphate 1-kinasePRO_0000220833Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei340 – 3401N6-acetyllysine; by EP300 and CREBBP1 Publication
Modified residuei383 – 3831N6-acetyllysine; by EP300 and CREBBP1 Publication
Modified residuei410 – 4101N6-acetyllysine; by EP300 and CREBBP1 Publication

Post-translational modificationi

Acetylation by EP300 and CREBBP destabilizes ITPK1, and down-regulates enzymatic activity. Deacetylated by SIRT1.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ13572.
PaxDbiQ13572.
PRIDEiQ13572.

PTM databases

PhosphoSiteiQ13572.

Expressioni

Tissue specificityi

Expressed in brain > heart > skeletal muscle = kidney = pancreas = liver = placenta > lung. In brain, it is expressed in cerebellum, cerebral cortex, medulla, spinal cord, occipital lobe, frontal lobe, temporal lobe and putamen.1 Publication

Gene expression databases

BgeeiQ13572.
ExpressionAtlasiQ13572. baseline and differential.
GenevestigatoriQ13572.

Organism-specific databases

HPAiHPA055230.

Interactioni

Subunit structurei

Monomer. Interacts with GPS1/COPS1.2 Publications

Protein-protein interaction databases

BioGridi109910. 10 interactions.
DIPiDIP-60016N.
IntActiQ13572. 2 interactions.
MINTiMINT-1463374.
STRINGi9606.ENSP00000267615.

Structurei

Secondary structure

414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 55Combined sources
Beta strandi9 – 135Combined sources
Helixi16 – 227Combined sources
Helixi24 – 329Combined sources
Turni33 – 353Combined sources
Beta strandi37 – 404Combined sources
Helixi48 – 503Combined sources
Beta strandi54 – 585Combined sources
Helixi61 – 688Combined sources
Helixi72 – 8716Combined sources
Beta strandi91 – 955Combined sources
Helixi97 – 1026Combined sources
Helixi106 – 12015Combined sources
Beta strandi130 – 1334Combined sources
Helixi138 – 1403Combined sources
Helixi141 – 1477Combined sources
Beta strandi152 – 1576Combined sources
Turni164 – 1674Combined sources
Beta strandi168 – 1725Combined sources
Helixi175 – 1773Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi196 – 2038Combined sources
Beta strandi206 – 2138Combined sources
Beta strandi228 – 2314Combined sources
Helixi232 – 2343Combined sources
Helixi243 – 2453Combined sources
Helixi259 – 27315Combined sources
Beta strandi277 – 2848Combined sources
Turni286 – 2883Combined sources
Beta strandi291 – 2999Combined sources
Helixi308 – 32417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ODTX-ray2.01X1-327[»]
2Q7DX-ray1.60A/B1-335[»]
2QB5X-ray1.80A/B1-335[»]
ProteinModelPortaliQ13572.
SMRiQ13572. Positions 6-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13572.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 325209ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ITPK1 family.Curated
Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG85132.
GeneTreeiENSGT00390000001278.
HOVERGENiHBG079462.
InParanoidiQ13572.
KOiK00913.
OMAiCSASPGC.
OrthoDBiEOG70GMG7.
PhylomeDBiQ13572.
TreeFamiTF329288.

Family and domain databases

InterProiIPR011761. ATP-grasp.
IPR008656. Inositol_tetrakis-P_1-kinase.
[Graphical view]
PfamiPF05770. Ins134_P3_kin. 1 hit.
[Graphical view]
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13572-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MQTFLKGKRV GYWLSEKKIK KLNFQAFAEL CRKRGMEVVQ LNLSRPIEEQ 
        60         70         80         90        100
GPLDVIIHKL TDVILEADQN DSQSLELVHR FQEYIDAHPE TIVLDPLPAI 
       110        120        130        140        150
RTLLDRSKSY ELIRKIEAYM EDDRICSPPF MELTSLCGDD TMRLLEKNGL 
       160        170        180        190        200
TFPFICKTRV AHGTNSHEMA IVFNQEGLNA IQPPCVVQNF INHNAVLYKV 
       210        220        230        240        250
FVVGESYTVV QRPSLKNFSA GTSDRESIFF NSHNVSKPES SSVLTELDKI 
       260        270        280        290        300
EGVFERPSDE VIRELSRALR QALGVSLFGI DIIINNQTGQ HAVIDINAFP 
       310        320        330        340        350
GYEGVSEFFT DLLNHIATVL QGQSTAMAAT GDVALLRHSK LLAEPAGGLV 
       360        370        380        390        400
GERTCSASPG CCGSMMGQDA PWKAEADAGG TAKLPHQRLG CNAGVSPSFQ 
       410 
QHCVASLATK ASSQ
Length:414
Mass (Da):45,621
Last modified:December 6, 2005 - v2
Checksum:iE89E2EE11971278E
GO
Isoform 2 (identifier: Q13572-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     302-314: YEGVSEFFTDLLN → DCQVCFIEGWKTD
     315-414: Missing.

Note: No experimental confirmation available.

Show »
Length:314
Mass (Da):35,632
Checksum:iDD10427FADBBB3E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561S → N in AAC50483. (PubMed:8662638)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei302 – 31413YEGVS…TDLLN → DCQVCFIEGWKTD in isoform 2. 1 PublicationVSP_016478Add
BLAST
Alternative sequencei315 – 414100Missing in isoform 2. 1 PublicationVSP_016479Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51336 mRNA. Translation: AAC50483.1.
AF279372 mRNA. Translation: AAG44835.1.
BC003622 mRNA. Translation: AAH03622.1.
BC007428 mRNA. Translation: AAH07428.1.
BC018192 mRNA. Translation: AAH18192.1.
CCDSiCCDS45157.1. [Q13572-2]
CCDS9907.1. [Q13572-1]
RefSeqiNP_001136065.1. NM_001142593.1. [Q13572-1]
NP_001136066.1. NM_001142594.1. [Q13572-2]
NP_055031.2. NM_014216.4. [Q13572-1]
UniGeneiHs.308122.

Genome annotation databases

EnsembliENST00000267615; ENSP00000267615; ENSG00000100605. [Q13572-1]
ENST00000354313; ENSP00000346272; ENSG00000100605. [Q13572-2]
ENST00000556603; ENSP00000451091; ENSG00000100605. [Q13572-1]
ENST00000614271; ENSP00000483767; ENSG00000274958. [Q13572-1]
ENST00000617836; ENSP00000480918; ENSG00000274958. [Q13572-2]
GeneIDi3705.
KEGGihsa:3705.
UCSCiuc001ybe.2. human. [Q13572-2]
uc001ybf.3. human. [Q13572-1]

Polymorphism databases

DMDMi83288249.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51336 mRNA. Translation: AAC50483.1.
AF279372 mRNA. Translation: AAG44835.1.
BC003622 mRNA. Translation: AAH03622.1.
BC007428 mRNA. Translation: AAH07428.1.
BC018192 mRNA. Translation: AAH18192.1.
CCDSiCCDS45157.1. [Q13572-2]
CCDS9907.1. [Q13572-1]
RefSeqiNP_001136065.1. NM_001142593.1. [Q13572-1]
NP_001136066.1. NM_001142594.1. [Q13572-2]
NP_055031.2. NM_014216.4. [Q13572-1]
UniGeneiHs.308122.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ODTX-ray2.01X1-327[»]
2Q7DX-ray1.60A/B1-335[»]
2QB5X-ray1.80A/B1-335[»]
ProteinModelPortaliQ13572.
SMRiQ13572. Positions 6-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109910. 10 interactions.
DIPiDIP-60016N.
IntActiQ13572. 2 interactions.
MINTiMINT-1463374.
STRINGi9606.ENSP00000267615.

Chemistry

ChEMBLiCHEMBL1938220.

PTM databases

PhosphoSiteiQ13572.

Polymorphism databases

DMDMi83288249.

Proteomic databases

MaxQBiQ13572.
PaxDbiQ13572.
PRIDEiQ13572.

Protocols and materials databases

DNASUi3705.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267615; ENSP00000267615; ENSG00000100605. [Q13572-1]
ENST00000354313; ENSP00000346272; ENSG00000100605. [Q13572-2]
ENST00000556603; ENSP00000451091; ENSG00000100605. [Q13572-1]
ENST00000614271; ENSP00000483767; ENSG00000274958. [Q13572-1]
ENST00000617836; ENSP00000480918; ENSG00000274958. [Q13572-2]
GeneIDi3705.
KEGGihsa:3705.
UCSCiuc001ybe.2. human. [Q13572-2]
uc001ybf.3. human. [Q13572-1]

Organism-specific databases

CTDi3705.
GeneCardsiGC14M093403.
H-InvDBHIX0037938.
HGNCiHGNC:6177. ITPK1.
HPAiHPA055230.
MIMi601838. gene.
neXtProtiNX_Q13572.
PharmGKBiPA29974.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG85132.
GeneTreeiENSGT00390000001278.
HOVERGENiHBG079462.
InParanoidiQ13572.
KOiK00913.
OMAiCSASPGC.
OrthoDBiEOG70GMG7.
PhylomeDBiQ13572.
TreeFamiTF329288.

Enzyme and pathway databases

BioCyciMetaCyc:HS02123-MONOMER.
BRENDAi2.7.1.134. 2681.
ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
SABIO-RKQ13572.

Miscellaneous databases

ChiTaRSiITPK1. human.
EvolutionaryTraceiQ13572.
GeneWikiiITPK1.
GenomeRNAii3705.
NextBioi14521.
PROiQ13572.
SOURCEiSearch...

Gene expression databases

BgeeiQ13572.
ExpressionAtlasiQ13572. baseline and differential.
GenevestigatoriQ13572.

Family and domain databases

InterProiIPR011761. ATP-grasp.
IPR008656. Inositol_tetrakis-P_1-kinase.
[Graphical view]
PfamiPF05770. Ins134_P3_kin. 1 hit.
[Graphical view]
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning and expression of the recombinant enzyme."
    Wilson M.P., Majerus P.W.
    J. Biol. Chem. 271:11904-11910(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, COFACTOR, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Multitasking in signal transduction by a promiscuous human Ins(3,4,5,6)P(4) 1-kinase/Ins(1,3,4)P(3) 5/6-kinase."
    Yang X., Shears S.B.
    Biochem. J. 351:551-555(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  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] (ISOFORMS 1 AND 2).
    Tissue: Eye and Muscle.
  4. "Inositol 1,3,4-trisphosphate 5/6-kinase is a protein kinase that phosphorylates the transcription factors c-Jun and ATF-2."
    Wilson M.P., Sun Y., Cao L., Majerus P.W.
    J. Biol. Chem. 276:40998-41004(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUTATIVE FUNCTION AS PROTEIN KINASE.
  5. "Regulation of Ins(3,4,5,6)P(4) signaling by a reversible kinase/phosphatase."
    Ho M.W.Y., Yang X., Carew M.A., Zhang T., Hua L., Kwon Y.-U., Chung S.-K., Adelt S., Vogel G., Riley A.M., Potter B.V.L., Shears S.B.
    Curr. Biol. 12:477-482(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1."
    Sun Y., Wilson M.P., Majerus P.W.
    J. Biol. Chem. 277:45759-45764(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPS1.
  7. "Inositol 1,3,4-trisphosphate 5/6-kinase inhibits tumor necrosis factor-induced apoptosis."
    Sun Y., Mochizuki Y., Majerus P.W.
    J. Biol. Chem. 278:43645-43653(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The Ins(1,3,4)P3 5/6-kinase/Ins(3,4,5,6)P4 1-kinase is not a protein kinase."
    Qian X., Mitchell J., Wei S.J., Williams J., Petrovich R.M., Shears S.B.
    Biochem. J. 389:389-395(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-106; LYS-157; GLY-163; ASP-281; ASP-295 AND ASN-297.
  9. "Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase."
    Miller G.J., Wilson M.P., Majerus P.W., Hurley J.H.
    Mol. Cell 18:201-212(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-18; HIS-58; LYS-59; ARG-106; HIS-162; GLY-163; HIS-167; GLN-188; HIS-193; LYS-199; ARG-212; SER-214; LEU-215; ASN-297 AND GLY-301.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Regulation of inositol 1,3,4-trisphosphate 5/6-kinase (ITPK1) by reversible lysine acetylation."
    Zhang C., Majerus P.W., Wilson M.P.
    Proc. Natl. Acad. Sci. U.S.A. 109:2290-2295(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-340; LYS-383 AND LYS-410.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-335 IN COMPLEXES WITH MANGANESE; ATP ANALOG AND ADP, FUNCTION, SUBUNIT.
  14. "Structure of human inositol 1,3,4-trisphosphate 5/6-kinase."
    Structural genomics consortium (SGC)
    Submitted (FEB-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-327.
+Additional computationally mapped references.

Entry informationi

Entry nameiITPK1_HUMAN
AccessioniPrimary (citable) accession number: Q13572
Secondary accession number(s): Q9BTL6, Q9H2E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: January 7, 2015
This is version 123 of the entry and version 2 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 14
    Human chromosome 14: 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.