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Q13572

- ITPK1_HUMAN

UniProt

Q13572 - ITPK1_HUMAN

Protein

Inositol-tetrakisphosphate 1-kinase

Gene

ITPK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
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    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

    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

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:6177. ITPK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    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

    ArrayExpressiQ13572.
    BgeeiQ13572.
    GenevestigatoriQ13572.

    Organism-specific databases

    HPAiHPA055230.

    Interactioni

    Subunit structurei

    Monomer. Interacts with GPS1/COPS1.2 Publications

    Protein-protein interaction databases

    BioGridi109910. 7 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 – 55
    Beta strandi9 – 135
    Helixi16 – 227
    Helixi24 – 329
    Turni33 – 353
    Beta strandi37 – 404
    Helixi48 – 503
    Beta strandi54 – 585
    Helixi61 – 688
    Helixi72 – 8716
    Beta strandi91 – 955
    Helixi97 – 1026
    Helixi106 – 12015
    Beta strandi130 – 1334
    Helixi138 – 1403
    Helixi141 – 1477
    Beta strandi152 – 1576
    Turni164 – 1674
    Beta strandi168 – 1725
    Helixi175 – 1773
    Beta strandi185 – 1895
    Beta strandi196 – 2038
    Beta strandi206 – 2138
    Beta strandi228 – 2314
    Helixi232 – 2343
    Helixi243 – 2453
    Helixi259 – 27315
    Beta strandi277 – 2848
    Turni286 – 2883
    Beta strandi291 – 2999
    Helixi308 – 32417

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG079462.
    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

    MQTFLKGKRV GYWLSEKKIK KLNFQAFAEL CRKRGMEVVQ LNLSRPIEEQ    50
    GPLDVIIHKL TDVILEADQN DSQSLELVHR FQEYIDAHPE TIVLDPLPAI 100
    RTLLDRSKSY ELIRKIEAYM EDDRICSPPF MELTSLCGDD TMRLLEKNGL 150
    TFPFICKTRV AHGTNSHEMA IVFNQEGLNA IQPPCVVQNF INHNAVLYKV 200
    FVVGESYTVV QRPSLKNFSA GTSDRESIFF NSHNVSKPES SSVLTELDKI 250
    EGVFERPSDE VIRELSRALR QALGVSLFGI DIIINNQTGQ HAVIDINAFP 300
    GYEGVSEFFT DLLNHIATVL QGQSTAMAAT GDVALLRHSK LLAEPAGGLV 350
    GERTCSASPG CCGSMMGQDA PWKAEADAGG TAKLPHQRLG CNAGVSPSFQ 400
    QHCVASLATK ASSQ 414
    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:
    EMBL
    GenBank
    DDBJ
    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]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS45157.1. [Q13572-2 ]
    CCDS9907.1. [Q13572-1 ]
    RefSeqi NP_001136065.1. NM_001142593.1. [Q13572-1 ]
    NP_001136066.1. NM_001142594.1. [Q13572-2 ]
    NP_055031.2. NM_014216.4. [Q13572-1 ]
    UniGenei Hs.308122.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ODT X-ray 2.01 X 1-327 [» ]
    2Q7D X-ray 1.60 A/B 1-335 [» ]
    2QB5 X-ray 1.80 A/B 1-335 [» ]
    ProteinModelPortali Q13572.
    SMRi Q13572. Positions 6-322.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109910. 7 interactions.
    DIPi DIP-60016N.
    IntActi Q13572. 2 interactions.
    MINTi MINT-1463374.
    STRINGi 9606.ENSP00000267615.

    Chemistry

    ChEMBLi CHEMBL1938220.

    PTM databases

    PhosphoSitei Q13572.

    Polymorphism databases

    DMDMi 83288249.

    Proteomic databases

    MaxQBi Q13572.
    PaxDbi Q13572.
    PRIDEi Q13572.

    Protocols and materials databases

    DNASUi 3705.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267615 ; ENSP00000267615 ; ENSG00000100605 . [Q13572-1 ]
    ENST00000354313 ; ENSP00000346272 ; ENSG00000100605 . [Q13572-2 ]
    ENST00000556603 ; ENSP00000451091 ; ENSG00000100605 . [Q13572-1 ]
    GeneIDi 3705.
    KEGGi hsa:3705.
    UCSCi uc001ybe.2. human. [Q13572-2 ]
    uc001ybf.3. human. [Q13572-1 ]

    Organism-specific databases

    CTDi 3705.
    GeneCardsi GC14M093403.
    H-InvDB HIX0037938.
    HGNCi HGNC:6177. ITPK1.
    HPAi HPA055230.
    MIMi 601838. gene.
    neXtProti NX_Q13572.
    PharmGKBi PA29974.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG85132.
    HOVERGENi HBG079462.
    KOi K00913.
    OMAi CSASPGC.
    OrthoDBi EOG70GMG7.
    PhylomeDBi Q13572.
    TreeFami TF329288.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02123-MONOMER.
    BRENDAi 2.7.1.134. 2681.
    Reactomei REACT_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-RK Q13572.

    Miscellaneous databases

    ChiTaRSi ITPK1. human.
    EvolutionaryTracei Q13572.
    GeneWikii ITPK1.
    GenomeRNAii 3705.
    NextBioi 14521.
    PROi Q13572.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13572.
    Bgeei Q13572.
    Genevestigatori Q13572.

    Family and domain databases

    InterProi IPR011761. ATP-grasp.
    IPR008656. Inositol_tetrakis-P_1-kinase.
    [Graphical view ]
    Pfami PF05770. Ins134_P3_kin. 1 hit.
    [Graphical view ]
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 120 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