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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: 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.4 Publications

Catalytic activityi

ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate.2 Publications
ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.2 Publications
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)P4

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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 1811D-myo-inositol 1,3,4-trisphosphate By similarity
Binding sitei106 – 1061ATP
Binding sitei157 – 1571ATP
Binding sitei167 – 16711D-myo-inositol 1,3,4-trisphosphate By similarity
Binding sitei199 – 19911D-myo-inositol 1,3,4-trisphosphate By 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-trisphosphate By similarity

Regions

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

GO - Molecular functioni

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

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-RKiQ13572.

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
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-kinase
PRO_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. 6 interactions.
DIPiDIP-60016N.
IntActiQ13572. 2 interactions.
MINTiMINT-1463374.
STRINGi9606.ENSP00000267615.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ13572.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 325209ATP-grasp
Add
BLAST

Sequence similaritiesi

Belongs to the ITPK1 family.
Contains 1 ATP-grasp domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei302 – 31413YEGVS…TDLLN → DCQVCFIEGWKTD in isoform 2.
VSP_016478Add
BLAST
Alternative sequencei315 – 414100Missing in isoform 2.
VSP_016479Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561S → N in AAC50483. 1 Publication

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...

Protein-protein interaction databases

BioGridi 109910. 6 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-InvDBi 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-RKi 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

« 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.

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: September 3, 2014
This is version 119 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

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