Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphatidylinositol 4-kinase type 2-alpha

Gene

PI4K2A

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

Functioni

Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).Curated6 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei152 – 1521ATP2 Publications
Binding sitei346 – 3461ATP2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 1377ATP2 Publications
Nucleotide bindingi261 – 2644ATP2 Publications

GO - Molecular functioni

  • 1-phosphatidylinositol 4-kinase activity Source: UniProtKB
  • AP-3 adaptor complex binding Source: UniProtKB
  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB

GO - Biological processi

  • basophil degranulation Source: Ensembl
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • phosphatidylinositol biosynthetic process Source: UniProtKB
  • phosphatidylinositol phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00573-MONOMER.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-1660514. Synthesis of PIPs at the Golgi membrane.
R-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
SIGNORiQ9BTU6.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-kinase type 2-alpha (EC:2.7.1.674 Publications)
Alternative name(s):
Phosphatidylinositol 4-kinase type II-alpha
Gene namesi
Name:PI4K2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:30031. PI4K2A.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: Reactome
  • dendrite Source: UniProtKB
  • early endosome membrane Source: Ensembl
  • endosome Source: UniProtKB
  • Golgi apparatus Source: UniProtKB-SubCell
  • growing cell tip Source: UniProtKB
  • host cell presynaptic membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • intrinsic component of membrane Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • membrane raft Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • neuronal cell body Source: UniProtKB
  • neuron projection Source: UniProtKB
  • perikaryon Source: Ensembl
  • presynaptic membrane Source: UniProtKB
  • protein complex Source: Ensembl
  • synaptic vesicle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane, Mitochondrion, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi129 – 1291R → E: Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-275 and E-276. 1 Publication
Mutagenesisi152 – 1521K → A: Abolishes enzyme activity. 2 Publications
Mutagenesisi157 – 1593EPY → APA: Abolishes enzyme activity. 1 Publication
Mutagenesisi163 – 1631N → A: Reduces enzyme activity. 1 Publication
Mutagenesisi165 – 1728KWTKWLQK → AAAAAAAA: Abolishes enzyme activity. 1 Publication
Mutagenesisi165 – 1651K → A: Abolishes enzyme activity; when associated with A-168 and A-172. 1 Publication
Mutagenesisi166 – 1661W → A: Reduces enzyme activity. 1 Publication
Mutagenesisi168 – 1681K → A: Abolishes enzyme activity; when associated with A-165 and A-172. 1 Publication
Mutagenesisi172 – 1721K → A: Abolishes enzyme activity; when associated with A-165 and A-168. 1 Publication
Mutagenesisi174 – 1785CCPCC → FFPFF: No effect on membrane-association. 1 Publication
Mutagenesisi174 – 1785CCPCC → SSPSS: Abolishes palmitoylation and impairs membrane-association. 2 Publications
Mutagenesisi184 – 1841L → A: Abolishes enzyme activity; when associated with A-349. 1 Publication
Mutagenesisi263 – 2631F → A: Abolishes enzyme activity; when associated with A-345. 1 Publication
Mutagenesisi269 – 2691D → A: Reduces enzyme activity by half. 1 Publication
Mutagenesisi275 – 2751R → A: Reduces enzyme activity. 1 Publication
Mutagenesisi275 – 2751R → E: Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-129 and E-276. 1 Publication
Mutagenesisi276 – 2761R → E: Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-129 and E-275. 1 Publication
Mutagenesisi308 – 3081D → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi345 – 3451I → A: Abolishes enzyme activity; when associated with A-263. 1 Publication
Mutagenesisi349 – 3491L → A: Abolishes enzyme activity; when associated with A-184. 1 Publication
Mutagenesisi359 – 3591W → A: Strongly reduced enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-365 and A-368. 1 Publication
Mutagenesisi365 – 3651Y → A: Reduces enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-368 and A-359. 1 Publication
Mutagenesisi368 – 3681W → A: Reduces enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-359 and A-365. 1 Publication
Mutagenesisi445 – 4451Q → A: Reduces enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA162399304.

Chemistry

ChEMBLiCHEMBL2096619.
GuidetoPHARMACOLOGYi2498.

Polymorphism and mutation databases

BioMutaiPI4K2A.
DMDMi74752344.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Phosphatidylinositol 4-kinase type 2-alphaPRO_0000285158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei9 – 91PhosphoserineCombined sources
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei47 – 471PhosphoserineCombined sources
Modified residuei51 – 511PhosphoserineCombined sources
Lipidationi174 – 1741S-palmitoyl cysteine2 Publications
Lipidationi175 – 1751S-palmitoyl cysteine2 Publications
Lipidationi177 – 1771S-palmitoyl cysteine2 Publications
Lipidationi178 – 1781S-palmitoyl cysteine2 Publications
Modified residuei462 – 4621PhosphoserineBy similarity

Post-translational modificationi

Palmitoylated by ZDHHC3 and ZDHHC7 in the CCPCC motif. Palmitoylation is cholesterol-dependent, and required for TGN localization.1 Publication
Ubiquitinated by ITCH; this does not lead to proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9BTU6.
MaxQBiQ9BTU6.
PaxDbiQ9BTU6.
PRIDEiQ9BTU6.

PTM databases

iPTMnetiQ9BTU6.
PhosphoSiteiQ9BTU6.
SwissPalmiQ9BTU6.

Expressioni

Tissue specificityi

Widely expressed. Highest expression is observed in kidney, brain, heart, skeletal muscle, and placenta and lowest expression is observed in colon, thymus, and small intestine.1 Publication

Gene expression databases

BgeeiQ9BTU6.
CleanExiHS_PI4K2A.
GenevisibleiQ9BTU6. HS.

Organism-specific databases

HPAiCAB030649.

Interactioni

Subunit structurei

Associates with the BLOC-1 and the AP-3 complexes; the BLOC-1 complex is required for optimal binding of PI4K2A to the AP-3 complex. Interacts with BLOC1S5 and DTNBP1 (PubMed:21998198). Interacts with FOS; this interaction may enhance phosphatidylinositol phosphorylation activity (By similarity). Interacts with ITCH (PubMed:23146885).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ITCHQ96J025EBI-3239392,EBI-1564678

GO - Molecular functioni

  • AP-3 adaptor complex binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120639. 22 interactions.
IntActiQ9BTU6. 6 interactions.
STRINGi9606.ENSP00000359665.

Chemistry

BindingDBiQ9BTU6.

Structurei

Secondary structure

1
479
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi78 – 9316Combined sources
Helixi95 – 995Combined sources
Helixi108 – 12215Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi147 – 1537Combined sources
Helixi154 – 1563Combined sources
Helixi167 – 1715Combined sources
Helixi189 – 20315Combined sources
Beta strandi211 – 2166Combined sources
Helixi225 – 2317Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi266 – 2694Combined sources
Helixi270 – 27910Combined sources
Helixi284 – 30421Combined sources
Beta strandi313 – 3186Combined sources
Beta strandi339 – 3446Combined sources
Turni359 – 3613Combined sources
Helixi365 – 3684Combined sources
Helixi370 – 3734Combined sources
Helixi378 – 38811Combined sources
Helixi391 – 40515Combined sources
Helixi413 – 43523Combined sources
Helixi440 – 4445Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HNDX-ray3.20A/B78-453[»]
4HNEX-ray2.95A/B78-453[»]
4PLAX-ray2.77A76-172[»]
A180-468[»]
4YC4X-ray2.58A76-172[»]
A180-468[»]
5EUTX-ray2.80A76-172[»]
A179-468[»]
5I0NX-ray2.28A180-468[»]
ProteinModelPortaliQ9BTU6.
SMRiQ9BTU6. Positions 98-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 438306PI3K/PI4KAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni157 – 1593Important for substrate binding1 Publication
Regioni165 – 17814Important for interaction with membranes2 PublicationsAdd
BLAST
Regioni268 – 2769Important for interaction with membranes1 Publication
Regioni359 – 36810Important for interaction with membranes1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 424Poly-Ala
Compositional biasi65 – 9733Ala-richAdd
BLAST

Sequence similaritiesi

Contains 1 PI3K/PI4K domain.Curated

Phylogenomic databases

eggNOGiKOG2381. Eukaryota.
ENOG410XP06. LUCA.
GeneTreeiENSGT00390000010434.
HOGENOMiHOG000294076.
HOVERGENiHBG059542.
InParanoidiQ9BTU6.
KOiK13711.
OMAiMIQRPLV.
OrthoDBiEOG7MKW5Z.
PhylomeDBiQ9BTU6.
TreeFamiTF314740.

Family and domain databases

InterProiIPR000403. PI3/4_kinase_cat_dom.
[Graphical view]
PfamiPF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BTU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDETSPLVSP ERAQPPDYTF PSGSGAHFPQ VPGGAVRVAA AAGSGPSPPG
60 70 80 90 100
SPGHDRERQP LLDRARGAAA QGQTQTVAAQ AQALAAQAAA AAHAAQAHRE
110 120 130 140 150
RNEFPEDPEF EAVVRQAELA IERCIFPERI YQGSSGSYFV KDPQGRIIAV
160 170 180 190 200
FKPKNEEPYG HLNPKWTKWL QKLCCPCCFG RDCLVLNQGY LSEAGASLVD
210 220 230 240 250
QKLELNIVPR TKVVYLASET FNYSAIDRVK SRGKRLALEK VPKVGQRFNR
260 270 280 290 300
IGLPPKVGSF QLFVEGYKDA DYWLRRFEAE PLPENTNRQL LLQFERLVVL
310 320 330 340 350
DYIIRNTDRG NDNWLIKYDC PMDSSSSRDT DWVVVKEPVI KVAAIDNGLA
360 370 380 390 400
FPLKHPDSWR AYPFYWAWLP QAKVPFSQEI KDLILPKISD PNFVKDLEED
410 420 430 440 450
LYELFKKDPG FDRGQFHKQI AVMRGQILNL TQALKDNKSP LHLVQMPPVI
460 470
VETARSHQRS SSESYTQSFQ SRKPFFSWW
Length:479
Mass (Da):54,022
Last modified:June 1, 2001 - v1
Checksum:i9C9F4CE23F197BBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ303098 mRNA. Translation: CAC38065.1.
BT007330 mRNA. Translation: AAP35994.1.
AL355315 Genomic DNA. Translation: CAI15460.1.
CH471066 Genomic DNA. Translation: EAW49906.1.
CH471066 Genomic DNA. Translation: EAW49907.1.
BC003167 mRNA. Translation: AAH03167.1.
AL353952 mRNA. Translation: CAB89254.1.
CCDSiCCDS7469.1.
PIRiT48687.
RefSeqiNP_060895.1. NM_018425.3.
UniGeneiHs.25300.

Genome annotation databases

EnsembliENST00000370631; ENSP00000359665; ENSG00000155252.
GeneIDi55361.
KEGGihsa:55361.
UCSCiuc001kog.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ303098 mRNA. Translation: CAC38065.1.
BT007330 mRNA. Translation: AAP35994.1.
AL355315 Genomic DNA. Translation: CAI15460.1.
CH471066 Genomic DNA. Translation: EAW49906.1.
CH471066 Genomic DNA. Translation: EAW49907.1.
BC003167 mRNA. Translation: AAH03167.1.
AL353952 mRNA. Translation: CAB89254.1.
CCDSiCCDS7469.1.
PIRiT48687.
RefSeqiNP_060895.1. NM_018425.3.
UniGeneiHs.25300.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HNDX-ray3.20A/B78-453[»]
4HNEX-ray2.95A/B78-453[»]
4PLAX-ray2.77A76-172[»]
A180-468[»]
4YC4X-ray2.58A76-172[»]
A180-468[»]
5EUTX-ray2.80A76-172[»]
A179-468[»]
5I0NX-ray2.28A180-468[»]
ProteinModelPortaliQ9BTU6.
SMRiQ9BTU6. Positions 98-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120639. 22 interactions.
IntActiQ9BTU6. 6 interactions.
STRINGi9606.ENSP00000359665.

Chemistry

BindingDBiQ9BTU6.
ChEMBLiCHEMBL2096619.
GuidetoPHARMACOLOGYi2498.

PTM databases

iPTMnetiQ9BTU6.
PhosphoSiteiQ9BTU6.
SwissPalmiQ9BTU6.

Polymorphism and mutation databases

BioMutaiPI4K2A.
DMDMi74752344.

Proteomic databases

EPDiQ9BTU6.
MaxQBiQ9BTU6.
PaxDbiQ9BTU6.
PRIDEiQ9BTU6.

Protocols and materials databases

DNASUi55361.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370631; ENSP00000359665; ENSG00000155252.
GeneIDi55361.
KEGGihsa:55361.
UCSCiuc001kog.2. human.

Organism-specific databases

CTDi55361.
GeneCardsiPI4K2A.
HGNCiHGNC:30031. PI4K2A.
HPAiCAB030649.
MIMi609763. gene.
neXtProtiNX_Q9BTU6.
PharmGKBiPA162399304.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2381. Eukaryota.
ENOG410XP06. LUCA.
GeneTreeiENSGT00390000010434.
HOGENOMiHOG000294076.
HOVERGENiHBG059542.
InParanoidiQ9BTU6.
KOiK13711.
OMAiMIQRPLV.
OrthoDBiEOG7MKW5Z.
PhylomeDBiQ9BTU6.
TreeFamiTF314740.

Enzyme and pathway databases

BioCyciMetaCyc:HS00573-MONOMER.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-1660514. Synthesis of PIPs at the Golgi membrane.
R-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
SIGNORiQ9BTU6.

Miscellaneous databases

ChiTaRSiPI4K2A. human.
GeneWikiiPI4K2A.
GenomeRNAii55361.
PROiQ9BTU6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BTU6.
CleanExiHS_PI4K2A.
GenevisibleiQ9BTU6. HS.

Family and domain databases

InterProiIPR000403. PI3/4_kinase_cat_dom.
[Graphical view]
PfamiPF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a human type II phosphatidylinositol 4-kinase reveals a novel lipid kinase family."
    Minogue S., Anderson J.S., Waugh M.G., dos Santos M., Corless S., Cramer R., Hsuan J.J.
    J. Biol. Chem. 276:16635-16640(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Skin.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 222-479.
    Tissue: Amygdala.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Phosphatidylinositol 4-kinase is required for endosomal trafficking and degradation of the EGF receptor."
    Minogue S., Waugh M.G., De Matteis M.A., Stephens D.J., Berditchevski F., Hsuan J.J.
    J. Cell Sci. 119:571-581(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Relationship between phosphatidylinositol 4-phosphate synthesis, membrane organization, and lateral diffusion of PI4KIIalpha at the trans-Golgi network."
    Minogue S., Chu K.M., Westover E.J., Covey D.F., Hsuan J.J., Waugh M.G.
    J. Lipid Res. 51:2314-2324(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse."
    Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.
    Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLOC1S5 AND DTNBP1.
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Phosphatidylinositol 4-kinase IIalpha function at endosomes is regulated by the ubiquitin ligase Itch."
    Mossinger J., Wieffer M., Krause E., Freund C., Gerth F., Krauss M., Haucke V.
    EMBO Rep. 13:1087-1094(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ITCH, UBIQUITINATION, FUNCTION.
  17. "Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner."
    Lu D., Sun H.Q., Wang H., Barylko B., Fukata Y., Fukata M., Albanesi J.P., Yin H.L.
    J. Biol. Chem. 287:21856-21865(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-174; CYS-175; CYS-177 AND CYS-178, MUTAGENESIS OF 174-CYS--CYS-178.
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-44; SER-47 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 76-172 AND 180-468 IN COMPLEX WITH ATP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-152; ASN-163; 165-LYS--LYS-172; ARG-275; ASP-308 AND GLN-445.
  22. "Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIalpha."
    Zhou Q., Li J., Yu H., Zhai Y., Gao Z., Liu Y., Pang X., Zhang L., Schulten K., Sun F., Chen C.
    Nat. Commun. 5:3552-3552(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 78-453 IN COMPLEX WITH ADP, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-129; LYS-152; 157-GLU--TYR-159; LYS-165; TRP-166; LYS-168; LYS-172; 174-CYS--CYS-178; LEU-184; PHE-263; ASP-269; ARG-275; ARG-276; ILE-345; LEU-349; TRP-359; TYR-365 AND TRP-368.

Entry informationi

Entry nameiP4K2A_HUMAN
AccessioniPrimary (citable) accession number: Q9BTU6
Secondary accession number(s): D3DR59, Q9NSG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 126 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 10
    Human chromosome 10: 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

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.