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Q9UBF8

- PI4KB_HUMAN

UniProt

Q9UBF8 - PI4KB_HUMAN

Protein

Phosphatidylinositol 4-kinase beta

Gene

PI4KB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by wortmannin. Increased kinase activity upon interaction with NCS1/FREQ By similarity.By similarity

    GO - Molecular functioni

    1. 1-phosphatidylinositol 4-kinase activity Source: Reactome
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. phosphatidylinositol biosynthetic process Source: Reactome
    2. phosphatidylinositol-mediated signaling Source: InterPro
    3. phospholipid metabolic process Source: Reactome
    4. receptor-mediated endocytosis Source: ProtInc
    5. signal transduction Source: ProtInc
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07046-MONOMER.
    ReactomeiREACT_120836. Synthesis of PIPs at the Golgi membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 4-kinase beta (EC:2.7.1.67)
    Short name:
    PI4K-beta
    Short name:
    PI4Kbeta
    Short name:
    PtdIns 4-kinase beta
    Alternative name(s):
    NPIK
    PI4K92
    Gene namesi
    Name:PI4KB
    Synonyms:PIK4CB
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8984. PI4KB.

    Subcellular locationi

    Endomembrane system. Mitochondrion outer membrane; Peripheral membrane protein. Rough endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus. Cytoplasmperinuclear region
    Note: Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. endosome Source: ProtInc
    4. Golgi membrane Source: Reactome
    5. mitochondrial outer membrane Source: UniProtKB-SubCell
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. plasma membrane Source: Ensembl
    8. rough endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162399420.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 816816Phosphatidylinositol 4-kinase betaPRO_0000088829Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei258 – 2581Phosphoserine3 Publications
    Modified residuei263 – 2631Phosphothreonine1 Publication
    Modified residuei266 – 2661Phosphoserine2 Publications
    Modified residuei277 – 2771Phosphoserine2 Publications
    Modified residuei294 – 2941Phosphoserine1 Publication
    Modified residuei428 – 4281Phosphoserine5 Publications
    Modified residuei438 – 4381Phosphothreonine1 Publication
    Modified residuei511 – 5111Phosphoserine3 Publications
    Modified residuei519 – 5191Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UBF8.
    PaxDbiQ9UBF8.
    PRIDEiQ9UBF8.

    PTM databases

    PhosphoSiteiQ9UBF8.

    Miscellaneous databases

    PMAP-CutDBQ9UBF8.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in heart, skeletal muscle, pancreas, testis and ovary. Weakly expressed in liver.3 Publications

    Gene expression databases

    ArrayExpressiQ9UBF8.
    BgeeiQ9UBF8.
    CleanExiHS_PI4KB.
    GenevestigatoriQ9UBF8.

    Organism-specific databases

    HPAiCAB022071.
    HPA006280.
    HPA006281.

    Interactioni

    Subunit structurei

    Interacts with ARF1 and ARF3 in the Golgi complex, but not with ARF4, ARF5 or ARF6. Interacts with NCS1/FREQ in a calcium-independent manner By similarity. Interacts with CALN1/CABP8 and CALN2/CABP7; in a calcium-dependent manner By similarity. This binding competes with NCS1/FREQ binding By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACBD3Q9H3P74EBI-1053214,EBI-1791792
    NSP034952EBI-1053214,EBI-2548993From a different organism.

    Protein-protein interaction databases

    BioGridi111316. 7 interactions.
    IntActiQ9UBF8. 8 interactions.
    MINTiMINT-1681077.
    STRINGi9606.ENSP00000271657.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4D0LX-ray2.94A/C/E121-799[»]
    4D0MX-ray6.00A/C/G/I/M/O/Q/S/W/Y/c/g121-799[»]
    ProteinModelPortaliQ9UBF8.
    SMRiQ9UBF8. Positions 523-798.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 242214PIK helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini558 – 765208PI3K/PI4KCuratedPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
    Contains 1 PIK helical domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5032.
    HOVERGENiHBG053597.
    InParanoidiQ9UBF8.
    KOiK00888.
    OrthoDBiEOG773XFQ.
    PhylomeDBiQ9UBF8.
    TreeFamiTF102042.

    Family and domain databases

    Gene3Di1.10.1070.11. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR027003. Phosphatidylino_kinase.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR015433. PI_Kinase.
    IPR001263. PInositide-3_kin_accessory_dom.
    [Graphical view]
    PANTHERiPTHR10048. PTHR10048. 1 hit.
    PTHR10048:SF22. PTHR10048:SF22. 1 hit.
    PfamiPF00454. PI3_PI4_kinase. 1 hit.
    [Graphical view]
    SMARTiSM00146. PI3Kc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    PS51545. PIK_HELICAL. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9UBF8-1) [UniParc]FASTAAdd to Basket

    Also known as: NPIK-B1 Publication

    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

    MGDTVVEPAP LKPTSEPTSG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK    50
    ACQEVLEKVK LLHGGVAVSS RGTPLELVNG DGVDSEIRCL DDPPAQIREE 100
    EDEMGAAVAS GTAKGARRRR QNNSAKQSWL LRLFESKLFD ISMAISYLYN 150
    SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL NMYIHMDEDV GDAIKPYIVH 200
    RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI LSDELKPAHR 250
    KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN 300
    EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ 350
    RLISELSLLN HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY 400
    VEVLECENFD TTSVPARIPE NRIRSTRSVE NLPECGITHE QRAGSFSTVP 450
    NYDNDDEAWS VDDIGELQVE LPEVHTNSCD NISQFSVDSI TSQESKEPVF 500
    IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK VRRIREGSPY 550
    GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI 600
    LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ 650
    RNFVQSCAGY CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN 700
    LGFETSAFKL TTEFVDVMGG LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI 750
    VEIMQQGSQL PCFHGSSTIR NLKERFHMSM TEEQLQLLVE QMVDGSMRSI 800
    TTKLYDGFQY LTNGIM 816
    Length:816
    Mass (Da):91,379
    Last modified:May 1, 2000 - v1
    Checksum:iCAD8791729BB4308
    GO
    Isoform 21 Publication (identifier: Q9UBF8-2) [UniParc]FASTAAdd to Basket

    Also known as: NPIK-C1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         304-318: Missing.

    Note: Contains a phosphoserine at position 294.

    Show »
    Length:801
    Mass (Da):89,807
    Checksum:i22E1ABA37AA9A2BD
    GO
    Isoform 3 (identifier: Q9UBF8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-332: Missing.

    Show »
    Length:484
    Mass (Da):54,976
    Checksum:i395A9DF64FC58A8C
    GO

    Sequence cautioni

    The sequence BAA21661.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAH70326.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW53450.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti216 – 2161L → V in AAC51156. (PubMed:9020160)Curated
    Sequence conflicti339 – 3391L → V in AAC51156. (PubMed:9020160)Curated
    Sequence conflicti340 – 3401A → V in AAC51156. (PubMed:9020160)Curated
    Sequence conflicti370 – 3701P → S in AAC51156. (PubMed:9020160)Curated
    Sequence conflicti446 – 4461F → S in BAG57793. (PubMed:14702039)Curated
    Sequence conflicti754 – 7541M → L in BAG57793. (PubMed:14702039)Curated
    Sequence conflicti796 – 7961S → G in BAG57793. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 332332Missing in isoform 3. 1 PublicationVSP_037133Add
    BLAST
    Alternative sequencei304 – 31815Missing in isoform 2. 3 PublicationsVSP_050627Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011121 mRNA. Translation: CAA09495.1.
    AJ011122 mRNA. No translation available.
    AJ011123 mRNA. Translation: CAA09496.1.
    AB005910 mRNA. Translation: BAA21661.1. Different initiation.
    U81802 mRNA. Translation: AAC51156.1.
    AK294606 mRNA. Translation: BAG57793.1.
    AL391069 Genomic DNA. Translation: CAH70324.1.
    AL391069 Genomic DNA. Translation: CAH70325.1.
    AL391069 Genomic DNA. Translation: CAH70326.1. Sequence problems.
    CH471121 Genomic DNA. Translation: EAW53449.1.
    CH471121 Genomic DNA. Translation: EAW53450.1. Sequence problems.
    BC000029 mRNA. Translation: AAH00029.1.
    BC040300 mRNA. Translation: AAH40300.1.
    CCDSiCCDS55637.1. [Q9UBF8-3]
    CCDS55638.1. [Q9UBF8-2]
    PIRiJC5706.
    RefSeqiNP_001185702.1. NM_001198773.1. [Q9UBF8-2]
    NP_001185703.1. NM_001198774.1. [Q9UBF8-2]
    NP_001185704.1. NM_001198775.1. [Q9UBF8-3]
    NP_002642.1. NM_002651.2.
    XP_005245318.1. XM_005245261.2. [Q9UBF8-1]
    XP_005245319.1. XM_005245262.2. [Q9UBF8-1]
    XP_005245320.1. XM_005245263.2. [Q9UBF8-1]
    UniGeneiHs.632465.

    Genome annotation databases

    EnsembliENST00000368872; ENSP00000357866; ENSG00000143393. [Q9UBF8-2]
    ENST00000368873; ENSP00000357867; ENSG00000143393. [Q9UBF8-1]
    ENST00000368874; ENSP00000357868; ENSG00000143393. [Q9UBF8-2]
    ENST00000368875; ENSP00000357869; ENSG00000143393.
    ENST00000529142; ENSP00000433149; ENSG00000143393. [Q9UBF8-3]
    GeneIDi5298.
    KEGGihsa:5298.
    UCSCiuc001exr.3. human. [Q9UBF8-1]
    uc001exs.3. human. [Q9UBF8-2]

    Polymorphism databases

    DMDMi38372507.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ011121 mRNA. Translation: CAA09495.1 .
    AJ011122 mRNA. No translation available.
    AJ011123 mRNA. Translation: CAA09496.1 .
    AB005910 mRNA. Translation: BAA21661.1 . Different initiation.
    U81802 mRNA. Translation: AAC51156.1 .
    AK294606 mRNA. Translation: BAG57793.1 .
    AL391069 Genomic DNA. Translation: CAH70324.1 .
    AL391069 Genomic DNA. Translation: CAH70325.1 .
    AL391069 Genomic DNA. Translation: CAH70326.1 . Sequence problems.
    CH471121 Genomic DNA. Translation: EAW53449.1 .
    CH471121 Genomic DNA. Translation: EAW53450.1 . Sequence problems.
    BC000029 mRNA. Translation: AAH00029.1 .
    BC040300 mRNA. Translation: AAH40300.1 .
    CCDSi CCDS55637.1. [Q9UBF8-3 ]
    CCDS55638.1. [Q9UBF8-2 ]
    PIRi JC5706.
    RefSeqi NP_001185702.1. NM_001198773.1. [Q9UBF8-2 ]
    NP_001185703.1. NM_001198774.1. [Q9UBF8-2 ]
    NP_001185704.1. NM_001198775.1. [Q9UBF8-3 ]
    NP_002642.1. NM_002651.2.
    XP_005245318.1. XM_005245261.2. [Q9UBF8-1 ]
    XP_005245319.1. XM_005245262.2. [Q9UBF8-1 ]
    XP_005245320.1. XM_005245263.2. [Q9UBF8-1 ]
    UniGenei Hs.632465.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4D0L X-ray 2.94 A/C/E 121-799 [» ]
    4D0M X-ray 6.00 A/C/G/I/M/O/Q/S/W/Y/c/g 121-799 [» ]
    ProteinModelPortali Q9UBF8.
    SMRi Q9UBF8. Positions 523-798.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111316. 7 interactions.
    IntActi Q9UBF8. 8 interactions.
    MINTi MINT-1681077.
    STRINGi 9606.ENSP00000271657.

    Chemistry

    BindingDBi Q9UBF8.
    ChEMBLi CHEMBL2096619.
    GuidetoPHARMACOLOGYi 2149.

    PTM databases

    PhosphoSitei Q9UBF8.

    Polymorphism databases

    DMDMi 38372507.

    Proteomic databases

    MaxQBi Q9UBF8.
    PaxDbi Q9UBF8.
    PRIDEi Q9UBF8.

    Protocols and materials databases

    DNASUi 5298.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368872 ; ENSP00000357866 ; ENSG00000143393 . [Q9UBF8-2 ]
    ENST00000368873 ; ENSP00000357867 ; ENSG00000143393 . [Q9UBF8-1 ]
    ENST00000368874 ; ENSP00000357868 ; ENSG00000143393 . [Q9UBF8-2 ]
    ENST00000368875 ; ENSP00000357869 ; ENSG00000143393 .
    ENST00000529142 ; ENSP00000433149 ; ENSG00000143393 . [Q9UBF8-3 ]
    GeneIDi 5298.
    KEGGi hsa:5298.
    UCSCi uc001exr.3. human. [Q9UBF8-1 ]
    uc001exs.3. human. [Q9UBF8-2 ]

    Organism-specific databases

    CTDi 5298.
    GeneCardsi GC01M151264.
    H-InvDB HIX0001056.
    HGNCi HGNC:8984. PI4KB.
    HPAi CAB022071.
    HPA006280.
    HPA006281.
    MIMi 602758. gene.
    neXtProti NX_Q9UBF8.
    PharmGKBi PA162399420.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5032.
    HOVERGENi HBG053597.
    InParanoidi Q9UBF8.
    KOi K00888.
    OrthoDBi EOG773XFQ.
    PhylomeDBi Q9UBF8.
    TreeFami TF102042.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07046-MONOMER.
    Reactomei REACT_120836. Synthesis of PIPs at the Golgi membrane.

    Miscellaneous databases

    ChiTaRSi PI4KB. human.
    GeneWikii PI4KB.
    GenomeRNAii 5298.
    NextBioi 20482.
    PMAP-CutDB Q9UBF8.
    PROi Q9UBF8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBF8.
    Bgeei Q9UBF8.
    CleanExi HS_PI4KB.
    Genevestigatori Q9UBF8.

    Family and domain databases

    Gene3Di 1.10.1070.11. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR027003. Phosphatidylino_kinase.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR015433. PI_Kinase.
    IPR001263. PInositide-3_kin_accessory_dom.
    [Graphical view ]
    PANTHERi PTHR10048. PTHR10048. 1 hit.
    PTHR10048:SF22. PTHR10048:SF22. 1 hit.
    Pfami PF00454. PI3_PI4_kinase. 1 hit.
    [Graphical view ]
    SMARTi SM00146. PI3Kc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    PS51545. PIK_HELICAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a novel human phosphatidylinositol 4-kinase."
      Suzuki K., Hirano H., Okutomi K., Suzuki M., Kuga Y., Fujiwara T., Kanemoto N., Isono K., Horie M.
      DNA Res. 4:273-280(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    2. "Complementary DNA cloning and chromosomal mapping of a novel phosphatidylinositol kinase gene."
      Saito T., Seki N., Ishii H., Ohira M., Hayashi A., Kozuma S., Hori T.-A.
      DNA Res. 4:301-305(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: BrainImported.
    3. "Cloning and characterization of a wortmannin-sensitive human phosphatidylinositol 4-kinase."
      Meyers R., Cantley L.C.
      J. Biol. Chem. 272:4384-4390(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ENZYME REGULATION, TISSUE SPECIFICITY.
      Tissue: Heart1 Publication.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 2).
      Tissue: BrainImported and TestisImported.
    8. "Subcellular locations of phosphatidylinositol 4-kinase isoforms."
      Wong K., Meyers R., Cantley L.C.
      J. Biol. Chem. 272:13236-13241(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex."
      Godi A., Pertile P., Meyers R., Marra P., Di Tullio G., Iurisci C., Luini A., Corda D., De Matteis M.A.
      Nat. Cell Biol. 1:280-287(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Human phosphatidylinositol 4-kinase isoform PI4K92. Expression of the recombinant enzyme and determination of multiple phosphorylation sites."
      Suer S., Sickmann A., Meyer H.E., Herberg F.W., Heilmeyer L.M.G. Jr.
      Eur. J. Biochem. 268:2099-2106(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-258; THR-263; SER-266; SER-277; SER-294; THR-438; SER-511 AND THR-519.
    11. Cited for: FUNCTION.
    12. "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-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta."
      Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.
      Traffic 8:1080-1092(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARF1 AND ARF3, SUBCELLULAR LOCATION.
    14. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-277; SER-428 AND SER-511, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-266 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPI4KB_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBF8
    Secondary accession number(s): B4DGI2
    , O15096, P78405, Q5VWB9, Q5VWC0, Q5VWC1, Q9BWR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 122 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 1
      Human chromosome 1: 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