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P48426

- PI42A_HUMAN

UniProt

P48426 - PI42A_HUMAN

Protein

Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha

Gene

PIP4K2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P. May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size.1 Publication

    Catalytic activityi

    ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.1 Publication

    Kineticsi

    1. KM=50 µM for phosphatidylinositol-5- phosphate1 Publication

    Vmax=466 pmol/min/µg enzyme1 Publication

    GO - Molecular functioni

    1. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: UniProtKB
    2. 1-phosphatidylinositol-5-phosphate 4-kinase activity Source: UniProtKB-EC
    3. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. megakaryocyte development Source: Ensembl
    2. phosphatidylinositol biosynthetic process Source: Reactome
    3. phosphatidylinositol phosphorylation Source: GOC
    4. phospholipid metabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07693-MONOMER.
    ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC:2.7.1.149)
    Alternative name(s):
    1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha
    Diphosphoinositide kinase 2-alpha
    PIP5KIII
    Phosphatidylinositol 5-phosphate 4-kinase type II alpha
    Short name:
    PI(5)P 4-kinase type II alpha
    Short name:
    PIP4KII-alpha
    PtdIns(4)P-5-kinase B isoform
    PtdIns(4)P-5-kinase C isoform
    PtdIns(5)P-4-kinase isoform 2-alpha
    Gene namesi
    Name:PIP4K2A
    Synonyms:PIP5K2, PIP5K2A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8997. PIP4K2A.

    Subcellular locationi

    Cell membrane By similarity. Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to light By similarity. Localization to the nucleus is modulated by the interaction with PIP4K2B.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1311G → L: Abolishes catalytic activity; when associated with F-138. 1 Publication
    Mutagenesisi138 – 1381Y → F: Abolishes catalytic activity; when associated with L-131. 1 Publication

    Organism-specific databases

    Orphaneti99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBiPA162399615.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Phosphatidylinositol 5-phosphate 4-kinase type-2 alphaPRO_0000185465Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei89 – 891N6-acetyllysine1 Publication
    Modified residuei145 – 1451N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48426.
    PaxDbiP48426.
    PeptideAtlasiP48426.
    PRIDEiP48426.

    2D gel databases

    OGPiP48426.

    PTM databases

    PhosphoSiteiP48426.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously, with high levels in the brain. Present in most tissues, except notably skeletal muscle and small intestine.2 Publications

    Gene expression databases

    ArrayExpressiP48426.
    BgeeiP48426.
    CleanExiHS_PIP4K2A.
    GenevestigatoriP48426.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with PIP4K2B. Interaction with PIP4K2B may regulate localization to the nucleus.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi111322. 5 interactions.
    IntActiP48426. 4 interactions.
    MINTiMINT-1507380.
    STRINGi9606.ENSP00000365757.

    Structurei

    Secondary structure

    1
    406
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 5217
    Helixi63 – 675
    Beta strandi69 – 8012
    Turni81 – 833
    Beta strandi86 – 949
    Helixi95 – 10410
    Helixi109 – 1179
    Beta strandi134 – 1363
    Beta strandi140 – 1478
    Helixi149 – 16820
    Turni169 – 1713
    Beta strandi178 – 1869
    Beta strandi189 – 1979
    Beta strandi202 – 2043
    Beta strandi207 – 2126
    Beta strandi215 – 2173
    Helixi223 – 2264
    Beta strandi228 – 2303
    Helixi235 – 2406
    Helixi249 – 26820
    Beta strandi271 – 2733
    Beta strandi275 – 2828
    Helixi283 – 2919
    Turni334 – 3363
    Beta strandi340 – 3423
    Beta strandi351 – 3588
    Beta strandi362 – 3643
    Helixi390 – 40415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YBXX-ray2.56A/B35-405[»]
    ProteinModelPortaliP48426.
    SMRiP48426. Positions 31-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 405373PIPKPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PIPK domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5253.
    HOGENOMiHOG000007832.
    HOVERGENiHBG000072.
    InParanoidiP48426.
    KOiK00920.
    OMAiIVECHGV.
    OrthoDBiEOG708VZZ.
    PhylomeDBiP48426.
    TreeFamiTF354315.

    Family and domain databases

    Gene3Di3.30.800.10. 1 hit.
    3.30.810.10. 1 hit.
    InterProiIPR023610. PInositol-4-P-5-kinase.
    IPR027483. PInositol-4-P-5-kinase_C.
    IPR002498. PInositol-4-P-5-kinase_core.
    IPR027484. PInositol-4-P-5-kinase_N.
    IPR016034. PInositol-4P-5-kinase_core_sub.
    [Graphical view]
    PANTHERiPTHR23086. PTHR23086. 1 hit.
    PfamiPF01504. PIP5K. 1 hit.
    [Graphical view]
    SMARTiSM00330. PIPKc. 1 hit.
    [Graphical view]
    PROSITEiPS51455. PIPK. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P48426-1) [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

    MATPGNLGSS VLASKTKTKK KHFVAQKVKL FRASDPLLSV LMWGVNHSIN    50
    ELSHVQIPVM LMPDDFKAYS KIKVDNHLFN KENMPSHFKF KEYCPMVFRN 100
    LRERFGIDDQ DFQNSLTRSA PLPNDSQARS GARFHTSYDK RYIIKTITSE 150
    DVAEMHNILK KYHQYIVECH GITLLPQFLG MYRLNVDGVE IYVIVTRNVF 200
    SHRLSVYRKY DLKGSTVARE ASDKEKAKEL PTLKDNDFIN EGQKIYIDDN 250
    NKKVFLEKLK KDVEFLAQLK LMDYSLLVGI HDVERAEQEE VECEENDGEE 300
    EGESDGTHPV GTPPDSPGNT LNSSPPLAPG EFDPNIDVYG IKCHENSPRK 350
    EVYFMAIIDI LTHYDAKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFLDF 400
    IGHILT 406
    Length:406
    Mass (Da):46,225
    Last modified:August 14, 2001 - v2
    Checksum:i5BAF0A27CC9EF376
    GO
    Isoform 2 (identifier: P48426-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:347
    Mass (Da):39,802
    Checksum:iE8E3F2DADE991A74
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1033LRE → CGK in AAB35041. (PubMed:7639683)Curated
    Sequence conflicti109 – 1091D → V in AAB35041. (PubMed:7639683)Curated
    Sequence conflicti143 – 1431I → M in AAB35041. (PubMed:7639683)Curated
    Sequence conflicti177 – 1782QF → HL in AAB35041. (PubMed:7639683)Curated
    Sequence conflicti333 – 3331D → E in AAB35041. (PubMed:7639683)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71L → I.
    Corresponds to variant rs11813789 [ dbSNP | Ensembl ].
    VAR_059764
    Natural varianti251 – 2511N → S.1 Publication
    Corresponds to variant rs10828317 [ dbSNP | Ensembl ].
    VAR_024565

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5959Missing in isoform 2. 1 PublicationVSP_056458Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14957 mRNA. Translation: AAA64835.2.
    S78798 mRNA. Translation: AAB35041.1.
    AL513128, AL157707, AL390318 Genomic DNA. Translation: CAH72211.1.
    AK294817 mRNA. Translation: BAG57933.1.
    EF445009 Genomic DNA. Translation: ACA06044.1.
    EF445009 Genomic DNA. Translation: ACA06045.1.
    AL157707, AL390318, AL513128 Genomic DNA. Translation: CAI39585.1.
    AL390318, AL157707, AL513128 Genomic DNA. Translation: CAH70526.1.
    CH471072 Genomic DNA. Translation: EAW86140.1.
    CH471072 Genomic DNA. Translation: EAW86141.1.
    BC018034 mRNA. Translation: AAH18034.1.
    CCDSiCCDS7141.1.
    PIRiA55967.
    S57217.
    RefSeqiNP_005019.2. NM_005028.4.
    UniGeneiHs.57079.

    Genome annotation databases

    EnsembliENST00000376573; ENSP00000365757; ENSG00000150867.
    ENST00000545335; ENSP00000442098; ENSG00000150867.
    GeneIDi5305.
    KEGGihsa:5305.
    UCSCiuc001irl.4. human.

    Polymorphism databases

    DMDMi18266879.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14957 mRNA. Translation: AAA64835.2 .
    S78798 mRNA. Translation: AAB35041.1 .
    AL513128 , AL157707 , AL390318 Genomic DNA. Translation: CAH72211.1 .
    AK294817 mRNA. Translation: BAG57933.1 .
    EF445009 Genomic DNA. Translation: ACA06044.1 .
    EF445009 Genomic DNA. Translation: ACA06045.1 .
    AL157707 , AL390318 , AL513128 Genomic DNA. Translation: CAI39585.1 .
    AL390318 , AL157707 , AL513128 Genomic DNA. Translation: CAH70526.1 .
    CH471072 Genomic DNA. Translation: EAW86140.1 .
    CH471072 Genomic DNA. Translation: EAW86141.1 .
    BC018034 mRNA. Translation: AAH18034.1 .
    CCDSi CCDS7141.1.
    PIRi A55967.
    S57217.
    RefSeqi NP_005019.2. NM_005028.4.
    UniGenei Hs.57079.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YBX X-ray 2.56 A/B 35-405 [» ]
    ProteinModelPortali P48426.
    SMRi P48426. Positions 31-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111322. 5 interactions.
    IntActi P48426. 4 interactions.
    MINTi MINT-1507380.
    STRINGi 9606.ENSP00000365757.

    Chemistry

    ChEMBLi CHEMBL1795194.

    PTM databases

    PhosphoSitei P48426.

    Polymorphism databases

    DMDMi 18266879.

    2D gel databases

    OGPi P48426.

    Proteomic databases

    MaxQBi P48426.
    PaxDbi P48426.
    PeptideAtlasi P48426.
    PRIDEi P48426.

    Protocols and materials databases

    DNASUi 5305.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376573 ; ENSP00000365757 ; ENSG00000150867 .
    ENST00000545335 ; ENSP00000442098 ; ENSG00000150867 .
    GeneIDi 5305.
    KEGGi hsa:5305.
    UCSCi uc001irl.4. human.

    Organism-specific databases

    CTDi 5305.
    GeneCardsi GC10M022823.
    HGNCi HGNC:8997. PIP4K2A.
    MIMi 603140. gene.
    neXtProti NX_P48426.
    Orphaneti 99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBi PA162399615.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5253.
    HOGENOMi HOG000007832.
    HOVERGENi HBG000072.
    InParanoidi P48426.
    KOi K00920.
    OMAi IVECHGV.
    OrthoDBi EOG708VZZ.
    PhylomeDBi P48426.
    TreeFami TF354315.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07693-MONOMER.
    Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    ChiTaRSi PIP4K2A. human.
    GeneWikii PIP4K2A.
    GenomeRNAii 5305.
    NextBioi 20506.
    PROi P48426.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48426.
    Bgeei P48426.
    CleanExi HS_PIP4K2A.
    Genevestigatori P48426.

    Family and domain databases

    Gene3Di 3.30.800.10. 1 hit.
    3.30.810.10. 1 hit.
    InterProi IPR023610. PInositol-4-P-5-kinase.
    IPR027483. PInositol-4-P-5-kinase_C.
    IPR002498. PInositol-4-P-5-kinase_core.
    IPR027484. PInositol-4-P-5-kinase_N.
    IPR016034. PInositol-4P-5-kinase_core_sub.
    [Graphical view ]
    PANTHERi PTHR23086. PTHR23086. 1 hit.
    Pfami PF01504. PIP5K. 1 hit.
    [Graphical view ]
    SMARTi SM00330. PIPKc. 1 hit.
    [Graphical view ]
    PROSITEi PS51455. PIPK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases."
      Boronenkov I.V., Anderson R.A.
      J. Biol. Chem. 270:2881-2884(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-42; 74-88; 93-112; 141-145; 254-259; 281-297 AND 383-406, TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. Boronenkov I.V.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 298-310 AND 381-382.
    3. "The cloning and sequence of the C isoform of PtdIns4P 5-kinase."
      Divecha N., Truong O., Hsuan J.J., Hinchliffe K.A., Irvine R.F.
      Biochem. J. 309:715-719(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-251.
      Tissue: Leukocyte.
    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 2).
      Tissue: Brain.
    5. NHLBI resequencing and genotyping service (RS&G)
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Hippocampus.
    9. "A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate."
      Rameh L.E., Tolias K.F., Duckworth B.C., Cantley L.C.
      Nature 390:192-196(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    10. "Regulation of extranuclear PtdIns5P production by phosphatidylinositol phosphate 4-kinase 2alpha."
      Wilcox A., Hinchliffe K.A.
      FEBS Lett. 582:1391-1394(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89 AND LYS-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "PIP4Kbeta interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha."
      Bultsma Y., Keune W.-J., Divecha N.
      Biochem. J. 430:223-235(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH PIP4K2B, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-131 AND TYR-138, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Localization, regulation and function of type II phosphatidylinositol 5-phosphate 4-kinases."
      Clarke J.H., Wang M., Irvine R.F.
      Adv. Enzyme Regul. 50:12-18(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPI42A_HUMAN
    AccessioniPrimary (citable) accession number: P48426
    Secondary accession number(s): B0YJ66
    , B4DGX2, D3DRV1, P53807, Q5VUX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 125 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3