Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q99755

- PI51A_HUMAN

UniProt

Q99755 - PI51A_HUMAN

Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha

Gene

PIP5K1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs.3 Publications

    Catalytic activityi

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. activation of Rac GTPase activity Source: UniProtKB
    3. cell chemotaxis Source: UniProtKB
    4. cell migration Source: UniProtKB
    5. fibroblast migration Source: Ensembl
    6. focal adhesion assembly Source: UniProtKB
    7. glycerophospholipid metabolic process Source: ProtInc
    8. keratinocyte differentiation Source: UniProtKB
    9. phagocytosis Source: UniProtKB
    10. phosphatidylinositol biosynthetic process Source: Reactome
    11. phosphatidylinositol phosphorylation Source: GOC
    12. phospholipid biosynthetic process Source: UniProtKB
    13. phospholipid metabolic process Source: Reactome
    14. protein targeting to plasma membrane Source: UniProtKB
    15. ruffle assembly Source: UniProtKB
    16. signal transduction Source: ProtInc
    17. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07047-MONOMER.
    BRENDAi2.7.1.68. 2681.
    ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
    SignaLinkiQ99755.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (EC:2.7.1.68)
    Short name:
    PIP5K1-alpha
    Short name:
    PtdIns(4)P-5-kinase 1 alpha
    Alternative name(s):
    68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha
    Phosphatidylinositol 4-phosphate 5-kinase type I alpha
    Short name:
    PIP5KIalpha
    Gene namesi
    Name:PIP5K1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8994. PIP5K1A.

    Subcellular locationi

    Cell membrane. Cytoplasm By similarity. Nucleus speckle. Cell projectionruffle
    Note: Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. lamellipodium Source: UniProtKB
    4. nuclear speck Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. plasma membrane Source: UniProtKB
    7. ruffle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi322 – 3221D → N: Does not affect targeting of RAC1 to the plasma membrane; when associated with Q-440. 1 Publication
    Mutagenesisi440 – 4401R → Q: Does not affect targeting of RAC1 to the plasma membrane; when associated with N-322. 1 Publication

    Organism-specific databases

    PharmGKBiPA33327.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 562562Phosphatidylinositol 4-phosphate 5-kinase type-1 alphaPRO_0000185456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki103 – 103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ99755.
    PaxDbiQ99755.
    PRIDEiQ99755.

    PTM databases

    PhosphoSiteiQ99755.

    Miscellaneous databases

    PMAP-CutDBQ99755.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in brain, lung and liver.

    Gene expression databases

    ArrayExpressiQ99755.
    BgeeiQ99755.
    CleanExiHS_PIP5K1A.
    GenevestigatoriQ99755.

    Organism-specific databases

    HPAiHPA029366.

    Interactioni

    Subunit structurei

    Interacts with RAC1 By similarity. Interacts with TUT1. Forms a complex with CDH1/E-cadherin, CTNNB1/beta-catenin and CTNND1 at the plasma membrane upon calcium stimulation.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi113983. 7 interactions.
    DIPiDIP-60649N.
    IntActiQ99755. 3 interactions.
    MINTiMINT-1406942.
    STRINGi9606.ENSP00000357883.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99755.
    SMRiQ99755. Positions 82-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 449369PIPKPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PIPK domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5148.
    HOGENOMiHOG000193876.
    HOVERGENiHBG052818.
    InParanoidiQ99755.
    KOiK00889.
    OMAiETEDHMG.
    OrthoDBiEOG70W3DM.
    PhylomeDBiQ99755.
    TreeFamiTF319618.

    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99755-1) [UniParc]FASTAAdd to Basket

    Also known as: PIP5KIalpha2

    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

    MASASSGPSS SVGFSSFDPA VPSCTLSSAA SGIKRPMASE VLEARQDSYI    50
    SLVPYASGMP IKKIGHRSVD SSGETTYKKT TSSALKGAIQ LGITHTVGSL 100
    STKPERDVLM QDFYVVESIF FPSEGSNLTP AHHYNDFRFK TYAPVAFRYF 150
    RELFGIRPDD YLYSLCSEPL IELCSSGASG SLFYVSSDDE FIIKTVQHKE 200
    AEFLQKLLPG YYMNLNQNPR TLLPKFYGLY CVQAGGKNIR IVVMNNLLPR 250
    SVKMHIKYDL KGSTYKRRAS QKEREKPLPT FKDLDFLQDI PDGLFLDADM 300
    YNALCKTLQR DCLVLQSFKI MDYSLLMSIH NIDHAQREPL SSETQYSVDT 350
    RRPAPQKALY STAMESIQGE ARRGGTMETD DHMGGIPARN SKGERLLLYI 400
    GIIDILQSYR FVKKLEHSWK ALVHDGDTVS VHRPGFYAER FQRFMCNTVF 450
    KKIPLKPSPS KKFRSGSSFS RRAGSSGNSC ITYQPSVSGE HKAQVTTKAE 500
    VEPGVHLGRP DVLPQTPPLE EISEGSPIPD PSFSPLVGET LQMLTTSTTL 550
    EKLEVAESEF TH 562
    Length:562
    Mass (Da):62,633
    Last modified:May 1, 1997 - v1
    Checksum:iA8F7988EB73506A0
    GO
    Isoform 2 (identifier: Q99755-2) [UniParc]FASTAAdd to Basket

    Also known as: PIP5KIalpha3

    The sequence of this isoform differs from the canonical sequence as follows:
         30-52: ASGIKRPMASEVLEARQDSYISL → SGIKRPMASE
         455-504: LKPSPSKKFRSGSSFSRRAGSSGNSCITYQPSVSGEHKAQVTTKAEVEPG → C

    Show »
    Length:500
    Mass (Da):56,053
    Checksum:i684F0C9C2DBE9EC4
    GO
    Isoform 3 (identifier: Q99755-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         30-52: ASGIKRPMASEVLEARQDSYISL → SGIKRPMASE

    Show »
    Length:549
    Mass (Da):61,187
    Checksum:i7CD48BFE175564A0
    GO
    Isoform 4 (identifier: Q99755-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         41-52: Missing.
         382-410: HMGGIPARNSKGERLLLYIGIIDILQSYR → Q

    Show »
    Length:522
    Mass (Da):58,119
    Checksum:i693CE47DBFC72B5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti257 – 2571K → E in BAG58542. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei30 – 5223ASGIK…SYISL → SGIKRPMASE in isoform 2 and isoform 3. 3 PublicationsVSP_016007Add
    BLAST
    Alternative sequencei41 – 5212Missing in isoform 4. 1 PublicationVSP_041912Add
    BLAST
    Alternative sequencei382 – 41029HMGGI…LQSYR → Q in isoform 4. 1 PublicationVSP_041913Add
    BLAST
    Alternative sequencei455 – 50450LKPSP…EVEPG → C in isoform 2. 2 PublicationsVSP_016008Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78575 mRNA. Translation: AAC50910.1.
    U78576 mRNA. Translation: AAC50911.1.
    U78577 mRNA. Translation: AAC50912.1.
    AK291015 mRNA. Translation: BAF83704.1.
    AK295691 mRNA. Translation: BAG58542.1.
    AL592424 Genomic DNA. Translation: CAI16386.1.
    AL592424 Genomic DNA. Translation: CAI16387.1.
    AL592424 Genomic DNA. Translation: CAI16388.1.
    CH471121 Genomic DNA. Translation: EAW53461.1.
    BC007833 mRNA. Translation: AAH07833.1.
    CCDSiCCDS44219.1. [Q99755-1]
    CCDS44220.1. [Q99755-4]
    CCDS44221.1. [Q99755-2]
    CCDS990.1. [Q99755-3]
    RefSeqiNP_001129108.1. NM_001135636.1. [Q99755-4]
    NP_001129109.1. NM_001135637.1. [Q99755-2]
    NP_001129110.1. NM_001135638.1. [Q99755-1]
    NP_003548.1. NM_003557.2. [Q99755-3]
    UniGeneiHs.655131.
    Hs.661888.

    Genome annotation databases

    EnsembliENST00000349792; ENSP00000271663; ENSG00000143398. [Q99755-3]
    ENST00000368888; ENSP00000357883; ENSG00000143398. [Q99755-1]
    ENST00000368890; ENSP00000357885; ENSG00000143398. [Q99755-2]
    ENST00000441902; ENSP00000415648; ENSG00000143398. [Q99755-4]
    GeneIDi8394.
    KEGGihsa:8394.
    UCSCiuc001exi.3. human. [Q99755-3]
    uc001exj.3. human. [Q99755-1]
    uc001exk.3. human. [Q99755-2]
    uc010pcu.2. human. [Q99755-4]

    Polymorphism databases

    DMDMi74752158.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78575 mRNA. Translation: AAC50910.1 .
    U78576 mRNA. Translation: AAC50911.1 .
    U78577 mRNA. Translation: AAC50912.1 .
    AK291015 mRNA. Translation: BAF83704.1 .
    AK295691 mRNA. Translation: BAG58542.1 .
    AL592424 Genomic DNA. Translation: CAI16386.1 .
    AL592424 Genomic DNA. Translation: CAI16387.1 .
    AL592424 Genomic DNA. Translation: CAI16388.1 .
    CH471121 Genomic DNA. Translation: EAW53461.1 .
    BC007833 mRNA. Translation: AAH07833.1 .
    CCDSi CCDS44219.1. [Q99755-1 ]
    CCDS44220.1. [Q99755-4 ]
    CCDS44221.1. [Q99755-2 ]
    CCDS990.1. [Q99755-3 ]
    RefSeqi NP_001129108.1. NM_001135636.1. [Q99755-4 ]
    NP_001129109.1. NM_001135637.1. [Q99755-2 ]
    NP_001129110.1. NM_001135638.1. [Q99755-1 ]
    NP_003548.1. NM_003557.2. [Q99755-3 ]
    UniGenei Hs.655131.
    Hs.661888.

    3D structure databases

    ProteinModelPortali Q99755.
    SMRi Q99755. Positions 82-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113983. 7 interactions.
    DIPi DIP-60649N.
    IntActi Q99755. 3 interactions.
    MINTi MINT-1406942.
    STRINGi 9606.ENSP00000357883.

    Chemistry

    BindingDBi Q99755.
    ChEMBLi CHEMBL5969.
    GuidetoPHARMACOLOGYi 2164.

    PTM databases

    PhosphoSitei Q99755.

    Polymorphism databases

    DMDMi 74752158.

    Proteomic databases

    MaxQBi Q99755.
    PaxDbi Q99755.
    PRIDEi Q99755.

    Protocols and materials databases

    DNASUi 8394.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000349792 ; ENSP00000271663 ; ENSG00000143398 . [Q99755-3 ]
    ENST00000368888 ; ENSP00000357883 ; ENSG00000143398 . [Q99755-1 ]
    ENST00000368890 ; ENSP00000357885 ; ENSG00000143398 . [Q99755-2 ]
    ENST00000441902 ; ENSP00000415648 ; ENSG00000143398 . [Q99755-4 ]
    GeneIDi 8394.
    KEGGi hsa:8394.
    UCSCi uc001exi.3. human. [Q99755-3 ]
    uc001exj.3. human. [Q99755-1 ]
    uc001exk.3. human. [Q99755-2 ]
    uc010pcu.2. human. [Q99755-4 ]

    Organism-specific databases

    CTDi 8394.
    GeneCardsi GC01P151170.
    HGNCi HGNC:8994. PIP5K1A.
    HPAi HPA029366.
    MIMi 603275. gene.
    neXtProti NX_Q99755.
    PharmGKBi PA33327.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5148.
    HOGENOMi HOG000193876.
    HOVERGENi HBG052818.
    InParanoidi Q99755.
    KOi K00889.
    OMAi ETEDHMG.
    OrthoDBi EOG70W3DM.
    PhylomeDBi Q99755.
    TreeFami TF319618.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07047-MONOMER.
    BRENDAi 2.7.1.68. 2681.
    Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
    SignaLinki Q99755.

    Miscellaneous databases

    ChiTaRSi PIP5K1A. human.
    GeneWikii PIP5K1A.
    GenomeRNAii 8394.
    NextBioi 31416.
    PMAP-CutDB Q99755.
    PROi Q99755.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99755.
    Bgeei Q99755.
    CleanExi HS_PIP5K1A.
    Genevestigatori Q99755.

    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. "Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family."
      Loijens J.C., Anderson R.A.
      J. Biol. Chem. 271:32937-32943(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Fetal brain.
    2. "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] (ISOFORMS 3 AND 4).
      Tissue: Hippocampus.
    3. "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].
    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] (ISOFORM 2).
      Tissue: Muscle.
    6. "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
      Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
      Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TUT1.
    7. "Phosphatidylinositol-4-phosphate 5-kinase 1alpha mediates extracellular calcium-induced keratinocyte differentiation."
      Xie Z., Chang S.M., Pennypacker S.D., Liao E.-Y., Bikle D.D.
      Mol. Biol. Cell 20:1695-1704(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN KERATINOCYTE DIFFERENTIATION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH CDH1; CTNNB1 AND CTNND1.
    8. "Type I PIPK-alpha regulates directed cell migration by modulating Rac1 plasma membrane targeting and activation."
      Chao W.-T., Daquinag A.C., Ashcroft F., Kunz J.
      J. Cell Biol. 190:247-262(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-322 AND ARG-440.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPI51A_HUMAN
    AccessioniPrimary (citable) accession number: Q99755
    Secondary accession number(s): A8K4Q0
    , B4DIN0, Q99754, Q99756
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    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

    Caution

    There is confusion in the literature with phosphatidylinositol 4-phosphate 5-kinase type I nomenclature due to the fact that frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-kinase type I alpha.Curated

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3