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)

D3ZSI8

- PI51A_RAT

UniProt

D3ZSI8 - PI51A_RAT

Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha

Gene

Pip5k1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 1 (20 Apr 2010)
      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 it acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs By similarity.By similarity

    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-EC
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: Ensembl
    2. activation of Rac GTPase activity Source: Ensembl
    3. cell chemotaxis Source: Ensembl
    4. fibroblast migration Source: Ensembl
    5. focal adhesion assembly Source: Ensembl
    6. phospholipid biosynthetic process Source: Ensembl
    7. protein targeting to plasma membrane Source: Ensembl
    8. ruffle assembly Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198600. Synthesis of PIPs at the plasma membrane.

    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
    Phosphatidylinositol 4-phosphate 5-kinase type I alpha
    Short name:
    PIP5KIalpha
    Gene namesi
    Name:Pip5k1a
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi1306127. Pip5k1a.

    Subcellular locationi

    Cell membrane By similarity. Nucleus speckle By similarity. Cytoplasm. Cell projectionruffle By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. lamellipodium Source: Ensembl
    3. mRNA cleavage and polyadenylation specificity factor complex Source: Ensembl
    4. nuclear speck Source: UniProtKB-SubCell
    5. ruffle membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 546546Phosphatidylinositol 4-phosphate 5-kinase type-1 alphaPRO_0000424437Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki87 – 87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Interactioni

    Subunit structurei

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 433369PIPKPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PIPK domain.PROSITE-ProRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00690000101870.
    OMAiETEDHMG.
    OrthoDBiEOG70W3DM.
    PhylomeDBiD3ZSI8.
    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]

    Sequencei

    Sequence statusi: Complete.

    D3ZSI8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASASSGPAA AGFSPLDSGV PAGTAASGIK RGTVSEGPYA SLMPVKKIGH    50
    RSVDSSGETT YKKTTSSALK GAIQLGITHT VGSLSTKPER DVLMQDFYVV 100
    ESIFFPSEGS NLTPAHHYND FRFKTYAPVA FRYFRELFGI RPDDYLYSLC 150
    SEPLIELSNS GASGSLFYVS SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN 200
    QNPRTLLPKF YGLYCVQAGG KNIRIVVMNN LLPRSVKMHM KYDLKGSTYK 250
    RRASQKEREK TLPTFKDLDF LQDIPDGLFL DADMYSALCK TLQRDCLVLQ 300
    SFKIMDYSLL MSIHNMDHAQ REPMNSETQY SIDTRRPAPQ KALYSTAMES 350
    IQGEARRGGT VETEDHMGGI PARNNKGERL LLYIGIIDIL QSYRFVKKLE 400
    HSWKALVHDG DTVSVHRPGF YAERFQRFMC NTVFKKIPLK PSPTKKFRSG 450
    PSFSRRSGPS GNSCTPSQPT ASGEHKAQVT TKAEVEPDIH LGRPDVLPQT 500
    PPLEEISEGS PVPGPSFSPA VGQPLQILNL SSTLEKLDVA ESELTH 546
    Length:546
    Mass (Da):60,605
    Last modified:April 20, 2010 - v1
    Checksum:iF0DF7489A100D9C3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY724476 mRNA. No translation available.
    AABR06019271 Genomic DNA. No translation available.
    UniGeneiRn.1836.

    Genome annotation databases

    EnsembliENSRNOT00000028609; ENSRNOP00000028609; ENSRNOG00000021068.
    UCSCiRGD:1306127. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY724476 mRNA. No translation available.
    AABR06019271 Genomic DNA. No translation available.
    UniGenei Rn.1836.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000028609 ; ENSRNOP00000028609 ; ENSRNOG00000021068 .
    UCSCi RGD:1306127. rat.

    Organism-specific databases

    RGDi 1306127. Pip5k1a.

    Phylogenomic databases

    GeneTreei ENSGT00690000101870.
    OMAi ETEDHMG.
    OrthoDBi EOG70W3DM.
    PhylomeDBi D3ZSI8.
    TreeFami TF319618.

    Enzyme and pathway databases

    Reactomei REACT_198600. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    NextBioi 35569837.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.

    Entry informationi

    Entry nameiPI51A_RAT
    AccessioniPrimary (citable) accession number: D3ZSI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2013
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 33 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3